Protein Name:
E3 ubiquitin/ISG15 ligase TRIM25
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UniprotKB/SwissProt ID: Q61510 (Q61510)
Gene Name:
Trim25
Organism: Mus musculus (Mouse)
Function: Functions as a ubiquitin E3 ligase and as an ISG15 E3 ligase. Involved in innate immune defense against viruses by mediating ubiquitination of RIGI and IFIH1. Mediates 'Lys-63'-linked polyubiquitination of the RIGI N-terminal CARD-like region and may play a role in signal transduction that leads to the production of interferons in response to viral infection. Mediates 'Lys-63'-linked polyubiquitination of IFIH1. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway. Mediates estrogen action in various target organs. Mediates the ubiquitination and subsequent proteasomal degradation of ZFHX3 (By similarity). Plays a role in promoting the restart of stalled replication forks via interaction with the KHDC3L-OOEP scaffold and subsequent ubiquitination of BLM, resulting in the recruitment and retainment of BLM at DNA replication forks (PubMed:29125140). Plays an essential role in the antiviral activity of ZAP/ZC3HAV1; an antiviral protein which inhibits the replication of certain viruses. Mechanistically, mediates 'Lys-63'-linked polyubiquitination of ZAP/ZC3HAV1 that is required for its optimal binding to target mRNA. Also mediates the ubiquitination of various substrates implicated in stress granule formation, nonsense-mediated mRNA decay, nucleoside synthesis and mRNA translation and stability (By similarity)
Other Modifications: View all modification sites in dbPTM
Protein Subcellular Localization: Cytoplasm. Cytoplasm, Stress granule. Nucleus
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Graphical Visualization of S-nitrosylation Sites:
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The S-nitrosylation sites of Q61510
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| No. |
Position |
S-nitrosylated Peptide |
Secondary Structure of S-nitrosylated Peptide |
Solvent Accessibility of nitrosylated Site |
PubMed ID |
| 1 |
106 |
SASSAATQVA C DHCLTEIAVK |
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| 2 |
529 |
WEVELQKNNF C GVGICYGSME |
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