| UniProt ID | TRI65_HUMAN | |
|---|---|---|
| UniProt AC | Q6PJ69 | |
| Protein Name | Tripartite motif-containing protein 65 | |
| Gene Name | TRIM65 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 517 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MAAQLLEEKLTCAICLGLYQDPVTLPCGHNFCGACIRDWWDRCGKACPECREPFPDGAELRRNVALSGVLEVVRAGPARDPGPDPGPGPDPAARCPRHGRPLELFCRTEGRCVCSVCTVRECRLHERALLDAERLKREAQLRASLEVTQQQATQAEGQLLELRKQSSQIQNSACILASWVSGKFSSLLQALEIQHTTALRSIEVAKTQALAQARDEEQRLRVHLEAVARHGCRIRELLEQVDEQTFLQESQLLQPPGPLGPLTPLQWDEDQQLGDLKQLLSRLCGLLLEEGSHPGAPAKPVDLAPVEAPGPLAPVPSTVCPLRRKLWQNYRNLTFDPVSANRHFYLSRQDQQVKHCRQSRGPGGPGSFELWQVQCAQSFQAGHHYWEVRASDHSVTLGVSYPQLPRCRLGPHTDNIGRGPCSWGLCVQEDSLQAWHNGEAQRLPGVSGRLLGMDLDLASGCLTFYSLEPQTQPLYTFHALFNQPLTPVFWLLEGRTLTLCHQPGAVFPLGPQEEVLS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAAQLLEEK ------CHHHHHHHH | 12.15 | 22223895 | |
| 144 | Phosphorylation | REAQLRASLEVTQQQ HHHHHHHHHHHHHHH | 20.73 | 22210691 | |
| 148 | Phosphorylation | LRASLEVTQQQATQA HHHHHHHHHHHHHHH | 15.98 | 22210691 | |
| 153 | Phosphorylation | EVTQQQATQAEGQLL HHHHHHHHHHHHHHH | 24.79 | 22210691 | |
| 167 | Phosphorylation | LELRKQSSQIQNSAC HHHHHHCHHHHHHHH | 28.89 | - | |
| 185 | Phosphorylation | SWVSGKFSSLLQALE HHHHCHHHHHHHHHH | 24.46 | - | |
| 206 | Ubiquitination | LRSIEVAKTQALAQA HHHHHHHHHHHHHHC | 46.47 | 27667366 | |
| 219 | Ubiquitination | QARDEEQRLRVHLEA HCCCHHHHHHHHHHH | 27.95 | 27667366 | |
| 277 | Ubiquitination | DQQLGDLKQLLSRLC CCCHHHHHHHHHHHH | 43.57 | - | |
| 299 | Ubiquitination | SHPGAPAKPVDLAPV CCCCCCCCCCCCCCC | 44.51 | 29967540 | |
| 317 | Phosphorylation | GPLAPVPSTVCPLRR CCCCCCCCCCCHHHH | 33.43 | 32142685 | |
| 325 | Ubiquitination | TVCPLRRKLWQNYRN CCCHHHHHHHHHHHC | 47.87 | 21906983 | |
| 334 | Phosphorylation | WQNYRNLTFDPVSAN HHHHHCCCCCCCCCC | 29.55 | 28857561 | |
| 338 | Ubiquitination | RNLTFDPVSANRHFY HCCCCCCCCCCCCEE | 10.19 | 21890473 | |
| 339 | Phosphorylation | NLTFDPVSANRHFYL CCCCCCCCCCCCEEE | 25.80 | 32142685 | |
| 342 | Methylation | FDPVSANRHFYLSRQ CCCCCCCCCEEECHH | 22.47 | 115918961 | |
| 367 | Phosphorylation | RGPGGPGSFELWQVQ CCCCCCCCEEEEEEE | 20.77 | - | |
| 413 | Phosphorylation | RCRLGPHTDNIGRGP CCCCCCCCCCCCCCC | 33.60 | - |
| 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 TRI65_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRI65_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 TRI65_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| MKRN3_HUMAN | MKRN3 | physical | 22493164 | |
| TNR6A_HUMAN | TNRC6A | physical | 24778252 |
| 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. | ||||||
loading...
| Acetylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |