| UniProt ID | T3JAM_HUMAN | |
|---|---|---|
| UniProt AC | Q9Y228 | |
| Protein Name | TRAF3-interacting JNK-activating modulator | |
| Gene Name | TRAF3IP3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 551 | |
| Subcellular Localization |
Membrane Single-pass type IV membrane protein . |
|
| Protein Description | May function as an adapter molecule that regulates TRAF3-mediated JNK activation.. | |
| Protein Sequence | MISPDPRPSPGLARWAESYEAKCERRQEIRESRRCRPNVTTCRQVGKTLRIQQREQLQRARLQQFFRRRNLELEEKGKAQHPQAREQGPSRRPGQVTVLKEPLSCARRISSPREQVTGTSSEVFPAQHPPPSGICRDLSDHLSSQAGGLPPQDTPIKKPPKHHRGTQTKAEGPTIKNDASQQTNYGVAVLDKEIIQLSDYLKEALQRELVLKQKMVILQDLLSTLIQASDSSWKGQLNEDKLKGKLRSLENQLYTCTQKYSPWGMKKVLLEMEDQKNSYEQKAKESLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLKRSEAEKLTLVTRVQQLQGLLQNQSLQLQEQEKLLTKKDQALPVWSPKSFPNEVEPEGTGKEKDWDLRDQLQKKTLQLQAKEKECRELHSELDNLSDEYLSCLRKLQHCREELNQSQQLPPRRQCGRWLPVLMVVIAAALAVFLANKDNLMI | |
| 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 | -----MISPDPRPSP -----CCCCCCCCCC | 23.19 | 23401153 | |
| 9 | Phosphorylation | ISPDPRPSPGLARWA CCCCCCCCCCHHHHH | 32.64 | 30108239 | |
| 78 | Ubiquitination | LELEEKGKAQHPQAR CHHHHCCCCCCCHHH | 56.81 | - | |
| 110 | Phosphorylation | LSCARRISSPREQVT CCCCHHCCCCCHHCC | 32.26 | 24247654 | |
| 111 | Phosphorylation | SCARRISSPREQVTG CCCHHCCCCCHHCCC | 26.13 | 28634298 | |
| 117 | Phosphorylation | SSPREQVTGTSSEVF CCCCHHCCCCCCCCC | 34.14 | 28634298 | |
| 119 | Phosphorylation | PREQVTGTSSEVFPA CCHHCCCCCCCCCCC | 21.51 | 28634298 | |
| 120 | Phosphorylation | REQVTGTSSEVFPAQ CHHCCCCCCCCCCCC | 26.33 | 28634298 | |
| 121 | Phosphorylation | EQVTGTSSEVFPAQH HHCCCCCCCCCCCCC | 37.30 | 28634298 | |
| 154 | Phosphorylation | GGLPPQDTPIKKPPK CCCCCCCCCCCCCCC | 22.97 | - | |
| 180 | Phosphorylation | PTIKNDASQQTNYGV CCCCCCHHHCCCCEE | 26.19 | - | |
| 183 | Phosphorylation | KNDASQQTNYGVAVL CCCHHHCCCCEEEEE | 23.83 | 22115753 | |
| 185 | Phosphorylation | DASQQTNYGVAVLDK CHHHCCCCEEEEECH | 19.16 | 22817900 | |
| 192 | Ubiquitination | YGVAVLDKEIIQLSD CEEEEECHHHHHHHH | 46.80 | - | |
| 202 | Ubiquitination | IQLSDYLKEALQREL HHHHHHHHHHHHHHH | 34.41 | - | |
| 254 | Phosphorylation | RSLENQLYTCTQKYS HHHHHHHHHHCHHCC | 7.04 | 22817900 | |
| 255 | Phosphorylation | SLENQLYTCTQKYSP HHHHHHHHHCHHCCC | 20.05 | 22115753 | |
| 257 | Phosphorylation | ENQLYTCTQKYSPWG HHHHHHHCHHCCCCC | 21.94 | 28122231 | |
| 260 | Phosphorylation | LYTCTQKYSPWGMKK HHHHCHHCCCCCHHH | 15.33 | 22817900 | |
