| UniProt ID | TRI23_HUMAN | |
|---|---|---|
| UniProt AC | P36406 | |
| Protein Name | E3 ubiquitin-protein ligase TRIM23 | |
| Gene Name | TRIM23 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 574 | |
| Subcellular Localization | Cytoplasm . Endomembrane system . Golgi apparatus membrane . Lysosome membrane . Membrane-associated with the Golgi complex and lysosomal structures. | |
| Protein Description | Acts as an E3 ubiquitin-protein ligase. Plays an essential role in autophagy activation during viral infection. Mechanistically, activates TANK-binding kinase 1/TBK1 by facilitating its dimerization and ability to phosphorylate the selective autophagy receptor SQSTM1. In order to achieve this function, TRIM23 mediates 'Lys-27'-linked auto-ubiquitination of its ADP-ribosylation factor (ARF) domain to induce its GTPase activity and its recruitment to autophagosomes. [PubMed: 28871090; (Microbial infection) Mediates TRAF6 auto-ubiquitination in the presence of human cytomegalovirus protein UL144, resulting in the virally controlled activation of NF-kappa-B stimulation at early times of HCMV infection.] | |
| Protein Sequence | MATLVVNKLGAGVDSGRQGSRGTAVVKVLECGVCEDVFSLQGDKVPRLLLCGHTVCHDCLTRLPLHGRAIRCPFDRQVTDLGDSGVWGLKKNFALLELLERLQNGPIGQYGAAEESIGISGESIIRCDEDEAHLASVYCTVCATHLCSECSQVTHSTKTLAKHRRVPLADKPHEKTMCSQHQVHAIEFVCLEEGCQTSPLMCCVCKEYGKHQGHKHSVLEPEANQIRASILDMAHCIRTFTEEISDYSRKLVGIVQHIEGGEQIVEDGIGMAHTEHVPGTAENARSCIRAYFYDLHETLCRQEEMALSVVDAHVREKLIWLRQQQEDMTILLSEVSAACLHCEKTLQQDDCRVVLAKQEITRLLETLQKQQQQFTEVADHIQLDASIPVTFTKDNRVHIGPKMEIRVVTLGLDGAGKTTILFKLKQDEFMQPIPTIGFNVETVEYKNLKFTIWDVGGKHKLRPLWKHYYLNTQAVVFVVDSSHRDRISEAHSELAKLLTEKELRDALLLIFANKQDVAGALSVEEITELLSLHKLCCGRSWYIQGCDARSGMGLYEGLDWLSRQLVAAGVLDVA | |
| 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 |
|---|---|---|---|---|---|
| 8 | Ubiquitination | MATLVVNKLGAGVDS CCEEEEECCCCCCCC | 36.37 | 22505724 | |
| 15 | Phosphorylation | KLGAGVDSGRQGSRG CCCCCCCCCCCCCCC | 33.21 | - | |
| 20 | Phosphorylation | VDSGRQGSRGTAVVK CCCCCCCCCCCEEEE | 21.14 | - | |
| 171 | Ubiquitination | RRVPLADKPHEKTMC CCCCCCCCCCHHCCC | 42.54 | 29967540 | |
| 325 | Ubiquitination | LIWLRQQQEDMTILL HHHHHHHHCCHHHHH | 40.08 | 27667366 | |
| 357 | Ubiquitination | DCRVVLAKQEITRLL CCEEEEHHHHHHHHH | 44.28 | 30230243 | |
| 386 | Phosphorylation | DHIQLDASIPVTFTK HHCEECCCCCEEEEC | 27.39 | - | |
| 442 | Phosphorylation | TIGFNVETVEYKNLK CCCEEEEEEEEECCE | 17.85 | 22468782 | |
| 445 | Phosphorylation | FNVETVEYKNLKFTI EEEEEEEEECCEEEE | 10.80 | 22468782 | |
| 458 | Acetylation | TIWDVGGKHKLRPLW EEEECCCCCCCCCCH | 31.47 | 7978559 | |
| 468 | Phosphorylation | LRPLWKHYYLNTQAV CCCCHHEEECCCCEE | 13.11 | 22817900 | |
| 469 | Phosphorylation | RPLWKHYYLNTQAVV CCCHHEEECCCCEEE | 8.00 | 22817900 | |
| 501 | Ubiquitination | LAKLLTEKELRDALL HHHHHCHHHHHHHHH | 57.73 | 33845483 | |
| 550 | Phosphorylation | IQGCDARSGMGLYEG EECCCCCCCCCHHHC | 34.55 | - |
| 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 TRI23_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRI23_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 TRI23_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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