HLA tumor antigen polypeptides with delivering aiding capping peptides and pharmaceutical composition comprising the same

Abstract

The present invention relates to an H LA tumor antigen polypeptide comprising a cell-penetrating peptide (HTAPP-CPP) use as a medicament in the therapeutic and prophylactic treatment of carcinomas. The HLA tumor antigen polypeptide comprises a cell-penetrating peptide (HTAPP-CPP) and further comprises HLA tumor antigen peptides (HTAP) associated with MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide (HTAPP). These HTAP are tumor-specific or tumor-associated. The HLA tumor antigen polypeptide (HTAPP) is provided as a tandem polypeptide or an overlapping tandem polypeptide, both comprising at least 2 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes. This invention further comprises a method for determining an pharmaceutical composition comprising HLA tumor antigen polypeptide(s), a method for preparing a formulation according to the invention, and the use of a composition and formulation according to the invention for the preparation of a pharmaceutical composition.

Description

[0001]HLA TUMOR ANTIGEN POLYPEPTIDES WITH DELIVERING AIDING CAPPING PEPTIDES AND PHARMACEUTICAL COMPOSITION COMPRISING THE SAME Technical area The invention pertains to HLA tumor antigen polypeptide comprising a delivery aiding capping peptide (HTAPP-DACP), which is a terminally attached cell penetrating peptide (CPP), for use as a medicament, in particular for the therapeutic and prophylactic treatment of carcinoma, particularly locally recurrent or metastatic carcinoma. The HLA tumor antigen polypeptide with a delivery aiding capping peptide (HTAPP-DACP) comprises HLA tumor antigen peptides (HTAP) associated with MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide (HTAPP). These HTAP are tumor-specific or tumor-associated and presented on tumor cell membranes. The HLA tumor antigen polypeptide features a scaffold amino acid sequence, also simply referred to as amino acid sequence, with options for extended sequences, high sequence identity to native HLA tumor antigen peptides, or minimal amino acid substitutions. The HLA tumor antigen polypeptide (HTAPP) may exist as a tandem polypeptide or an overlapping tandem polypeptide, both comprising at least 2 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes. This invention offers a versatile approach to treating carcinoma by leveraging HLA tumor antigen peptides and their various polypeptide compositions, enhancing treatment efficacy for recurrent or metastatic carcinoma and further comprises a pharmaceutical composition comprising HTAPP-DACP(s), a method for determining an pharmaceutical composition comprising HLA tumor antigen polypeptide(s), a method for preparing a formulation according to the invention, and the use of a formulation according to the invention for the preparation of a pharmaceutical composition for the treatment of malignancies, leukemias and neoplasms. State of the art Despite interdisciplinary approaches and exhaustion of classical therapies, cancers remain among the leading causes of death. In general, cancer is treated by established methods such as surgical tumor removal (resection), chemotherapy and / or radiotherapy. In particular, the development of resistance by cancer cells during chemotherapy and / or radiotherapy mostly prevents the complete removal of all cancer cells from a subject's body. Newer therapeutic concepts aim to involve the subject's own immune system in the overall therapeutic concept by using specific measures such as antibody therapy against immunosuppressors and recombinant immunoinformatics (i.e. treatment with information carriers). A prerequisite for the success of such a strategy is the recognition of tumor-specific or tumor-associated antigens or epitopes by the immune system of the subject whose effector functions (by the immune cells) are to be enhanced. Tumor cells differ biologically substantially from their non-malignant cells of origin. These differences are due to genetic alterations acquired during tumor development, which lead, among other things, to the formation of qualitatively or quantitatively altered molecular structures in the tumor cells. If such tumor-associated structures are recognized by the specific immune system of the tumor-bearing host, they are referred to as tumor-associated epitopes. Cancer / testis antigens (CTAs) refer to a group of tumor-associated proteins expressed by tumors of various histological origins, among others (Fratta et al., Molecular Oncology, 5(2), April 2011, 164-182). In healthy adult vertebrates, expression of these proteins is restricted to male germ cells. However, in cancer, expression of these developmental antigens is often reactivated and thus can serve as a site of immune activation. Many of the CTAs are oncogenes and are involved in cellular processes such as cell growth and division, inhibition of apoptosis, and metastasis. They are often causative for oncogenesis and malignant transformation and are therefore classified as tumor antigens. The expression of CTAs in different malignancies is heterogeneous and often correlates with tumor progression, which is why they also serve as biomarkers for tumor disease progression. HLA antigen peptides of such CTAs are often presented as degradation products on the surface of tumor cells. It is known that such presentation of CTA-derived HLA antigen peptides can be used for the development of new treatment modalities combining drug treatment with anti-CTA- targeted immunotherapy. Human leukocyte antigens (also called HLA system, HL antigens, histocompatibility antigens, human leukocyte antigen) are a group of human genes that are central to the function of the immune system. The HLA system is known as the major histocompatibility complex (MHC) and is found in all vertebrates. There are two types of MHCs, namely class I MHC molecules (herein also referred to as "class I MHC complexes" or "class I HLA complexes") and class II MHC molecules (herein also referred to as "class II MHC complexes" or "class II HLA complexes"). Both are found on the cell surface of all nucleated cells in the bodies of mandibular vertebrates. MHC molecules consist of two polypeptide chains, an α-chain heavy chain and a β-chain light chain (see also Figs.1 and 2). Class I MHC molecules are expressed on the cell surface of all nucleated cells and recognized by CD8+ T cells (also referred to as T killer cells or cytotoxic T cells). Class II MHC molecules are mainly exposed on the cell surface of antigen-presenting cells and recognized by CD4+ T cells (also referred to as T helper cells). In blood cells, class I MHC molecules are exposed on the cell surface of platelets, but not on red blood cells. Their function is to present peptide fragments of non-self-proteins on their cell surface and transfer them out of the cell into killer T cells (also cytotoxic T cells) to trigger an immediate immune system response against a specific non-self-antigen presented using an MHC class I protein. Because MHC class I molecules present peptides derived from cytosolic proteins, the pathway of presentation of MHC class I molecules is often referred to as the cytosolic or endogenous pathway. Here, HLA antigen peptides serve as mediators between the corresponding MHC complex presented on the cell surface and the T cell receptor. Class I HLA complexes (HLA-A, B, and C) present intracellular antigen peptide fragments (herein "HLA antigen peptides corresponding to MHC class I complexes" or "type 1 HLA antigen peptides" comprising 7 to 11, predominantly 9 amino acids - so-called nonamers - in their sequence) towards T killer cells (also cytotoxic T cells), whereas HLA class II complexes (HLA-DR, DQ and DP) present exogenously derived antigen peptides (herein "HLA antigen peptides corresponding to MHC class II complexes" or "HLA antigen peptides of type 2" comprising more than 11 amino acids, preferably 12 to 17 amino acids in their sequence) towards T helper cells. In humans, HLA antigen peptides of class I, corresponding to MHC class I, are subdivided into HLA-A, HLA-B, and HLA-C antigen peptides. It is known from the prior art that binding of HLA antigen peptides corresponding to MHC class II complexes to the peptide binding pocket of the corresponding class II HLA complexes occurs primarily via the discrete anchor residues in amino acid positions 1, 4, 6 / 7, and 9 of the HLA antigen peptides (see, e.g., Sinigaglia and Hammer (1995), J. Exp. Med., 181, 449-451). Particularly preferred according to the prior art is the interaction between the peptide binding pocket motif of the class II HLA complex and the discrete anchor residues in amino acid positions 6 and 9 of the HLA antigen peptides corresponding to MHC class II complexes. The amino acid residues in amino acid positions 2, 3, 5, 7 and 8 of the respective HLA antigen peptides are thereby available for interaction with the T-cell receptor (Sant' Angelo et al. (2002), Recognition of core and flanking amino acids of MHC class II-bound peptides by the T-cell receptor, Eur J Immunol, 32(9), 2510-20). In contrast, for HLA antigen peptides corresponding to MHC class I complexes, the amino acid positions 1, 2, and 9 have been postulated as the primary anchor residues relative to the corresponding class I HLA complex (see, for example, Binkowski et al. (2012), PLoS ONE, 7(8), e41710; Yamada (1999), Tissue Antigens, 54(4), 325-32). A new study in the USA is currently investigating the specific efficacy of only one HLA antigen peptide in the treatment of cancer (see WO 2013 / 135266, Inderberg-Suso et al. (2012), Oncoimmunology., 1(5), 670-686 and Slingluff (2011), Cancer J., 17(5), 343-350). Therefore, the therapeutic spectrum is very limited and by applying only one HLA antigen peptide, the efficacy is questionable. This is particularly true in a tumor entity such as carcinoma, which is characterized by low homogeneity (i.e., high heterogeneity) and lack of initial immunogenicity compared to other tumor entities. Clinically effective targeted immunoinformation and stimulation therapies therefore rely on a multifactorial information approach. A major disadvantage of cancer immunotherapies is therefore that they are based on the fact that the individual mutation pattern (signatures) of the tumor of each cancer subject must be decoded. Synthetic vaccines, for example RNA-based vaccines, are then produced to match the determined profile of the mutation pattern for each individual subject (so-called vaccine production). The vaccines obtained in this way can then only be used for the individual treatment of this particular subject. In principle, these novel vaccines in cancer immunotherapy are therefore not suitable for other subjects with the same tumor but can only be used for a single subject whose mutanoma was previously analyzed for vaccine production. WO 2016 / 187508 A2 discloses a pharmaceutical composition comprising a plurality of neoantigenic peptides and a pharmaceutically acceptable carrier, wherein each neoantigenic peptide comprises a tumor-specific neoepitope capable of binding to an HLA protein in a subject and comprises a tumor-specific mutation present in a subject. In addition, the composition comprises neoantigenic peptides comprising tumor-specific mutations present in a subset of subjects in a population of subjects suffering from cancer. Disadvantageously, it is only revealed here that a small percentage of the population, namely 5%, can be covered and furthermore no statement is made as to how different amino acid mutations in related genes can be covered. Furthermore, only single HLA antigen peptides are administered, not tandem or overlapping HLA tumor antigen polypeptides. The patent specification WO 03100432 A2 describes a method for identifying immunoreactive peptides, particularly in the context of tumor-related diseases. The method involves several key steps: (a) obtaining samples from both tumor tissue and corresponding healthy tissue, (b) determining the tumor-specific expression profile, (c) isolating and analyzing antigenic peptides from the tumor tissue sample, (d) comparing the data from steps (b) and (c), and (e) identifying peptides based on matched data. The antigenic peptides are identified as MHC ligands, and various analytical techniques such as microarray analysis, reverse transcriptase-polymerase chain reaction, and mass spectrometry are used in the process. On the downside, this approach does not provide guidance on how to screen for presented peptides on the tumor cell surface and does not disclose an approach to treat a group of subjects with different mutations or a method to combine different antigenic peptides on a single immunogenic HLA tumor antigen polypeptide. The specification WO 2019099440 A1 describes an alternative approach to immunogenic cancer therapy utilizing multi- functional chimeric antigen receptor (CAR)-based compositions. These compositions are designed to direct immune responses, particularly against hyperproliferative disorders like cancer. The key innovation involves the incorporation of an Adapter, which grants the capacity to modulate and redirect CAR cell-mediated immune responses both in laboratory settings (in vitro) and within the body (in vivo). Notably, certain embodiments include genetic modifications in CAR cells to suppress or eliminate the expression of specific antigenic determinants. While this approach offers promise for cancer treatment, it also has potential drawbacks such as cytokine release syndrome (CRS), potentially life-threatening uncontrolled release of cytokines, off-target effects, limited target antigens and antigens expressed on the surface of CAR-T cells, and difficulties in providing a general group therapy approach. The patent specification US 2019 / 307868 A1 discloses polypeptides comprising tumor-specific neoantigenic peptide(s) capable of binding to HLA class I and neoantigenic peptide(s) capable of binding to HLA class II, wherein the neoantigenic peptides are derived from mutations in genes such as BRAF, EGFR, ESR1, KIT, PTEN, or TP53. In addition, the specification discloses that such neoantigenic peptides may be assembled into multi-epitope vaccine constructs by linking individual HLA-binding peptides with appropriate linkers, and further contemplates the formulation of longer neoantigenic peptides. These longer peptides may be designed in several embodiments, for example by extending each binding peptide by 2–5 amino acids at the N- and C-termini, by concatenating multiple binding peptides with extended sequences, or by tiling overlapping peptides over an entire stretch of novel tumor-specific amino acids. Moreover, D1 discloses the potential incorporation of an in vivo delivery system, such as a cell-penetrating peptide exemplified by a TAT peptide, to facilitate efficient uptake of the vaccine components, although the disclosure remains inherently unclear regarding the precise nature or sequence of such delivery aiding peptides. Disadvantageously, while D1 provides a design of personalized neoantigen vaccines, it does not specify the exact lengths, amino acid compositions, or processing characteristics of the multi-epitope constructs, nor does it elucidate a robust strategy to address heterogeneous mutation profiles across a broad patient population. Patent specification CN 113069537 A discloses a fusion protein nanovaccine based on RAS variant neoepitope for the treatment of various tumors. In this disclosure, a fusion protein is constructed by randomly concatenating at least four different 17-amino acid RAS neoantigen peptides, each derived from the wild-type RAS protein but having substitutions at critical positions (e.g., amino acids 12, 13, 61, or 146) to represent common RAS mutations-with intervening (GGGGS)₃ linker sequences. In addition, the disclosed fusion protein is recombinantly expressed in Escherichia coli, purified, and then combined with an immunologic adjuvant (poly-ICLC) and degradable chitosan nanoparticles to form a nanovaccine formulation suitable for subcutaneous or intramuscular administration. While this approach may offer the advantage of increased antigen volume through the fusion of multiple neoepitopes, it is disadvantageous in that the reliance on random peptide concatenation may lead to variability in antigen processing and presentation, and the need for complexity of the nanoparticle formulation could affect the reproducibility and uniformity of the immune response across subjects. Some specifications relate to the use of single HLA-A or HLA-B tumor antigens or a combination thereof as "short peptides". For example, WO 2018145020 A1 discloses KRAS peptide vaccine compositions and methods of use for eliciting an anti-tumor immune response in subjects suffering from KRAS-associated malignancies. In the disclosure, the vaccine comprises a plurality of KRAS-derived peptides, typically 15 to 17 amino acids in length, selected based on a multi-algorithm scoring system to predict high binding affinity to various MHC class II alleles, thereby targeting both wild- type and mutant KRAS epitopes (including, in particular, mutations at codon 12). It does not disclose any delivery aiding mechanisms. Document CA 3140204 A1 discloses a pharmaceutical composition for the treatment or prophylaxis of breast cancer comprising a defined combination of HLA tumor antigen peptides comprising from 4 to 8 HLA-A tumor antigen peptides together with at least 2 HLA class II peptides. The disclosure further provides a method for identifying and selecting said peptides by integrating tumor-specific transcriptome and exome sequencing data with ligandome analysis. WO2002064057 A2 discloses methods and compositions for enhancing antitumor immunity by using cell-penetrating peptides (CPPs) to mediate intracellular delivery of antigens, for example antigenic peptides, to immune effector cells, particularly mature dendritic cells (DCs). Disadvantageously, however the disclosure only relates to examples in which a single tumor antigen peptide, for example a 9‐mer derived from TRP2, which is covalently linked to a cell‐penetrating peptide to facilitate intracellular delivery into dendritic cells. In summary, there is a current need in cancer immunotherapy, particularly in terms of generalization to subject populations that share the same cancer type and HLA alleles, and to induce a more robust, potent, and reliable immune response with one composition. To date, there are no approaches in the prior art to efficiently solve such a problem. Objection of the Invention / Technical Problem Thus, it is an object of the present invention - in contrast to fully individualized cancer immunotherapy - to provide a pharmaceutical composition for different subjects or a specifically predetermined group of subjects (i.e., for a specific group of subjects with at least one identical HLA allele) who have overlap in the mutanoma of the malignant or neoplastic tissue (carcinoma) (derivation of subject groups). Particularly preferred is a solution for a group of subjects who have the same mutanoma or at least a single amino acid mutation of a gene associated with the same mutanoma, a uniform composition approach comprising HLA antigen peptides is sought. It is therefore an object of the present invention to provide pharmacologically active agents, as well as pharmaceutical compositions comprising such active agents, which can be used for the diagnosis, prevention and / or treatment of cancer and other diseases and disorders listed herein; and to provide methods for the diagnosis, prevention and / or treatment of such cancers involving the administration and / or use of such agents and compositions. In particular, it is an object of the invention to provide such pharmacologically active agents, pharmaceutical compositions and / or methods that have certain advantages over the active agents, compositions and / or methods currently in use and / or known in the prior art. These advantages result from the following further description. In particular, it is an object of the invention to provide therapeutically active HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP), wherein the HLA tumor antigen peptides (HTAP) are tumor-exclusive or tumor-associated and presented on the cell membrane of the associated tumor cell, which can be used as pharmacologically active HLA tumor antigen peptides or as pharmacologically active agents, and to provide pharmaceutical compositions containing same, for the diagnosis, prevention and / or treatment of carcinomas and other diseases and disorders, in particular cancers, as set forth herein; and to provide methods for the diagnosis, prevention and / or treatment of such diseases and disorders involving the administration and / or use of such therapeutically active HLA tumor antigen peptides and compositions. In particular, it is a specific task of the present invention to provide such HLA tumor antigen peptides suitable for prophylactic, therapeutic and / or diagnostic use in warm-blooded animals, especially in a mammal and most particularly in a human. Another obstacle that has not been addressed in the current state of the art is that amino acid mutations can occur in the same cancers and even in the same genes, but at different sites. Solution To overcome the technical problems of the prior art, a preferred embodiment of the present invention comprises a pharmaceutical composition for use as and / or as a medicament, in particular for use in and / or for the therapeutic and / or prophylactic treatment of a carcinoma, particularly preferably a locally recurrent or metastatic carcinoma, in particular in a subject or group of subjects suffering from or at risk of suffering from a carcinoma, comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP), wherein the HLA tumor antigen peptides (HTAP) are tumor-exclusive or tumor-associated and presented on the cell membrane of the associated tumor cell and correspond to an amino acid sequence of a transcribed mutant gene, wherein the HLA tumor antigen polypeptide comprises a scaffold amino acid sequence, also referred to as amino acid sequence, preferably between 15 and 45, more preferably between 17 and 40 amino acids, a) wherein the scaffold amino acid sequence comprises, in addition to HLA tumor antigen peptide(s), up to 1 to 30 amino acids (long HLA tumor antigen polypeptide); and / or b) wherein the scaffold amino acid sequence comprises an HLA tumor antigen peptide(s) with at least 90% sequence identity similarity to the native HLA tumor antigen peptide (similarity HLA tumor antigen polypeptide); and / or c) wherein at least one of the amino acid sequences comprises an HLA tumor antigen peptide having an amino acid sequence comprising or consisting essentially of only one amino acid substitution relative to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide), wherein an HLA tumor antigen polypeptide is a tandem polypeptide comprising or consisting of at least 2 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes; and / or wherein an HLA tumor antigen polypeptide is an overlapping tandem polypeptide comprising or consisting of at least 2 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes which overlap in their amino acid sequence. The problem is solved especially by an HLA tumor antigen polypeptide (HTAPP) comprising a delivery aiding capping peptide (DACP), wherein the HLA tumor antigen polypeptide corresponds to at least two HLA tumor antigen peptides (HTAP), preferably 2 to 20 different HTAPs, more preferably 2 to 10 different HTAPs, corresponding to MHC class I and / or class II complexes, wherein the HLA tumor antigen peptides (HTAP) are arranged on the HLA tumor antigen polypeptide (HTAPP), wherein the HLA tumor antigen peptides (HTPA)s arranged on the HLA tumor antigen polypeptide (HTAPP) are preferably different from each other, wherein the HLA tumor antigen peptides (HTAP) are tumor-exclusive or tumor-associated and presented on the cell membrane of the associated tumor cell and correspond to an amino acid sequence of a transcribed mutant gene, wherein the HLA tumor antigen polypeptide comprises or consists of an amino acid sequence, preferably an antigenic amino acid sequence, more preferably a backbone antigenic amino acid sequence, wherein the amino acid sequence comprises or consists of between 15 and 45 amino acids, wherein the DACP is preferably not a part of the amino acid sequence, wherein a) the amino acid sequence comprises, in addition to HLA tumor antigen peptide(s), up to 1 to 30 amino acids (long HLA tumor antigen polypeptide); and / or b) the amino acid sequence comprises an HLA tumor antigen peptide(s) with at least 90% sequence identity similarity to the native HLA tumor antigen peptide (similarity HLA tumor antigen polypeptide); and / or c) the amino acid sequences comprises an HLA tumor antigen peptide having an amino acid sequence comprising of only one amino acid substitution relative to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide), wherein i) an HLA tumor antigen polypeptide is a tandem polypeptide comprising at least 2 HLA tumor antigen peptides, preferably 2 to 20 different HTAPs, more preferably 2 to 10 different HTAPs, corresponding to MHC class I and / or class II complexes; and / or ii) an HLA tumor antigen polypeptide is an overlapping tandem polypeptide comprising at least 2 HLA tumor antigen peptides, preferably 2 to 20 different HTAPs, more preferably 2 to 10 different HTAPs, corresponding to MHC class I and / or class II complexes which overlap in their amino acid sequence, wherein the DACP comprises a positively charged and amphipathic sequence with a total percentage of 33% to 89% of arginine (R) and lysine (K) residues, and wherein the DACP is between 10 and 20 amino acids in length and wherein the DACP is directly or indirectly, in particular via a linker, preferably indirectly via a linker, wherein the linker as disclosed herein is preferably between 3 and 5 amino acids in length, most preferably selected from GPGPG, AAY or AYY, attached to the C- or N-terminus of the HTAPP, and wherein the DACP is a cell-penetrating peptide (CPP), and wherein the HTAPP-DACP preferably has an total amino acid sequence length between 30 and 60 amino acids, more preferably between 31 and 55 amino acids. This has the technical advantage of providing an antigenic polypeptide design that can be produced in high yields, has an improved immunogenic response compared to short HTAP peptides corresponding to MHC class I or II complexes, and a compact length, preferably between 30 and 60 amino acids, which increases chemical and biochemical stability and has a lower chance to lead to folding or tertiary / quaternary protein alignment problems that could reduce immunogenicity. It also provides a CPP as a delivery group which, especially in this compact design, enhances the immunogenicity of the HLA tumour antigen polypeptide (HTAPP) comprising a delivery aiding capping peptide (DACP), short HTAPP-DACP, compared to HTAPPs without capping peptides, as demonstrated by the examples herein. The solution of the task further includes a method of determining a pharmaceutical composition comprising or consisting of HLA tumor antigen polypeptides according to the current invention. According to the invention, these tasks are fulfilled by a pharmaceutical composition for use in the treatment or profilaxis of carcinomas, in particular locally recurrent or metastatic carcinomas in a subject or group of subjects suffering or suspected of suffering from carcinomas, in particular wherein the composition comprises HLA tumor antigen peptides selected from the group consisting of SEQ-ID-Nos.: 1 to 17 and / or 18 to 31 and / or 32 to 37 and / or 40 to 68. Further advantageous embodiments are given in the subclaims. Another obstacle with the group approach to cancer immunotherapy is that the patent mutations may be in the same cancers and even in the same genes, but in different locations. An approach that has not yet been pursued in this regard is to present multimerized polypeptides on which several peptides corresponding to HLA complexes are arranged, which advantageously cover different mutated genes simultaneously. By introducing more and more mutanomes from different subjects into a bioinformatic pipeline with feedback, increasingly precise HLA tumor antigen polypeptides (HTAPP) comprising many different mutated gene segments expressed and corresponding to widespread HLA alleles can be generated and successively improved. Thus, a pharmaceutical composition of preferably 5 to 12 HTAPPs can be formed, which match at least one mutated gene and one HLA allele of a group of subjects suffering or at risk from suffering from cancer. Preferably, each single HTAPP already covers different combinations of the most frequently mutated gene segments and HLA peptides. By arranging a carefully selected number of HLA tumor antigen peptides on HLA tumor antigen polypeptides, the exact mixture of which is tailored to the HLA alleles of the specific subject, an effective single therapy can be formed from a manageable number of HTAPPs. Description According to a particularly preferred embodiment of the present invention, the pharmaceutical composition consists exclusively of a carrier liquid (preferably water, a pharmaceutically acceptable saline solution and / or pharmaceutically DMSO - such compositions of carrier liquids are known to the skilled person and are, for example, in the range of 30% DMSO and 70% water), in which a pharmacologically effective amount of 4 to 8 HLA-A tumor antigen peptides corresponding to the MHC class I complexes and 2 tumor antigen peptides corresponding to the MHC class II complexes are dissolved or suspended, and an adjuvant. Pharmaceutical composition and suitable dosage forms for application of the pharmaceutically active HLA tumor antigen peptides are prepared according to standard procedures known in the prior art and are readily applicable to any new or improved process for their preparation. Particularly advantageously, administering the aforementioned combination of a pharmacologically effective amount of the HLA tumor antigen peptides to the subject or group of subjects suffering from carcinoma effectively reduces the CA 15-3 level. CA 15-3 (Cancer antigen 15-3) is a so-called glycoprotein used as a specific tumor marker in carcinoma. The CA 15-3 value is a laboratory value that rises significantly above the threshold value in certain cancers, especially carcinomas. In healthy individuals, the CA 15-3 threshold is below 31 enzyme units per milliliter (< 31 U / ml). Preferably, administering the pharmacologically effective amount of tumor antigen peptides to the subject or group of subjects suffering from carcinoma reduces the CA 15-3 value below 60 U / ml, more preferably below 50 U / ml, most preferably to a range below 40 U / ml and a normal value (< 31 U / ml). Particularly preferably, administering the pharmacologically effective amount of HLA tumor antigen peptides to the subject or group of subjects thus effectively prolongs the progression-free survival of the individual, preferably by at least 2 to 5 years. Contrary to conventional approaches, it is a surprising finding of the present invention that tumor antigen peptides having a KD-value in the range between 50 and 500 nM trigger effector cells (i.e., cytotoxic T cells), contrary to conventional in silico binding prediction models that have considered them to have low binding. Rather, it is of particular advantage for the efficacy of the tumor antigen peptides that the HLA tumor antigen peptides used for treatment are immunogenic in the subject or group of subjects with at least one identical HLA allele, which can be determined in advance with an immunogenicity assay (e.g., by Western blot, ELISA techniques, especially by ELISPOT, preferably via interferon-gamma, interferon-alpha or interleukin (IL-2), or immunodetection with microscopic analysis). As described herein, but without limitation to any explanation, mechanism of action, or hypothesis in the present invention, two distinct classes of HTAPPs corresponding to amino acid sequences of the invention have been determined based on their ability to enhance the interaction of class I MHC complexes and class II MHC complexes, respectively, with at least one T cell receptor (particularly in the detection method described below in embodiment 3). These two classes of amino acid sequences of the invention are (as described below): - "HLA tumor antigen polypeptides (HTAPP) corresponding to MHC class I and II complexes": (see particularly preferred examples in Table 1). - "HLA tumor antigen polypeptides (HTAPP) comprising delivering aiding capping peptides (DACP) corresponding to MHC class II complexes": (see particularly preferred examples in Tables 2 to 5). Advantageously, the use / application of the pharmaceutical composition according to the invention or the specific combination of tumor antigen peptides contained therein corresponding to the MHC class I complexes and MHC class II complexes to the subject or group of subjects with at least one identical HLA allele is not merely a passive immunization (as in the case of treatment with antibodies, e.g. Herceptin) but an active immunization (i.e. specific activation of the T cells or B helper cells via information carriers). Because of the specific activation of MHC class II molecules, which are mainly exposed on the cell surface of antigen-presenting cells, by means of the tumor antigen peptides corresponding to the MHC class II complexes, CD4+ T cells (also called T helper cells) and B cells are specifically activated. For binding to a T cell receptor, an HLA tumor antigen peptide of the invention typically has in its amino acid sequence one or more amino acid residues or one or more segments of amino acid residues (i.e., with each "segment" comprising two or more amino acid residues located adjacent to or in close proximity to each other, i.e. in the primary or tertiary structure of the amino acid sequence) through which the amino acid sequence of the invention can bind to a T cell receptor (in particular a binding pocket thereof), the amino acid residues or portions of the amino acid residues thus forming the "anchor" for binding to a T cell receptor (also referred to herein as "anchor amino acids"). The determination of this "anchor" can be determined, for example, by in silico methods (e.g., the artificial neural network NNAlign used in the publicly available NetMHC-4.0) or by targeted mutation (insertions or substitutions in the amino acid sequence of HLA tumor antigen peptides). The HLA tumor antigen peptides provided by the present invention are preferably in substantially isolated form (as defined herein) or form part of a protein or polypeptide, which may comprise or consist essentially of one or more HLA tumor antigen peptides of the invention, and which may optionally further comprise one or more pharmaceutically active HLA tumor antigen peptide(s) (all of which are optionally joined via one or more linkers in a so-called oligopeptide). For example, and without limitation, the tumor antigen peptides of the invention may be used as a binding moiety in such a protein or polypeptide, which may optionally include one or more additional amino acid sequences that may serve as a binding moiety (i.e., against one or more targets other than a T cell receptor) to provide a monovalent, multivalent, or multispecific polypeptide of the invention as described herein, respectively. Such protein or polypeptide may also be in substantially isolated form (as defined herein). A pharmaceutical composition comprising a specific combination of HLA tumor antigen peptides corresponding to MHC class I complexes and HLA tumor antigen peptides corresponding to MHC class II complexes disclosed herein has been shown to be particularly advantageous as it is capable of specifically activating T cells as well as specifically activating B cells. In some embodiments, the present invention also relates to a pharmaceutical composition, a kit (or parts thereof), a method for determining / identifying a pharmacologically active HLA tumor antigen peptide corresponding to class I and / or class II MHC complexes, a method for preparing a formulation according to the invention, and the use of a formulation according to the invention for the preparation of a pharmaceutical composition for the treatment of cancer, in particular / mammary carcinoma. In particular, the polypeptides and pharmaceutical compositions of the present invention may be used for the prevention and treatment of cancers, particularly / cancers, characterized by mutation(s) (herein "amino acid substitutions") altered wild-type HLA antigen peptides corresponding to MHC class I complexes and / or corresponding to MHC class II complexes (so-called HLA tumor antigen peptides, as defined herein). In general, the treatment of cancer of the invention of a subject or group of subjects is (are) carried out in advance by classical methods such as chemotherapy, radiotherapy and / or cancer immunotherapy. Classical methods for the treatment of cancers of the invention are, for example, surgical tumor removal (resection), chemotherapy and / or radiation therapy, with two or even all three treatment methods frequently being applied simultaneously to a subject. Cancer immunotherapy methods are divided into active and passive immunization. In active immunization, the subject is administered substances that are intended to trigger an immune response in his or her immune system. In passive immunization, antibodies or antibody fragments are used. In adoptive immunotherapy (i.e. passive immunotherapy, as comparable to antibody treatment without direct immunomodulation), leukocytes are removed from the subject, cultured ex vivo, and then re-injected into the subject. If the treatment does not destroy all cells of the tumor and its metastases, further treatment of cancer is significantly hampered by the development of