| UniProt ID | TRAF1_HUMAN | |
|---|---|---|
| UniProt AC | Q13077 | |
| Protein Name | TNF receptor-associated factor 1 | |
| Gene Name | TRAF1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 416 | |
| Subcellular Localization | ||
| Protein Description | Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2.. | |
| Protein Sequence | MASSSGSSPRPAPDENEFPFGCPPTVCQDPKEPRALCCAGCLSENPRNGEDQICPKCRGEDLQSISPGSRLRTQEKAHPEVAEAGIGCPFAGVGCSFKGSPQSVQEHEVTSQTSHLNLLLGFMKQWKARLGCGLESGPMALEQNLSDLQLQAAVEVAGDLEVDCYRAPCSESQEELALQHFMKEKLLAELEGKLRVFENIVAVLNKEVEASHLALATSIHQSQLDRERILSLEQRVVELQQTLAQKDQALGKLEQSLRLMEEASFDGTFLWKITNVTRRCHESACGRTVSLFSPAFYTAKYGYKLCLRLYLNGDGTGKRTHLSLFIVIMRGEYDALLPWPFRNKVTFMLLDQNNREHAIDAFRPDLSSASFQRPQSETNVASGCPLFFPLSKLQSPKHAYVKDDTMFLKCIVETST | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MASSSGSSPR -----CCCCCCCCCC | 24.60 | 30108239 | |
| 4 | Phosphorylation | ----MASSSGSSPRP ----CCCCCCCCCCC | 29.22 | 30108239 | |
| 5 | Phosphorylation | ---MASSSGSSPRPA ---CCCCCCCCCCCC | 39.95 | 28450419 | |
| 7 | Phosphorylation | -MASSSGSSPRPAPD -CCCCCCCCCCCCCC | 38.83 | 30108239 | |
| 8 | Phosphorylation | MASSSGSSPRPAPDE CCCCCCCCCCCCCCC | 28.58 | 29507054 | |
| 43 | Phosphorylation | LCCAGCLSENPRNGE EEECCCCCCCCCCCC | 39.13 | 30108239 | |
| 61 | Ubiquitination | CPKCRGEDLQSISPG CCCCCCCCCCCCCCC | 53.48 | 22817900 | |
| 63 | Ubiquitination | KCRGEDLQSISPGSR CCCCCCCCCCCCCCC | 51.55 | 22817900 | |
| 64 | Phosphorylation | CRGEDLQSISPGSRL CCCCCCCCCCCCCCC | 32.12 | 28450419 | |
| 66 | Phosphorylation | GEDLQSISPGSRLRT CCCCCCCCCCCCCCC | 28.58 | 30266825 | |
| 69 | Phosphorylation | LQSISPGSRLRTQEK CCCCCCCCCCCCCHH | 31.37 | 30266825 | |
| 71 | Ubiquitination | SISPGSRLRTQEKAH CCCCCCCCCCCHHHC | 8.12 | 22817900 | |
| 96 | Phosphorylation | PFAGVGCSFKGSPQS CCCCCCCCCCCCCCC | 24.86 | 30108239 | |
| 100 | Phosphorylation | VGCSFKGSPQSVQEH CCCCCCCCCCCHHEE | 21.98 | 30108239 | |
| 103 | Phosphorylation | SFKGSPQSVQEHEVT CCCCCCCCHHEEECC | 29.20 | 30108239 | |
| 110 | Phosphorylation | SVQEHEVTSQTSHLN CHHEEECCCHHHHHH | 16.48 | 30108239 | |
| 111 | Phosphorylation | VQEHEVTSQTSHLNL HHEEECCCHHHHHHH | 36.31 | 30108239 | |
| 113 | Phosphorylation | EHEVTSQTSHLNLLL EEECCCHHHHHHHHH | 20.20 | 30108239 | |
| 114 | Phosphorylation | HEVTSQTSHLNLLLG EECCCHHHHHHHHHH | 20.52 | 30108239 | |
| 124 | Ubiquitination | NLLLGFMKQWKARLG HHHHHHHHHHHHHHC | 51.23 | 22817900 | |
| 127 | Ubiquitination | LGFMKQWKARLGCGL HHHHHHHHHHHCCCC | 22.57 | 22817900 | |
| 146 | Phosphorylation | MALEQNLSDLQLQAA CCHHHCHHHHHHHHH | 43.77 | - | |
| 170 | Phosphorylation | DCYRAPCSESQEELA EEEECCCCCCHHHHH | 38.94 | 30108239 | |
| 172 | Phosphorylation | YRAPCSESQEELALQ EECCCCCCHHHHHHH | 26.97 | 30108239 | |
| 183 | Ubiquitination | LALQHFMKEKLLAEL HHHHHHHHHHHHHHH | 51.24 | 22817900 | |
| 185 | Ubiquitination | LQHFMKEKLLAELEG HHHHHHHHHHHHHHH | 43.19 | 22817900 | |
| 193 | Ubiquitination | LLAELEGKLRVFENI HHHHHHHHHHHHHHH | 24.60 | 22817900 | |
| 275 | Ubiquitination | TFLWKITNVTRRCHE EEEEEEECHHHHHHH | 36.31 | 25015289 | |
| 310 | Phosphorylation | YKLCLRLYLNGDGTG CEEEEEEEECCCCCC | 7.53 | - | |
| 316 | Phosphorylation | LYLNGDGTGKRTHLS EEECCCCCCCCCEEE | 44.24 | - | |
| 320 | Phosphorylation | GDGTGKRTHLSLFIV CCCCCCCCEEEEEEE | 30.56 | 22210691 | |
| 323 | Phosphorylation | TGKRTHLSLFIVIMR CCCCCEEEEEEEEEC | 17.40 | 22210691 | |
| 395 | Phosphorylation | FPLSKLQSPKHAYVK EEHHHCCCCCCEEEC | 46.48 | 26091039 | |
| 397 | Ubiquitination | LSKLQSPKHAYVKDD HHHCCCCCCEEECCC | 46.22 | 25015289 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| - | K | Ubiquitination | E3 ubiquitin ligase | RNF31 | Q96EP0 | PMID:25996949 |
| - | K | Ubiquitination | E3 ubiquitin ligase | BIRC2 | Q13490 | PMID:15468071 |
| - | K | Ubiquitination | E3 ubiquitin ligase | BIRC3 | Q13489 | PMID:15468071 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRAF1_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of TRAF1_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Ubiquitylation | |
| Reference | PubMed |
| "Mass spectrometric analysis of tumor necrosis factor receptor-associated factor 1 ubiquitination mediated by cellular inhibitor ofapoptosis 2."; Lee J.S., Hong U.S., Lee T.H., Yoon S.K., Yoon J.B.; Proteomics 4:3376-3382(2004). Cited for: UBIQUITINATION AT LYS-185 AND LYS-193, MASS SPECTROMETRY, ANDMUTAGENESIS OF LYS-185 AND LYS-193. | |