| 261 | Phosphorylation | YTCTQKYSPWGMKKV HHHCHHCCCCCHHHH | 22.63 | 27080861 | |
| 267 | Ubiquitination | YSPWGMKKVLLEMED CCCCCHHHHHHHHHH | 29.26 | 17203973 | |
| 272 | Sulfoxidation | MKKVLLEMEDQKNSY HHHHHHHHHHHCCHH | 7.49 | 21406390 | |
| 276 | Ubiquitination | LLEMEDQKNSYEQKA HHHHHHHCCHHHHHH | 61.25 | - | |
| 294 | Ubiquitination | LQKVLEEKMNAEQQL HHHHHHHHCCHHHHH | 28.25 | - | |
| 295 | Sulfoxidation | QKVLEEKMNAEQQLQ HHHHHHHCCHHHHHH | 6.94 | 21406390 | |
| 314 | Ubiquitination | SLALAEQKCEEWRSQ HHHHHHHHHHHHHHH | 34.81 | - | |
| 320 | Phosphorylation | QKCEEWRSQYEALKE HHHHHHHHHHHHHHH | 37.88 | 22115753 | |
| 322 | Phosphorylation | CEEWRSQYEALKEDW HHHHHHHHHHHHHHH | 12.38 | 28796482 | |
| 326 | Ubiquitination | RSQYEALKEDWRTLG HHHHHHHHHHHHHHH | 61.75 | - | |
| 349 | Ubiquitination | QLHVLQSKLQGADSR HHHHHHHHHCCCCHH | 31.69 | - | |
| 349 | Acetylation | QLHVLQSKLQGADSR HHHHHHHHHCCCCHH | 31.69 | 25953088 | |
| 360 | Sulfoxidation | ADSRDLQMNQALRFL CCHHHHHHHHHHHHH | 5.36 | 21406390 | |
| 377 | Ubiquitination | EHQQLQAKIECLQGD HHHHHHHHHHHHHCC | 26.52 | - | |
| 400 | Ubiquitination | QDLQDQLKRSEAEKL HHHHHHHHHHHHHHH | 48.52 | - | |
| 406 | Ubiquitination | LKRSEAEKLTLVTRV HHHHHHHHHHHHHHH | 54.54 | - | |
| 445 | Phosphorylation | DQALPVWSPKSFPNE HHCCCCCCCCCCCCC | 23.76 | 22115753 | |
| 447 | Ubiquitination | ALPVWSPKSFPNEVE CCCCCCCCCCCCCCC | 60.25 | - | |
| 448 | Phosphorylation | LPVWSPKSFPNEVEP CCCCCCCCCCCCCCC | 49.69 | 26074081 | |
| 462 | Ubiquitination | PEGTGKEKDWDLRDQ CCCCCCCCCCCHHHH | 68.55 | - | |
| 472 | Ubiquitination | DLRDQLQKKTLQLQA CHHHHHHHHHHHHHH | 57.21 | - | |
| 473 | Ubiquitination | LRDQLQKKTLQLQAK HHHHHHHHHHHHHHH | 41.32 | - | |
| 480 | Ubiquitination | KTLQLQAKEKECREL HHHHHHHHHHHHHHH | 57.25 | - | |
| 498 | Phosphorylation | LDNLSDEYLSCLRKL HHHCCHHHHHHHHHH | 14.65 | 27642862 | |
| 500 | Phosphorylation | NLSDEYLSCLRKLQH HCCHHHHHHHHHHHH | 15.37 | 24719451 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of T3JAM_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of T3JAM_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 T3JAM_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 |
| "The proteomic reactor facilitates the analysis of affinity-purifiedproteins by mass spectrometry: application for identifyingubiquitinated proteins in human cells."; Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,Haines D.S., Figeys D.; J. Proteome Res. 6:298-305(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-267, AND MASSSPECTROMETRY. | |