resistance. Thus, the present invention also comprises a pharmaceutical composition for the treatment of cancers, as described above, following the classical methods for the treatment of cancers, namely after unsuccessful surgical tumor removal (resection), chemotherapy and / or radiotherapy. It is a particular achievement of the inventors to have found that, for effective treatment, the HLA-A antigen peptides used according to the invention are actually presented on the cell surface of cells of the malignant tissue (in particular carcinoma) to be treated in the individual to be treated. Therefore, the pharmaceutical composition to be applied comprises HLA tumor antigen peptides presented on the surface of tumor cells of the subject's or group of subjects' carcinoma, as determined by ultra-high performance liquid chromatography (UHPCL) in conjunction with ESI mass spectrometry (MS) prior to application and assembly of the pharmaceutical composition. By such ligandome assay, unlike conventional cancer immunotherapies, the binding ability of the HLA-A antigen peptides according to the invention towards the corresponding class I and / or class II MHC complex has already been proven in advance. According to a preferred embodiment of the invention, at least 60%, preferably at least 80%, most preferably 90%, ideally all of the HLA tumor antigen peptides contained in the pharmaceutical composition to be applied are presented on the surface of the tumor cells of the subject's or group of subjects' carcinoma as determined by methods as described herein. It has been found by the inventors of the present invention that the HLA-A antigen peptides explicitly disclosed herein corresponding to MHC class I are particularly suitable for use in the treatment of carcinomas in subjects or a group of subjects having at least one identical HLA allele exhibiting subtype A*01 and / or A*02. That is, the HLA-A tumor antigen peptides used herein preferably bind to the corresponding MHC class I complex of subtype A*01 and / or A*02. According to a particularly preferred embodiment, the individuals (subjects or a group of subjects) have the haplotype with the subgroup A*01:01, A*02:01, A*02:03, A*02:06, A*02:786, A*03:01, A*11:01, A*24:02, A*30:01, A*30:02, A*31:01, A*32:01, A*33:01, A*68:01, A*68:02, B*07:02, B*08:01, B*15:01, B*35:01, B*40:01, B*44:02, B*57:01, B*57:37, B*58:01, C*03:04, C*04:01, C*06:02, C*07:02, E*01:01, and E*01:03. Particularly, according to a particularly preferred embodiment, the individuals (subjects or a group of subjects) have the haplotype with the subgroup DQA1*01:01, DQB*102:01, DQB1*05:01, DQB1*06:02, DRB1*01:01, DRB1*15:01. It is true that the pharmaceutical composition according to the invention could be used for the tissue-independent treatment of malignancies, neoplasms, and / or leukemias (i.e., unlike conventional preparations, the cancer subtypes do not initially play a role), so that the pharmaceutical composition can be applied across tissues for use as an anticancer drug. However, it was found that the administration / application of the specific combination of 2 to 25 HLA tumor antigen peptides corresponding to MHC class I complexes arranged on at least one HLA tumor antigen polypeptide according to the invention can be used particularly advantageously for the treatment of cancer. According to a particularly preferred embodiment of the present invention, at least one HLA-A antigen peptide of the composition is a tumor-exclusive HLA-A antigen peptide (i.e., a cancer-testis antigen (CTA) that does not (no longer) appear beyond the immunoprivileged spermatocytes in the healthy / normal tissue of the subject / group of subjects, or a so-called neoantigen peptide), and wherein specific binding of the tumor-exclusive HLA-A antigen peptide occurs with a specific dissociation (K D) in the range of 10 to 50 nM, as determined by surface plasmon resonance. It is also an outstanding achievement of the inventors to have discovered that a pharmaceutical composition based on HLA antigen peptides is particularly effective when both T lymphocytes (T cells for short) and B lymphocytes (B cells for short) are activated by them. T cells belong to the lymphocyte cell group and play an important role in the human immune system. T cells recognize antigens via a specific receptor, the so-called T cell receptor (TCR). However, for this to happen, the antigen must be offered by an antigen-presenting cell (APC). Stable binding of the T cell to the antigen-presenting cell requires the participation of so-called auxiliary proteins. These include CD4 and CD8 (CD = "Cluster of Differentiation"). T cells carrying the CD4 trait are also called CD4-positive T cells or T helper cells. In normal adult blood, CD4+ T cells account for 27-57% of lymphocytes, or approximately 310-1570 cells / µl. The group of CD8-positive (CD8+) T cells, which also includes regulatory T cells, contains the cytotoxic T cells or T killer cells. They play a special role in killing the body's own cells that are infected by viruses. This property of cellular immune defense is critical in the present invention, as the molecular and genetic alterations of tumor cells can be recognized and lysed by this T cell population. In contrast, B cells are the only cells capable of producing antibodies and, together with T cells, make up the crucial component of the adaptive immune system. While T cells are involved in the cell-mediated immune response, B cells are the carriers of the humoral immune response (and responsible for the formation of antibodies). A pharmaceutical composition has been shown to comprise the tumor-exclusive or tumor-associated HLA antigen peptides whose expression level in the tumor cells is at least three times higher than in the healthy cells of the subject or the specifically determined group of subjects having at least one identical HLA allele, as determined for example by qPCR, and wherein the tumor-associated HLA tumor antigen peptides are associated with proliferation, invasiveness, angiogenesis and an increase in cytokeratin production of the carcinoma, have particularly effective pharmacological effects in the treatment of carcinomas. Particularly preferably, each individual HLA tumor antigen polypeptide used herein for the treatment of carcinoma is present in the pharmaceutical composition at an absolute concentration (i.e., administration dose) of at least from 100 to 600 µg, preferably from 300 to 600 µg. In the meantime, it has been shown in further experiments that pharmaceutical compositions containing an absolute concentration of > 600 µg per HLA tumor antigen peptide, i.e. at least 700 to 1,200 µg, preferably from 800 to 1,200 µg, are particularly preferred, as this greatly intensifies the information (the activation and / or training of the immune system). This is particularly advantageous if the immune system of the subject to be treated is already weakened by pre- treatment with a standard therapy procedure (e.g. at least one operation, radiation, chemotherapy and / or hormone therapy). In addition, the absolute concentration per HLA tumor antigen peptide is preferred, as this substantially minimizes the influence of degradation of the HLA tumor antigen peptides (e.g., by ligases) after their application to the subject. It is highly convenient that the pharmaceutical composition comprises an adjuvant which, when the composition is applied to a subject, is capable of forming a granuloma at the site of application. The advantage in the formation of a granuloma is that a depot effect can thus be achieved, whereby the HLA tumor antigen peptides are advantageously stored at the site of application in the manner of a reservoir and can be delivered to the organism of the subject over a longer period of time. Particularly advantageously, therefore, weekly applications of the pharmaceutical composition according to the invention are omitted. Preferably, the application of the pharmaceutical composition for the treatment of cancer diseases within the meaning of the invention, when used over a longer period of time, therefore only has to be carried out every 2 weeks, particularly preferably only once a month. In this regard, the pharmaceutical composition is preferably applied subcutaneously or intradermally and, preferably substantially simultaneously at least 2, more preferably at least 3 application sites, typically at 3 to 4 application sites remote from a tumor lesion and / or the cancerous lymph node area. The essentially simultaneous (successive) application at several application sites has the advantage that, particularly in the case of application of high absolute concentrations of the individual HLA tumor antigen polypeptides (i.e. administration dose) in the range of > 600 µg, which require larger application volumes (> 1 mL) for complete dissolution of the individual HLA tumor antigen polypeptides, the application of the application solution, which has only a limited shelf life after opening, is carried out as simultaneously as possible. Preferably, the pharmaceutical composition comprising each individual HLA tumor antigen polypeptide in the composition at an absolute concentration (i.e., administration dose) of 300 to 600 µg need only be administered intradermally or subcutaneously once every 2 weeks, preferably once every 4 weeks, for a period of at least one year to a subject or a specifically identified group of subjects having at least one identical HLA allele. It has been found that a pharmaceutical composition in which at least one HLA tumor antigen peptide has at least one mutation with respect to the wild-type HLA tumor antigen peptide (as detailed below) that results in an increase, preferably to < 500 nm, most preferably < 50 nm of the specific binding affinity to the T cell receptor (KD -value) of the individual treated with HLA tumor antigen peptide compared to the wild type of HLA tumor antigen polypeptide, show particularly beneficial effects in the treatment of carcinomas. According to a preferred embodiment of the present invention, the pharmaceutical composition is used for the treatment of cancer as monotherapy or in combination with other known therapies and / or compounds for the treatment of cancer. In this regard, the pharmaceutical composition will be administered as a first-line therapy to the subject or group of subjects with at least one identical HLA allele (so-called adjuvant monotherapy). Alternatively, it may be provided that the subject or group of subjects to be treated with the pharmaceutical composition with at least one identical HLA allele has already received at least one standard therapy procedure (e.g., at least one surgery, radiation, chemotherapy, and / or hormone therapy) in advance. Most preferably, the cancer to be treated is a hormone positive, HER2 / neu or triple negative cancer. The present invention also includes HLA tumor antigen peptides corresponding to MHC class I complexes or MHC class II complexes, particularly for use in treating or profiling carcinoma in a subject or group of subjects suffering or suspected of suffering from carcinoma, suffering therefrom, or for a pharmaceutical composition according to the invention, wherein the HLA tumor antigen peptides are located on an HLA tumor antigen polypeptide and thus comprise or represent a portion of amino acid sequences selected from the group consisting of those shown in SEQ-ID-Nos.: 1 to 37, 40 to 68, each representing an HLA tumor antigen polypeptide according to the invention, or having at least one mutation, preferably an amino acid substitution, with respect to one of the said amino acid sequences, or comprising a portion of the amino acid sequence 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98 or 99% identical to SEQ-ID-Nos.: 1 to 37, 40 to 68. Particularly preferred in this regard is the use of the foregoing HLA tumor antigen peptides in a method of treating carcinomas, particularly locally recurrent or metastatic carcinomas in a subject or group of subjects having at least one identical HLA allele, the method comprising administering / applying to the subject or group of subjects a treatment regimen comprising a pharmacologically effective amount of at least one of the foregoing HLA tumor antigen peptides. In order for the immune system of the individual to whom the HLA tumor antigen peptides or pharmaceutical composition according to the invention is administered to still be fully functional and thus easier to train, it is advantageous if the individual has not yet received radiation, chemotherapy, and / or hormone therapy against the cancer, especially locally recurrent or metastatic cancer, and / or has not received prior adjuvant chemotherapy in recurrence for 12 months or less since the last dose of a chemotherapeutic agent. Particularly preferably, the treatment regimen described herein, especially using at least one aforementioned HLA tumor antigen peptide of the invention, effectively prolongs progression-free survival of the individual. An "HLA-A tumor antigen peptide corresponding to MHC class I complexes" is defined herein as an "HLA tumor antigen peptide of the invention" or "amino acid sequence of the invention" (as defined herein) comprising: a) an amino acid sequence consisting of 7 to 11 amino acids; and / or b) a neoantigen peptide having an amino acid sequence consisting of 7 to 11 amino acids, which is i) is analogous to at least one HLA-A antigen peptide exposed on the cell surface of cells from malignant and / or neoplastic tissue (in particular carcinoma) of the individual to be treated, and ii) in its amino acid sequence at least one amino acid exchange with the wild type of this HLA-A neoantigen peptide (so-called "HLA-A neoantigen peptide") and iii) has at least a 3-fold increased specific affinity towards the T cell receptor of endogenous T cells It is an outstanding achievement of the inventors to have recognized that HLA-A neoantigen peptides which in their amino acid sequence compared to the wild type of this HLA-A antigen peptide have at least one amino acid exchange in the amino acid positions 1 (N-terminus), 2, 7 / 8 and / or the C-terminus, have an at least 4-fold, particularly preferably at least 5-fold, most preferably at least 8-fold increased specific affinity (KD) towards the T cell receptor of the endogenous T cells and are therefore particularly preferably used for the composition according to the invention. Particularly preferably, the amino acid exchange in the amino acid sequence of the HLA-A antigen peptide is a single amino acid exchange in amino acid position 1 (N-terminus), 2, 7 / 8 or the C-terminus. Preferably, the amino acid exchange in the amino acid sequence of the HLA-A neoantigen relative to the wild type of this HLA-A antigen peptide is a C / Y, A / V, D / Y, E / K, P / L, N / D, or T / M exchange. Preferably, the HLA-A peptide or HLA-A neoantigen has a specific activity (KD) towards the T cell receptor, as determined by any suitable detection method known to the skilled person in the prior art, of less than 100 nM, more preferably less than 75 nM or most preferably less than 50 nM, such as less than 40 nM, 35 nM, 30 nM, 25 nM or 20 nM. Preferably, the HLA-A tumor antigen peptide or the HLA-A neoantigen is present in the pharmaceutical composition according to the invention at a concentration, as defined above, of at least 100 to 600 µg, alternatively preferably at an absolute concentration of > 600 µg relative to the volume of the pharmaceutical composition to be applied. Preferably, the HLA-A tumor antigen peptides or HLA-A neoantigens are selected as defined in (b)above. The use of compounds, constructs, proteins or polypeptides as defined according to the invention, which consist of at least two identical or different peptide sequences of HLA tumor antigen peptides and / or HLA neoantigens, has the further advantage that the longer amino acid sequences of the compounds, constructs, proteins or polypeptides result in a longer retention time in the tissue of the subject after application, whereby the compounds, constructs, proteins or polypeptides after application to the subject can be broken down, for example, by the body's own enzymes into smaller fragments (pharmaceutically active form comprising at least 7 to 11 amino acids) which have a biologically desired function in the sense of the invention. by endogenous enzymes into smaller fragments (pharmaceutically active form comprising at least 7 to 11 amino acids) which have a biologically desired function in the sense of the invention. That is, the individual fragments of the oligopeptide exhibit activity as HLA-A, HLA-B or HLA-C tumor antigen peptides and thus contribute to the activation of T cells. In a particular embodiment, any HLA-A peptide sequence may be a humanized and / or sequence optimized sequence as further described herein. An "HLA-B antigen peptide" is defined herein as an "HLA-B antigen peptide of the invention" or "amino acid sequence of the invention" (as defined herein) comprising: a) an amino acid sequence consisting of 12 to 17 amino acids; and / or b) a neoantigen peptide with an amino acid sequence consisting of 12 to 17 amino acids, which is i) is analogous to at least one HLA-B antigen peptide exposed on the cell surface of cells from malignant and / or neoplastic tissue (in particular carcinoma) of the individual to be treated, and ii) in its amino acid sequence at least one amino acid exchange with the wild type of this HLA-B antigen peptide (so-called "HLA-B neoantigen peptide") and iii) has at least a 3-fold increased specific affinity towards the T cell receptor of endogenous T cells Furthermore, the inventors have recognized that HLA-B neoantigen peptides which in their amino acid sequence have at least one amino acid exchange in amino acid positions 3, 8 and / or 10 compared to the wild type of this HLA-B antigen peptide, have an at least 4-fold, particularly preferably at least 7-fold increased specific affinity towards the T cell receptor of the body's own T cells and are therefore particularly preferred for use in the formulation according to the invention. Particularly preferably, the amino acid exchange in the amino acid sequence of the HLA-B antigen peptide is a single amino acid exchange in amino acid position 3, 8, or 10. Preferably, the amino acid exchange in the amino acid sequence of the HLA-B neoantigen relative to the wild-type of this HLA-B antigenic peptide is an E / A, E / K, R / W, or D / A exchange. Preferably, the HLA-B antigen peptide or the HLA-B neoantigen peptide has a specific activity (K D) towards the T cell receptor, as determined by any suitable detection method known to the skilled person in the prior art, of less than 100 nM, more preferably less than 75 nM or most preferably less than 50 nM, such as less than 40 nM, 35 nM, 30 nM, 25 nM or 20 nM. Preferably, the HLA-B tumor antigen peptide or the HLA-B neoantigen is present in the pharmaceutical composition according to the invention at a concentration, as defined above, of at least 100 to 600 µg, alternatively preferably at an absolute concentration of > 600 µg relative to the volume of the pharmaceutical composition to be applied. Preferably, the HLA-B peptides or HLA-B neoantigens are selected as defined above in point b) The use of compounds, constructs, proteins or polypeptides as defined according to the invention, which consist of at least two identical or different peptide sequences of HLA tumor antigen peptides and / or HLA neoantigens, has the further advantage that the longer amino acid sequences of the compounds, constructs, proteins or polypeptides result in a longer retention time in the tissue of the subject after application, whereby the compounds, constructs, proteins or polypeptides after application to the subject can be broken down, for example, by the body's own enzymes into smaller fragments (pharmaceutically active form comprising at least 7 to 11 amino acids) which have a biologically desired function in the sense of the invention. by endogenous enzymes into smaller fragments (pharmaceutically active form comprising at least 7 to 11 amino acids) which have a biologically desired function in the sense of the invention. That is, the individual fragments of the oligopeptide exhibit activity as HLA-A, HLA-B or HLA-C tumor antigen peptides and thus contribute to the activation of T cells. In a particular embodiment, any HLA-B peptide sequence may be a humanized and / or sequence optimized sequence as further described herein. An "HLA-C antigen peptide" is defined herein as an "HLA antigen peptide of the invention" or "amino acid sequence of the invention" (as defined herein) comprising: an amino acid sequence consisting of 8 to 11 amino acids; and / or a) a neoantigen peptide having an amino acid sequence consisting of 8 to 11 amino acids which is i) is analogous to at least one HLA-C antigen peptide exposed on the cell surface of cells from malignant and / or neoplastic tissue (in particular carcinoma) of the individual to be treated, and ii) in its amino acid sequence at least one amino acid exchange with the wild type of this HLA-C peptide (so-called "HLA-C neoantigen peptide") and iii) has at least a 3-fold increased specific affinity towards the T cell receptor of endogenous T cells Furthermore, the inventors have recognized that HLA-C neoantigen peptides which in their amino acid sequence compared to the wild type of this HLA-C antigen peptide have at least one amino acid exchange in the amino acid positions 1 (N-terminus), 4 and / or the C-terminus, have an at least 4-fold, particularly preferably at least 5-fold, very particularly preferably at least 7-fold increased specific affinity towards the T cell receptor of the endogenous T cells and are therefore particularly preferably used for the formulation according to the invention. Particularly preferably, the amino acid exchange in the amino acid sequence of the HLA-C antigen peptide is a single amino acid exchange in amino acid position 1 (N-terminus), 4, or the C-terminus. Preferably, the amino acid exchange in the amino acid sequence of the HLA-C neoantigen peptide relative to the wild type of this HLA-C antigen peptide is a C / Y, A / P, L / F or T / M exchange. Preferably, the HLA-C antigen peptide or the HLA-C neoantigen peptide has a specific activity (K D) towards the T cell receptor, as determined by any suitable detection method known to the skilled person in the prior art, of less than 100 nM, more preferably less than 75 nM or most preferably less than 50 nM, such as less than 40 nM, 35 nM, 30 nM, 25 nM or 20 nM. Preferably, the HLA-C tumor antigen peptide or the HLA-C neoantigen is present in the pharmaceutical composition according to the invention at a concentration, as defined above, of at least 100 to 600 µg, alternatively preferably at an absolute concentration of > 600 µg relative to the volume of the pharmaceutical composition to be applied. Preferably, the HLA-C antigen peptides or HLA-C neoantigen peptides are selected as defined above in point b) The use of compounds, constructs, proteins or polypeptides as according to the invention, which consist of at least two identical or different peptide sequences of HLA tumor antigen peptides and / or HLA neoantigens, has the further advantage that the longer amino acid sequences of the compounds, constructs, proteins or polypeptides result in a longer retention time in the tissue of the subject after application, whereby the compounds, constructs, proteins or polypeptides after application to the subject can be broken down, for example, by the body's own enzymes into smaller fragments (pharmaceutically active form comprising at least 7 to 11 amino acids) which have a biologically desired function in the sense of the invention. by endogenous enzymes into smaller fragments (pharmaceutically active form comprising at least 7 to 11 amino acids) which have a biologically desired function in the sense of the invention. That is, the individual fragments of the oligopeptide exhibit activity as HLA-A, HLA-B or HLA-C tumor antigen peptides and thus contribute to the activation of T cells. In a particular embodiment, any HLA-C antigen peptide sequence may be a humanized and / or sequence optimized sequence as further described herein. An "HLA Class II antigen peptide" is defined herein as an "HLA peptide of the invention" or "amino acid sequence of the invention" (as defined herein) comprising: a) an amino acid sequence consisting of 13 to 20 amino acids, particularly preferably 13 to 17 amino acids; and / or b) a neoantigen having an amino acid sequence consisting of 13 to 20 amino acids, particularly preferably 13 to 17 amino acids, which i) is analogous to at least one class II HLA peptide exposed on the cell surface of cells from malignant and / or neoplastic tissue (in particular carcinoma) of the individual to be treated, and ii) in its amino acid sequence at least one amino acid exchange compared to the wild type of this class II HLA peptide (so-called "class II HLA neoantigen") and iii) has at least a 3-fold increased specific affinity towards the T cell receptor of endogenous T cells Furthermore, the inventors have recognized that HLA neoantigens of class II, which in their amino acid sequence compared to the wild type of this HLA peptide of class II have at least one amino acid exchange in amino acid positions 3, 6, 10, 12, 13 and / or 14, particularly preferably in amino acid positions 12 and / or 14, have an at least 4-fold increased specific affinity towards the T cell receptor of the body's own T cells and are therefore particularly preferred for the formulation according to the invention. Preferably, the amino acid exchange in the amino acid sequence of the class II HLA neoantigen relative to the wild type of this class II HLA peptide is an E / K, E / A, D / Y, or T / M exchange. Preferably, the class II HLA peptide or class II HLA neoantigen has a specific activity (KD ) towards the T cell receptor, as determined by any suitable detection method known to the skilled person in the prior art, of less than 100 nM, more preferably less than 75 nM or most preferably less than 50 nM, such as less than 40 nM, 35 nM, 30 nM, 25 nM or 20 nM. Preferably, the HLA tumor antigen peptide corresponding to class II MHC complexes or the HLA neoantigen corresponding to class II MHC complexes is present in the pharmaceutical composition according to the invention at a concentration, as defined above, of at least 100 to 600 µg, alternatively preferably at an absolute concentration of > 600 µg relative to the volume of the pharmaceutical composition to be applied. The use of compounds, constructs, proteins or polypeptides as defined according to the invention, which consist of at least two identical or different peptide sequences of HLA tumor antigen peptides and / or HLA neoantigens, has the further advantage that the longer amino acid sequences of the compounds, constructs, proteins or polypeptides result in a longer retention time in the tissue of the subject after application, whereby the compounds, constructs, proteins or polypeptides after application to the subject can be broken down, for example, by the body's own enzymes into smaller fragments (pharmaceutically active form comprising at least 7 to 11 amino acids) which have a biologically desired function in the sense of the invention. by endogenous enzymes into smaller fragments (pharmaceutically active form comprising at least 7 to 11 amino acids) which have a biologically desired function in the sense of the invention. That is, the individual fragments of the oligopeptide exhibit activity as HLA-A, HLA-B or HLA-C tumor antigen peptides and thus contribute to the activation of T cells. In a particular embodiment, any class II HLA peptide sequence may be a humanized and / or sequence optimized sequence as further described herein. The use of at least one HLA tumor antigen peptides corresponding to class II MHC complexes comprised in at least one HLA tumor antigen polypeptide for the treatment of cancer according to the invention has the significant advantage that B cells are also activated in a targeted manner in the subject to be treated. The use of HLA tumor antigen peptides of class II according to the invention has the further advantage that HLA antigen peptides, which have longer amino acid sequences than HLA tumor antigen peptides of class I, can be broken down by the body's own enzymes, for example, into smaller fragments (comprising at least 7 to 11 amino acids) after application to the test person, which have an activity as HLA-A, HLA-B or HLA-C antigen peptides and thus contribute to the activation of T cells. "Fragment" means a portion of a polypeptide that preferably contains at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95% or more of the total length of the reference polypeptide. A fragment may contain 7, 8, 9, 10, 11, 12, 13, 14, 15, or more amino acids. In particular, amino acid sequences and polypeptides of the invention are preferred as defined in the claims and those in which: at least one HLA tumor antigen peptide is analogous to at least one HLA tumor antigen peptide exposed on the cell surface of cells from malignant and / or neoplastic tissue of the individual to be treated, which peptide has in its amino acid sequence at least one amino acid exchange compared to the wild type of said HLA tumor antigen peptide (i.e., HLA neoantigen peptide).HLA neoantigen peptide) and, compared to the wild type of this HLA tumor antigen peptide, has at least a 3-fold increased specific affinity towards the T cell receptor of the endogenous T cells. It is an outstanding achievement of the inventors to have found that a pharmaceutical composition containing more than 3, preferably between 5 and 25 such HLA tumor antigen peptides is particularly effective. The pharmaceutical composition according to the invention therefore preferably contains at least 5, very preferably at least 8, most preferably 10 of the HLA tumor antigen peptides corresponding to class I and / or class II MHC complexes arranged on HLA tumor antigen polypeptides, in particular those selected from the list consisting of SEQ-ID-Nos.: 1 to 37, 40 to 68. A further outstanding achievement of the inventors is to have found that, in particular in vitro and in vivo, the potency of HLA tumor antigen peptides can be particularly enhanced by arranging them on tandem or overlapping HLA tumor antigen polypeptides, preferably the potency, measured e.g. as [nspots / pM] via an ELISpot method, of these HLA tumor antigen polypeptides being 1-10, particularly preferably 1.5-5 times higher than that of individual HLA tumor antigen peptides. e.g. as [nspots / pM] via an ELISpot method, of these HLA tumor antigen polypeptides is 1-10, particularly preferably 1.5- 5 times higher than that of the individual HLA tumor antigen peptides associated with the HLA tumor antigen polypeptide. It is a great achievement of the inventors to have found that multimerization of HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes by their arrangement on at least one HLA tumor antigen polypeptide (HTAPP), wherein the HLA tumor antigen peptides (HTAP) are tumor-exclusive or tumor-associated and are presented on the cell membrane of the associated tumor cell and correspond to an amino acid sequence of a transcribed mutant gene, the in vitro and in vivo effect of such HLA tumor antigen polypeptides is greatly enhanced compared to the single related HLA tumor antigen peptides. Moreover, a single HLA tumor antigen polypeptide may advantageously correspond to at least one, preferably at least two, more preferably at least three, most preferably at least 5, alternatively preferably at least 6, most preferably at least 8 HLA tumor antigens that correspond to MHC I or II class complexes, and as such may be predisposed for use in a subject or group of subjects, preferably a group of subjects. Preferably, a monovalent amino acid sequence (or a polypeptide comprising only one amino acid sequence of the invention) used in the invention is such a one as to bind to a T cell receptor of endogenous T cells with a 3-fold increased specific affinity compared to the corresponding wild-type HLA peptide sequence. It should be noted that "may specifically bind to" and "specifically binds to" are used interchangeably herein and refer to the ability to bind specifically to the corresponding specified entity. It is important in connection with the present invention that the diagnosis of the cancer(s) is made in advance by the treating physician. It is possible and preferred to combine amino acid sequences belonging to different classes of HLA tumor antigen peptides used in the invention in a single HLA tumor antigen polypeptide of the invention. In particular, it has been demonstrated that the combination of HLA-A, HLA-B and / or HLA-C tumor antigen peptides and / or corresponding neoantigen peptides in a single polypeptide of the invention have unique binding properties. By one skilled in the art, the specific activity (KD) of the polypeptides of the invention comprising more than one component of the amino acid sequence of the HLA-A, HLA-B and / or HLA-C tumor antigen peptides and / or neoantigen peptides corresponding to the MHC complexes of class I and / or II can be determined according to one of the detection methods described above / below, wherein the compounds, constructs, proteins or polypeptides of the invention preferably have a specific activity similar to the specific activity of each of their components, i.e. a specific activity similar to the specific activity of each of the (individual components of the) amino acid sequences of class I and / or II contained in the compounds, constructs, proteins or polypeptides of the invention. Some specific, but not limiting, examples of the above preferred compounds, constructs, proteins or polypeptides are compounds, constructs, proteins or polypeptides that either. Some specific, but not limiting, examples of such compounds, constructs, proteins or polypeptides of the invention are set forth, for example, in Tables 1-6 or are apparent to those skilled in the art based on the present disclosure. According to another preferred embodiment of the present invention, the HLA tumor antigen polypeptide is present (in each case) as a single-membered amino acid sequence, i.e. not as an element of compounds, constructs, proteins or polypeptides consisting of at least two identical or different amino acid sequences for HLA tumor antigen peptides / neoantigens, in which the HLA tumor antigen peptides / neoantigens are connected to each other by suitable linkers. Preferably, the HLA tumor antigen peptides of the invention exhibit specific activity towards T cell receptors (T cells are used for this purpose), which can be determined using any suitable detection method known to those skilled in the art, such as EliSpot AlphaScreen detection methods (as described herein) or cell-based detection methods (as described herein). Preferably, the blocking activity is determined using a cell-based detection method. In particular, the compounds, constructs, proteins or polypeptides of the invention comprising an amino acid sequence of an HLA tumor antigen peptide of the invention and belonging to MHC class I (as defined herein) preferably have a specific affinity of 10 to 50 nM towards the corresponding T cell receptor. It is also within the scope of the present invention that an amino acid sequence of the invention may bind to two or more class I and / or class II MHC complexes, epitopes, components, domains or subunits of a class I and / or class II MHC complex. In such a case, the MHC complexes, epitopes, components, domains or subunits of an MHC complex to which the amino acid sequences and / or polypeptides of the invention bind may be substantially the same or different (and in the latter case, the amino acid sequences and polypeptides of the invention may bind to such different complexes, epitopes, components, domains or subunits of a class I and / or II MHC complex, including combinations thereof, with an affinity and / or specificity that may be the same or different). It is also expected that the polypeptides of the invention will generally bind to all naturally occurring or synthetic analogs, variants, mutants, components and fragments of a class I and / or class II MHC complex, respectively. Also in such a case, the amino acid sequences and polypeptides of the invention may bind to such analogs, variants, mutants, alleles, components and fragments with an affinity and / or specificity equal to or different from the affinity and specificity with which the amino acid sequences of the invention bind to the wild types of the class I and / or II MHC complex, respectively. It is also within the scope of the present invention that the amino acid sequences and polypeptides of the invention bind to some analogs, variants or mutants of a class I and / or class II MHC complex, but not others. In a specific, but not limiting, embodiment of the present invention, compounds, constructs, proteins or polypeptides comprising an HLA tumor antigen peptide of the invention may have an increased half-life in serum compared to the amino acid sequence from which they were derived. For example, an amino acid sequence of the present invention may be linked (chemically or otherwise) to one or more groups or moieties that extend half-life (such as PEG) such that they are a derivative of an amino acid sequence of the invention with increased half-life. In general, the compounds or polypeptides of the invention with increased half-life preferably have a half-life that is at least 1.5 times, preferably at least 2 times, such as at least 5 times, for example at least 10 times or more than 20 times higher than the half-life of the corresponding amino acid sequence of the invention per se. For example, the compounds or polypeptides of the invention with increased half-life have a half-life that is more than 1 hour, preferably more than 2 hours, more preferably more than 6 hours, such as more than 