| UniProt ID | TRI63_HUMAN | |
|---|---|---|
| UniProt AC | Q969Q1 | |
| Protein Name | E3 ubiquitin-protein ligase TRIM63 | |
| Gene Name | TRIM63 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 353 | |
| Subcellular Localization | Cytoplasm. Nucleus. Cytoplasm, myofibril, sarcomere, M line. Cytoplasm, myofibril, sarcomere, Z line. Colocalizes with TNNI3 in myocytes (By similarity). Localizes to the M- and Z-lines in skeletal muscle.. | |
| Protein Description | E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.. | |
| Protein Sequence | MDYKSSLIQDGNPMENLEKQLICPICLEMFTKPVVILPCQHNLCRKCANDIFQAANPYWTSRGSSVSMSGGRFRCPTCRHEVIMDRHGVYGLQRNLLVENIIDIYKQECSSRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSMCKVFGIHKACEVAPLQSVFQGQKTELNNCISMLVAGNDRVQTIITQLEDSRRVTKENSHQVKEELSQKFDTLYAILDEKKSELLQRITQEQEKKLSFIEALIQQYQEQLDKSTKLVETAIQSLDEPGGATFLLTAKQLIKSIVEASKGCQLGKTEQGFENMDFFTLDLEHIADALRAIDFGTDEEEEEFIEEEDQEEEESTEGKEEGHQ | |
| 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 |
|---|---|---|---|---|---|
| 64 | Phosphorylation | PYWTSRGSSVSMSGG CCCCCCCCCEEECCC | 26.85 | 22817900 | |
| 67 | Phosphorylation | TSRGSSVSMSGGRFR CCCCCCEEECCCEEE | 14.80 | 22817900 | |
| 69 | Phosphorylation | RGSSVSMSGGRFRCP CCCCEEECCCEEECC | 30.50 | 22817900 | |
| 118 | Phosphorylation | SRPLQKGSHPMCKEH CCCCCCCCCCCCCCC | 31.30 | 25690035 | |
| 186 | Phosphorylation | AGNDRVQTIITQLED HCCHHHHHHHHHHHH | 16.10 | 26270265 | |
| 189 | Phosphorylation | DRVQTIITQLEDSRR HHHHHHHHHHHHHCC | 24.21 | 26270265 | |
| 194 | Phosphorylation | IITQLEDSRRVTKEN HHHHHHHHCCCCCCC | 16.77 | 26270265 | |
| 285 | Phosphorylation | TAKQLIKSIVEASKG CHHHHHHHHHHHHCC | 25.52 | 27762562 | |
| 290 | O-linked_Glycosylation | IKSIVEASKGCQLGK HHHHHHHHCCCCCCC | 18.97 | 30379171 |
| 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 TRI63_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRI63_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 TRI63_HUMAN !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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