Protein:MTAP |
Protein Summary |
Gene summary |
| Gene name: MTAP | ASpdb.0 ID: 4507 | Gene | Gene symbol | MTAP | Gene ID | 4507 |
| Gene name | methylthioadenosine phosphorylase |
| Synonyms | BDMF|DMSFH|DMSMFH|HEL-249|LGMBF|MSAP|c86fus |
| Cytomap | 9p21.3 |
| Type of gene | protein-coding |
| Description | S-methyl-5'-thioadenosine phosphorylase5'-methylthioadenosine phosphorylaseMTA phosphorylaseMTAPaseMeSAdo phosphorylaseepididymis luminal protein 249epididymis secretory sperm binding protein |
| Modification date | 20240305 |
| UniProtAcc | Q13126 |
Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | MTAP | GO:0005654 | nucleoplasm | - |
| Gene | MTAP | GO:0005829 | cytosol | - |
| Gene | MTAP | GO:0006738 | nicotinamide riboside catabolic process | 19001417 |
AS Summary |
Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| Q13126-1 | Q13126-1_5tc5_A.pdb | 5TC5 | X-ray | 1.96 | A | 1 | 281 |
ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| Q13126 | MTAP | Q13126-1 | Q13126-2 | 283 | 346 | 272 | 283 | Substitution | NMAQFSVLLPRH | MIKFQMILSEGYHPFNIQESPFYRGLLDFPSVGHGRGKKCLSAPAIILRPPQPRGTVTTFKVSWSKDQTYICMKS | 272 | 346 |
| Q13126 | MTAP | Q13126-1 | Q13126-3 | 283 | 334 | 272 | 283 | Substitution | NMAQFSVLLPRH | MIKFQMILSEGYHPFNIQESPFYRGLLDFPSVGHGRGEILPLSPLDLAGYCFQQPMQPPCPDS | 272 | 334 |
| Q13126 | MTAP | Q13126-1 | Q13126-4 | 283 | 280 | 272 | 283 | Substitution | NMAQFSVLLPRH | VRSAFQLPP | 272 | 280 |
| Q13126 | MTAP | Q13126-1 | Q13126-5 | 283 | 305 | 231 | 283 | Substitution | VSVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH | MIKFQMILSEGYHPFNIQESPFYRGLLDFPSVGHGRGKKCLSAPAIILRPPQPRGTVTTFKVSWSKDQTYICMKS | 231 | 305 |
| Q13126 | MTAP | Q13126-1 | Q13126-6 | 283 | 293 | 231 | 283 | Substitution | VSVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH | MIKFQMILSEGYHPFNIQESPFYRGLLDFPSVGHGRGEILPLSPLDLAGYCFQQPMQPPCPDS | 231 | 293 |
| Q13126 | MTAP | Q13126-1 | Q13126-7 | 283 | 239 | 232 | 283 | Substitution | SVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH | RSAFQLPP | 232 | 239 |
Multiple sequence alignment of our canonical and alternatively spliced MTAP |
Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of MTAP |
| UniProt-id | ENSG | ENST | ENSP |
| Q13126-1 | ENSG00000099810.21 | ENST00000644715.2 | ENSP00000494373.1 |
| Q13126-3 | ENSG00000099810.21 | ENST00000580900.5 | ENSP00000463424.1 |
| UniProt-id | NM ID | NP ID |
| Q13126-1 | NM_002451.3 | NP_002442.2 |
Amino acid sequences of our canonical and alternatively spliced MTAP |
| accession_id | Protein sequence |
| Q13126-1 | MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHTIMPSKVNYQANIWALKEEGCTHVI VTTACGSLREEIQPGDIVIIDQFIDRTTMRPQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSR AESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNL |
| Q13126-2 | MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHTIMPSKVNYQANIWALKEEGCTHVI VTTACGSLREEIQPGDIVIIDQFIDRTTMRPQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSR AESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNL |
| Q13126-3 | MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHTIMPSKVNYQANIWALKEEGCTHVI VTTACGSLREEIQPGDIVIIDQFIDRTTMRPQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSR AESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNL |
| Q13126-4 | MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHTIMPSKVNYQANIWALKEEGCTHVI VTTACGSLREEIQPGDIVIIDQFIDRTTMRPQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSR AESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNL |
| Q13126-5 | MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHTIMPSKVNYQANIWALKEEGCTHVI VTTACGSLREEIQPGDIVIIDQFIDRTTMRPQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSR AESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAMIKFQMILSEGYHPFNIQESPFYRGLLDFPSVGHGRGKKC |
| Q13126-6 | MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHTIMPSKVNYQANIWALKEEGCTHVI VTTACGSLREEIQPGDIVIIDQFIDRTTMRPQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSR AESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAMIKFQMILSEGYHPFNIQESPFYRGLLDFPSVGHGRGEIL |
| Q13126-7 | MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHTIMPSKVNYQANIWALKEEGCTHVI VTTACGSLREEIQPGDIVIIDQFIDRTTMRPQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSR |
Protein Functional Features |
Main function of this protein. (from UniProt) |
| MTAP (go to UniProt):Q13126 |
Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
Gene Isoform Structures and Expression Levels for MTAP |
Gene structures of our canonical and alternative spliced genes of MTAP* Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
Expression levels of gene isoforms across GTEx. |
Expression levels of gene isoforms across TCGA. |
Protein Structures |
PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of Q13126-1 |
| 3D view using mol* of Q13126-2 |
| 3D view using mol* of Q13126-3 |
| 3D view using mol* of Q13126-4 |
| 3D view using mol* of Q13126-5 |
| 3D view using mol* of Q13126-6 |
| 3D view using mol* of Q13126-7 |
pLDDT Score Distribution |
pLDDT score distribution of the predicted protein structures from AlphaFold2* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
Ramachandran Plot of Protein Structures |
Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
Potential Active Site Information |
The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| Q13126-1 | 1.136 | 92 | 1.163 | 258.279 | 0.391 | 0.883 | 1.152 | 2.149 | 0.823 | 2.612 | 0.976 | 17,18,60,61,65,69,93,94,95,96,172,177,178,194,195, 196,197,219,220,222,233,236,237,240 |
| Q13126-2 | 1.153 | 100 | 1.195 | 245.931 | 0.405 | 0.855 | 1.086 | 1.889 | 0.79 | 2.39 | 1.024 | 17,18,60,61,65,69,93,94,95,96,172,175,177,178,194, 195,196,197,219,220,222,231,233,236,237 |
| Q13126-3 | 1.149 | 104 | 1.187 | 251.076 | 0.402 | 0.857 | 1.167 | 1.98 | 0.819 | 2.417 | 0.953 | 17,18,20,60,61,65,67,68,69,93,94,95,96,172,175,177 ,178,194,195,196,197,219,220,222,231,233,236,237,2 40 |
| Q13126-4 | 1.104 | 131 | 1.155 | 320.705 | 0.484 | 0.776 | 0.975 | 1.242 | 0.769 | 1.615 | 1.132 | 17,18,19,20,60,61,65,67,68,69,92,93,94,95,96,172,1 75,177,178,194,195,196,197,217,219,220,222,231,233 ,236,237,240,244,247 |
| Q13126-5 | 1.111 | 201 | 1.169 | 488.775 | 0.464 | 0.772 | 1.018 | 1.792 | 0.719 | 2.493 | 1.083 | 10,12,14,50,51,52,53,55,90,107,109,148,151,152,154 ,155,156,158,159,161,215,217,233,234,235,236,237,2 38,239,240,241,242,243,244 |
| Q13126-6 | 1.124 | 112 | 1.143 | 268.912 | 0.429 | 0.861 | 1.14 | 1.661 | 0.963 | 1.724 | 1.404 | 17,18,20,60,61,65,68,69,93,94,95,96,172,175,177,17 8,194,195,196,197,219,220,222,232,234,237,238 |
| Q13126-7 | 1.054 | 88 | 1.071 | 297.381 | 0.409 | 0.809 | 1.098 | 1.539 | 0.908 | 1.696 | 1.286 | 17,18,60,61,65,69,93,94,95,96,172,175,177,178,194, 195,196,197,219,220,222,231 |
Protein Structure and Feature Comparision |
Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of Q13126-1_Q13126-1_5tc5_A.pdb |
Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q13126-1_5tc5_A_Q13126-2.pdb |
| 3D view using mol* of Q13126-1_5tc5_A_Q13126-3.pdb |
| 3D view using mol* of Q13126-1_5tc5_A_Q13126-4.pdb |
| 3D view using mol* of Q13126-1_5tc5_A_Q13126-5.pdb |
| 3D view using mol* of Q13126-1_5tc5_A_Q13126-6.pdb |
| 3D view using mol* of Q13126-1_5tc5_A_Q13126-7.pdb |
Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q13126-1_Q13126-2.pdb |
| 3D view using mol* of Q13126-1_Q13126-3.pdb |
| 3D view using mol* of Q13126-1_Q13126-4.pdb |
| 3D view using mol* of Q13126-1_Q13126-5.pdb |
| 3D view using mol* of Q13126-1_Q13126-6.pdb |
| 3D view using mol* of Q13126-1_Q13126-7.pdb |
Protein Feature Comparison of the protein sequendary structures among the protiens. |
Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
Protein-Protein Interaction |
Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to MTAP |
Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| Q13126 | MTAP | DB02933 | 5'-Deoxy-5'-(Methylthio)-Tubercidin | experimental | |
| Q13126 | MTAP | DB02281 | Formycin | experimental | |
| Q13126 | MTAP | DB02282 | 5'-S-methyl-5'-thioadenosine | experimental | |
| Q13126 | MTAP | DB02158 | (2S,3S,4R,5S)-2-(4-Amino-4,5-dihydro-1H-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[(methylsulfanyl)methyl]-3,4-pyrrolidinediol | experimental | |
| Q13126 | MTAP | DB00173 | Adenine | approved, nutraceutical |
Related Diseases to MTAP |
Previous studies relating to the alternative splicing of MTAP and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| MTAP | 11566337 | Identification of a 1.2 Kb cDNA fragment from a region on 9p21 commonly deleted in multiple tumor types. | Chromosome band 9p21 is a frequent target of homozygous deletion in many tumor types. Putative tumor suppressor genes, CDKN2A (p16), p14(ARF) and CDKN2B (p15), were localized to 9p21. However, there have been reports that suggest that there may be other genes targeted for inactivation in the region. We have developed a method to search for transcribed sequences within large genomic regions. We tested our approach in a 100-kilobase region on 9p21, which is 40 kilobases telomeric to CDKN2A. The method, termed expressed sequence selection (ESS), resulted in the isolation of genomic fragments known to be from 9q21 that are homologous to transcribed sequences. One fragment was used to obtain a 1.2 kilobase cDNA. The sequence of the 5' half of the cDNA was almost identical to exons 3-5 of the MTAP gene, which maps to chromosome band 9p21. The 3' portion of the cDNA had sequence homology to the ALA gene, which maps to chromosome arm 9q. Using Northern blot analysis, the 1.2 Kb cDNA identified several widely expressed transcripts ranging from 1 Kb to 8.5 Kb and displayed a complex pattern of alternative splicing in which certain exons of the 1.2 Kb cDNA are excluded from some of the splice products. Using cancer tissue Northern blots, we could show that all of the transcripts are absent from a leukemia cell line and a lung cancer cell line (K562, A549) with homozygous, genomic deletions within chromosome band 9p21. In addition, the 7 Kb transcript is also absent from two additional tumor cell lines (Molt4, a leukemia derived cell line, and in G361, a melanoma derived cell line) with homozygous deletions. Further investigation will determine whether the difference in the expression pattern between the 7 Kb transcript compared with the other sized transcripts could be due to specific targeting for alteration in certain tumor types. | D009369 | Neoplasms |
Clinically important variants in MTAP |
(ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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