12 hours or even more than 24, 48 or 72 hours higher compared to the corresponding amino acid sequence of the invention per se. In general, when an HLA tumor antigen peptide of the invention (or a compound, construct or polypeptide comprising the same) is intended for administration to a subject (for example, for therapeutic and / or diagnostic purposes, as defined herein), it is preferably either an amino acid sequence that does not naturally occur in the subject; or, if naturally occurring in the subject, it is in substantially isolated and at the same time concentrated form (as defined herein). In addition, it will also be apparent to those skilled in the art that, for pharmaceutical use, the HLA tumor antigen peptides of the invention (and the compounds, constructs and polypeptides comprising the same) will be directed against a human T cell receptor including combinations thereof as defined in the claims; wherein, for veterinary purposes, the polypeptides of the invention are preferentially directed against a T cell receptor including combinations thereof (as defined in the claims) from the species to be treated or are at least cross-reactive towards a T cell receptor including combinations thereof from the species to be treated. Th cancer to be treated is preferably a hormone positive, HER2 / neu or triple negative cancer. In the context of the present invention, the features of the invention designated "comprising" are intended to be understood to include the more limited description of "consisting of" or "consisting essentially of" the same features of the present invention. The term "and / or" is used to specifically disclose the two features or components together or separately. Therefore, the term "and / or" as used, for example, in the phrase "I and / or II" in the present disclosure includes "I and II", "I or II", "I" and "II". A pharmaceutical composition is to be understood herein as a so-called informatic that can be administered to a subject or a group of subjects with at least one identical HLA allele and which contains the combination of HLA tumor antigen peptides arranged on HLA tumor antigen polypeptides according to the invention in the concentration disclosed herein, wherein an HLA tumor antigen polypeptides and its comprised HLA tumor antigen peptide(s) represents an information carrier. This means that the arrangement of amino acids in the amino acid sequence of the HLA tumor antigen polypeptides ("code") induces a sequence-specific activation of the immune system, in particular of T cells (by HLA tumor antigen peptides corresponding to MHC class I complexes) and / or B cells (by HLA tumor antigen peptides corresponding to MHC class II complexes). Thus, the in vitro or in vivo loading of MHC class I complexes or MHC class II complexes of the tumor cells with the HLA tumor antigen peptides of the pharmaceutical composition according to the invention having an identical or slightly modified amino acid sequence with HLA tumor antigen peptides and their corresponding HLA tumor antigen polypeptides, respectively, renders contacting T cells with said HLA tumor antigen peptides tumor cells sensitive to lysis of the tumor cells of the tissue or tissue resection by specific cytotoxic or specifically activated T lymphocytes. However, the primary objective of the present invention is not to load tumor cells with HLA tumor antigen peptides in vitro or in vivo, but to induce specific activation and training of the immune system, in particular of T cells and B cells against tumor cells. For this reason, the pharmaceutical composition according to the invention is preferably applied subcutaneously or intradermally and, preferably substantially simultaneously (i.e., successively) at least 2, particularly preferably at least 3, sites of application remote from a tumor lesion and / or the cancerous lymph node area. This has the particular advantage that the immune system or the T cells, respectively, which recognize the applied HLA tumor antigen peptides, process this information applied in the form of tumor antigen peptides and consequently specifically recognize and lyse tumor cells presenting these HLA tumor antigen peptides on their surface. Therefore, the method according to the invention has the advantage that in case the signals emitted by the tumor towards the immune system are too weak (passive) or the tumor actively secretes substances that promote its growth (stimulate macrophages) (active e.g. TREX or BD1 ramp up), the immune system, in particular the T cells can be trained to the presence of the tumor even if the signals emitted by the tumor are too weak. The signals emitted by the tumor are too weak when the presentation of HLA tumor antigen peptides on the cell surface of the tumor cells is low or decreases in response to cytotoxic T cell attacks that have occurred (escapemechanism). For the purposes of the present invention, an HLA tumor antigen peptide, also sometimes simply referred to as HLA antigen peptide, is an HLA tumor antigen peptide if it is a tumor-exclusive HLA antigen peptide (i.e. expressed and / or exposed exclusively by tumor cells; a cancer testis antigen (CTA) that is no longer present in the healthy / normal tissue of the adult subject / group of subjects; or a so-called neoantigen peptide) or a tumor-associated HLA antigen peptide. Analogously, an HLA antigen polypeptide is an HLA tumor antigen polypeptide if at least one, preferably two HLA tumor antigen peptides are arranged on it, preferably executed as a tandem or overlapping HLA tumor antigen polypeptide. "Tumor-exclusive HLA antigen peptides" are mutated HLA antigen peptides resulting, for example, from a mutation of a gene, where the mutation of the gene is causative for tumor growth and / or is related to oncogenesis. They are also referred to as “tumor-exclusive antigen(s)”, short TEA(s) or as “tumor-specific antigen(s)”, short TSA(s). The mutated gene product in the tumor is specific for the individual subject or a certain group of subjects with at least one identical HLA allele. "Tumor-associated HLA antigen peptides" include non-mutated HLA antigen peptides expressed in the adult stage only in some tissues of the subject or a specific group of subjects with at least one identical HLA allele, but also in tumor cells. They are also referred to as “tumor-associated antigen(s)” or TAA(s). The immunogenicity of tumor-associated HLA antigen peptides is usually low, since their presence in healthy cells can produce immunological tolerance (immune tolerance). Nevertheless, the induction of a strong immune response against HLA antigen peptides that are merely tumor-associated carries the risk of an autoimmune response. In some preferred embodiments, targeting TAAs may be advantageous if they are preferably overexpressed by at least a factor of 3, more preferably by at least a factor of 5, especially if they are associated with tumor growth and can complement a strong immune response. "Tumor-exclusive HLA antigen polypeptides" comprise at least one mutated HLA antigen peptides resulting, for example, from a mutation of a gene, where the mutation of the gene is causative for tumor growth and / or is related to oncogenesis. The mutated gene product in the tumor is specific for the individual subject or a certain group of subjects with at least one identical HLA allele. "Tumor-associated HLA antigen polypeptides" comprise at least a non-mutated HLA antigen peptides expressed in the adult stage only in some tissues of the subject or a specific group of subjects with at least one identical HLA allele, but also in tumor cells. The immunogenicity of tumor-associated HLA antigen peptides is usually low, since their presence in healthy cells can produce immunological tolerance (immune tolerance). Nevertheless, the induction of a strong immune response against HLA antigen peptides that are merely tumor-associated carries the risk of an autoimmune response. In some preferred embodiments, targeting TAAs with Tumor-associated HLA antigen polypeptides may be advantageous if they are preferably overexpressed by at least a factor of 3, more preferably by at least a factor of 5, especially if they are associated with tumor growth and can complement a strong immune response. A chimeric human leukocyte antigen (HLA) allele, also known as a fusion HLA allele, is an allele created by combining or fusing sequences from two different HLA alleles. This can occur naturally during the process of meiosis. In the context of the present invention, these chimeric HLA alleles can be considered as two different HLA alleles, since they also occur individually in subjects. This has the advantage that an HLA tumor antigen polypeptide comprising a chimeric HLA tumor antigen peptide corresponding to a chimeric HLA allele is a tandem peptide with all the advantages set forth herein. A “tandem polypeptide”, also referred to as “tandem HLA tumor antigen polypeptide” or “tandem polypeptide of the invention” or simply “tandem peptide” comprises or consist of at least 2 HLA tumor antigen peptides according to the invention corresponding to MHC class I and / or class II complexes. The individual HLA tumor antigen peptides may be directly connected or bound by an amino acid linker. A linker is preferably between 3 and 5 amino acids in length, most preferably selected from GPGPG, AAY or AYY. This allows for better flexibility of the peptide backbone and allows for cleaving of a HTAPP into fragments, which may be processed into MHC class I and / or II complex inside of a cell. Providing the fragments in the form of a tandem HTAPP instead of a mixture of smaller fragments comprising the HTAPP is more effective and represents an improvement over the prior art. The process of creating tandem peptides may be referred to as linking, which may include the use of a linker sequence or also directly fusing the amino acid sequences of the HLA tumor antigen peptides and / or HLA tumor antigen polypeptides together. Furthermore, in a preferred embodiment of the present invention, a tandem polypeptide comprising at least two HLA tumor antigen peptides linked by a linker, preferably selected from AAY or AYY, can be readily cleaved, preferably enzymatically. This allows the HLA tumor antigen peptide to be precisely matched to an MHC class I and / or class II complex and, at the same time, has the advantage that a single polypeptide can be used to simultaneously target different epitopes of a mutant cell, preferably a cancer cell. An “overlapping tandem polypeptide”, also referred to as “overlapping tandem HLA tumor antigen polypeptide” or “overlapping tandem polypeptide of the invention” or simply “overlapping peptide” comprises or consist of at least 2 HLA tumor antigen peptides according to the invention corresponding to MHC class I and / or class II complexes, which overlap in their amino acid sequence. Overlap in the context of the inventions means that the individual amino acid sequences of at least two different HLA tumor antigen peptides share a partial consecutive sequence of their amino acid sequence. Preferably, this overlap consists of a single amino acid, more preferably two amino acids, most preferably at least three amino acids, but never exceeds the total length of either peptide minus one amino acid to ensure that the amino acid sequence of the peptides cannot be congruent. This advantageously allows to effectively multimerize an HLA tumor antigen polypeptide and increase the density of matching HLA alleles and mutated genes, thus allowing an efficient polypeptide formation with a length of preferably between 15 and 45, preferably between 17 and 40 amino acids, while reducing the risk of disadvantages associated with longer amino acid chains, especially peptide folding, tertiary structure interactions, increased risk of enzymatic or chemical cleavage and degradation. A “delivery aiding capping peptide” (DACP) in the sense of the current invention is a peptide, i.e., a short amino acid sequence, preferably between 10 and 20 amino acids in length, that can be directly or indirectly (via a linker) attached to the C- or N-terminus of an HLA tumor antigen polypeptide according to the present invention. Advantageously, this peptide increases the ability of HTAPP to enter or penetrate the cell, allowing it to enter the cell more easily, which is critical due to the presentation mechanism of MHC class I and II complexes on the surface of a cancerous cell: MHC class I molecules are central to cellular immune defense by presenting intracellular antigenic peptides on the surface of almost all nucleated cells. This pathway begins with the degradation of intracellular proteins by the proteasome. The resulting peptides are then transported to the endoplasmic reticulum (ER) via the transporter associated with antigen processing (TAP). In the ER, these peptides are loaded onto MHC class I molecules, which are then transported to the cell surface via the Golgi apparatus. Upon presentation, these complexes can be recognized by CD8+ cytotoxic T cells, leading to the destruction of cells that have abnormal or pathogen-derived peptides, such as those from tumor cells or virus-infected cells. MHC class II molecules are mainly expressed on the surface of antigen-presenting cells and play a critical role in the immune system by presenting extracellular antigenic peptides to CD4+ helper T cells. These molecules scavenge exogenous antigens that are taken up into the cell by endocytosis and then processed in endosomes. MHC class II molecules synthesized in the ER are transported to endosomes, where the invariant chain (II) occupying the peptide-binding groove is replaced by antigenic peptides with the help of HLA-DM. The peptide-MHC class II complexes are then expressed on the cell surface, where they are recognized by T helper cells and trigger an adaptive immune response in which other immune cells are activated. Therefore, it is highly desirable, especially for HLA class I complexes, to be able to efficiently enter the intracellular space of a cancer cell to effectively present the epitope. They can then be transported by a transporter associated with antigen processing (TAP) to the endoplasmic reticulum (ER), where they are encoded on the corresponding MHC class I complexes. An immunogenic HLA tumor antigen peptide is also referred to herein as an "epitope". According to a preferred embodiment of the present invention, MHC complexes corresponding to tumor-exclusive or tumor-associated HLA antigen peptides are associated with proliferation, invasiveness, angiogenesis, and an increase in cytokeratin production of carcinoma. The skilled person is aware of relevant databases and literature listing these effects (e.g., the National Center for Biotechnology Information (NCBI) databases). The HLA tumor antigen polypeptide(s) (HTAPPs) and HTAPP-DACPs of the present invention, alongside the Tumor- Associated Antigens (TAAs) and Tumor-Exclusive Antigens (TEAs), preferably the peptides disclosed in sequences SEQ.-ID-No.: 1 to 481, especially preferably selected from the list comprising SEQ.-ID-No.: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149, 150, 151, 152, 153, 154, 155, 156, 157, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 173, 174, 175, 176, 177, 178, 179, 180, 181, 182, 183, 184, 185, 186, 187, 188, 189, 190, 191, 192, 193, 194, 195, 196, 197, 198, 199, 200, 201, 202, 203, 204, 205, 206, 207, 208, 209, 210, 211, 212, 213, 214, 215, 216, 217, 218, 219, 220, 221, 222, 223, 224, 225, 226, 227, 228, 229, 230, 231, 232, 233, 234, 235, 236, 237, 238, 239, 240, 241, 242, 243, 244, 245, 246, 247, 248, 249, 250, 251, 252, 253, 254, 255, 256, 257, 258, 259, 260, 261, 262, 263, 264, 265, 266, 267, 268, 269, 270, 271, 272, 273, 274, 275, 276, 277, 278, 279, 280, 281, 282, 283, 284, 285, 286, 287, 288, 289, 290, 291, 292, 293, 294, 295, 296, 297, 298, 299, 300, 301, 302, 303, 304, 305, 306, 307, 308, 309, 310, 311, 312, 313, 314, 315, 316, 317, 318, 319, 320, 321, 322, 323, 324, 325, 326, 327, 328, 329, 330, 331, 332, 333, 334, 335, 336, 337, 338, 339, 340, 341, 342, 343, 344, 345, 346, 347, 348, 349, 350, 351, 352, 353, 354, 355, 356, 357, 358, 359, 360, 361, 362, 363, 364, 365, 366, 367, 368, 369, 370, 371, 372, 373, 374, 375, 376, 377, 378, 379, 380, 381, 382, 383, 384, 385, 386, 387, 388, 389, 390, 391, 392, 393, 394, 395, 396, 397, 398, 399, 400, 401, 402, 403, 404, 405, 406, 407, 408, 409, 410, 411, 412, 413, 414, 415, 416, 417, 418, 419, 420, 421, 422, 423, 424, 425, 426, 427, 428, 429, 430, 431, 432, 433, 434, 435, 436, 437, 438, 439, 440, 441, 442, 443, 444, 445, 446, 447, 448, 449, 450, 451, 452, 453, 454, 455, 456, 457, 458, 459, 460, 461, 462, 463, 464, 465, 466, 467, 468, 469, 470, 471, 472, 473, 474, 475, 476, 477, 478, 479, 480, and 481, may be employed either individually or in various combinations within immunogenic therapies for the treatment and / or prophylaxis in a subject or group of subjects suffering from or at risk from suffering from cancer. These therapies are preferably directed towards immunotherapeutic approaches, including but not limited to Chimeric Antigen Receptor T-cell (CAR-T) therapies, RNA / DNA-based pharmaceuticals and / or vaccines and / or pharmaceutical compositions, and peptide pharmaceuticals and / or vaccinations and / or pharmaceutical compositions. Furthermore, the invention encompasses the disclosure of peptide sequences along with their corresponding RNA and DNA nucleotide sequences, which are responsible for transcribing the aforementioned peptides. The at least one HLA tumor antigen polypeptide within the scope of the present invention is particularly formulated for subcutaneous administration. The term / concept "composition" therefore refers to the provision of at least one HLA tumor antigen peptide and an adjuvant in a pharmaceutical formulation that allows good applicability and includes solutions, in particular injection solutions and infusion solutions, concentrates for the preparation of injection and infusion preparations, powders for the preparation of injection and infusion preparations and subcutaneous implants. Pharmaceutical compositions are prepared by dissolving or suspending the determined HLA tumor antigen peptides in a carrier liquid (i.e., a pharmacologically acceptable vehicle), optionally with the addition of other excipients such as wetting agents, dyes, permeation enhancers, resorption enhancers, preservatives, antioxidants, light stabilizers. The carrier fluid is preferably selected from the group consisting of Sodium Chloride Injection Solution, Ringers Injection Solution, Isotonic Dextrose, Sterile Water, Dextrose Solution, Lactated Ringers Injection Solution, Distilled Water, or mixtures thereof, for local injection. It is particularly advantageous for good solubility of the determined HLA tumor antigen polypeptides if their amino acid sequence has the lowest possible number of hydrophobic amino acids. Preferably, dimethyl sulfoxide (DMSO), ethoxyethylene diglycol, ethanol, phosphatidylcholines, propylene glycol dipelargonates (DPPG), or glycolysed ethoxylated glycerides are suitable permeation promoters. According to a preferred embodiment of the present invention, the pharmaceutical composition comprises water, a pharmaceutically acceptable saline solution and / or DMSO. For example, pharmaceutical compositions comprising a mixture of about 30% DMSO and 70% water are suitable for application. Another preferred mixture comprises 25% DMSO and 75% water. A higher water content is desirable because DMSO, while largely nontoxic, is associated with side effects such as unpleasant odor and may mediate the entry of other toxins into the body. The term "class I HLA tumor antigen peptide (corresponding to MHC complexes)" as used herein refers to a peptide sequence that is bound to or immunogenic for the class I MHC complex (HLA complex in humans). The class I HLA protein complex is used for antigen presentation on the cell surface and comprises a heavy chain with 3 domains (α1, α2, and α3) and the β2-microglobulin (β2M). The term "class II HLA tumor antigen peptide (corresponding to MHC complexes)" refers to a polypeptide sequence that is bound or immunogenic to the class II MHC complex (in humans, the HLA complex). The class II HLA protein complex is used for antigen presentation on the cell surface and consists of two chains of nearly equal size, an α-chain and a non-covalently bound β-chain, each chain having two extracellular domains (α1 and α2 and β1 and β2). As such, the polypeptides and pharmaceutical compositions of the present invention (as defined herein) may be used for use and / or particulary as a medicament in the prevention and treatment of cancer (also referred to herein as "cancer of the invention" or as “carcinoma”, or to as “malignant tissue”, or to as “cancerous tissue”). In general, the "cancer of the invention" may be defined as diseases and disorders that can be appropriately prevented and / or treated by appropriate administration of either a tumor antigen peptide or a pharmaceutical composition of the invention (and more particularly, a pharmaceutically effective amount thereof) to a subject (i.e., a person having the disease or disorder, or at least one symptom thereof, and / or who is at risk of acquiring or developing such disease or disorder). Preferably, a cancer of the invention may be selected but is not limited to the list comprising breast cancer, lung cancer, prostate cancer, colon cancer, stomach cancer, liver cancer, cervical cancer, bladder cancer, non-Hodgkin's lymphoma, skin cancer, thyroid cancer, kidney cancer, ovarian cancer, pancreatic cancer, and esophageal cancer. For the purposes of the present invention, a "peptide sequence" (e.g., an HLA tumor antigen peptide or an HLA tumor antigen peptide arranged on an HLA tumor antigen polypeptide) having a "native sequence" comprises a peptide sequence having the same (i.e., unmodified) amino acid sequence as a naturally occurring peptide sequence in the subject. Such a peptide sequence with a "native sequence" can be isolated from nature or produced recombinantly or synthetically. In particular, the term peptide sequence having a "native sequence" includes naturally occurring truncated or secreted forms of the peptide sequence (e.g., an extracellular domain sequence), naturally occurring variants (e.g., alternatively spliced forms), and naturally occurring allelic variants of the peptide sequence. In this context, the pharmaceutical composition is preferably applied subcutaneously ("under the skin"), or intradermally ("into the skin"), or intramuscularly ("into the muscle"). The application may be intramuscular as an injection into the thigh (vastus lateralis muscle), preferably into the upper arm (deltoid muscle). As further described herein, the amino acid sequences used in the invention are single variable HLA antigen peptide domains ("HLAs" or "HLA complex"). A single variable HLA antigen peptide domain is (as further defined herein) a region within the amino acid sequence of a protein that can be distinguished from its surrounding sequence based on defined characteristics. Amino acid sequences or regions within the amino acid sequence of a protein of the invention that are HLAs are also referred to herein as "HLAs of the invention." Some preferred examples of single variable HLA tumor antigen peptide domains suitable for use in the invention are apparent from the further description herein and include, in particular, HLA- A, HLA-B and HLA-C antigen peptides corresponding to MHC class I complexes and HLA-DR, DQ and DP antigen peptides corresponding to MHC class II complexes. Such neoantigen peptides (i.e., HLA tumor antigen peptides expressed and / or exposed exclusively by tumor cells) that have less than 100% sequence identity or similarity to the native HLA tumor antigen peptide are preferably characterized by an amino acid substitution in the amino acid sequence for the purposes of the present invention. The following terms are used to describe the sequence relationships between two or more amino acid sequences or polypeptide sequences: "reference sequence," "amino acid exchange," "sequence identity," "percentage of sequence identity," and "substantial identity." In the context of the present invention, the term "amino acid substitution" or amino acid exchange refers to the substitution of one amino acid for another amino acid within the amino acid sequence of the HLA antigen peptide to be synthesized relative to the wild type of such HLA tumor antigen peptide (i.e., native HLA antigen peptide). "Sequence identity," "percentage of sequence identity," or identity or similarity with respect to such amino acid sequence is defined herein as the percentage of amino acid residues in the amino acid sequence of the polypeptide that is identical (i.e., same residue) or similar (i.e., amino acid residue from the same group based on common side chain characteristics, see below) to the amino acid sequence of the wild type. According to a preferred embodiment of the present invention, the amino acid substitution for the HLA tumor antigen peptide corresponding to the class I and / or class II MHC complexes comprises at least one substitution at any position within the amino acid sequence relative to the wild type of that HLA peptide. According to another preferred embodiment of the present invention, the amino acid exchange for the HLA tumor antigen peptide corresponding to class I and / or class II MHC complexes comprises at least one of a D / Y, a C / Y, an A / V, a T / M, an E / A, or a D / A exchange at any position within the amino acid sequence relative to the wild type of said HLA peptide. The amino acids used herein are abbreviated according to the generally accepted single letter code of the IUPAC Nomenclature Commission. Where two amino acids are separated by a hyphen ( / ), this indicates that at a specific amino acid position in the amino acid sequence concerned, the wild-type amino acid (left side of the hyphen) has been replaced by another amino acid (right side of the hyphen). To determine / derive preferred anchor positions and a preferred specific amino acid exchange in the amino acid sequence of HLA tumor antigen peptides, in silico modeling methods are particularly suitable, such as by means of the algorithm NetMHC 4.0 (http: / / www.cbs.dtu.dk / services / NetMHC / ) based on the publications by Andreatta and Nielsen (Bioinformatics (2016) Feb 15;32(4):511-7) and Nielsen et al. (Protein Sci., (2003) 12:1007-17). The term "cancer" pertains to a complex group of diseases characterized by uncontrolled cell growth and proliferation, which can originate in various tissues and organs throughout the body. Cancer may be incited by a myriad of factors, whether sourced externally, such as through exposure to carcinogens, or driven by internal genetic mutations or malfunctions, leading to the development and progression of malignant tumors. In humans, "cancer" broadly encompasses a spectrum of conditions that induce pain, dysfunction, and distress, both physically and emotionally, to the individual impacted, and potentially imposes social and psychological burdens upon those in close association with them. This all-encompassing perspective on cancer may, at times, also embrace a variety of facets related to the disease, such as secondary symptoms, anomalies in physiological structures and functions, and implications of specific cancer treatments or therapies. In this context, cancer refers to but is not limited to, cancers that predominantly threaten individuals, namely: Lung, Breast, Colorectal, Prostate, Stomach, Liver, Cervical, Thyroid, Bladder, Non-Hodgkin Lymphoma, Kidney, Leukemia, Pancreatic, Ovarian, and Esophageal cancers. Importantly, it is recognized that confronting and managing cancer can significantly reshape an individual’s life perspective and personality due to the profound challenges and adjustments invariably associated with diagnosis, treatment, and survivorship. In this context, the term "mutanoma" is a neologism of "mutation" and "carcinoma" and is intended to emphasize the central role of genetic mutations in the formation and development of neoplasms. As such, a mutanoma is the sum of genetic mutations in a subject or group of subjects who have cancer or are at risk of developing cancer. For purposes of comparing two or more amino acid sequences, the percentage of "sequence identity" between a first amino acid sequence and a second amino acid sequence may be calculated or determined by dividing the number of amino acids in the first amino acid sequence that are identical to amino acids at corresponding positions in the second amino acid sequence, by [the total number of amino acids in the first amino acid sequence] and multiplying by [100%], wherein each deletion, insertion, substitution or addition of an amino acid in the second amino acid sequence - compared to the first amino acid sequence - is considered as a difference to a single amino acid (position).The term "therapeutic treatment" relates to any treatment which improves the health status and / or prolongs (increases) the lifespan of an individual. Said treatment may eliminate the disease in an individual, arrest or slow the development of a disease in an individual, inhibit or slow the development of a disease in an individual, decrease the frequency or severity of symptoms in an individual, and / or decrease the recurrence in an individual who currently has or who previously has had a disease. The terms "prophylactic treatment" or "preventive treatment" relate to any treatment that is intended to prevent a disease from occurring in an individual. The terms "prophylactic treatment" or "preventive treatment" are used herein interchangeably. The amino acids used herein are abbreviated according to the generally accepted 15 one-letter code of the IUPAC Nomenclature Commission. Where two amino acids are separated by a hyphen ( / ), this indicates that at a specific amino acid position in the amino acid sequence concerned, the wild-type amino acid (left side of the hyphen) has been replaced by another amino acid (right side of the hyphen). In the present invention, the amino acids (IUPAC one-letter code) S, T, C, N, Q, Y are considered hydrophilic acids; the amino acids (IUPAC one-letter code) A, F, G, I, L, M, P, V, W are considered hydrophobic acids; the amino acids (IUPAC one-letter code) D, E, are considered acidic; the amino acids (IUPAC one-letter code) R, K, H are considered basic acids. The terms "immunization" or "vaccination" describe the process of administering an antigen to an individual with the purpose of inducing an immune response, for example, for therapeutic or prophylactic reasons. An HLA tumor antigen polypeptide is "immunogenic" if the tumor cells expose on their cell surface at least one corresponding MHC class I complex and / or at least one corresponding MHC class II complex that recognizes and binds to the HLA tumor antigen peptide, i.e. the HLA tumor antigen peptide exhibits a high specific activity towards this MHC class I complex and / or MHC class II complex. The immunogenicity of the HLA tumor antigen peptide can be determined by Western blot, ELISA techniques, in particular by ELISPOT or immunodetection with microscopic analysis. The HLA tumor antigen peptides of the present invention are preferentially immunogenic and are therefore also referred to as immunogenic HLA tumor antigen peptides ("epitopes"). The immunogenicity of the HLA tumor antigen peptides can be determined by suitable detection methods. Such methods are known to the skilled person and / or described herein. The HLA tumor antigen polypeptides of the present invention are preferentially immunogenic and are therefore also referred to as immunogenic HLA tumor antigen peptides ("epitopes"). The immunogenicity of the HLA tumor antigen polypeptides can be determined by suitable detection methods. Such methods are known to the skilled person and / or described herein. The term "specific affinity" or "specific binding affinity" of the HLA tumor antigen peptide towards the T cell receptor (TCR) refers to the specific and reversible binding of the HLA peptide to the TCR of the endogenous T cells. This "specific affinity" according to the present invention is expressed in moles via the dissociation constant (K D) determined by ligand binding assays. Alternatively, the "specific affinity" of the HLA tumor antigen peptide can be determined by in silico methods. According to a preferred embodiment of the present invention, at least one HLA tumor antigen peptide is a tumor- exclusive HLA tumor antigen peptide (i.e., a cancer-testis antigen (CTA) that no longer occurs in the healthy / normal tissue of the subject / group of subjects or a so-called neoantigen peptide), and wherein the specific binding affinity of the tumor-exclusive HLA tumor antigen peptide is determined against the corresponding MHC class I complex with a KDin the range of 10 to 50 nM, as determined by surface plasmon resonance. According to a preferred embodiment of the present invention, at least one HLA tumor antigen polypeptide is a tumor- exclusive HLA tumor antigen polypeptide (i.e., a cancer-testis antigen (CTA) that no longer occurs in the healthy / normal tissue of the subject / group of subjects or a so-called neoantigen peptide), and wherein the specific binding affinity of the tumor-exclusive HLA tumor antigen polypeptide is determined against the corresponding MHC class I and / or II complex with a KDin the range of 10 to 50 nM, as determined by surface plasmon resonance. Based on conventional in silico binding prediction models (modeling), tumor antigen peptides with a KDof <50 nM are generally considered strong-binding and those with a KD between 50 and 500 nM are considered weak-binding tumor antigen peptides. However, in the in vivo determinations according to the invention, it has now been shown that the KDvalue is not necessarily important. Surprisingly, it was found that tumor antigen peptides that had a KDvalue in the range of 50 to 500 nM triggered effector cells (i.e., cytotoxic T cells) contrary to conventional in silico binding prediction models that considered them to have low binding. Thus, it is essential for tumor antigen peptide efficacy that the tumor antigen peptides are immunogenic. The term "active substance enhancer / adjuvant" refers to an adjuvant which triggers and / or enhances the effect of the HLA peptides in the first place. In principle, all commonly used adjuvants known to the skilled person are suitable for the production of a formulation according to the invention. The term "individual" (also referred to herein as "subject" or "patient") is used interchangeably with the term "subject" to mean any mammal that is being treated for an abnormal physiological condition or has been diagnosed with a disease. The terms "individual" and "subject" as used in the present invention include mammals, such as a rodent, a carnivore, a cloven-hoofed animal, an odd-toed ungulate, or a primate. In particularly preferred embodiments, the subject is a human. Where reference is made herein to a “subject group” or a “group of subjects” or a "patient group", reference is always made to a group of individuals, preferably human beings, who all have at least one, preferably at least two, most preferably at least three identical HLA allele(s). It is permissible that subjects to be treated with the pharmaceutical composition have received a standard therapy procedure (e.g., at least one surgery, radiation, chemotherapy, and / or hormone therapy). The terms "individual" and "subject" as used in the present invention include mammals, such as a rodent, a cloven- hoofed animal, an odd-toed ungulate, or a primate. In particularly preferred embodiments, the subject is a human. Unless otherwise stated, the terms "individual" and "subject" do not denote a particular age, and thus encompass adults, elderlies, children, and newborns. In some embodiments, the term "subject" includes humans of age of at least 50, at least 55, at least 60, at least 65, at least 70, or older. In some embodiments, the term "subject" includes humans of age of at least 65, such as 65 to 80, 65 to 75, or 65 to 70. However, the pharmaceutical composition may also be administered as a first-line therapy to the subject or specifically identified group of subjects with at least one identical HLA allele. According to a preferred embodiment of the present invention, the individual has not yet received chemotherapy for locally recurrent or metastatic cancer and / or has not received prior adjuvant chemotherapy in recurrence for 12 months or less since the last dose. Particularly preferably, the individual has the haplotype with subgroup A*01 or A*02. A "haplotype" (an abbreviation for "haploid genotype") is the sum of the composition of all specific alleles (= specific fingerprint) of a subject and denotes a variant of a nucleotide sequence on one and the same chromosome in the genome of a living being. A specific haplotype can be individual-, population- or species-specific. For the purposes of this invention, the transcriptome comprises the sum of all genes transcribed at a given time in a cell, i.e. transcribed from the DNA sequence into mRNA sequences, i.e. the totality of all as well as the quantification of the individual mRNA molecules produced in a cell. However, the creation of the transcriptome does not yet allow any statement about the "correctness" of the transcribed mRNA sequences. In this context, the term "building a transcriptome" as used in the present disclosure refers to the analysis of the transcriptome as the sum of all genes transcribed in a cell at a given time point preferably by quantitative real-time (RT)- PCR followed by DNA microarray or subsequent DNA sequencing. Typically, constructing the transcriptome of the tissue sample provided in step (a) of the determination procedure of the invention comprises acquiring more than 40,000 coding DNA sequence (raw data). In genetics, the exome is the totality of the exons of an organism, i.e. all sections that potentially code for proteins. In humans, the exome comprises about 23,000 genes with approximately 50 million nucleobases. Whole exome sequencing (WES) examines all exons, i.e. the sections coding for proteins in the genome of a tissue section (i.e. healthy tissue or tumor tissue of a test person). Genetic diagnostics focuses on these 1-2% of the human genome, where 85% of known disease-causing mutations are found. Accordingly, exome analysis involves sequencing the exome of the subject (and other relatives, if applicable), evaluating the sequence data, and summarizing the results in a medical report. This diagnostic procedure is the method of choice to find the cause of the disease, especially in subjects with complex or unspecific symptoms and a diagnosis that has often remained unexplained for years. Compared to Whole Exome Sequencing (WES), in which all protein-coding regions of the approximately 23,000 known genes are enriched and sequenced, Clinical Exome Sequencing (CES) enriches a subset of the exome. In WES, the focus is on determining disease-associated genes described in the Human Gene Mutation Database (HGMD). For the purposes of the present invention, the proteome refers to the totality of all proteins of at least one cell in a malignant or neoplastic tissue / tissue section or a cell compartment thereof, under precisely defined conditions and at a specific point in time. The proteome of a cell can be determined by proteome sequencing and is linked to the genome of that cell via the transcriptome. Immunotherapies are based on deciphering the individual mutation pattern (signature) of the tumor of each cancer subject. Based on the profile of the mutation pattern, synthetic vaccines, for example RNA-based vaccines, are produced for each individual subject according to conventional treatment approaches (i.e. vaccine production or production of the informaticum according to the invention). These are subsequently used for the individual treatment of the subject. Basically, these novel vaccines are no good for other subjects with the same tumor, but can only be used for the respective subject whose mutanoma has been previously analyzed for vaccine production or production of the informaticum of the invention. Therefore, it is an outstanding achievement of the inventors to have recognized that different subjects have overlap in the mutanoma of the malignant or neoplastic tissue / tissue resection thereof. Advantageously, different subjects can be divided into uniform subject groups such that at least 50% of the HLA peptides of the formulation according to the invention is compatible with the mutanoma of the subject group. The totality of all HLA tumor antigen peptides presented on the cell surface via MHC molecules is referred to as the (HLA) ligandome for the purposes of the invention. It is assumed that more than 105HLA molecules are expressed on the cell surface and the number of identical HLA peptides presented can vary from a few to up to 10,000 copies per cell. Consequently, approximately 10,000 different HLA peptides are presented on a cell in varying proportions. The ligandome is influenced by various physiological, intrinsic as well as pathological (e.g. cancer or necrosis) factors such as cell type or tissue type, infection or transformation of the cell, or simply the current state of the cell, which depends on nutrient situation or external stress factors, resulting in changes in the HLA peptides presented. At the beginning of the analysis of the HLA ligandome, for example, Edman degradation can be used to gain first insights into the presented peptides. On the one hand, it is possible in this way to determine the general peptide motif of an allele via pool sequencing, and on the other hand, individual peptide sequences can already be determined via the analysis of individual reversed phase high performance liquid chromatography (RP-HPLC) fractions. Alternatively or complementarily, the analysis of the ligandome can be performed by using modern mass spectrometers in proteomics, with which it is possible to unambiguously determine the sequences of many individual ligands. Two methods are used for the ionization of the peptides or proteins required for this purpose: Electrospray ionization (ESI) and matrix-assisted laser desorption / ionization (MALDI). In ESI, coupling with an RP-HPLC system is common. However, as mass spectrometers have become more sensitive, capillary electrophoresis (CE) has also been used as an analytical separation method. In order to achieve a higher sample throughput and increased sensitivity in ligandome analysis, the so-called UHPLC systems (ultra high performance liquid chromatography) can be used. These HPLC systems use only 2 μm diameter materials as packing material for separation columns, resulting in improved speed, efficiency and chromatographic separation. In order to achieve a higher sample throughput and increased sensitivity in ligandome analysis, the so-called UHPLC systems (ultra-high performance liquid chromatography) can be used. These HPLC systems use only 2.2 to 1.7 μm diameter materials as packing material for separation columns, resulting in improved speed, efficiency, and chromatographic separation. In ESI mass spectrometry, the direct coupling of HPLC and ESI interface allows on-line separation of the sample, which, in combination with an autosampler, enables a fully automated measurement procedure. Because of the continuous solvent flow from the HPLC, samples can be measured in a relatively short time. ESI mass spectrometry uses a wide range of instruments for analysis such as quadrupole time-of-flight mass spectrometers, linear quadrupole ion traps, triple quadrupoles, or ion trap-orbitrap hybrid systems. This advantageously allows the identification of hundreds of HLA peptides in one measurement. IFNγ ELISpot analysis (for protocol see A. Lalvani, R. Brookes, S. Hambleton, W. J. Britton, A. V.S. Hill, A. J. McMichael, J Exp Med 1997; 186 (6): 859–865) was performed ex vivo (without further in vitro culturing for expansion) using PBMCs depleted of CD4+ and enriched for CD8+ T cells (CD8+ effectors), or depleted of CD8+ and enriched for CD4+ T cells (CD4+ effectors). Tests were performed in duplicate and with a positive and negative control, Multiscreen filter plates (Merck Millipore) pre-coated with IFNγ-specific antibodies (ELISpotPro kit, Mabtech).267.000 Cells were used per plate. Plates were scanned using an AID Classic Robot ELISPOT Reader and analyzed by AID ELISPOT 7.0 software (AID Autoimmun Diagnostika). Antigen Peptides (except negative and positive control group) were done in duplicates, spot counts were taken as mean values of each duplicate. The term "deriving a ranking" in the context of the present invention refers to determining / selecting the quantity and affinity of HLA peptides exposed on the cell surface of the cells of the harvested tissue (or a tissue section thereof). Using the previous analyses, a cumulative ranking for the HLA tumor antigen peptides with respect to protein quality and specific affinity (KD) towards the T cell receptor of the endogenous T cells is derived. Thereby, with regard to protein quality, especially content-related factors for tumor progression, such as invasiveness, angiogenesis, but also escape mechanisms of the tumor against immune attack are evaluated. In another embodiment, the highest-ranked sequence possibilities may be further qualified by their existence in a database of possible HLA tumor antigen peptides with a high specific affinity to the endogenous T cell receptors (as defined herein) predicted from sequence data, particularly one that is restricted to the organism / proband from which the HLA tumor antigen peptide was obtained. In another embodiment, the highest ranked sequence possibilities may be further qualified by the separation coordinates of the HLA tumor antigen peptide (e.g., isoelectric point and molecular weight of a protein) and / or its monomer composition. To provide (tumor) antigen peptides, synthetic or isolated HLA tumor antigen peptides derived from the cumulative ranking can in principle be used for the preparation of the (drug) formulations of the present invention and for the preparation of the pharmaceutical composition (as so-called informatics). However, it is a good idea to use synthetic HLA peptides. Processes for the synthetic production of peptides are known to the skilled person. Examples of such production methods are the Merrifield solid-phase peptide synthesis, the Bailey peptide synthesis and the N-carboxylic anhydride method. A further object of the present invention is also (pharmaceutical-) formulations in different dosage forms which contain the combination of active ingredients according to the invention and optionally further active ingredients and / or excipients. Preferred drug formulations are tablets, chewable tablets, chewing gums, coated tablets, capsules, drops, juices, syrups, suppositories, transmucal therapeutic systems, transdermal therapeutic systems, solutions, injections, emulsions, suspensions, easily reconstitutable dry preparations, powders or sprays. Particularly preferred drug formulations are injections or solutions. Alternatively, the drug formulation is present in a suitable application device, preferably as a lyophilizate in a syringe, which allows in situ reconstitution with a pharmaceutically acceptable solution (e.g., saline). Preferably, the (drug) formulations according to the invention are suitable for oral, intravenous, intramuscular, subcutaneous, intrathecal, epidural, buccal, sublingual, pulmonary, rectal, transdermal, nasal or intracerebroventricular administration, with (drug) formulations for subcutaneous or intravenous administration being particularly preferred. Methods known in the prior art for the preparation of pharmaceutical compositions or dosage forms are found in, for example, "Remington's Pharmaceutical Sciences". Pharmaceutical compositions for parenteral administration may contain, for example, excipients, sterile water, or saline, polyalkylene glycols, such as polyethylene glycols, oils of vegetable origin, or hydrogenated naphthalenes. Biocompatible, biodegradable lactide polymer, lactide / glycolide copolymers, or polyoxyethylene-polyoxypropylene copolymers can be used to control the release of the compounds. Other potentially useful parenteral delivery systems for the therapeutic anti-prion compounds include ethylene vinyl acetate copolymer particles, osmotic pumps, implantable infusion systems, and liposomes. In the context of the current invention, artificial intelligence (AI), also referred to machine learning, network, deep learning network, weighted network, neural network, is defined as any machine learning (ML), deep learning (DL), or other model specifically tailored to run and optimize the selection of HLA tumor antigen peptides. Especially, these models are adept at comparing, evaluating, weighting, and transforming a multitude of parameters associated with amino acid sequences and their biochemical interactions. Machine Learning, also referred to as neural network, or machine learning model, for the purposes of this invention, means any algorithm that can use machine learning to build a model based on sample data, referred to as training data, to make predictions or decisions. This algorithm does not have to be explicitly programmed for these circumstances but builds its model exclusively on the training data set. In a preferred embodiment of the present invention, traditional machine learning models, such as support vector machines, random forests, and gradient boosting machines, are utilized. These models offer the advantage of beinginterpretable and relatively swift in their training phase. Their strength lies in their ability to perform exceptionally wel l onstructured data, making them less susceptible to overfitting when the dataset size is limited. In an especially preferred embodiment a random forest is used, which has the advantage of having feature importance included directly into the model. Preferably within the scope of the present invention, deep learning models, including Convolutional Neural Networks and Recurrent Neural Networks, are employed for tasks involving unstructured data. These models are particularly proficient in handling vast datasets, such as images or sequences, and have the innate capability to autonomously extract salient features from the data. In a preferred embodiment, transformer-based models like BERT, BART, and LAMA are incorporated. These models, especially effective for sequence data, can discern intricate patterns and relationships within the data when pre-trained on extensive corpora. Their potential is further amplified when fine-tuned on domain-specific data. Preferably within the scope of the present invention, a hybrid approach is adopted that amalgamates the strengths of different architectures. For instance, a fusion of Convolutional Neural Networks with Recurrent Neural Networks can be employed to extract and process features. In a preferred embodiment of the present invention, ensemble models, which harness the power of multiple models through techniques like bagging or boosting, are utilized. These models offer a robust solution by aggregating predictions, enhancing accuracy, and reducing overfitting. The present invention comprises a pharmaceutical composition for use as a medicament, in particular for use in the therapeutic and / or prophylactic treatment of a carcinoma, particularly preferably a locally recurrent or metastatic carcinoma, especially preferably a carcinoma selected from the list comprising pancreatic cancer (PaCa), liver metastasis (LMCa); bone cancer metastasis (BMCa), prostate cancer (PrCa), Breast Cancer (BrCa), Uterine Cancer (UCa), Brain Cancer (BrnCa), Bladder Cancer (BlCa), Thymus Cancer (ThCa), Biliary Tract Cancer (BiTCa), Skin Cancer (SkCa), Thyroid Cancer (ThdCa), Lung Cancer (LuCa), Colorectal Cancer (CoCa), Esophageal Cancer (EsCa), Stomach Cancer (StCa), Head and Neck Cancer (HNCa), in particular in a subject or group of subjects suffering from or at risk of suffering from a carcinoma, comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP), wherein the pharmacologically effective amount is preferably an absolute concentration (i.e., administration dose) of the HLA tumor antigen peptides (HTAP) or the HLA tumor antigen polypeptides (HTAPP) in a range of 100 to 1000 µg, corresponding to MHC class I and / or class II complexes, preferably a number HTAP in the numerical range obtained by combining any two of the following end point values: 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, arranged on at least one, preferably between 2 to 7 HLA tumor antigen polypeptide(s) (HTAPP), wherein the HLA tumor antigen peptides (HTAP) are tumor-exclusive or tumor-associated and presented on the cell membrane of the exclusive and / or associated tumor cell and correspond to an amino acid sequence of a transcribed mutant gene, wherein the HLA tumor antigen polypeptide comprises a scaffold amino acid sequence, preferably between 15 and 45, more preferably between 17 and 40 amino acids, alternatively preferred the amino acids of the scaffold, also referred to as backbone of the amino acid sequence, is in the numerical range obtained by combining any two of the following end point values: 15, 16, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, and 45, a) wherein the scaffold amino acid comprises, in addition to HLA tumor antigen peptide(s), up to 1 to 30 amino acids, (long HLA tumor antigen polypeptide); and / or b) wherein the scaffold amino acid comprises an HLA tumor antigen peptide(s) with at least 90% sequence identity similarity to the native HLA tumor antigen peptide (similarity HLA tumor antigen polypeptide); and / or c) wherein at least one of the amino acid sequences comprises an HLA tumor antigen peptide having an amino acid sequence comprising or consisting essentially of only one amino acid substitution relative to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide), wherein which overlap in their amino acid sequence. In a preferred embodiment of the pharmaceutical composition for the treatment of carcinoma, the scaffold amino acid sequence within the HLA tumor antigen polypeptide(s) (HTAPP) introduces unique variations tailored to specific needs. The invention further discloses a long HLA tumor antigen polypeptide (a), wherein the scaffold amino acid sequence in this embodiment comprises up to 1 to 30 amino acids in addition to the HLA tumor antigen peptide(s). This longer sequence could increase the stability of the polypeptide and allow more efficient delivery to amino acid sequences present on carcinoma cells. The presence of additional amino acids in the scaffold amino acid sequence could also increase the affinity of the polypeptide for its corresponding MHC class I and / or II complex, improving specificity and reducing potential off-target effects. The invention also encompasses a similar HLA tumor antigen polypeptide. In a preferred embodiment, the scaffold amino acid comprises HLA tumor antigen peptide(s) that have at least 90% sequence identity similarity to the native HLA tumor antigen peptide. By maintaining such a high degree of similarity to the native peptide, this composition could better mimic the natural interactions in the body. This would likely enhance the therapeutic effect by ensuring that the immune system recognizes and efficiently attacks tumor cells. In addition, these modifications may increase binding affinity, allow for the inclusion of additional HLA alleles, or reduce unwanted intra- or intermolecular interactions. The invention also includes an embodiment relating to (c) a substitution HLA tumor antigen polypeptide in which the amino acid sequence of the HLA tumor antigen peptide has a minor modification: an amino acid sequence that either comprises, or consists essentially of, only one amino acid substitution compared to the native HLA tumor antigen peptide. This single substitution can significantly alter the properties of the peptide, potentially increasing its binding affinity or altering its immunogenic properties. This could result in the pharmaceutical composition eliciting a stronger and more targeted immune response against carcinoma cells. The tailored designs of the scaffold amino acid sequences in these embodiments offer specific advantages when incorporated into pharmaceutical compositions for the treatment of carcinoma. By manipulating the structure and sequence of the HLA tumor antigen polypeptide(s), the therapeutic potential of the drug can be optimized to ensure efficient targeting and elimination of carcinoma cells. Variations - from extended sequences to minor substitutions - provide the opportunity to tailor treatment to the type of carcinoma and genetic makeup of the subject or group of subjects. However, these adaptations, which are feasible and obvious to the person skilled in the art when carrying out the method according to the invention with little effort, advantageously allow for lower side effects, the inclusion of new HLA alleles and cancer-related mutated genes of a subject or group of subjects included lead to higher pharmaceutical composition efficacy and better treatment results. A “scaffold amino acid sequence”, also referred to simply as “amino acid sequence” or “antigenic amino acid sequence” in the sense of the present invention is a sequence of amino acids linked by an amide bond, also referred to as a peptide sequence. Preferably, a scaffold amino acid sequence is linear. Preferably, the scaffold amino acid sequence of an HTAPP comprises between 15 and 45, more preferably between 17 and 40 amino acids to reduce the risk of protein folding and degradation that may increase with peptide size. In some preferred embodiments, where the HTAPP comprises a delivery aiding peptide (DACP) corresponding to a cell-penetrating peptide (CPP), the amino acid sequence of the HTAPP comprises the HTAP sequences but not the DACP sequence, which is preferably between 10 and 20 amino acids in length. The total added length of the HTAPP-DACP sequence is between 30 and 80 amino acids, preferably between 30 and 60 amino acids, most preferably between 31 and 55 amino acids. The total length may include, in addition to the amino acid sequence of HTAPP and DACP, peptide linker sequences. The main technical advantage of this is to archive an effective design with a high immunogenic content or payload of the antigenic HTAPP amino acid sequence with the delivery aiding cell-penetrating peptide (CPP). Shorter and longer amino acid sequences face different degradation or folding problems and this total length has been identified as a preferred length range for effective antigenic peptides. In an especially preferred embodiment of the current invention, the pharmaceutical composition may be used for the treatment of any cancer which has at least one mutation in a gene expressed on the surface of the mutant cell (epitope) or a gene which is overexpressed at least by factor three, more preferably factor 5 in relation to native genes in healthy cells. The type of cancer that can be treated by the composition according to the invention can preferably be selected from (but is by no means limited to) the list consisting of: pancreatic cancer (PaCa), liver metastasis (LMCa); bone cancer metastasis (BMCa), prostate cancer (PrCa), Breast Cancer (BrCa), Uterine Cancer (UCa), Brain Cancer (BrnCa), Bladder Cancer (BlCa), Thymus Cancer (ThCa), Biliary Tract Cancer (BiTCa), Skin Cancer (SkCa), Thyroid Cancer (ThdCa), Lung Cancer (LuCa), Colorectal Cancer (CoCa), Esophageal Cancer (EsCa), Stomach Cancer (StCa), Head and Neck Cancer (HNCa). More preferably, the type of cancer that can be treated by the composition according to the invention can be selected from (but is by no means limited to) the list consisting of: Breast Cancer, Prostate Cancer, Pancreatic Cancer, Kidney Cancer, Testicular Cancer, and Osteosarcoma (Bone Cancer). Advantageously, the pharmaceutical composition comprises only linked tandem polypeptides in a particularly preferred embodiment, the efficacy of the immune response can be optimized with respect to potentially exposed MHC class I and / or II complexes carrying the HLA tumor antigen peptides, corresponding to genes associated with a carcinoma and the HLA alleles of a subject, thereby eliciting a stronger and more responsive immune response, as exemplified by some of the preferred HTAPPs of the invention in the examples, particularly in Fig.7A and Fig.7B, is shown. This has the additional technical advantage, that fusion, chimeric or combination of genes related to the carcinoma can be targeted at once. The drastic effect of the combination is especially well documented in figure 7B, were the linking of the two HLA tumor antigen polypeptides SEQ-ID-No.: 77 and SEQ-ID-No.: 78 to the tandem peptide SEQ-ID-No.: 8 led to an increase in Elispot count of more than 237% in relation to the more immunogenic single HTAP which shows a synergistic effect of this step. In a particularly preferred embodiment, the tandem polypeptide may comprise one HTAP linked to another HTAP, which are each related to different HLA alleles and different genes associated or exclusive for a specific cancer type. This allows for more diverse targeting. In another preferred embodiment, at least one HTAPPs can be linked with a HTAP or another HTAPP together to form a tandem polypeptide in the sense of the present invention, preferably combining different genes and HLA peptides. Advantageously, this can be used in a group approach to target a broad range of different mutations in genes commonly associated with a particular type of cancer and associated with an HLA ligandome of a broad range of subjects, wherein at least one HLA allele in each subject is matched to the pharmaceutical composition comprising tandem HTAPPs as defined in the present invention. The effect of the process of linking multiple HLA tumor antigen peptides on a single tandem HLA tumor antigen polypeptide, preferably by a AAY or AYY linker, is preferably at least a 10% boost in immune response, as determined by in vivo or in ex vivo Elispot Sport count difference, more preferably at least 20%, particularly preferably at least 30%, most preferably at least 50%. Advantageously, the pharmaceutical composition comprises only overlapping tandem polypeptides in a particularly preferred embodiment, the efficacy of the immune response can be optimized with respect to potentially exposed MHC class I and II complexes carrying the HLA tumor antigen peptides, corresponding to genes associated with a carcinoma and the HLA alleles of a subject, thereby eliciting a stronger and more responsive immune response, as exemplified by some of the preferred HTAPPs of the invention in the examples, particularly in Fig.7A and Fig.7B, is shown. The effect of the multimerization process of overlapping multiple HLA tumor antigen peptides on a single HLA tumor antigen polypeptide is preferably at least a 10% boost in immune response, as determined by in vivo or in ex vivo Elispot Sport count difference, more preferably at least 20%, particularly preferably at least 30%, most preferably at least 50%. In a particularly preferred embodiment, the pharmaceutical composition comprises at least one overlapping tandem polypeptide and may further utilize HTAPs. This can be used in cases where a subject or group of subjects has a very specific mutation or set of mutations associated with a carcinoma that can be selectively targeted by using a tailored set of additional short HTAPs that are less expensive to synthesize and can be made on a laboratory scale if needed. In a particularly preferred embodiment, an overlapping tandem peptide comprises at least two, more preferably at least three, most preferably at least five different HLA tumor antigen peptides which are overlapping in their amino acid sequences. This creates a stronger immune response, since the absolute amount of peptides is limited per injection by practical means and side effects, therefore including more potential immunogenic sequences on a single polypeptide is highly advantageous. A further clinical gain in the use of the pharmaceutical composition in the treatment of a subject or of a subject or group of subjects having at least one identical HLA allele can be achieved when the pharmaceutical composition, further, comprises a pharmacologically effective amount of at least one HLA-A tumor antigen peptide, preferably 1, 2, 3, 4 or 5 HLA-AB tumor antigen peptide(s) corresponding to MHC class I complexes and / or of at least one HLA-B tumor antigen peptide, preferably 1, 2, 3, 4 or 5 HLA-B tumor antigen peptide(s) corresponding to MHC class I complexes and / or at least one HLA-C tumor antigen peptide, preferably 1, 2, 3, 4 or 5 HLA-C tumor antigen peptide(s) corresponding to MHC class I complexes. It is understood that also the HLA-B tumor antigen peptide(s) or HLA-C tumor antigen peptide(s) corresponding to the specific haplotype of the subject or group of subjects having at least one identical HLA allele are selected for treatment or prophylaxis. In an especially preferred embodiment, an HLA tumor antigen polypeptide of the invention comprises at least one HLA-A and HLA-B tumor antigen peptide. In an especially preferred embodiment, an HLA tumor antigen polypeptide of the invention comprises at least one HLA class I and class II HLA tumor antigen peptide. According to a preferred embodiment of the present invention, the pharmaceutical composition according to the invention comprises 2-25, alternatively preferably at least 4, 6, 7, 8, 9, 10, 12, 14, 16, 18 ,20 or 25 HLA tumor antigen peptides corresponding to MHC class I complexes and / or MHC class II complexes arranged on at least one, preferably 2, more preferably 3, particularly preferably 4, especially preferably 5, most preferably 7 HLA tumor antigen polypeptide(s), and / or at least one HLA tumor antigen peptide which is analogous to at least one HLA tumor antigen peptide exposed on the cell surface of cells from malignant and / or neoplastic tissue (in particular carcinoma) of the individual to be treated, which in its amino acid sequence has at least one amino acid exchange with respect to the wild type of this HLA antigen peptide (so-called neoantigen peptide) and at least a 3-fold increased specific affinity towards the T cell receptor of the body's own T cells (correspondingly measured and / or expressed as KD value). Particularly good success was achieved with pharmaceutical compositions having at least 12, 14, 16, 18, 20 HLA tumor antigen peptides corresponding to MHC class I complexes and / or MHC class II complexes arranged on HLA tumor antigen polypeptides. Furthermore, in some preferred embodiments of the pharmaceutical composition according to the disclosure, a tandem polypeptide comprises at least one HLA tumor antigen peptide corresponding to MHC class I complexes and at least one HLA tumor antigen peptide corresponding to MHC class II complexes, and / or wherein the overlapping tandem polypeptide comprises at least one HLA tumor antigen peptide corresponding to MHC class I complexes and at least one HLA tumor antigen peptide corresponding to MHC class II complexes. In a further advantageous embodiment, the inventors have found that short HLA tumor antigen peptides, for example HLA class I, are less effective than multimerized HTAPPs containing the said HTAPs. This may be attributed to decomposition, since a single cleaving of a HTAP leads to loss of the information, while the fragments of a tandem or overlapping tandem HTAPP may be still immunogenic. Furthermore, it is an outstanding achievement to have found that by overlapping HTAPs onto HTAPPs, rather than simply coupling the HTAPs to fragments, production costs can be dramatically reduced. The production cost and yield of a peptide scales with the power of the amino acids it contains, as each coupling step must be multiplied by the associated yield (on the order of 95-99% in modern solid-state synthesis). Thus, a tandem polypeptide quickly becomes uneconomical to produce. Preferably, the pharmaceutical composition for use as disclosed herein comprises an HLA tumor antigen polypeptide corresponding to HLA tumor antigen peptides corresponding to MHC class I and class II complexes selected from the group consisting of the amino acid sequences set forth in SEQ ID Nos: 1 to 17, 69 and 76. Preferably these sequences are used to treat a subject with a prostate, bone metastasis or pancreas cancer, as indicated by the cancer type in table 1. Advantageously, the working principle of compositions according to the current invention have been demonstrated. In a preferred embodiment, the pharmaceutical composition for use as disclosed herein comprises an HLA tumor antigen polypeptide corresponding to MHC class I and class II complexes which are selected from the group consisting of the amino acid sequences set forth in SEQ-ID-Nos.: 1 to 17, 69, 76 and have at least one amino acid substitution relative to said amino acid sequences. This advantageously allows for adaptation for other mutations encountered or to match additional genes or HLA alleles. In a preferred embodiment, the pharmaceutical composition for use as disclosed herein comprises an HLA tumor antigen polypeptide corresponding to MHC class I and class II complexes which are selected from the group consisting of the amino acid sequences set forth in SEQ-ID-Nos.: 1 to 17, 69, 76 and have at least 90%, more preferably 95% sequence identity to these sequences. This advantageously allows for adaptation for other mutations encountered or to match additional genes or HLA alleles. In some preferred embodiments the pharmaceutical composition comprises at least one HTAPP, wherein the HLA tumor antigen polypeptide comprises, in addition to the HLA tumor antigen peptides, a delivery aiding capping peptide (DACP) attached to a terminal part of its scaffold amino acid sequence, wherein the DACP is preferably selected from the list consisting of penetratin, TAT-derived, R9-TAT, DVP3, and DVP6 (DACP-1 to DACP-5). These peptides are also known as CPPs, which are DACPs in the spirit of the current invention, if they are chemically bound terminally to a HTAPP directly or by a linker. In a preferred embodiment the DACP is directly attached, especially chemically bound, to the HTAPP, in another preferred embodiment the DACP is attached to the HTAPP by a linker. In some preferred embodiments, the linker is easily enzymatically or chemically cleavable, thus enabling a decomposition in the cytosol by enzymes, for example the proteasome. In the context of protein synthesis within a cell, MHC class I molecules typically present endogenous antigens - those that originate from the cell, such as abnormal or cancerous proteins - while MHC class II molecules present exogenous antigens that have been taken up by the cell. These processes are mediated by HLA alleles, which are highly polymorphic genes encoding MHC molecules. The presentation of HLA tumor antigen peptides by MHC molecules is an essential prerequisite for the activation of T cells, which are central to the immune system's ability to recognize and destroy cancer cells in accordance with the current invention. By coupling HLA antigen polypeptides with DACPs, they can be better transported into the cell interior, where the sequences can associate with MHC complexes either fragmented or whole. It is an outstanding achievement of the inventors to have found out that in particular tandem or overlapping HLA tumor antigen polypeptides linked to DACP (HTAPP-DACP) elicit a particularly strong ex and in vivo immunoreaction. In a preferred embodiment of the invention, the use of a DACP enhances this mechanism of immune surveillance. As a short amino acid sequence, preferably between 10 and 20 amino acids, the DACP can bind directly or indirectly (via a linker) to the HLA tumor antigen polypeptide. The DACP facilitates the entry or penetration of the HTAPP into the cell. This may be enabled because of the high content in basic polar amino acid residues in the amino acid sequence of the DACP sequence. This increased cellular uptake is particularly beneficial because MHC molecules must present tumor- derived peptides on the cell surface to elicit an immune response, but especially for HLA class I antigen peptides corresponding to MHC class I complexes, incorporation into the cancer cell cytostome must occur before an immune response is elicited. By increasing the ability of HTAPPs to enter cells, DACPs enhance the presentation efficiency of MHC class I and / or II complexes. The presentation of tumor antigens by MHC molecules on the surface of cancer cells is then recognized by T cells. For MHC class I, this leads to the activation of cytotoxic T cells that can directly kill tumor cells. For MHC class II, interaction with T helper cells leads to recruitment and activation of other immune cells, further enhancing the immune response against the tumor. By combining HTAPP with DACP, the invention can enhance the immunogenicity of tumor antigens, resulting in a more robust and effective immune response that specifically targets cancer cells. While cell penetrating agents are known in the prior art, the use of DACPs, preferably (but not limited to) penetratin (SEQ ID NO: DACP-1), in the context of multimerized HLA tumor antigen polypeptides in a pharmaceutical composition is novel and represents an outstanding achievement of the inventors. By combining multiple synergistic effects to enhance the immunogenic effect of the HLA antigen peptides, the overlap or tandemization of HTAPs on larger HTAPPs allows for multiple fragments that can be associated with different genes and different HLA alleles and therefore can be presented on a variety of MHC complexes, in conjunction with the delivery mechanism that allows for extremely precise and effective targeting of carcinomas in a subject or group of subjects. In a particularly preferred embodiment, the HLA tumor antigen polypeptide (HTAPP) comprising a delivery aiding capping peptide (DACP) has a scaffold amino acid sequence length, preferably a total amino acid sequence length, between 30 and 60 amino acids, more preferably between 31 and 55 amino acids. This enables the technical realization of the composition through relatively low-cost peptide synthesis. In a particularly preferred embodiment, the HTAPPs are no longer than 70 amino acids, preferably no longer than 60 amino acids, because the inventors have found that elongation beyond a certain point leads to undesirable tertiary structural interactions between the amino acids of the scaffold amino acid sequence. This may lead to a reduced effectiveness of the delivery and reduce the efficiency of the immunization, furthermore, increasing the cost and lowering the yield of the peptides. In some preferred embodiments of the pharmaceutical composition according the invention for use as recited herein, wherein the HLA tumor antigen polypeptide comprises a amphipathic delivery aiding capping peptide (DACP), wherein the delivery aiding capping peptide comprises a positively charged and amphipathic sequence with a total percentage of 33% to 89% of arginine (R)and lysine (K) residues and preferably a high content of amphipathic phenylalanine (F), and tryptophan (W) residues, most preferably selected from the group consisting of the amino acid sequences set forth in SEQ IDs DACP-1 to DACP-31, preferably DACP-1 to DACP-25. The inventors found that basic polar amino acids are associated with good cell-modifying properties because they can interact with the polar phospholipid portion of a eukaryotic cell membrane. The percentages of amino acids comprising the delivery aiding capping peptide (DACP) add up to 100%, in particular the addition of the percentages of 10 to 30% arginine (R), preferably 11 to 25% arginine (R) residues and a percentage of 10 to 30% lysine (K) residues, preferably 14 to 25% lysine (K) residues and preferably a high content of amphipathic phenylalanine (F) and tryptophan (W) residues adds up to 100%. Further advantageous compositions are listed in Table 3. In some alternatively preferred embodiments, delivery aiding capping peptides (DACP) comprising or consisting of up to 100% arginine R and / or lysine K amino acids are especially preferred. In embodiments related to arginine, these may be cyclic, which may increase the cell penetrating capabilities of these capping peptides. In a preferred embodiment of the pharmaceutical composition according to the present invention for use in the treatment or prophylaxis of cancer the HLA tumor antigen polypeptide(s) (HTAPP) comprising a delivery aiding capping peptide (DACP) is / are selected from the HLA tumor antigen polypeptide(s) consisting of the group of amino acid sequences set forth in SEQ-ID-Nos.: 1 to 17, 69 and 76 and the delivery aiding capping peptide (DACP) is selected from the group consisting of DACP-1 to DACP-31, preferably DACP-1 to DACP-25, more preferably DACP-1 to DACP-5, most preferably DACP-1. Particulary In another preferred embodiment of the pharmaceutical composition according to the present invention for use in the treatment or prophylaxis of cancer the HLA tumor antigen polypeptide(s) (HTAPP) comprising a delivery aiding capping peptide (DACP) is / are selected from the group consisting of the amino acid sequences set forth in in SEQ-ID-Nos.: 18 to 37, 40 to 68, 70, 71, 81 and 84, preferably 18 to 31, 32 to 36, 40, 43 to 44, 47 to 54, 57 to 64, 67 to 68 and 70, 71, 81, 84. These sequences are immunogenic and tested, particularly preferentially in the context of metastatic cancer, even more preferentially in the treatment of prostate and pancreatic cancer in the context of the genes indicated in Tables 2, 4, 5, and 6. In some preferred embodiments of the pharmaceutical composition according to the present invention for use in the HLA tumor antigen polypeptide(s) (HTAPP) comprising a delivery aiding capping peptide (DACP) is / are selected from the group consisting of the amino acid sequences set forth in in SEQ-ID-Nos.: 18 to 37, 40 to 68, 70, 71, 81 and 84, preferably 18 to 31, 32 to 36, 40, 43 to 44, 47 to 54, 57 to 64, 67 to 68 and 70, 71, 81, 84, and have at least one amino acid substitution relative to said amino acid sequences. The following list some preferred embodiments of the current invention. In some embodiments, the pharmaceutical composition for the treatment of cancer, especially pancreas tumors, comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 1, 2 and 3, which are related to the genes KRAS, ADAM8-NUP50 and CEMIP2 and a subject or group of subjects with at least one of the following HLA alleles A*02:786, C*03:04 and C*06:02. In some embodiments, any one of HLA tumor antigen polypeptide(s) comprise an amino acid sequence 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98 or 99% identical to SEQ-ID-Nos.: 1, 2 and 3. In some embodiments, the pharmaceutical composition for the treatment of cancer, especially prostate tumors, comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 4, 5 and 6, which are related to the genes SMC4, KDM3A and SEMA4D-L-SEMAD4D and a subject or group of subjects with at least one of the following HLA alleles A*02:01, DRB1*15:01 and DRB1*01:01. In some embodiments, any one of HLA tumor antigen polypeptide(s) comprise an amino acid sequence 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98 or 99% identical to SEQ-ID-Nos.: 4, 5 and 6. In some embodiments, the pharmaceutical composition for the treatment of cancer, especially prostate tumors, comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 7, 8 and 9, which are related to the genes TNC, LAMC1, DLX1, FOLH1 and TMEFF2 and a subject or group of subjects with at least one of the following HLA alleles A*03:01, B*07:02 and B*35:01. In some embodiments, any one of HLA tumor antigen polypeptide(s) comprise an amino acid sequence 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98 or 99% identical to SEQ-ID-Nos.: 7, 8 and 9. In some embodiments, the pharmaceutical composition for the treatment of cancer, especially prostate tumors, comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 10, 11 and 12, which are related to the genes DIP2A; LAMC1 and POTEG; POTEH and a subject or group of subjects with at least one of the following HLA alleles DQA1*01:01, A*03:01 and B*07:02. In some embodiments, any one of HLA tumor antigen polypeptide(s) comprise an amino acid sequence 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98 or 99% identical to SEQ-ID-Nos.: 10, 11 and 12. In some embodiments, the pharmaceutical composition for the treatment of cancer, especially prostate tumors, comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 14, 15 and 83, which are related to the genes KLK3, TMEFF2, TMEFF2 and ABLIM1,PLD3 and a subject or group of subjects with at least one of the following HLA alleles A*02:01 and A*03:01. In some embodiments, any one of HLA tumor antigen polypeptide(s) comprise an amino acid sequence 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98 or 99% identical to SEQ-ID-Nos.: 13, 14 and 15. In some embodiments, the pharmaceutical composition for the treatment of cancer, especially prostate tumors, comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 16 and 17, which are related to the genes DXL1 and / or FOLH1 and a subject or group of subjects with at least one of the following HLA alleles E*01:01 and E*01:03. In some embodiments, any one of HLA tumor antigen polypeptide(s) comprise an amino acid sequence 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98 or 99% identical to SEQ-ID-Nos.: 16 and 17. In some preferred embodiments, the pharmaceutical composition for the treatment of cancer, especially pancreas tumors, comprising a pharmacologically effective amount comprising 2 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 1 and 3, which are related to the genes KRAS and CEMIP2 and a subject or group of subjects with at least one of the following HLA alleles A*02:786 and DQA1*01:01. In some embodiments, any one of HLA tumor antigen polypeptide(s) comprise an amino acid sequence 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98 or 99% identical to SEQ-ID-Nos.: 1 and 3." In some preferred embodiments, the pharmaceutical composition for the treatment of cancer, especially pancreas tumors, comprising a pharmacologically effective amount comprising 2 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 1 and 2, which are related to the genes KRAS and ADAM8- NUP50 and a subject or group of subjects with at least one of the following HLA alleles A*02:786 and C*06:02. In some embodiments, any one of HLA tumor antigen polypeptide(s) comprise an amino acid sequence 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98 or 99% identical to SEQ-ID-Nos.: 1 and 2. In some preferred embodiments, the pharmaceutical composition for the treatment of cancer, especially pancreas tumors, comprising a pharmacologically effective amount comprising 2 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 2 and 3, which are related to the genes ADAM8-NUP50 and CEMIP2 and a subject or group of subjects with at least one of the following HLA alleles C*06:02 and DQA1*01:01. In some embodiments, any one of HLA tumor antigen polypeptide(s) comprise an amino acid sequence 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98 or 99% identical to SEQ-ID-Nos.: 2 and 3. In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in KRAS are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 1, 18, 37, 46, 47, 49, 55, 56, 65, 67, and 68. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in ADAM8-NUP50 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 2 and 19. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in CEMIP2 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 3 and 20. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in SMC4 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 4 and 21. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in KDM3A are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 5 and 22. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in SEMA4D-SEMAD4D are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 6. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in TNC-LAMC1 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 7 and 23. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in DLX1-FOLH1 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 8, 16, 17, and 31. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in TMEFF2 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 9, 14, and 28. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in LUZP2 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 10 and 24. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in TMPRSS2-ERG are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 11 and 25. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in EXT2-CACNA2D1 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 11 and 25. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in POTEG; POTEH are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 12 and 26. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in KLK3 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 83. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in ABLIM1; PLD3 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 15 and 29. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in DXL1 and / or FOLH1 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 8, 16, 17, and 31. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in MMP11 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-NO.: 32. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in CEACAM5 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-NO.: 33. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in TP53 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 34, 35, 50, 51, 52, 57, 58, 62, and 63. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in PIK3CA are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 36 and 44. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in KRAS are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 1, 18, 37, 46, 47, 55, 56, 65, 67, and 68. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in U2AF1 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 38. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in FBXW7 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 40 and 41. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in EGFR are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 42 and 61. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in MMP1 are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 43. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in PIK3CA are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 36, 44, and 64. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In some embodiments, a subject or a group of subjects with cancer and a mutation which is related to a mutation in BRAF are treated by a pharmaceutical composition comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprises a HTAPP selected from SEQ-ID-Nos.: 45. In some embodiments, each of the HLA tumor antigen polypeptides may comprise an amino acid sequence having an amino acid sequence consisting essentially of only one amino acid substitution compared to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide). In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*02:786 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 1 and 18. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele C*03:04 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 1 and 18. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele C*06:02 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 1, 2, 18, and 19. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele B*57:37 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 2 and 19. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele DQA1*01:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 3, 4, 5, 12, 20, 21, 22, and 26. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele B*07:02 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 7, 8, 9, 12, 23, 26, 28, 32, 34, 43, and 54. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele B*35:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 7, 12, 23, and 26. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele C*07:02 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 9, 15, 29, 32, and 43. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*02:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 4, 8, 9, 12, 14, 21, 28, 32, 33, 36, 40, 42, 43, 46, 47, 49, 53, 54, 57, and 58. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*03:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 7, 9, 11, 15, 23, 25, 29, 32, 34, 43, 44, 45, 48, and 54. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele E*01:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 16, 17, and 31. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele E*01:03 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 16, 17, and 31. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele DQB1*02:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 3 and 20. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele DQB1*05:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 4, 5, 12, 21, 22, 24 and 26. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele DRB1*15:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 5, 9, and 22. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele DRB1*01:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 6. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele C*04:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 12 and 26. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele DQB1*06:02 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 26. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele DQB1*05:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 26. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*24:02 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 32, 43, 53, and 54. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*01:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 32, 33, 43, 54, and 57. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*11:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 32, 33, 34, 36, 40, 41, 43, 44, 45, 46, 47, 48, 49, 57, 61, 64, 66, 67, and 68. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*30:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 34, 37, 41, 44, 45, 60, 61, and 64. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*31:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 34, 35, 41, 45, 57, 61, 62, and 63. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*68:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 34, 35, 36, 40, 41, 44, 45, 46, 47, 48, 49, 50, 51, 57, 61, 62, 63, 66, 67, and 68. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*68:02 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 36, 40, 41, 42, 46, 47, 50, 51, 55, and 56. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele B*15:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 32, 33, 42, 43, 53, and 57. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele B*57:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 37, 41, 42, 44, 45, 58, 62, and 64. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele B*58:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 41, 42, 44, 45, 58, and 62. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*02:03 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 36, 40, 41, 46, 47, 55, 56, 59, 65, 66, 67, and 68. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*02:06 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 36, 41, 42, 46, 47, 52, 55, 56, 65, 66, 67, and 68. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*33:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 35, 45, 50, 51, 52, 62, and 63. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele B*15:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 32, 33, 42, 43, and 57. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*32:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 42 and 58. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*26:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 42. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*23:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 42 and 58. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele B*08:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 60, 61, and 66. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele B*44:02 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 64. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele B*40:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 53. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele A*30:02 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 34. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele C*07:02 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 32, 43 and 53. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele DQA1*01:01-DQB1*05:01 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 26. In a preferred embodiment, a subject or group of subjects carrying at least the HLA allele DQA1*01:01-DQB1*06:02 is treated with a pharmaceutical composition comprising a pharmacologically effective amount comprising from 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP) comprising HTAPP(s) selected from SEQ-ID-Nos.: 26. In some preferred embodiments of the pharmaceutical composition according to the current invention, the HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes correspond to an amino acid sequence of a transcribed mutant gene exclusive and / or associated with a carcinoma with at least one amino acid substitution compared to the native gene, wherein said gene is preferably selected from the list consisting of ABCA2, ABLIM1, ADAM8, ADAM8-NUP50, AFP, AFF2, ASIP, BRAF, CACNA2D1, CAMK1, CAN13, CCL28, CD33, CEACAM5, CEMIP2, COL10A1, CST1, CTBP2, D2HGDH, DENND4, DHRS2, DIP2A, DIP2C, DLX, DLX1, DLX1-FOLH1, EGFR, ELL3, ESR1, EXT2, EXT2-CACNA2D1, FA83A, FBXO2, FBXW7, FOLH1, GNAS, GRB14, GRIPAP1, HIVEP2, KDM3A, KIAA1804, KIT, KLK3, KRAS, LAMC1, LRRC8A, LRRC9, LUZP2, MAGEC1, MAP3K9, MMP1, MMP11, MTOR, NASP, NGAL, OPA1, PCDHGA11, PCSK1, PCM1, PLEC, PLD3, PLK1, PPFIA1-SHANK2, PRKAG1, PRR21, POTEG, POTEH, PTEN, PYGO2, RBBP6, RGS12, RIF1, RPAP1, S10A7, S10A8, S100A7, SALL3, SAMD9L, SEMA4D, SEMA4D- SEMAD4D, SEHL2, SHANK2, SHS, SLC30A8, SMG8, SMC4, STIM1, STK11IP, STK40, STON2, STS, TDRD1, TMEFF2, TMPRSS2-ERG, TNC, TP53, TP53BP2, TRANK1, TRAP1, U2AF1, UHRF1, ZC3H12A, ZC3H12C and ZDHHC18, particularly preferably selected from the list consisting of ABLIM1, ADAM8-NUP50, BRAF, CEACAM5, CEMIP2, COL10A1, CST1, DLX1-FOLH1, EGFR, EXT2-CACNA2D1, FBXW7, GNAS, KLK3, KDM3A, KRAS, LUZP2, MMP1, MMP11, PIK3CA, PLD3, POTEG, POTEH, SEMA4D-SEMAD4D, SMC4, TMEFF2, TMPRSS2-ERG, TP53, TNC-LAMC1 and U2AF1. These genes or combinations of these genes in the form of chimeras or fusion genes have been associated with cancer, preferably prostate, breast, pancreatic, liver, and bone cancers and their associated metastases. The use of chimeric or fusion genes is particularly preferred, especially when separated by a linker, preferably AAY or AYY or another easily cleavable sequence, since stand fragments are immunogenic and correspond to MHC complexes. In a preferred embodiment, the pharmaceutical composition for the treatment or prophylaxis of cancer in a subject or a group of subjects the administering the pharmacologically effective amount of the tumor antigen peptides to the subject or group of subjects suffering from carcinoma is effective to reduce a tumor marker level, preferably the tumor marker is selected from the list consisting of CEA, PSA, CA 125, CA 19-9, AFP, hCG, HER2 / neu, BRCA1, BRCA2, EGFR, CA 15- 3, CA 27.29. It is particularly preferred that the tumor marker targeted by this composition is selected from a list that includes CEA, PSA, CA 125, CA 19-9, AFP, hCG, HER2 / neu, BRCA1, BRCA2, EGFR, CA 15-3, and CA 27.29. Each of these tumor markers is indicative of specific types of carcinomas: CEA (Carcinoembryonic Antigen) is often associated with colorectal cancer, but it can also be elevated in other cancers such as pancreatic, stomach, breast, and lung cancer. In a preferred embodiment, the composition targets CEA to treat colorectal cancer. PSA (Prostate-Specific Antigen) is a marker for prostate cancer. Preferred is a composition that specifically targets PSA for the treatment of prostate cancer. CA 125 is primarily associated with ovarian cancer. Particularly preferred is a composition that targets CA 125 for ovarian cancer treatment. CA 19-9 is commonly linked with pancreatic and liver cancer. In a preferred embodiment, the composition is formulated to reduce CA 19-9 levels, offering potential therapeutic effects for pancreatic or liver cancer patients. AFP (Alpha-fetoprotein) is a marker for liver cancer and certain types of testicular cancers. Preferred is a composition that targets AFP for these cancer types. hCG (Human Chorionic Gonadotropin) can be indicative of germ cell tumors. In a preferred embodiment, the composition targets hCG for the treatment of germ cell tumors. HER2 / neu is associated with aggressive forms of breast cancer. Particularly preferred is a composition that targets HER2 / neu for breast cancer treatment. BRCA1 and BRCA2 are genes associated with a higher risk of breast and ovarian cancer. In a preferred embodiment, the composition is formulated to target mutations in these genes, offering potential therapeutic effects for patients with these genetic predispositions. EGFR (Epidermal Growth Factor Receptor) is linked with lung, colorectal, and pancreatic cancers. Preferred is a composition that specifically targets EGFR for the treatment of these cancer types. CA 15-3 and CA 27.29 are both markers for breast cancer. In a preferred embodiment, the composition targets either CA 15-3 or CA 27.29 for the treatment of breast cancer. The technical advantage of this composition lies in its ability to target a broad spectrum of tumor markers, offering a versatile approach to cancer treatment. Alternatively, the composition can be formulated to specifically target one or a subset of these tumor markers, allowing for specialized treatment options based on the specific cancer type. The units of the tumor marker levels can be determined using standard oncological diagnostic methods, ensuring accurate monitoring of treatment efficacy. In another preferred embodiment of the pharmaceutical composition the HLA tumor antigen polypeptides corresponding to HLA tumor antigen peptides corresponding to MHC class I and class II complexes, respectively, are immunogenic HLA tumor antigen polypeptides as determined by an immunogenicity assay, in particular by Western blot, ELISA techniques, ELISPOT or immunodetection with microscopic analysis; preferably by at least a factor of 2, even more preferably by at least a factor of 3 of the response of a corresponding blind test. This ensures the immunogenic effect of the HTAPPs in accordance with the current invention. Preferably, the HLA tumor antigen peptides of the composition of the invention are presented on the surface of the tumor cells of the carcinoma of at least one subject, preferably a group of subjects, as determined by ultra-high performance liquid chromatography (UHPCL) in combination with ESI mass spectrometry (MS). These methods allow rapid identification of the appropriate MHC class I and II complexes corresponding to HTAPs on HTAPPs. The immune response is directly related to the number of MHC complexes presented on the cell surface, which are recognized by T cells that can then induce apoptosis of the targeted tumor cell. In an especially preferred embodiment of the pharmaceutical composition according to the current invention for use therapeutic agent or prophylactic agent against a tumor in a subject or group of subject suffering or at risk from suffering from cancer, at least one HLA tumor antigen polypeptide is selected to match at least one, more preferably at least two, most preferably at least 5 HLA tumor antigen peptides that are presented on the surface of the tumor cells of the subject’s or group of subjects’ carcinoma as determined by ultra-high performance liquid chromatography (UHPCL) in conjunction with ESI mass spectrometry (MS). By targeting several different MHC class I and II complexes, a composition can be created that is robust and tolerates slight changes in genes of the same cancer type in different patients or different HLA alleles if at least one HLA allele and one gene mutation are the same with respect to the cancer type. Preferably the expression level of at least one HLA tumor antigen peptide in the tumor cells is at least three times higher than in the healthy cells of the subject or group of subjects having at least one identical HLA allele as determined by qPCR, and whereas the HLA tumor antigen peptides are associated with proliferation, invasiveness, angiogenesis, and an increase in cytokeratin production in carcinoma. This ensures a specific targeting of the tumor cell and reduces the possibility of an autoimmune response. In an especially preferred embodiment of the invention, the pharmaceutical composition comprises: - at least one HLA tumor antigen peptide is a tumor exclusive HLA tumor antigen peptide, and - specific binding of the tumor-exclusive HLA tumor antigen peptide determined against the corresponding MHC class I complex with a KD in the range of 10 to 50 nM occurs as determined by surface plasmon resonance. In a preferred embodiment of the invention, the pharmaceutical composition comprises an the pharmacologically effective amount of each individual HLA tumor antigen polypeptide in the composition in an absolute concentration (i.e., administration dose) ranges from 100 to 1000 µg. In a more preferred embodiment, the individual dose is 300 µg per antigen polypeptide. In a particularly preferred embodiment, the total dose of all HLA tumor antigen polypeptides in the composition of the invention is between 600 to 10000 µg, more preferably between 1000 and 6000 µg. This ensures that a strong immunogenic response is generated while the side effects of the application are minimized. In some embodiments of the pharmaceutical composition according to the current invention, the composition comprises an adjuvant which, when the composition is applied to a subject, is capable of forming a granuloma at the site of application. This allows to store the HLA tumor antigen polypeptides at the site of the application an releases them into the organism of a subject over an extended period of time, preferably between 1 and 14 days. In a particularly preferred embodiment, the use of Montanide ISA 51 VG has proven to be suitable. After application of the (drug-) formulation to the test person, this forms a so-called granuloma which advantageously stores the HLA tumor antigen peptides in the form of a reservoir at the site of application and releases them into the organism of the test person over a longer period of time. Particularly advantageously, therefore, weekly applications of the (drug-) formulation according to the invention are omitted. Preferably, the application of the (drug-) formulation for the treatment of cancer diseases in the sense of the invention, when used over a longer period of time, therefore only has -to be -carried out every 2 weeks, particularly preferably only once a month. It has been found that the application of the pharmaceutical composition according to the present invention for the treatment or prophylaxis of carcinoma subcutaneously or intradermally and, preferably substantially simultaneously at t least 2 sites of application, preferably at least 4 sites of application, remote from a tumor lesion and / or the cancerous lymph node area is advantageous. This ensures a controlled release of the HLA tumor antigen polypeptides in a controlled manner. In some preferred embodiments of the pharmaceutical composition at least one HLA tumor antigen peptide has at least one mutation relative to the wild-type HLA tumor antigen peptide (the mutanoma) that results in an increase in affinity for the T cell receptor of the individual treated with HLA tumor antigen peptide compared to the wild-type HLA tumor antigen peptide. This enhances the affinity for MHC class I and class II complexes significantly, thus ensuring a more robust immune answer. Preferred examples of this amino acid exchange can be found in the tables 1,2 and 4 to 6. Particularly preferably, the HLA tumor antigen peptide with a mutation is arranged on an HLA tumor antigen polypeptide. The pharmaceutical composition according to the present invention is suitable for the treatment or prophylaxis of almost all types of cancer, provided that at least two HLA antigen peptides can be matched with at least one, preferably two, HLA alleles and genes associated with cancer cells and presented on their epitope. Therefore, in some preferred embodiments the pharmaceutical composition is used for the treatment of carcinoma as monotherapy or in combination with other known therapies and / or compounds for the treatment of carcinoma, preferably is selected from the list consisting of breast cancer, lung cancer, prostate cancer, colon cancer, stomach cancer, liver cancer, cervical cancer, bladder cancer, non-Hodgkin's lymphoma, skin cancer, thyroid cancer, kidney cancer, ovarian cancer, pancreatic cancer, and esophageal cancer. In some preferred embodiments of the invention, the subjects to be treated with the pharmaceutical composition have received a standard therapy procedure (e.g., at least one of surgery, radiation, chemotherapy, and / or hormone therapy). A common problem in cancer is relapse and the inability to remove the entire cancer. Pharmaceutical composition is a mild and specific therapy and can therefore complement existing invasive or drug-based therapies, especially in metastatic cancers. In some preferred embodiments the pharmaceutical composition is administered as a first-line therapy to the subject or group of subjects having at least one identical HLA allele. This allows a more cost effective and broader application of the immune therapy. In another preferred embodiment the pharmaceutical composition according to the present invention for the treatment or prophylaxis of carcinoma is administered to a group of subjects having at least one, preferably two, more preferably three, most preferably five identical allele and at least one HLA tumor antigen polypeptide(s) presented on the cell membrane of the associated tumor cell corresponding to an amino acid sequence of a tumor antigen polypeptide as disclosed herein. The group therapeutic approach allows broader access to this novel and inventive approach, which is hampered by the cost of determining and synthesizing an individualized therapy. By identifying common HLA alleles associated with specific cancers, a composition according to the present invention can be applied to a larger group of subjects. The shared allele is preferably selected from the list comprising of A*01:01, A*02:01, A*02:03, A*02:06, are represented by the preferred sequences disclosed in tables 1,2 and 4 to 6. In a preferred embodiment related to the administration of the composition to a group of subjects sharing at least one common HLA allele, the pharmaceutical composition comprising each individual HLA tumor antigen peptide, more preferably each HLA tumor antigen polypeptide in the pharmaceutical composition at an absolute concentration (i.e., administration dose) of 100 to 1000 µg is administered intradermally or subcutaneously once every 2 weeks for a period of at least one year to a subject or group of subjects having at least one identical HLA allele. This provides an effective treatment suitable for broad-spectrum use. It has been an outstanding achievement of the inventors to have found a way to increase the efficacy of HLA antigen- based immunotherapeutic agents by including tandem and overlapping tandem polypeptides that exhibit a dramatically enhanced immunogenic response. Therefore, although it is advantageous to use a composition of HLA tumor antigen polypeptides for the reasons disclosed herein, in some preferred embodiments, a single HLA tumor antigen polypeptide may be used as an agent for the treatment of carcinoma or for a pharmaceutical composition according to the present invention. In a preferred embodiment of the current invention, an HLA tumor antigen polypeptide corresponding to HLA tumor antigen polypeptides corresponding to MHC class I complexes or MHC class II complexes is used for the treatment of carcinomas or for a pharmaceutical composition according to the current invention, in particular for use in the and / or particulary as a medicament for therapeutic and / or prophylactic treatment of a carcinoma, particularly preferably a locally recurrent or metastatic carcinoma, in particular in a subject or group of subjects suffering from or at risk of suffering from a carcinoma, comprising at least two tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) (HTAPP), wherein the HLA tumor antigen peptides (HTAP) are tumor-exclusive or tumor-associated and presented on the cell membrane of the associated tumor cell and correspond to an amino acid sequence of a transcribed mutant gene, wherein the HLA tumor antigen polypeptide comprises a scaffold amino acid sequence, preferably between 15 and 45, more preferably between 17 and 40 amino acids, a) wherein the scaffold amino acid sequence comprises, in addition to HLA tumor antigen peptide(s), up to 1 to 30 amino acids (long HLA tumor antigen polypeptide); and / or b) wherein the scaffold amino acid sequence comprises an HLA tumor antigen peptide(s) with at least 90% sequence identity similarity to the native HLA tumor antigen peptide (similarity HLA tumor antigen polypeptide); and / or c) wherein at least one of the amino acid sequences comprises an HLA tumor antigen peptide having an amino acid sequence comprising or consisting essentially of only one amino acid substitution relative to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide), wherein an HLA tumor antigen polypeptide is a tandem polypeptide comprising or consisting of at least 2 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes; and / or an HLA tumor antigen polypeptide is an overlapping tandem polypeptide comprising or consisting of at least 2 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes which overlap in their amino acid sequence, wherein the HLA tumor antigen polypeptide is preferably selected from the group consisting of the amino acid sequences set forth in SEQ-ID-Nos.: 1 to 17, 69 and 76. These represent immunogenic sequences, as determined by Elispot and case studies, therefore demonstrating the effectiveness of the HTAPPs as disclosed herein. The use of single HTAPPs is associated with lesser cost and easier manufacturing, therefore allowing a simpler access to this new therapeutic approach. In an especially preferred embodiment the HLA tumor antigen polypeptide comprises a delivery aiding capping peptide (DACP) and is preferably selected from the group consisting of the amino acid sequences set forth in in SEQ-ID-Nos.: 18 to 37, 40 to 68, 70, 71, 81 and 84, more preferably 18 to 31, 32 to 36, 40, 43 to 44, 47 to 54, 57 to 64, 67 to 68, 70, 71, 81 and 84. Preferably the HLA tumor antigen polypeptide is used in the treatment of carcinomas, particularly locally recurrent or metastatic carcinomas in an individual, the method comprising administering to the individual a treatment regimen comprising a pharmacologically effective amount of the HLA tumor antigen polypeptide, wherein the pharmacologically effective amount is preferably an absolute concentration (i.e., administration dose) of 100 to 1000 µg. Preferably the HTAPP is used when the individual has not yet received radiation, chemotherapy, and / or hormone therapy for the cancer, particularly locally recurrent or metastatic cancer, and / or has not received prior adjuvant chemotherapy in recurrence for 12 months or less since the last dose of a chemotherapeutic agent. Advantageously, the HTAPP can be used when the treatment regimen is effective to prolong progression-free survival of the individual by at least 2 to 5 years. This allows for prophylaxis of recurrence and minimizes the risk of autoimmune response, as the HTAPP can be tailored to known metastatic or recurrent cancers, while treating a later stage cancer does require a stronger immune response which is typically associated with a composition in accordance with the current invention. The HLA tumor antigen peptides are preferably immunogenic in the subject or group of subjects, as determined by means of an immunogenicity assay, in particular by Western blot, ELISA techniques, in particular by ELISPOT, AFM or immunodetection with microscopic analysis. This ensures that HTAPPs are effective when used as a single therapeutic agent. The scope of the invention naturally also includes a method of determining a pharmaceutical composition preferably comprising or consisting of HLA tumor antigen polypeptides according to the current invention, comprising monitoring tissue resection of a subject or group of subjects suffering from or suspected of suffering from carcinoma, the method comprising the steps of: a) providing a tumor tissue sample (sample tissue) and a healthy cell sample of the subject or group of subjects, wherein said method step (a) of providing the tissue sample does not itself comprise any surgical intervention in the subject or one of the subjects of the group of subjects, then b) sequencing the sample tissue and determine the following parameters using the provided tissue sample from step (a), providing a transcriptome, then c) creating a pre-selection of HLA tumor antigen peptides matching the MHC class I and class II complexes from the mRNA transcriptome of step b) using bioinformatics methods, weighting up- and / or down-regulated mRNA, HLA subtypes of the subject or subject group, association with proliferation, invasiveness, angiogenesis and an increase in cytokeratin production, exome sequence as well as presentation on the associated tumor cells using algorithms, databases and neural networks, then d) creating an HLA tumor antigen polypeptide composition with a bioinformatic feedback loop pipeline, then e) testing the immunogenicity of the HLA tumor antigen polypeptides determined in step d) by means of an immunogenicity test, in particular by Western blot, ELISA techniques, in particular by ELISPOT, AFM or immunodetection with microscopic analysis, wherein the bioinformatic feedback loop pipeline comprises the at least the steps of i) weighting the sequences of the HLA tumor antigen peptides with neural networks and weighting algorithms, comprising at least the weighting factors selected from the list comprising MHC class I and II binding affinity scores; presentation score on tumor cell line; overexpression score, preferably at least factor 3 in relation to healthy cells; proliferation, invasiveness, angiogenesis and an increase in cytokeratin production scores; distribution factor in a group of subjects suffering from the same tumor type, more preferably the same tumor cell line; point mutation score, sequence identity score, robustness score, exome portion score, then ii) matching at least two, preferably three, more preferably four, most preferably 5–10 HLA tumor antigen peptides selected in step i) in the amino acid sequence of an HLA tumor antigen polypeptide using weighting algorithms and / or neural networks, thus creating at least one, more preferably at least three, most preferably 5-10 HLA tumor antigen polypeptide(s), then iii) assembling a pharmaceutical composition comprising at least two HLA tumor antigen polypeptides generated in step ii), wherein the composition comprising at least two HLA tumor antigen polypeptides is fed back to step i) to generate a feedback loop, in particular a feedback loop relating to a group of subjects, validating the sequence score, preferably checking for a high overexpression score at least once, preferably further training the neural network. In a preferred embodiment related to step a), the method begins with the provision of a tumor tissue sample, also referred to as the "sample tissue", and a healthy cell sample from the subject or group of subjects. The tumor tissue sample is typically obtained from a subject diagnosed with or suspected of having carcinoma. This sample provides a source of tumor-specific genetic material, which can be compared to the genetic material from healthy cells to identify mutations or other genetic changes associated with the tumor. In addition, the healthy cell sample serves as a control or reference sample. Preferably, this sample is obtained from the same subject or group of subjects from whom the tumor tissue sample was obtained. The healthy cell sample provides a basic genetic profile of the subject that allows identification of tumor-specific genetic alterations. Particularly preferably, the healthy cell sample is a blood sample. In the context of the present invention, the step a) involves obtaining a healthy cell sample, which serves as a foundational reference to discern genetic changes that are specific to the tumor. This healthy cell sample can be derived from various tissue types, each offering unique advantages based on the requirements of the study and the accessibility of the tissue. One preferred source is the peripheral blood mononuclear cells (PBMCs), which are blood cells with a round nucleus, such as lymphocytes and monocytes. PBMCs are readily available and can be isolated from blood samples using standard techniques such as density gradient centrifugation. Their use is particularly advantageous because they can represent the immune status of an individual, as they comprise a diverse mixture of cell types. In another embodiment, skin cells obtained from a skin biopsy or swab that provide a sample of epithelial cells may also be a potential source of the healthy cell sample. Further preferred are cheek cells obtained by a simple swab from the inside of the cheek, which advantageously are another non-invasive source of DNA. In certain preferred cases, more invasive sources such as bone marrow may also be considered, as it is rich in stem cells and other cell types. Furthermore, according to the invention, the use of body fluids such as urine or saliva, which contain excreted cells, can also be used as a DNA source. In some preferred embodiments, the transcriptome of the tumor cells is extracted from sample tissue extracted from a subject in a biopsy, preferably a sample which is Formalin-Fixed, Paraffin-Embedded (FFPE) Tissue, Liquid Biopsy, Cryopreserved Tissue, RNAlater Stabilized Tissue, Fine Needle Aspiration (FNA) Biopsy, Cell Blocks, Flash Freezing in Liquid Nitrogen, Touch Preps / Imprints, Microdissection, Vitreous or Glycerol Preservation. Advantageously FFPE allows long-term preservation and histological examination; liquid biopsy provides a minimally invasive option for detection of tumor DNA or cells in fluids; cryopreserved and RNAlater-stabilized tissues ensure cellular integrity for RNA analysis; FNA biopsy allows less invasive tissue collection; Cell blocks facilitate histological examination of fluid-based specimens; rapid freezing preserves molecular profiles; touch-preps / imprints enable rapid cytological analysis; microdissection enables targeted cell or tissue isolation; vitreous or glycerol preservation methods maintain enzymatic and structural integrity for specialized analyses. These alternatives to fresh-frozen tissue samples are designed to meet the various analytical needs and constraints of clinical and research settings. In the context of the present invention and the context of the method of identifying pharmaceutical compositions comprising HLA tumor antigen polypeptides (HTAPP), a comprehensive understanding of the HLA ligandome is essential. By comparing the HLA ligandome of tumor cells with that of healthy cells, such as PBMCs, tumor-specific antigens can be determined against which the immune system can act. PBMCs are particularly important for determining the HLA ligandome. Not only do they provide a snapshot of a person's immune status, but they also serve as a reservoir of HLA molecules. Analysis of the peptides presented by these molecules can reveal a person's HLA ligandome. Comparison between the HLA ligandome of PBMCs or other healthy cell samples and that of tumor cells facilitates the identification of peptides that are presented only in tumor cells and thus represent potential targets for immunotherapy. Preferably, the sample of healthy cells, whether from PBMCs or other tissue types, can be used to identify tumor-specific antigens. Providing a reference HLA ligandome ensures that the identified antigens are truly tumor-specific, eliminating the possibility that they are merely natural variations or peptides commonly found in healthy cells. This distinction is beneficial for the technical functionality of the method and a derived pharmaceutical composition, especially when adapted for use as a group-adaptable cancer immunotherapy. In a preferred embodiment, both DNA and RNA are carefully extracted from biopsy tissue samples, preferably from preserved tissue samples that have been evaluated by a qualified pathologist. The standard method for nucleic acid isolation may be Qiagen's AllPrep DNA / RNA Mini Kit or a comparable system. In another embodiment, DNA from Healthy Body Cells may be isolated from EDTA-treated blood samples using Qiagen's QIA Symphony DSP DNA Mini Kit 96, which provides a baseline of normal tissue for comparative analysis. For whole-exome sequencing (WES), the Twist Human Core Exome Kit with RefSeq and Mitochondrial Panel from Twist Bioscience or a comparable system can be used for library preparation. At the same time, the KAPA RNA HyperPrep Kit with RiboErase Globin from Roche or a comparable system can be used for RNA sequencing library preparation (RNA- seq). Both DNA and RNA libraries undergo rigorous quality control, including fluorescence-based quantification and fragment length analysis. Sequencing can then be performed on the NovaSeq 6000 system using 2x100 base pair paired-end reads or a comparable system. Alternatively, DNA and RNA isolation from biopsy samples can be performed using comparable extraction kits that provide equivalent purity and yield, such as the MagMAX DNA / RNA Kits or PureLink Genomic DNA / RNA Kits. Similarly, alternative methods such as magnetic bead-based purification can be used. For library preparation at WES and RNA- seq, kits can be used that provide similar coverage and specificity, such as the NEBNext Ultra II or Agilent SureSelect kits. Quality control can also be performed using alternative methods such as capillary electrophoresis or spectrophotometry. For sequencing, platforms equivalent to the NovaSeq 6000 can be considered, such as the Illumina HiSeq or Ion Torrent systems, which offer similar read lengths and throughput. These alternatives provide flexibility in the molecular profiling process and allow adaptation to different laboratory environments and available resources while maintaining the integrity of the pharmaceutical compositions obtained from the tissue samples. It is particularly preferred that the method of providing these tissue samples does not involve any surgical intervention in the subject or any subject within the group. This means that the samples are preferably obtained through non-invasive or minimally invasive methods. For example, the tumor tissue sample could be obtained through a biopsy using a fine needle, while the healthy cell sample could be obtained from a blood sample or cheek swab. The technical advantage of using both a tumor tissue sample and a healthy cell sample is that it allows for a more accurate comparison of genetic material, ensuring that any identified mutations or genetic changes are truly associated with the tumor and not just natural variations in the subject's DNA. Additionally, by avoiding surgical intervention, the method minimizes the risk and discomfort to the subject. As an alternative embodiment, the tumor tissue sample and the healthy cell sample could be obtained from different subjects within the same group, provided that they share similar genetic backgrounds or other relevant characteristics. This could be useful in situations where it is not possible or practical to obtain both samples from the same subject. For the units of measurement used in step a), the amount of tissue or cells required would depend on the sequencing technology and methods used. Sequencing methods in accordance with the current invention require only 10 nanograms to 100 micrograms of DNA. In summary, step a) of the present method is critical to ensure that subsequent steps of the method of the invention for determining a pharmaceutical composition are based on accurate and relevant genetic information. By comparing the genetic material from the tumor tissue sample with that from the healthy cell sample, the method can identify tumor- specific genetic alterations that are then used to determine potential HLA tumor antigen polypeptides. In a preferred embodiment, the method includes sequencing the tissue sample obtained in step (a). This sequencing can be performed using any appropriate sequencing technology, e.g., next generation sequencing (NGS) methods, preferably including, but not limited to, Illumina sequencing, ion torrent sequencing, or nanopore sequencing. The goal of the sequencing step is to generate a comprehensive data set of the nucleotide sequences present in the sample tissue. Included in this step are sequencing methods, preferably whole genome sequencing (WGS), whole exome sequencing (WES), RNA sequencing (RNA-Seq), targeted sequencing, single cell sequencing, long-read sequencing, chromatin immunoprecipitation sequencing (ChIP-Seq), and methylome sequencing. As part of this method, the transcriptome data of step b) can be further analyzed to identify potential HLA tumor antigen peptides, as described herein. In one embodiment of the invention related to step b), Whole Genome Sequencing (WGS) is employed, offering a comprehensive view of the entire genome. The technical effect of this method is its ability to detect all genetic variations, although it can be time-consuming. This can be measured using platforms like Illumina's HiSeq or NovaSeq systems, which provide high-throughput sequencing capabilities. Another embodiment utilizes Whole Exome Sequencing (WES), targeting only the coding regions of genes. Its technical effect lies in its cost-effectiveness and efficiency, focusing solely on regions where disease-causing mutations are most likely to occur. Platforms such as the Agilent SureSelect or NimbleGen SeqCap can be used for exome capture, followed by sequencing on Illumina platforms. In another embodiment, RNA sequencing (RNA-Seq) is used to understand the active gene expression profile of a sample. This has the advantage of identifying differentially expressed genes that are critical to understanding tumor behavior and immune response. This can be measured using the Illumina TruSeq RNA Library Prep Kit, followed by sequencing on an Illumina platform. Another variant is targeted sequencing, which focuses on specific genes or regions of interest. This provides the technical effect of precision, ensuring detailed analysis of known cancer- or immune-related genes. This can be achieved by using custom panels on platforms such as Illumina's MiSeq or NextSeq. In the context of step b), single cell sequencing is another option that offers insights into cellular heterogeneity. The technical effect in the context of this invention is the ability to detect genetic differences at the single cell level, which is critical for understanding tumor diversity and resistance mechanisms. Platforms such as 10x Genomics' Chromium system can be used for single cell isolation and library preparation, followed by sequencing on Illumina platforms. In a particular embodiment of step b), long-read sequencing is used, whereby longer DNA fragments are captured to provide a more comprehensive genetic overview. The technical effect associated with this method for determining a pharmaceutical composition is the resolution of complex genomic regions and detection of structural variants. This can be measured using the Pacific Biosciences Sequel System or Oxford Nanopore Technologies' MinION. Another embodiment of step b) involves Chromatin Immunoprecipitation Sequencing (ChIP-Seq) to study protein-DNA interactions. Its technical effect is the identification of DNA regions interacting with specific proteins, providing insights into gene regulation in cancer. This can be set up using kits like the MAGnify Chromatin Immunoprecipitation System, followed by sequencing on platforms like Illumina's HiSeq. Finally, one embodiment of methylome sequencing focuses on DNA methylation patterns. The technical effect is to understand epigenetic changes that play a critical role in gene regulation and carcinogenesis. This can be measured using bisulfite conversion kits such as the Zymo EZ DNA Methylation Kit, followed by sequencing on Illumina platforms. After obtaining the sequence data, the method further comprises determining specific parameters from the provided tissue sample. Particularly preferred is the generation of a transcriptome representing the totality of all RNA molecules, including mRNA, rRNA, tRNA and other non-coding RNA produced in a cell or cell population. The transcriptome provides information about the genes that are actively expressed at a given time. Weighting factors, comprised the invention may comprise input parameters, output parameters, calculated values or database knowledge. The weighting factors comprise bioinformatical information and biochemical information about the peptide sequences and may preferably be weighted automatically by a weighting algorithm and / or machine learning algorithm. In some preferred embodiments, the weighting factors are selected from the list comprising or consisting of corresponding HLA alleles (of the amino acid sequence), MHC class I and II binding affinity scores (predicted and / or determined binding affinity of the peptide to MHC molecules); immunogenicity score (predicted or extracted from a database), presentation score on tumor cell line (determined for a patient or a group of patients); presentation percentile; overexpression score, preferably at least factor 3 in relation to healthy cells; processing score (probability of amino acid sequence being processed into a MHC class I and / or class II complex), tumor associated scores, for example proliferation, invasiveness, angiogenesis and an increase in cytokeratin production scores; distribution factor in a group of subjects suffering from the same tumor type, more preferably the same tumor cell line; point mutation score, sequence identity score, robustness score, exome portion score, biochemical scores including but not limited to pI (isoelectric point of the peptide, indicating the pH at which the peptide carries no net electrical charge), GRAVY (grand Average of Hydropathicity, which indicates the hydrophobic or hydrophilic nature of the peptide), length of the amino acid sequence (in amino acids), charge (under physiological conditions), molecular weight (of the amino acid sequence), instability (the instability index of the peptide). The percentiles of the individual scores might be also used in addition or instead of the score to further increase or decrease the weight of individual scores. Preferably, at least 4 different biochemical scores and at least 7, more preferably 10 other weighting scores are utilized in a method according to the invention. This enables much more accurate in silico prediction of in vivo behavior, in particular the use of biochemical properties in conjunction with affinity and presentation, processing scores allows multidimensional scoring and ranking of individual amino acid sequences combined into HTAPPs and HTAPP-DACPs. In an especially preferred embodiments, the weighting factors used for weighting comprise or consist of at least MHC class I and II binding affinity scores; immunogenicity score, presentation score on tumor cell line; presentation percentile; overexpression score of at least factor 3 in relation to healthy cells; processing score, distribution factor in a group of subjects suffering from the same tumor type; point mutation score; sequence identity score; robustness score; exome portion score; and biochemical scores, wherein biochemical scores comprise or consist of pI, GRAVY, length of the amino acid sequence, charge, molecular weight, and instability. These weighting factors, especially in combination, allow a more realistic and effective simulation of a composition that archives a strong and substantial immunogenic response in vivo. In a particularly preferred embodiment of the present invention, cancer hallmarks as described in Fig.11 are utilized as an additional criterion during the peptide selection process. In this process, the ten distinct cancer hallmarks (HS-1 to HS-10), which are linked to Gene Ontology (GO) pathways, are aligned with the genes and mutations associated with specific cancers. The selection score for each peptide is determined by the cumulative count of associated cancer hallmarks. According to this embodiment, only those HLA tumor antigen peptides that correspond to at least one, and more preferably to a range of two to ten, cancer hallmarks are selected for the composition of a pharmaceutical composition according to the current invention. Output parameters may include model prediction score and model probability score, which in turn may be used to validate the weighting algorithm and be used as input for a subsequent weighting algorithm and / or machine learning algorithm. The technical advantage of creating a transcriptome is that it allows identification of genes that are up- or down- regulated in tumor cells compared to healthy cells. This differential gene expression can provide insight into the molecular mechanisms that control tumor growth and progression. In particular, in a preferred embodiment, genes that are overexpressed by at least a factor of two, preferably a factor of three, compared to healthy tissue are preferentially identified. Preferably, the method of the invention in step b) focuses primarily on the mRNA component of the transcriptome. mRNA or messenger RNA carries the genetic information copied from DNA in the form of a series of three-base code words, each of which specifies a particular amino acid. Another preferred embodiment provides for is the use of RNA-Seq, a method that employs NGS, to determine the presence and amount of RNA in a biological sample at a given time. RNA-Seq can be used to generate the transcriptome and can provide both quantitative and qualitative data about the transcriptome. To determine the units of the transcriptome, one can measure the number of reads or fragments associated with a particular gene or region of interest. This can provide information about the relative abundance of different transcripts in the sample. In a preferred embodiment related to step c), the method involves the generation of a pre-selection of HLA tumor antigen peptides corresponding to MHC class I and class II complexes. This pre-selection is derived from the mRNA transcriptome obtained in step b) and serves as a crucial step to narrow down potential candidates for further analysis and validation. The bioinformatics methods employed are essential for the accurate identification and selection of these relevant HLA tumor antigen peptides. By weighting the up- and / or down-regulated mRNA, the method can prioritize genes that are either overexpressed or repressed in tumor cells compared to their healthy counterparts. In addition, it is essential to consider the different HLA subtypes expressed by subjects. Different subjects may have different HLA subtypes. By taking these into account, the method ensures that the peptides selected are both relevant and specific to the subject or group of subjects being studied. Another important aspect is the association of the selected peptides with parameters indicative of cancer aggressiveness, such as proliferation, invasiveness, angiogenesis, and increased cytokeratin production. In a particularly preferred embodiment, the entire HLA ligandome of a subject or group of subjects is determined and taken into account. In a further preferred embodiment, at least 1 to 30, preferably 2 to 25, more preferably 3 to 20, most preferably 4 to 20 HLA alleles of the subject or group of subjects are taken into account. In some embodiments, the exome sequence that provides detailed information about the protein coding regions of the genome is also considered. This ensures that the selected peptides are derived from genes that are actively transcribed and translated in tumor cells. In addition, it is critical that these peptides are presented on the surface of tumor cells so that they are accessible and recognizable to the immune system. This represents a marked difference from many prior art methods, for recognition of HLA tumor antigen peptides attached to HLA tumor antigen polypeptides corresponding to MHC class I and II complexes the sequence must be presented on the cell surface to be effective. To achieve this comprehensive selection, the method preferentially employs a combination of advanced algorithms, databases, and neural networks. These tools are capable of processing large amounts of data and detecting patterns that might be missed by conventional methods. In particular, the use of neural networks provides a significant advantage by enabling the identification of complicated patterns and relationships in the data. One of the key technical advantages of this step is the ability to ensure that the peptides selected are highly relevant to both the tumor and the subject. By integrating multiple parameters and drawing from advanced algorithms, databases, and neural networks, the method maximizes the likelihood that the peptides will be effective targets for immune responses. Alternatively, the method could consider other parameters, such as metabolic activity, factors from the tumor microenvironment, or mechanisms of immune evasion. For quantification, techniques such as qRT-PCR can be used to determine mRNA levels, which provide a relative measure of gene expression. Genotyping methods can be used to determine HLA subtypes. In addition, assays such as MTT, wound healing, tube formation, and immunohistochemistry can be used to determine units related to proliferation, invasiveness, angiogenesis, and cytokeratin production. This process provides a more holistic understanding of the tumor and its characteristics, allowing the pharmaceutical composition to be more effective and customizable in accordance with the invention. In the context of the present invention, differential expression of genes in tumor tissue compared to healthy tissue provides valuable insights into tumor biology and potential therapeutic targets. Up-regulated genes, also referred to as overexpressed genes or overexpressed genes in the context of the present invention, are genes that exhibit increased expression in tumor tissue, while down-regulated genes are those that exhibit decreased expression. To accurately measure the fold change in gene expression and identify significantly up- or down-regulated genes, quantitative analysis of gene expression levels in tumor tissue compared to healthy tissue is performed. Techniques such as quantitative real- time PCR (qRT-PCR) or RNA sequencing (RNA-Seq) can be used for this purpose. One of the main technical advantages of identifying and targeting overexpressed tumor genes is the potential reduction of autoimmune responses. By targeting genes that are predominantly expressed in tumor cells rather than healthy cells, the immune system is less likely to attack healthy cells. This approach thus minimizes the risk of autoimmune reactions. Therefore, in some preferred embodiments, the method ensures selectivity by focusing on genes with significant overexpression factors. For example, genes whose expression levels are elevated in tumor tissue compared to healthy tissue are considered significantly upregulated, preferably by overexpression factor 2, more preferably by overexpression factor 3, and most preferably by overexpression factor 4. This selectivity ensures that the identified HLA tumor antigen peptides are more likely to be specific for tumor cells, leading to more targeted and effective therapeutic interventions, allowing for technical advantages such as lower risk of autoimmune reactions and higher therapeutic selectivity. In an alternative embodiment of the present invention, the method can be extended to include proteomic data. Analysis of the protein products of overexpressed genes can provide further insight into the functional consequences of gene upregulation. Techniques such as mass spectrometry can be used to identify and quantify proteins that are overexpressed in tumor cells. This approach provides a more comprehensive view of the tumor molecular landscape, potentially identifying additional therapeutic targets and increasing the robustness of the method. Preferably, the integration of quantitative gene expression data and proteomic data may improve the potential of the method to identify pharmaceutical compositions. According to a preferred embodiment of the method for determining pharmaceutically active HLA tumor antigen peptides, immediately after providing the tissue sample of the subject or subject group in step (a), the genes selected from the list comprising ABCA2, ABLIM1, ADAM8, AFP, AFF2, ASIP, BRAF, CACNA2D1, CAMK1, CAN13, CCL28, CD33, CEACAM5, CEMIP2, COL10A1, CST1, CTBP2, D2HGDH, DENND4, DHRS2, DIP2A, DIP2C, DLX, DLX1, DXL1, EGFR, ELL3, ESR1, EXT2, EXT2-CACNA2D1, FA83A, FBXO2, FOLH1, GNAS, GRB14, GRIPAP1, HIVEP2, KDM3A, KIAA1804, KIT, KLK3, KRAS, LAMC1, LRRC8A, LRRC9, LUZP2, MAGEC1, MAP3K9, MMP1, MMP11, MTOR, NASP, NGAL, OPA1, PCDHGA11, PCSK1, PCM1, PLEC, PLD3, PLK1, PPFIA1-SHANK2, PRKAG1, PRR21, PTEN, PYGO2, RBBP6, RGS12, RIF1, RPAP1, S10A7, S10A8, S100A7, SALL3, SAMD9L, SEMA4D, SEHL2, SHANK2, SHS, SLC30A8, SMG8, SMC4, STIM1, STK11IP, STK40, STON2, STS, TDRD1, TMEFF2, TNC, TP53, TP53BP2, TRANK1, TRAP1, U2AF1, UHRF1, ZC3H12A, ZC3H12C and ZDHHC18, particularly preferably selected from the list consisting of ABLIM1, ADAM8-NUP50, BRAF, CEACAM5, CEMIP2, COL10A1, CST1, DLX1-FOLH1, EGFR, EXT2-CACNA2D1, FBXW7, GNAS, KLK3, KDM3A, KRAS, LUZP2, MMP1, MMP11, PIK3CA, PLD3, POTEG, POTEH, SEMA4D- SEMAD4D, SMC4, TMEFF2, TMPRSS2-ERG, TP53, TNC-LAMC1 and U2AF1 are examined for the presence of mutations. Particularly preferably, determining whether the HLA tumor antigen peptides are presented on the surface of the cells of the tissue sample of the subject or group of subjects provided in step a) is performed by ultra-high performance liquid chromatography (UHPCL) in conjunction with ESI mass spectrometry (MS). Preferably, the transcriptome is generated by RT-PCR, followed by DNA microarray or DNA sequencing. Particularly preferably, the method for determining a class I and / or class II HLA tumor antigen peptide comprises generating an exome sequencing for said tissue sample. It is also desirable that the method for determining a pharmaceutically active class I and / or class II HLA tumor antigen peptide in comprises matching the determined amino acid sequences of the HLA tumor antigen peptides corresponding to the class I and / or class II MHC complexes with a set, collection, or library of amino acid sequences to rank in terms of protein quantity (i.e. factors associated with proliferation, invasiveness, angiogenesis and / or an increase in cytokeratin production of carcinoma) and specific affinity towards the T cell receptor of endogenous T cells (content factors for tumor progression, such as invasiveness, angiogenesis, but also escape mechanisms of the tumor towards immune attack). The method also comprises matching the determined parameters with amino acid sequences of the HLA tumor antigen peptides with a set, collection, or library of amino acid sequences of healthy expression data for amino acid sequences that can bind to or have affinity for MHC class I complexes or MHC class II complexes, including combinations thereof. In such a method, the series, collection, or library of amino acid sequences may be an appropriate series, collection, or library of amino acid sequences. For example, the series, collection, or library of amino acid sequences may be a series, collection, or library of class I and class II HLA tumor antigen peptides and / or MHC complexes (as described herein), such as a native series, collection, or library of class I and class II HLA tumor antigen peptides and / or MHC complexes; be a synthetic or semi-synthetic series, collection or library of class I and class II HLA tumor antigen peptides and / or MHC complexes and / or a series; be a collection or library of class I and class II HLA tumor antigen peptides and / or MHC complexes that have been subjected to affinity maturation. In a preferred embodiment, in order to specify the pharmaceutical efficacy of the HLA tumor antigen peptides determined by the derived ranking and to prevent or minimize the risk of an autoimmune response in the subject by the administration of the determined HLA tumor antigen peptides, an immunogenicity test is performed with the HLA tumor antigen peptides (pre-)determined by the determination method according to the invention, in particular by means of Western blot, ELISA and an immunogenicity test, in particular by means of Western blot, ELISA techniques, in particular by means of ELISPOT, AFM or immunodetection with microscopic analysis, is carried out with the -HLA tumor antigen peptides (pre-)determined by the determination method according to the invention. Advantageously, in this embodiment of the method for determining at least one pharmaceutically active HLA tumor antigen peptide, the time-consuming and costly generation of a transcriptome and exome sequencing for this tissue sample can be dispensed with. In a particularly preferred embodiment, the autoimmune response is individually calculated and weighted in the bioinformatics feedback loop pipeline by inferring the pharmaceutical composition determined with respect to the subject's ligandome and a reweighting process, the immunogenicity of a HTAPP peptide selected from the pharmaceutical composition determined by the method described herein. Thus, advantageously, in this embodiment of the method for determination, at least the time-consuming and costly generation of a transcriptome and exome sequencing for this tissue sample can be omitted. In a preferred embodiment of the method in accordance with the current invention, the tissue sample from the subject or group of subjects in step (a) is screened for commonly mutated genes exclusive for and / or associated with a carcinoma present in the group of subjects are analyzed for the presence of mutations. This has the advantage that the patient can be quickly categorized and pre-trained datasets and neural networks can be used for the patient's specific mutanomas or cancers. In this way, patients can be categorized into groups that can be treated with the same pool of HTAPPs or the same pharmaceutical composition that includes a set of HTAPPs optimized for that set of common mutations. In a particularly preferred embodiment of the invention relating to the method of determining pharmaceutical compositions, the tissue sample provided in step (a) is the tissue sample of a carcinoma from a group of subjects suffering from or at risk of suffering from the same type of carcinoma, preferably a recurrent or metastatic carcinoma. Particularly preferred is the treatment of previously "incurable" metastatic carcinomas that can be treated by a pharmaceutical composition, provided that the composition comprises at least one HTAPP comprising a HTAP corresponding to an HLA allele in the patient or group of patients that matches at least one mutation on a common gene between the metastatic carcinoma and the parent carcinoma. In a preferred embodiment, the determination of whether the HLA tumor antigen peptides are presented on the surface of the cells of the tissue sample of the subject or group of subjects provided in step (a) is performed by ultra-high performance liquid chromatography (UHPCL) in conjunction with ESI mass spectrometry (MS). This allows for efficient and quick identification of potential sites and may be utilized in quickly categorizing subjects in groups. In a particularly preferred embodiment of the method, the bioinformatics feedback loop pipeline comprises at least one neural network trained on a group of subjects sharing at least one common HLA allele and a similar, preferably the same, tumor type. Advantageously, pre-training increases the efficiency and specificity of MHC complex affinities, biochemical behavior, and correlated genes, thus enabling a group therapeutic approach for immunological cancer therapies. Moreover, the pre-selection of HLA tumor antigen peptides is constantly expanding with new patients, thus increasing the potential pool of HTAPPs according to the present invention. In some preferred embodiments related to the method of determination of a pharmaceutical composition in accordance with the current invention, the HLA tumor antigen polypeptides of the composition assembled in step iii) are individually tested for least for overexpression of a factor of at least three in an individual subject, preferably by application of step i) of the bioinformatic feedback loop pipeline. This allows, especially when pursuing a generalized group therapeutic HTAPP drug composition, that each individual is pre-tested for adverse reactions such as autoimmune reactions. This method can therefore combine a generalized approach to immunological cancer therapeutics and individualized therapeutics by using compositions that can be tailored to both an individual and a group. A further, in particular cost-reduced embodiment of the method according to the invention for determining at least one HLA tumor antigen peptide corresponding to the MHC complexes of class I and / or II for a pharmaceutical composition according to the invention provides that exclusively (i.e. without prior preparation of a transcriptome, exome sequencing) the HLA tumor antigen peptides of class I and / or II are determined, i.e. without prior preparation of a transcriptome, exome sequencing) the HLA tumor antigen peptides of class I and / or II are determined which are exposed on the cell surface of cells from malignant and / or neoplastic tissue of the individual to be treated (so-called determination of the ligandome). The procedure here consists of the following steps: a) Providing a tissue sample from a tissue resection of a subject who preferably has, or is suspected of having, locally recurrent / mammary carcinoma; and b) determining / selecting the HLA tumor antigen peptides exposed on the cell surface of the cells of the sampled tissue according to the determination of the parameters based on the provided tissue sample from step (a) according to step (b) of the aforementioned method for determining pharmaceutically active HLA tumor antigen peptides (as defined above); and c) Determine the affinity of the HLA tumor antigen peptides exposed on the cell surface of the cells of the harvested tissue toward the T cell receptor of the endogenous T cells; and d) Derive a ranking in terms of protein quantity (as specified herein) and specific affinity (KD) toward endogenous T cell receptors; wherein the sequence and / or combination of sequences is an HLA tumor antigen peptide corresponding to MHC class I complexes and / or MHC class II complexes or a combination of HLA tumor antigen peptides thereof, and wherein the individual sequences are selected from the sequences of a database of nucleic acids. In a preferred embodiment at least two HLA tumor antigen peptides are arranged on an HLA tumor antigen polypeptide in accordance with the current invention. In the context of group therapeutics, one embodiment of the present invention also includes an innovative approach to adaptable cancer immunotherapies. This approach leverages multimerized HLA tumor antigen polypeptides (HTAPPs) that are uniquely designed to contain at least two tandem or overlapping HLA tumor antigen peptides. These peptides are selected to correspond to MHC class I and / or class II complexes and to match the amino acid sequence of mutant genes commonly found in cancers with at least one shared mutated gene across a group of subjects with at least one common HLA allele. The concept underlying this embodiment is to bridge the gap between common mutations observed in various cancers and the predominant HLA tumor antigens detected in the HLA ligandome of a large group of subjects or potential subjects. In a preferred embodiment of the present invention, relating to a pharmaceutical composition for group therapy, multimerized HLA tumor antigen polypeptides on which multiple peptides corresponding to HLA complexes are arranged provides advantageous coverage of different mutant genes in a group of subjects simultaneously. By introducing more and more mutanomes from different subjects into a bioinformatic pipeline with feedback, increasingly precise HLA tumor antigen polypeptides (HTAPPs) can be generated and successively improved, expressing many different mutant gene segments and corresponding to widespread HLA alleles. Thus, a growing pool of HTAPPs can be generated, which can then be easily tailored to a specific subject. Preferably, a single HTAPP already covers different combinations of the most commonly mutated gene segments and HLA alleles in a group of subjects. By combining a number of these peptides, the precise mixture of which is tailored to the HLA alleles of the particular subject, an effective single therapy can be formed from a manageable number of HTAPPs. Preferably, databases with the most frequent mutated gene sequences, e.g. COSMIC (Catalogue Of Somatic Mutations In Cancer), TCGA (The Cancer Genome Atlas), ClinVar, ExAC (Exome Aggregation Consortium), gnomAD (Genome Aggregation Database), ICGC (International Cancer Genome Consortium), dbSNP, HGMD (Human Gene Mutation Database), cBioPortal, OncoKB, CIViC (Clinical Interpretation of Variants in Cancer) are used, which together with the most frequent alleles of a group that has cancer or is at risk of developing cancer, preferably cover a broad part of the population, preferably 90%, more preferably 95%, most preferably 98%. That allows advantageously to share the treatment of a whole group of people suffering from cancer who have at least one HLA allele and a gene mutation related to the cancer and presented on the surface of the cancer cells. In an alternative embodiment, the invention aims to create a reservoir of therapeutic options, also referred to as pool or pharmaceutical composition pool, that can be tailored to both individual and group needs. Hereby, a pharmaceutical composition pool contains a set of HTAPPs, for example, a pool of 5 to 100, more preferably a pool of 10 to 75, most preferably, a pool of 10 to 50. Each HTAPP in this pool is designed to target a multitude of specific mutation-HLA tumor antigen pairing, preferably at least 1 to 10, more preferably 2-8, thereby providing broad coverage of potential therapeutic targets. However, given the heterogeneity of cancer and the unique genetic nature of subjects, the invention also introduces a method for refining this broad approach. Based on a subject's specific HLA ligandome and the gene mutations identified in their tumor, a subset of the pool of these HTAPPs, preferably 2 to 10, more preferably 3 to 7, can be selected. This curated subset of the pool is then used to generate a therapeutic composition that, while tailored to the subject's unique genetic landscape, still benefits from the generalized approach of the broader HTAPP group. In a preferred approach, in a method of determining a pharmaceutical composition comprising or consisting of HLA tumor antigen polypeptides according to the current invention, this pool approach is integrated into step III) of the pharmaceutical composition determination and creation, where the specific HLA ligandome and tumor mutations of a specific subject are first processed in the bioinformatic feedback loop pipeline, to further increase the specificity and scope of the models contained in it. The technical implications of this innovative approach are, first, that by maintaining a broad set of HTAPPs, the invention ensures that a wide range of mutations and HLA ligandomes can be addressed, increasing the potential applicability of the therapy to a diverse subject population. Second, the ability to refine and select a subset of HTAPPs based on individual subject data ensures that the therapy remains personalized, potentially increasing its efficacy. This dual approach, combining the advantages of both broad-spectrum and personalized therapies, offers a novel paradigm in cancer immunotherapy. It not only streamlines the therapeutic process by reducing the need for entirely bespoke treatments but also enhances the potential success rate by ensuring that the therapy is closely aligned with the subject's unique genetic and immunological profile. In summary, this embodiment of the invention represents a new approach to cancer immunotherapy not yet found in the prior art that combines the advantages of broad-spectrum treatments, e.g., regulatory hurdles, cost, applicability, and resource intensity, with the precision of personalized medicine. The present invention further comprises a process for preparing a pharmaceutical composition or (drug-) formulation according to the invention-, wherein the process comprises the following steps: (a) Determining at least a pharmacologically effective amount, preferably an absolute concentration (i.e., administration dose) of each HLA tumor antigen polypeptide or HLA tumor antigen peptide from 100 to 1000 µg, comprising 2 to 25 HLA tumor antigen peptides arranged on at least one HLA tumor antigen polypeptide(s) corresponding to MHC class I and / or class II complexes exposed on the cell surface of cells from a carcinoma of the subject or group of subjects to be treated with at least one identical HLA allele by the determination method of the invention. (b) synthesizing at least one HLA tumor antigen polypeptide(s) comprising the 2 to 25 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes determined in step a); and (c) Preparing the pharmaceutical composition according to the invention comprising at least the 2 to 25 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) synthesized in step b), and an adjuvant as defined herein. The present invention also comprises the use of the pharmaceutical composition or (drug-) formulation according to the invention for the preparation of a medicament or a combination preparation for the treatment of malignancies, leukemias and neoplasms, in particular cancer. The synthesis of the HTAPPs comprising the HTAP(s) according to the process for preparing a pharmaceutical composition of the invention comprises a solid state synthesis. Preferably, the peptides may be prepared by standard procedures in accordance with GMP standards. The peptides (HTAPPs) may be prepared by any peptide synthesis and subsequent purification and verification known to those skilled in the art, preferably via an Fmoc (9- fluorenylmethoxycarbonyl) SPPS (solid-phase peptide synthesis) with reversed-phase high-performance liquid chromatography (RP-HPLC) purification and HPLC HRMS control of the peptides obtained. Also encompassed by the invention is a pharmaceutical composition comprising an HLA peptide as defined in the invention and a pharmaceutically acceptable excipient. The invention also relates to an HLA tumor antigen peptide or a neoantigen peptide of the invention for use in the preparation of a formulation (such as, without limitation, a pharmaceutical formulation, as further described herein) for the treatment of cancer, either in vitro (e.g. in an in vitro or cellular detection method) or in vivo (such as, for example, in a unicellular or multicellular organism and more particularly in a mammal and more particularly in a human being, such as, for example, a human being at risk of developing or suffering from a cancer of the inventions). The present invention further comprises a Combination drug for use and / or particulary in the treatment of carcinoma with simultaneous, separate, or sequential administration, comprising the following two separate preparations (a) and (b): (a) a first preparation comprising, together with a pharmaceutically acceptable carrier or diluent, a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) according to the invention, and optionally determined by the method of the invention , and (b) a second preparation comprising, together with a pharmaceutically acceptable carrier or diluent, an anticancer agent selected from the group consisting of anticancer alkylating agents, anticancer antimetabolites, anticancer antibiotics, herbal anticancer agents, platinum-coordinated anticancer complex compounds, anticancer camptothecin derivatives, anticancer tyrosine kinase inhibitors, monoclonal antibodies, interferons, interleukins, biological response modifiers, and other anticancer agents, or a pharmaceutically acceptable salt thereof. In a preferred embodiment the second preparation is a monoclonal antibody, in particular against an immunosuppressive protein selected from the group consisting of CTLA4, GM-CFS, TReg, EpCam, IDO, MIC, PDL1, Fas and PD1-L, TRAIL. The combination preparation according to the invention is particularly suitable for use and / or particulary as a medicament in the treatment or profilaxis of carcinomas, in particular locally recurrent or metastatic mammary carcinomas in a subject or group of subjects who have or are suspected of having a carcinoma. Particularly preferably, the first preparation of the combination preparation according to the invention is administered subcutaneously. Particularly good experience has been made in the administration of the pharmaceutical composition according to the invention (first preparation) in combination with the administration of herbal anticancer drugs, in particular artesunate and / or curcumin as the second preparation. Nevertheless, the combined administration of the pharmaceutical composition according to the invention (first preparation) in combination with a monoclonal antibody, in particular against immunosuppressive proteins selected from the group consisting of CTLA4 (herein e.g. Ipilimumab - Yervoy®), PDL1 (herein e.g. Nivolumab - Opdivo) , PD1-L, also EpCam, IDO, MIC, Fas and TRAIL; specifically: as estrogen inhibitor for hormone positive subjects from the group of aromatase inhibitors - (herein e.g. Letrozole and / or the estrogen blocker Fulvestrant); as antibody against HER2 positive subjects: Herceptin (TDM-1) as a second preparation. In a particularly preferred embodiment, the drug combination may be used in conjunction with other cancer therapies. These may include, but are not limited to, surgical intervention, radiotherapy, hormone therapy, chemotherapy, or other individual therapies. For purposes of the present invention, a surgical procedure involves the removal of tumor masses or affected tissues from the body. Following such surgery, the drug may be administered to target remaining tumor cells to increase the overall effectiveness of the treatment. Radiation therapy in the context of the present invention uses high energy radiation to damage or kill cancer cells. Following radiation therapy, the pharmaceutical composition may be administered to target potentially radioresistant tumor cells, providing a comprehensive treatment approach. Hormone therapy, as conceived in the present invention, is used for cancers that are sensitive to hormones and is aimed at stopping the production of, or blocking the action of, hormones that promote these cancers. When combined with hormonal therapy, the pharmaceutical composition can provide a dual approach that targets both the hormonal aspect and specific HLA tumor antigens. Finally, chemotherapy, as understood in the context of the present invention, uses drugs to kill or inhibit rapidly dividing cancer cells. After chemotherapy, the introduction of drugs may target residual or resistant tumor cells to increase the overall efficacy of treatment. In one embodiment, the pharmaceutical composition according to the invention comprising HLA tumor antigen polypeptides is used as a sole therapy. By focusing the specific tumor genes through the HLA antigen peptides, the technical effect is that the therapy has fewer off-target effects and thus potentially fewer side effects than some other therapies, particularly much more non-specific conventional chemotherapies. The technical advantage of this approach is its precision, which may provide subjects with a better tolerated treatment with fewer systemic complications. In another embodiment, the pharmaceutical composition is administered after a surgical procedure. In this case, after the majority of the tumor mass has been physically removed, the immunotherapy acts on any residual or microscopic tumor cells that may have remained. The technical advantage of this combined approach is a potential reduction in cancer recurrence rates, allowing for a two-pronged attack on cancer. In another embodiment, the pharmaceutical composition is used after radiation therapy. After radiation has damaged or killed many tumor cells, immunotherapy can then target surviving cells that may be more resistant to radiation. The technical advantage here is to target radiation-resistant populations, aiming for more comprehensive tumor cell eradication and potentially preventing or delaying relapse. In another preferred embodiment, where the pharmaceutical composition of the invention is administered after chemotherapy, the combination aims to increase overall efficacy. The chemotherapy may reduce the overall tumor burden, and the subsequent immunotherapeutic approach may target residual or resistant cells. The technical advantage of this approach is the potential synergy between the cytotoxic effects of chemotherapy and the targeted immune response elicited by HLA tumor antigen polypeptide-based therapy, which may result in increased overall survival and improved quality of life for subjects. Also disclosed is a business method comprising marketing 2 to 25 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) for the treatment of cancer in a human to effectively reduce a tumor marker score of a subject or group of subjects having at least one identical HLA allele, in particular to increase progression-free survival or reduce the likelihood of cancer recurrence or increase subject survival. In some embodiments, the marketing is followed by treatment of the subject with the combination of HLA tumor antigen peptides. It is also important for the ranking to identify factors that play a significant role in tumor progression (i.e., the increase in size and / or metastasis of tumors). Characteristic of tumor progression is an increased growth rate, as well as increased invasiveness of the tumor. Invasiveness refers to the extent of tissue-penetrating growth of a malignant tumor from its site of origin into adjacent tissue structures. Angiogenesis describes the formation of new blood vessels from an existing vascular system and is a component of both physiological processes (e.g. embryogenesis, wound healing) and pathological processes (e.g. diabetic retinopathy, chronic polyarthritis, tumor growth). It has been known for a long time that new vessel formation (angiogenesis) occurs in cancer, which is referred to as tumor angiogenesis. Tumors are composed of cells that, like all other cells in the body, require nutrients and oxygen. In fact, because cancer cells divide frequently, their need is particularly high. And that is why a tumor needs its own blood vessels. When a tumor develops, it initially does not yet have its own blood vessels. Its growth is therefore severely restricted. Without its own blood vessels, it does not grow larger than 1 to 2 millimeters. The formation of metastases also interacts with tumor angiogenesis, because tumor cells must reach surrounding blood vessels to do so. Only then can they be transported to distant regions of the body and form metastases there. For example, it is known that there is an interdependence between class I HLA and integrin β to stimulate signal transduction and cell proliferation. In this regard, integrin β-mediated cell migration depends on its interaction with class I HLA molecules (Zhang and Reed, Hum Immunol.2012 Dec, 73(12), 1239-1244). An HLA peptide of the invention, or a composition or formulation containing the same, may be used for modulating a class I and / or class II HLA complex, including combinations thereof, either in vitro (e.g., in an in vitro or cellular detection method) or in vivo (e.g. in a unicellular or in a multicellular organism and in particular in a mammal and more particularly in a human being, such as a human being at risk of developing or suffering from a cancer of the invention). In the context of the present invention, "modulating" or "modulating" substantially means increasing the specific affinity of T cell towards a tumor-exclusive or tumor-associated MHC class I complex or MHC class II complex, respectively, of the malignant and / or neoplastic tissue, as measured by an appropriate in vitro, cellular or in vivo detection method (such as those referred to herein). In particular, "modulate" or "modulate" means to increase the specific affinity of endogenous T cells of the subject or group of subjects, respectively, towards a tumor-exclusive or tumor-associated MHC class I complex or MHC class II complex of the malignant and / or neoplastic tissue, by at least 1%, preferably at least 5%, such as 10% or at least 25%, for example by at least 50%, at least 60%, at least 70%, at least 80% or 90% or more compared to the affinity of T cells towards a tumor-exclusive or tumor-associated MHC class I complex or MHC class II complex of the malignant and / or neoplastic tissue in the same detection method under the same conditions but without the presence or prior application of the HLA tumor antigen peptides of the pharmaceutical composition of the invention (as defined herein). In a particular embodiment, the invention comprises a method, wherein the expression profile of at least five, preferably at least six, most preferably at least 6 marker genes is determined. As mentioned above, the marker genes are also defined by variants, this expression profile is compared to the expression profile of a "reference". For example, a reference can be the expression profile of healthy tissue (e.g., intestinal tissue or tissue of the liver, lung, etc.). Tissue from the affected individual (proband) can be used as "healthy tissue" here, whereby this tissue is known not to be proliferatively altered or even metastatic. Appropriate examples are shown in the experimental part of the invention. However, data from tissues of foreign individuals, preferably healthy individuals, can also be used as a "reference" or "reference value". As set forth herein, according to the invention, in the method for the detection of a carcinoma, at least 6, but preferably at least 8, and most preferably at least 10 of the HLA tumor antigen peptides shown herein corresponding to MHC class I complexes or MHC class I complexes are to be determined. Brief description of the drawings Herein shows: Fig.1: Schematic representation of HLA-A-mediated binding of a T cell receptor to a class I MHC molecule, showing the anchor (amino acid) residues of the HLA-A antigen peptide (7-11 amino acids in length). Fig.2: Schematic representation of HLA-B-mediated binding of a T cell receptor to an MHC molecule, showing the anchor (amino acid) residues of the HLA-B antigen peptide (12-17 amino acids in length). Fig.3A: Flowchart illustrating the bioinformatic method in accordance with the current invention, including steps a) to e) for determining a pharmaceutical composition of the invention comprising or consisting of HLA tumor antigen polypeptides. Fig.3B: Detailed illustration of the bioinformatic method according to the invention, in particular with steps c) and d) and highlighting the bioinformatic feedback loop. Fig.4: Therapeutic scheme for the treatment of a subject with prostate cancer with a pharmaceutical composition in accordance with the current invention (example 3). Fig.5A: IFN-γ ELISPOT assay results of the selected peptides SEQ-ID-Nos.: 1, 18, 2, 19, 3, 20. Depicted Plates and Spot Numbers / 200k PBMCs. Elispot-IVS (In Vitro Stimulation) and Elispot-ExViVo (Ex Vivo) Immunoassays depicted. Fig.5B: CA19-9 cancer marker levels of the subject throughout the treatment, initial immunization (1) and immunization boost (2) with the pharmaceutical composition in accordance with the current invention marked. Fig.5C: CEA marker levels of the subject throughout the treatment, initial immunization (1) and immunization boost (2) with the pharmaceutical composition in accordance with the current invention marked. Fig.5D: MRI scan was performed before and approximately three and six months after the start of PrCa-PC1 immunization. Decrease of the tumor von 24,83 mm to 14 mm could be detected as consequence of the treatment with the pharmaceutical composition. Fig.5E: Immuno-monitoring of the subject during the treatment, immunization boost (2) with the pharmaceutical composition in accordance with the current invention and chemotherapy (3) marked. Fig.6: Therapeutic scheme for the treatment of a subject with prostate cancer with bone metastasis with a pharmaceutical composition as sole therapy in accordance with the current invention (example 4). Fig.7A IFN-γ ELISPOT assay results of the selected peptides SEQ-ID-Nos.:E4-1 to E4-11, E4-13 to E4-26 and negative and positive control. Depicted Plates and Spots / 25.000 PBMCs. Fig.7B IFN-γ ELISPOT assay results of the selected peptides SEQ-ID-Nos.:E4-1 to E4-11, E4-13 to E4-26 and negative and positive control. Depicted Plates and Spots / 25.000 PBMCs, results of the modifications of the HTAPPs and HTAPs according to the current invention (elongation, multimerization, tandemization and delivery aiding capping peptide addition). Fig.8 IFN-γ ELISPOT assay results of the PrCa-PC2 pharmaceutical composition and negative control. Depicted Plates and Spots / Million. Fig.9A PSA level of the subject during the time of subject diagnosis and treatment with a pharmaceutical composition according to the invention (PrCa-PC1). Fig.9B Subject examinations before and after treatment with a pharmaceutical composition according to the invention (3 months) (determined by PSMA-PET CT). Fig.9C Examinations before and after treatment (8 months) with a pharmaceutical composition according to the invention (determined by MRI). Fig.10 Demonstrates the increased pharmaceutical efficacy (ca.30%) of the immunogenically tested HTAPP(s) and HTAPP-DACP(s) of this disclosure compared to their corresponding HTAP(s) that were not tandemized or overlapped or bound to a delivery aiding capping peptide. Fig.11 Illustrates the 10 classes of hallmark of cancer used as weighting factors in the determination of HTAPP and HTAPP-DACPs of the current invention. Detailed description of the drawings: Fig.3A is a flowchart illustrating steps a) to e) of a method for determining a pharmaceutical composition according to the current invention. The method is also preferably aimed at monitoring tissue resection of subjects with suspected or confirmed carcinoma to derive HLA tumor antigen polypeptides for pharmaceutical use. In detail, the steps are as follows: • Step a) An icon indicates the provision of a tumor tissue sample and a healthy cell sample from the subject or a group of subjects. The method specifically indicates that no surgical procedure is associated with this provision. This in no way limits the treating physician in his or her treatment decision and method for obtaining the sample. • Step b) The tumor tissue sample is subjected to sequencing, represented by a sequencer symbol. This step results in the generation of a transcriptome and preferably an exome from the provided tissue sample. • Step c) to d) A computer icon with algorithms and neural networks shows the bioinformatics steps. In this phase, a pre-selection of HLA tumor antigen peptides is made. These peptides match the MHC class I and II complexes derived from the mRNA transcriptome from step b). This selection takes into account various factors such as mRNA regulation, HLA subtypes, tumor-associated properties such as proliferation and invasiveness, exome sequence, and presentation on the associated tumor cells. The subsequent step, represented by a loop around the computer, shows the generation of an HLA tumor antigen polypeptide composition via a bioinformatics feedback loop pipeline. • Step e) The last icon, resembling a lab setting, signifies the testing of the immunogenicity of the HLA tumor antigen polypeptides determined in the previous step. This testing can be achieved using techniques like Western blot, ELISA (especially ELISPOT), AFM, or microscopic analysis-based immunodetection. This allows for verification of the method as well as serving as quality assurance und subject safety measure. The distinctive feature of this method is the bioinformatic feedback loop pipeline. It involves steps i) to iii) (depicted in Fig 3B), which respectively entail weighting the sequences of the HLA tumor antigen peptides using neural networks and algorithms, matching selected HLA tumor antigen peptides in the amino acid sequence to form HLA tumor antigen polypeptides, and assembling a pharmaceutical composition. This composition is then fed back to create a feedback loop, particularly for a subject group, to validate the sequence score and potentially further train the neural network. The figure Fig 3B shows a flowchart providing a detailed overview of steps c) and d) of the described method for the determination of a pharmaceutical composition containing HLA tumor antigen polypeptides. In detail: • Step c) Starting on the left: o The first icon shows a transcriptome from step B), e.g., a whole sequence exome from the tumor tissue sample and a healthy tissue sample. o The second icon shows a cancer cell with an exposed MHC class I and / or II receptor on its cell surface (also called epitope), symbolizing the analysis of the transcriptome data related to the protenome, an important step that ensures that the selected mutations in the tumor tissue sample are also on the cell surface and thus accessible to T cells. o The third icon embodies an MHC complex with a matching HLA tumor antigen peptide. This phase highlights the calculation of various factors such as binding affinity values associated with the MHC complex and the corresponding HLA tumor antigen peptide. o The fourth computer-like symbol shows the preselection of HLA tumor antigen peptides based on the previous determinations, including but not limited to physicochemical properties of the peptides, stability, overexpression, matching with HLA alleles and tumor exclusive or associated genes, conformation and others. These preselected HLA tumor antigen peptides are then fed into the bioinformatics feedback loop. • Step d) On the right side, the bioinformatics feedback loop pipeline is the focus, represented by a circular diagram with three different elements: o (i) The top symbol, with the network shown illustrative, illustrates the neural networks and algorithms used to weight the sequences of HLA tumor antigen peptides based on multiple factors, including MHC class I and II binding affinity scores and other attributes. o (ii) The central symbol, represented as vertical strings with specifically highlighted segments, symbolizes the amino acid sequence alignment process of the selected HLA tumor antigen peptides to create the HLA tumor antigen polypeptides. The highlighted sections draw attention to the matched or selected sequences. o (iii) The bottom icon shows the resulting HLA tumor antigen polypeptide compositions based on the selection and matches from the previous steps. A series of arrows navigates from step i) to step ii), on to step iii) and back to step i). This sequence illustrates the mechanism of the feedback loop and highlights how the assembled pharmaceutical composition is fed back for validation of sequence evaluation and possible further refinement through training of the neural network. To the right of the circular loop, a final symbol in the form of a test tube indicates that the pharmaceutical composition has been finalized as a finished informatic, i.e., virtual drug (i.e., prior to synthesis of the HTAPPs), in the sense of the present invention, after the changes in the feedback loop. Design examples With reference to the following figures and examples of embodiments, the present invention will be explained in more detail without limiting the invention thereto. The following tables list HLA tumor antigen polypeptides, all of which have been tested and are immunogenic. SEQ-ID- Nos.: 1 to 84 list some preferred, but not limiting, examples of amino acid sequences of HLA tumor antigen polypeptides of the invention, each of which is another embodiment of the present invention. The sequences marked with ref. (reference) are included for illustrative reasons and may not represent sequences of the invention. a a a a a a a a a a a a a C m MCrCrCrCrCrCrCrCrCrCrCrenP / P P P P P P P P P Pe a oL / a / a / a / a / a / a / a / a / a / a / ag C.rrr inca a a C C C C C C C C C a C C a C ad P ora Ca Ca M M M M M M M MCrM MCrMCret ,C a c P P P B B B B B B B B P B B P B Palsie sr at ]e stM vitatop / e pstop5 5,0,5,5,5,5,5,5,5,5,5,5,csils,2 91 64 33 76 03 15 9 3 5 5 7 6 2e m En[3 4 2 2 2 3 – 3 82 41 41 – 02 31 2 0psr– 3 2e ercrina ecA K M4hteA15 C7 6 L 1 1,n n 3 7 V 7s o oeitE.R...4 P nbe aut....MS / CitV S R F R T 0 G …gs d M b 2 99 1 67 63 72 7 A A Q3 A A;A C4 M Aeu 1 3 0 5 9 3 1tG A L V S A T T T E T TV5 6 B S 3 1 A A 3 A A / L A 6 T R V A Ta;tsuis at1m 0:d s nat5 a e)10*1)s0:10:s m PrP 5 B A e AT0;*Q 1 1 5 0 1 D0:0: *1TviHlH(2 0:1 B;3 1 1 10 0;1;B 1 2 1(ale60:Q0:0: *A*10:0:0:0:Qs Celel0*2DlM0- 1 1 5 3;1 B 4 0 5 6 5D- 1ellL aC ,; *1 r A0:0* *0:R*0*0*1*0:L 4 B 1 1 A B;2 D;C;1 1 1 B B B 1aeH 0:7 Q0*Q 2 20*2 1 1 1 Q Q R 2 20*3A c L na g 330:7 D;1 A D;0:70:7 A;0:70:50:50:5D-D- D;0:70:7 1 A0:1H cin*d C5*1 0:Q 1 0 1 :0:0*0*100: *3*3*3*1 0 1 :0:1 0:0*0*Q0*g cniitn;B o 6;1 D;5 1 B;B;5 C B B B 1 1 B C D 8 2 1 1 1,2;2;2;1 2;1;1;E 2;1d a psnere7:20:0*6 10A:1*02 1*10:0:1*010:0:0:0: *01*10*0:0:0:0:B B 3 2 B 7 7 7 7 A A 1 B 2 3 7 1o crp nr0a o*0*Q0*R R0*0*R0 0 0 0 0 0 0*0c A C D A D D A A D*B* * *Q Q R* * *s B B B D D D A A C Eerrpa ocCa e P D v 4 2iFt(D Fcst0 A H Ee n 5 M E 3p e 1 T M D 1s m P U E 1 C H OT- L Her irS- L P 1L- P LrOiepN- 8 2 A D M O 4 A 2;F 1FI2,1 2 Fe xs / S MPI4 3 AL-F- F A G C ER- FF 1,hee C 1 E 2 T 1MIS 1t,n A A M M M C X)T e M E L L O R D E M D E N L MPIOFIB G X G K A Ms P A C S K S T D T D L P R T A R DPPSAILTHE(n K i S s e P ed s L V D n VSIitp o S K H G e p N S L p se SEIVylrF D So d Npn H F S L LIInae n FNIA G Dg o e A S F DTIS Lititd nitD AYIS S K L EHIM G L M N T K K autritpe E C Y S L G P N Y N A T K Y F FSIo s p blyIK T VVE A G G A P D A A R F A N P m u o u L KIE A At s PA T A V C A T A F E A N L L L V L R M VVIK L T L QL A TTYIQ K Y L E G Adine S K Y R Q W S P L L Y L S Q K S A A Y F S L c g Y F Y L V Y A A S YH a iotG G n V A H N Y S V L A A L P L D P Y A S P T R F HL A L T A M A A d A G D T T A R ASIL LenriH H KYIA ArW L S mro V S Q F F D C A V P T P M N T Q S H W S Aefa m A L L F D R ATIRVIL L G N A STIA Se,re u G S G V P R KLS N P L GL G G VL C T V G p p.)rTV S F FIR L S K M D T Y E N Q A R Pfyotre A c L VL N E N P G FLRIV K L D K R C R Y S H K A L Q T V K L EKIN P F PPIS P R Ete n M K L L S L S H R Qsic L n a.ac1c,et:.a - oeletQ b m sN- o E 0 1 2 3 4 5 6 7arSDI1 2 3 4 5 6 7 8 9 1 1 1 1 1 1 1 1 T a n p detale,a a a a a a r aCrerCrCrCrCrCrc mPd n / P / P / P P P. o a a a / a / a / an aina a a C a a a a aarrcrC C C C C C C C)csio a a a M M M MCrCrMCC arCrMCcrs s P P P B B B B P P B P P B PP AatT s]H( atM s etop / st5,5,0,0 0 0 0 5 5 0 0 5 0 0elmp opllesi nls 7 E 4 0 4 3 0,4 0 4,7,5,6,7,7,6,0,2,4,5en[5 33 74 82 34 13 43 91 23 43 32 14ao AbL aHC A K M 1 4 Lg MA6)1)niB;n 5 1 o 3 V A 74 Ads itE...T A P A Tnio sut..nC / T TC / pastits s V S 2 9 R F R M0io1 6 6 7 s A u A QC / … A A CC4 / Ae b 1 9 0 7 3 1 T 3 5 A Trratu 3 5 9 e S G A 3 L V S 1 TF–(3 – E A T R A T(–ocm er )v e sitviclP A 1 1e a T0p C H:e(2; ; ;0:1 5s M0:1 1 1 1 1 20r Lle6*1*00:20:10:50-:40:0:1 1ri,rel el *- 5 6 B B e0*10h*3*10*0R RtcaC,n A;10:1 1 B0: *0*1 C 1 1 D D;)a L 4 0:7 B 0 A;20;*1 1 B B;1 2 2 2 3PccHg 33:Q*Q 7 D 1 D0:1 70:0:Q Q DD 0:0:0:70:70:C0* ;A;A 5 5- -5 7 1Aitaind C5;*1 Q 1 1 10B0:D0:0:0: *Q 13 31 13 0 0*0*0B D0: * *0:0: * * *D-ern;1;5 5; ;5 B;B;1 1 B;B;C C EP c o 6 P n p 8 20105 101 201 20 02 1;1,1;1A a se7:20: *6 10: * * *2 1 1 10:30: *7 10:30: * *7 1 10:70:0:0:0:Tp rr0 0A0B B B0 0B0 0A A02 0 3 0 5 3 1H(a o* *Q*Q R Q A D D D* *Q A C D*A*Q Q0c A C D B D D*B*A*A*B*E s C e a d Pit(;1pst2e n 0 D2 G H FFpe 5 P 1 A R E T E 3 D 1g mi)U C NE- O M L Hni rs(N C 2 PT- P Lp e p e,M A S,2;2 Op n 8 2 A A 2CS G F 1 F Fa xc eePTGS MI4 3 L,1 - 2 R E A,l.A A M C M C S T P T 2 FMIF 1 PIE L E L g R D E M G XniOerD K A C S K N X T R E M O T P D M B T A M T DdPia SILyrEe n viliK e K e sdn K W Kh o K K Ktips W K M K K K W K Kwe K W R K r M K R K W Wse d M N W M K Kditn)K R K K Q K R M K M a P K R C N K K W K R R K K F M K R K R R K R p n A W Q W K NWN R W Rep o K K K W WIR W Q N K NylitD- M F M M K Q F K MKIN Q K F QF M Q outitP P RWIRKR R R MWIR Q F M RWIR Fps A NIR N N R RKIR R VWIRKIWIR NWIn b T Q e u H Q R Q Q N F N Q V Q SKIN QKIQKIgits (F F F Q R Q R Q F Q e AWF F F L Q F L R RndidWiItDWI IK AWIA R S EWIT KWIL a cKIKI IWIM KKKrap E Q MKIA L P NIo o e Q E p K QKINKIF QSIR R Q G Q A K Q F R m uni ly RIT VVtm o L KIE E R G R G D A E R A N R L Q P aPT A V C T L R F L L R E N T K V F MA L,A e n S VVIK L E E W P F YYIT Y L Y R G V SHp eg K Y Y R Q S A S A Y Y G F Y Y S A Y V A PdyetitG n V AL P L H P A M A K H T L A A G A P Arr re.)A G H D D H T A A L R T L L K E A A L Vefcrero V A S QF F D P W S A T P W S H V S Aenra c m L L F G D R S GTIA EL N L STIYL S p c n , a u V P R KLIN V A G G C T R L Y L A V Gfsc TV S F F S D Q S Po A V E N R F R R E R C Y Yteneta L L N A Q T P K L I E Q D K P F P R D SsietH K L L E M R RIL S H K QL.gs2dor-eletpbata Q uCrE -:.o SDIN 81 91 02 12 2 3 4 5 6 7 8 9 0 1a 2 2 2 2 2 2 2 2 3 3 T m P Table 3: A list of preferred delivery aiding capping peptides (DACP). ID.: SEQ-ID- Amino Acid Sequence designation % of R % of K % R + K No.: DACP-1 482 –RQIKIWFQNRRMKWKK Penetratin 18.75% 25.00% 43,75% DACP-2 483 –RKKRRQRRR TAT- 66.67% 22.22% 88,89% derived DACP-3 484 –GRRRRRRRRRPPQ R9-TAT 69.23% 0.00% 69,23% DACP-4 485 –RKKRRRESRKKRRRES DVP3 50.00% 25.00% 75,00% DACP-5 486 –GRPRESGKKRKRKRLKP DVP6 29.41% 29.41% 58,82% DACP-6 487 –RKQIKIWFQNRRMKKKWI – 22.22% 22.22% 44,44% DACP-7 488 –RQFWIWQNRKWIKIK – 21.43% 14.29% 35,72% DACP-8 489 –RQIKVWFQRKWIKK – 21.43% 21.43% 42,86% DACP-9 490 –KIQRKIWFQNRRMKVKWKI – 21.05% 21.05% 42,10% DACP-10 491 –RKIIWFQNRMKWIK – 21.43% 14.29% 35,72% DACP-11 492 –IKVRQWFQNRRMIKWK – 23.53% 11.76% 35,29% DACP-12 493 –RQIKIWFQNRKWKK – 14.29% 21.43% 35,72% DACP-13 494 –RQIKIWFQNRRMKIKW – 21.05% 15.79% 36,84% DACP-14 495 –RKQIKVWFQNRRMKWK – 25.00% 12.50% 37,50% DACP-15 496 –NRRMRQIKIWFQKWKIK – 17.65% 23.53% 41,18% DACP-16 497 –RQIKIWFVNRKMWKQRI – 23.53% 11.76% 35,29% DACP-17 498 –QRIKVWFQRKWKIKK – 20.00% 20.00% 40,00% DACP-18 499 –RQIKIWFRMKWKIK – 20.00% 13.33% 33,33% DACP-19 500 –QRIKFWIVNRKMKQRIKIW – 21.05% 21.05% 42,10% DACP-20 501 –IRQKIWFQNRKMVK – 21.43% 14.29% 35,72% DACP-21 502 –RQIKFWIQNRIKWKWK – 18.75% 25.00% 43,75% DACP-22 503 –KIRQIWFQNRRMKWKRFKI – 22.22% 22.22% 44,44% DACP-23 504 –RQIKIQWFNRRWVKKMWIK – 21.05% 21.05% 42,10% DACP-24 505 –RIQKKIWFQNRKWIKM – 23.53% 11.76% 35,29% DACP-25 506 –QRKIKIWFQNRRMKVWKIKI – 22.22% 22.22% 44,44% DACP-26 507 –AAYRRRRRRRRRR – 76.92% 0.00% 76.92% DACP-27 508 –AAY–Cyclic(RRRRRRRRRR) – 76.92% 0.00% 76.92% DACP-28 509 –AAYR–Cyclic(RRRRRRRRR) – 76.92% 0.00% 76.92% DACP-29 510 –AAYRRRRRRRRR – 75.0% 0.00% 75.0% DACP-30 511 –AAY–Cyclic(RRRRRRRRR) – 75.0% 0.00% 75.0% DACP-31 512 –AAYR–Cyclic(RRRRRRRR) – 75.0% 0.00% 75.0%)s(5 en 1 M e 1 A A 7 7 1 A G P C A 35 3 C S W W R C F S S R S 5 3 A F P 3 A A A F A 3 3 3 l.eM r EKM C P T P TIX X 5 5 5 R G MKP K- -B F BIR R R G R F E M P B K K E K P T P T P T evitcepst / ]eropstk o7,2,3,0,7,7,2,0,risilp 0 s 028,5 178,50,0 045,70,52,8,4 30,2,02,1 6 4 5en[ - -9 0 3 0 5 4 2 9 6 5 6 7hE p 7 2 3 2 1 4 9 3 2 1 1 5 5 1 3 1 2 2 2t,ypareh 1;1 2t 0:0:0p.8 6:s5 27 uot *rnge B*0 A C m 2 0:2; ; ;0 1 0 1 0 3 0 1 201 201 ot ir7:0:8:1: : :80:8 d eetpx0*3 6 3 0 0 6 6C*A*A*A*A*A*A*ale;1;1;1;1; ; ;A;e T O0 01 1 1 1ry: :0 0 0 0 0 0l2: : : : : :P b08 3 3 2 1 3 3a*6*0*0*3*1*0*0rSIL A;A A A A A A*AefE1;1;1 1;1;1;2; ;n0 0 0 0 0 0 01 0 1 0 1 0 1 1eri: : : : : : : : : :0:0:p,e 3)n01 3 2 3 0 2 4 7 1 2 2 1 s*A*0A*0A*3A*0A*2 5 1 0 0 3A*A* * * * *P o; ; ; ; ; ; ;B;A;A;A AC p 1 1 2 6 1 1 2 1 1 1 6;6;A s)-0 0 0 0 0 0 0 0 01 1 1 6Ders:P 1:1 1:1 7:0 2:0 8:8:8:3:10:30:20:20:80:20:00:2P d A* *6 6 6 0 1 3 0 0 6 0 3 0P n T A A*B*A*A*A*A*A*A*A*A*A*A*A*A*A A a r H(;1;1;1 1;1;2;1;6;2;1;1;1; ; ; ; ;T H e(c01010308010:80:101 1 1 1 1 1 le: : : : : :20:40:00:70:10:10:00:80:30:30:...

Claims

Claims 1. An HLA tumor antigen polypeptide (HTAPP) comprising a delivery aiding capping peptide (DACP), wherein the HLA tumor antigen polypeptide corresponds to at least two HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, wherein the HLA tumor antigen peptides (HTAP) are arranged on the HLA tumor antigen polypeptide (HTAPP), wherein the HLA tumor antigen peptides (HTAP) are tumor-exclusive or tumor-associated and presented on the cell membrane of the associated tumor cell and correspond to an amino acid sequence of a transcribed mutant gene, wherein the HLA tumor antigen polypeptide comprises an amino acid sequence, wherein the amino acid sequence comprises between 15 and 45 amino acids, wherein a) the amino acid sequence comprises, in addition to HLA tumor antigen peptide(s), up to 1 to 30 amino acids (long HLA tumor antigen polypeptide); and / or b) the amino acid sequence comprises HLA tumor antigen peptide(s) with at least 90% sequence identity similarity to the native HLA tumor antigen peptide (similarity HLA tumor antigen polypeptide); and / or c) the amino acid sequences comprises an HLA tumor antigen peptide having an amino acid sequence comprising of only one amino acid substitution relative to the amino acid sequence of the native HLA tumor antigen peptide (substitution HLA tumor antigen polypeptide), wherein i) an HLA tumor antigen polypeptide is a tandem polypeptide comprising at least 2 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes; and / or ii) an HLA tumor antigen polypeptide is an overlapping tandem polypeptide comprising at least 2 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes which overlap in their amino acid sequence, characterized in that the DACP comprises a positively charged and amphipathic sequence with a total percentage of 33% to 89% of arginine (R) and lysine (K) residues, and wherein the DACP is between 10 and 20 amino acids in length and wherein the DACP is directly or indirectly, via a linker, attached to the C- or N-terminus of the HTAPP and wherein the DACP is a cell-penetrating peptide (CPP), and wherein the HTAPP-DACP has a total amino acid sequence length between 30 and 60 amino acids.

2. The HLA tumor antigen polypeptide (HTAPP) comprising a delivery aiding capping peptide (DACP) according to claim 1 , wherein the HLA tumor antigen polypeptide(s) (HTAPP) comprising a delivery aiding capping peptide (DACP) is / are selected from the HLA tumor antigen polypeptide(s) consisting of the group of amino acid sequences set forth in SEQ-ID-Nos.: 1 to 17, 69 and 76.

3. The HLA tumor antigen polypeptide (HTAPP) comprising a delivery aiding capping peptide (DACP) according to claim 1 or 2, wherein the delivery aiding capping peptide (DACP) is selected from the group consisting of penetratin (DACP-1), TAT-derived, R9-TAT, DVP3, DVP6, or DACP-6 to DACP-31.

4. The HLA tumor antigen polypeptide (HTAPP) comprising a delivery aiding capping peptide (DACP) according to any claims 1 to 3, wherein the wherein the HLA tumor antigen polypeptide(s) (HTAPP) comprising a delivery aiding capping peptide (DACP) is / are selected from the group consisting of the amino acid sequences set forth in in SEQ- ID-Nos.: 18 to 37, 40 to 68, 70, 71, 81 and 84.

5. The HLA tumor antigen polypeptide (HTAPP) comprising a delivery aiding capping peptide (DACP) according to any claims 1 to 4 as a medicament in the treatment carcinomas, the treatment comprising administering to the individual a treatment regimen comprising a pharmacologically effective amount of the HLA tumor antigen peptide.

6. The HLA tumor antigen polypeptide (HTAPP) comprising a delivery aiding capping peptide (DACP) according to any claims 1 to 5 as a medicament in the treatment of carcinomas, wherein the individual has not yet received radiation, chemotherapy, and / or hormone therapy for the cancer, and / or has not received prior adjuvant chemotherapy in recurrence for 12 months or less since the last dose of a chemotherapeutic agent.

7. The HLA tumor antigen polypeptide (HTAPP) comprising a delivery aiding capping peptide (DACP) according to any claims 1 to 6 as a medicament in the treatment of carcinomas, wherein the treatment regimen is effective to prolong progression-free survival of the individual.

8. The HLA tumor antigen polypeptide (HTAPP) comprising a delivery aiding capping peptide (DACP) according to any claims 1 to 7, which are immunogenic in the subject or group of subjects, determined by means of an immunogenicity assay.

9. A pharmaceutical composition as a medicament for the therapeutic and / or prophylactic treatment of a carcinoma in a subject or group of subjects suffering from or at risk of suffering from a carcinoma, comprising a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide comprising a delivery aiding capping peptide (DACP) according to claim 1.

10. The pharmaceutical composition as a medicament according to claim 9, wherein the tandem polypeptide comprises at least one HLA tumor antigen peptide corresponding to MHC class I complexes and at least one HLA tumor antigen peptide corresponding to MHC class II complexes, and / or wherein the overlapping tandem polypeptide comprises at least one HLA tumor antigen peptide corresponding to MHC class I complexes and at least one HLA tumor antigen peptide corresponding to MHC class II complexes.

11. The pharmaceutical composition as a medicament according to claims 9 or 10, wherein the HLA tumor antigen polypeptides corresponding to HLA tumor antigen peptides corresponding to MHC class I and class II complexes are selected from the group consisting of the amino acid sequences set forth in SEQ-ID-Nos.: 1 to 17, 69 and 76.

12. The pharmaceutical composition as a medicament according to claim 12, wherein the HLA tumor antigen peptides corresponding to MHC class I and class II complexes are selected from the group consisting of the amino acid sequences set forth in SEQ-ID-Nos.: 1 to 17, 69 and 76 and have at least one amino acid substitution relative to said amino acid sequences.

13. The pharmaceutical composition as a medicament according to any one of claims 9 to 12, wherein the HLA tumor antigen peptides (HTAP) corresponding to MHC class I and / or class II complexes correspond to an amino acid sequence of a transcribed mutant gene exclusive for and / or associated with a carcinoma with at least one amino acid substitution compared to the native gene, fusion-based neoantigens spanning the breakpoint regions of two genes , or aberrantly expressed genes as tumor associated antigen (TAA) or cancer testis antigen (CTA) wherein said gene is selected from the list consisting of ABCA2, ABLIM1, ADAM8, ADAM8-NUP50, AFP, AFF2, ASIP, BRAF, CACNA2D1, CAMK1, CAN13, CCL28, CD33, CEACAM5, CEMIP2, COL10A1, CST1, CTBP2, D2HGDH, DENND4, DHRS2, DIP2A, DIP2C, DLX1, EGFR, ELL3, ESR1, EXT2, EXT2-CACNA2D1, FA83A, FBXO2, FBXW7, FOLH1, GNAS, GRB14, GRIPAP1, HIVEP2, KDM3A, KIAA1804, KIT, KLK3, KRAS, LAMC1, LRRC8A, LRRC9, LUZP2, MAGEC1, MAP3K9, MMP1, MMP11, MTOR, NASP, NGAL, OPA1, PCDHGA11, PCSK1, PCM1,PLEC, PLD3, PLK1, PPFIA1-SHANK2, PRKAG1, PRR21, POTEG, POTEH, PTEN, PYGO2, RBBP6, RGS12, RIF1, RPAP1, S10A7, S10A8, S100A7, SALL3, SAMD9L, SEMA4D, SEHL2, SHANK2, SHS, SLC30A8, SMG8, SMC4, STIM1, STK11IP, STK40, STON2, STS, TDRD1, TMEFF2, TMPRSS2-ERG, TNC, TP53, TP53BP2, TRANK1, TRAP1, U2AF1, UHRF1, ZC3H12A, ZC3H12C and ZDHHC18.

14. The pharmaceutical composition as a medicament according to any one of claims 9 to 13, wherein administering the pharmacologically effective amount of the tumor antigen peptides to the subject or group of subjects suffering from carcinoma is effective to reduce a tumor marker level, wherein the tumor marker is selected from the list consisting of CEA, PSA, CA 125, CA 19-9, AFP, hCG, HER2 / neu, BRCA1, BRCA2, EGFR, CA 15-3, CA 27.

29.

15. The pharmaceutical composition as a medicament according to any one of claims 9 to 14, wherein the HLA tumor antigen polypeptides corresponding to HLA tumor antigen peptides corresponding to MHC class I and class II complexes, respectively, are immunogenic HLA tumor antigen polypeptides as determined by an immunogenicity assay, by Western blot, ELISA techniques, ELISPOT or immunodetection with microscopic analysis; by at least a factor of 2 of the response of a corresponding blind test.

16. The pharmaceutical composition as a medicament according to any one of claims 9 to 15, wherein the HLA tumor antigen peptides are presented on the surface of the tumor cells of the carcinoma of at least one subject as determined by ultra-high performance liquid chromatography (UHPCL) in combination with ESI mass spectrometry (MS).

17. The pharmaceutical composition as a medicament according to any one of claims 9 to 16, wherein at least one HLA tumor antigen polypeptide is selected to match at least one HLA tumor antigen peptides that are presented on the surface of the tumor cells of the subject's or group of subjects' carcinoma as determined by ultra-high performance liquid chromatography (UHPCL) in conjunction with ESI mass spectrometry (MS).

18. The pharmaceutical composition as a medicament according to any one of claims 9 to 17, wherein the expression level of at least one HLA tumor antigen peptide in the tumor cells is at least three times higher than in the healthy cells of the subject or group of subjects having at least one identical HLA allele as determined by NGS or qPCR, and whereas the HLA tumor antigen peptides are associated with proliferation, invasiveness, angiogenesis, and an increase in cytokeratin production in carcinoma.

19. The pharmaceutical composition as a medicament according to any one of claims 9 to 18, wherein: - at least one HLA tumor antigen peptide is a tumor exclusive HLA tumor antigen peptide, and - specific binding of the tumor-exclusive HLA tumor antigen peptide determined against the corresponding MHC class I complex with a KD < 500 nM occurs as determined in-silico by bioinformatic tools.

20. The pharmaceutical composition as a medicament according to any one of claims 9 to 19, wherein the pharmacologically effective amount of each individual HLA tumor antigen polypeptide in the composition in an absolute concentration (i.e., administration dose) ranges from 100 to 1000 µg.

21. The pharmaceutical composition as a medicament according to any one of claims 9 to 20 for use as recited in claim 5, wherein the composition comprises an adjuvant which, when the composition is applied to a subject, is capable of forming a granuloma at the site of application.

22. The pharmaceutical composition as a medicament according to any one of claims 9 to 21, wherein the pharmaceutical composition is applied subcutaneously or intradermally and remote from a tumor lesion and / or the cancerous lymph node area.

23. The pharmaceutical composition as a medicament according to any one of claims 9 to 22, wherein at least one HLA tumor antigen peptide has at least one mutation relative to the wild-type HLA tumor antigen peptide (the mutanoma) that results in an increase in affinity for the T cell receptor of the individual treated with HLA tumor antigen peptide compared to the wild-type HLA tumor antigen peptide.

24. The pharmaceutical composition as a medicament according to any one of claims 9 to 23, wherein the pharmaceutical composition is used for the treatment of carcinoma as monotherapy or in combination with other known therapies and / or compounds for the treatment of carcinoma and is selected from the list consisting of pancreatic cancer (PaCa), liver metastasis (LMCa); bone cancer metastasis (BMCa), prostate cancer (PrCa), Breast Cancer (BrCa), Uterine Cancer (UCa), Brain Cancer (BrnCa), Bladder Cancer (BlCa), Thymus Cancer (ThCa), Biliary Tract Cancer (BiTCa), Skin Cancer (SkCa), Thyroid Cancer (ThdCa), Lung Cancer (LuCa), Colorectal Cancer (CoCa), Esophageal Cancer (EsCa), Stomach Cancer (StCa), Head and Neck Cancer (HNCa).

25. The pharmaceutical composition as a medicament according to any one of claims 9 to 24, wherein subjects to be treated with the pharmaceutical composition have received a standard therapy procedure (e.g., at least one of surgery, radiation, chemotherapy, and / or hormone therapy).

26. The pharmaceutical composition as a medicament according to any one of claims 9 to 25, wherein the pharmaceutical composition is administered as a first-line therapy to the subject or group of subjects having at least one identical HLA allele.

27. The pharmaceutical composition as a medicament according to any one of claims 9 to 26, wherein the pharmaceutical composition is administered to a group of subjects having at least one identical allele and at least one HLA tumor antigen polypeptide(s) presented on the cell membrane of the exclusive and / or associated tumor cell corresponding to an amino acid sequence of a tumor antigen polypeptide according to any one of the preceding claims.

28. The pharmaceutical composition as a medicament according to any one of claims 9 to 27, wherein the pharmaceutical composition, wherein the pharmaceutical composition is administered to a group of subjects having at least one identical allele, wherein the allele is selected from the list comprising of A*01:01, A*02:01, A*02:03, A*02:06, A*02:786, A*03:01, A*11:01, A*24:02, A*30:01, A*30:02, A*31:01, A*32:01, A*33:01, A*68:01, A*68:02, B*07:02, B*08:01, B*15:01, B*35:01, B*40:01, B*44:02, B*57:01, B*57:37, B*58:01, C*03:04, C*04:01, C*06:02, C*07:02, DQA1*01:01, DQB*102:01, DQB1*05:01, DQB1*06:02, DRB1*01:01, DRB1*15:01, E*01:01, and E*01:

03.

29. The pharmaceutical composition as a medicament according to any one of claims 9 to 28, wherein the pharmaceutical composition comprising each individual HLA tumor antigen polypeptide in the pharmaceutical composition at an absolute concentration (i.e., administration dose) of 100 to 1000 µg is administered intradermally or subcutaneously once every 2 weeks for a period of at least one year to a subject or group of subjects having at least one identical HLA allele.

30. A method for determining a pharmaceutical composition as a medicament according to claims 9 to 29, comprising or consisting of HLA tumor antigen polypeptides according to claims 1 to 8, comprising monitoring tissue resection of a subject or group of subjects suffering from or suspected of suffering from carcinoma, the method comprising the steps of: a) providing a tumor tissue sample (sample tissue) and a healthy cell sample of the subject or group of subjects, wherein said method step (a) of providing the tissue sample does not itself comprise any surgical intervention in the subject or one of the subjects of the group of subjects, thenb) sequencing the sample tissue and determine the following parameters using the provided tissue sample from step (a), providing whole exome and transcriptome, then c) creating a pre-selection of HLA tumor antigen peptides matching the MHC class I and class II complexes from the DNA whole exome and mRNA transcriptome of step b) using bioinformatics methods, somatic mutation discovery, weighting up- and / or down-regulated mRNA, HLA subtypes of the subject or subject group, association with proliferation, invasiveness, angiogenesis and an increase in cytokeratin production, exome sequence as well as presentation on the exclusive and / or associated tumor cells using algorithms, databases and neural networks, then d) creating an HLA tumor antigen polypeptide composition with a bioinformatic feedback loop pipeline, then e) testing the immunogenicity of the HLA tumor antigen polypeptides determined in step d) by means of an immunogenicity test, characterized in that the bioinformatic feedback loop pipeline comprises the at least the steps of i) weighting the sequences of the HLA tumor antigen peptides with neural networks and / or machine learning and / or weighting algorithms, wherein the weighting factors are selected from the list comprising of corresponding HLA alleles, MHC class I and II binding affinity scores; immunogenicity score, presentation score on tumor cell line; presentation percentile; overexpression score of at least factor 3 in relation to healthy cells; processing score, tumor associated scores; distribution factor in a group of subjects suffering from the same tumor type; point mutation score; sequence identity score; robustness score; exome portion score; biochemical scores, including pI, GRAVY, length of the amino acid sequence, charge, molecular weight, instability, then ii) matching at least two HLA tumor antigen peptides selected in step i) in the amino acid sequence of an HLA tumor antigen polypeptide using weighting algorithms and neural networks, thus creating at least one HLA tumor antigen polypeptide(s), then iii) assembling a pharmaceutical composition comprising at least two HLA tumor antigen polypeptides generated in step ii), wherein the composition comprising at least two HLA tumor antigen polypeptides is fed back to step i) to generate a feedback loop, validating the sequence score, checking for a high overexpression score at least once.

31. The method of claim 30, wherein after providing the tissue sample from the subject or group of subjects in step (a), commonly mutated genes exclusive for and / or associated with a carcinoma present in the group of subjects are analyzed for the presence of mutations.

32. The method according to claim 30 or 31, wherein the tissue sample provided in step (a) is the tissue sample of a carcinoma from a group of subjects suffering from or at risk of suffering from the same type of carcinoma.

33. The method of any one of claims 30 to 31, wherein determining whether the HLA tumor antigen peptides are presented on the surface of the cells of the tissue sample of the subject or group of subjects provided in step (a) is performed by ultra-high performance liquid chromatography (UHPCL) in conjunction with ESI mass spectrometry (MS).

34. The method of any one of claims 30 to 31, wherein the bioinformatics feedback loop pipeline comprises at least one neural network trained on a group of subjects having at least one common HLA allele and a similar tumor type.

35. The method of any one of claims 30 to 31, wherein the HLA tumor antigen polypeptides of the composition assembled in step iii) are individually tested at least for overexpression of a factor of at least three in an individual subject by application of step i) of the bioinformatic feedback loop pipeline.

36. A process for preparing a pharmaceutical composition according to any one of claims 9 to 29, comprising the following steps: (a) Determining at least a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides arranged on at least one HLA tumor antigen polypeptide(s) comprising a delivery aiding capping peptide according to any claims 1 to 13, corresponding to MHC class I and / or class II complexes exposed on the cell surface of cells from a carcinoma of the subject or group of subjects to be treated with at least one identical HLA allele by the determination method of any one of claims 35 to 40; (b) synthesizing at least one HLA tumor antigen polypeptide(s) comprising the 2 to 25 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes determined in step a); and (c) Preparing the pharmaceutical composition according to the invention comprising at least the 2 to 25 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) synthesized in step b), and an adjuvant as defined herein.

37. Combination drug for use in the treatment of carcinoma with simultaneous, separate, or sequential administration, comprising the following two separate preparations (a) and (b): (a) a first preparation comprising, together with a pharmaceutically acceptable carrier or diluent, a pharmacologically effective amount comprising 2 to 25 HLA tumor antigen peptides corresponding to MHC class I and / or class II complexes, arranged on at least one HLA tumor antigen polypeptide(s) comprising of any one a delivery aiding capping peptide of claims 1 to 13, and optionally determined by the method of any one of claims 38 to 43, and (b) a second preparation comprising, together with a pharmaceutically acceptable carrier or diluent, an anticancer agent selected from the group consisting of anticancer alkylating agents, anticancer antimetabolites, anticancer antibiotics, herbal anticancer agents, platinum-coordinated anticancer complex compounds, anticancer camptothecin derivatives, anticancer tyrosine kinase inhibitors, monoclonal antibodies, interferons, interleukins, biological response modifiers, and other anticancer agents, or a pharmaceutically acceptable salt thereof.

38. The combination preparation according to claim 42, wherein the second preparation is a monoclonal antibody.

39. The combination preparation of claim 42 or 43, wherein the second preparation is a hormone inhibitor for hormone positive subjects.

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