Q96A61 · TRI52_HUMAN
- ProteinE3 ubiquitin-protein ligase TRIM52
- GeneTRIM52
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids297 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin-protein ligase (PubMed:27667714).
Positively regulates the NF-kappa-B signaling pathway (PubMed:27667714, PubMed:28073078).
Positively regulates the NF-kappa-B signaling pathway (PubMed:27667714, PubMed:28073078).
(Microbial infection) Exhibits antiviral activity against Japanese encephalitis virus (JEV). Ubiquitinates the viral non-structural protein 2 (NS2A) and targets it for proteasome-mediated degradation.
Miscellaneous
Arose via a partial duplication of the TRIM41 gene, followed by independent loss or pseudogenization of TRIM52 in multiple mammalian and primate lineages.
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | transcription coactivator activity | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | zinc ion binding | |
Biological Process | defense response to virus | |
Biological Process | positive regulation of canonical NF-kappaB signal transduction | |
Biological Process | positive regulation of NF-kappaB transcription factor activity | |
Biological Process | protein autoubiquitination | |
Biological Process | protein ubiquitination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase TRIM52
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96A61
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
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The viewer provides 316 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056280 | 1-297 | E3 ubiquitin-protein ligase TRIM52 | |||
Sequence: MAGYATTPSPMQTLQEEAVCAICLDYFKDPVSISCGHNFCRGCVTQLWSKEDEEDQNEEEDEWEEEEDEEAVGAMDGWDGSIREVLYRGNADEELFQDQDDDELWLGDSGITNWDNVDYMWDEEEEEEEEDQDYYLGGLRPDLRIDVYREEEILEAYDEDEDEELYPDIHPPPSLPLPGQFTCPQCRKSFTRRSFRPNLQLANMVQIIRQMCPTPYRGNRSNDQGMCFKHQEALKLFCEVDKEAICVVCRESRSHKQHSVLPLEEVVQEYQEIKLETTLVGILQIEQESIHSKAYNQ |
Post-translational modification
Autoubiquitinated (PubMed:27667714).
Polyubiquitinated (PubMed:20596523, PubMed:27667714).
Undergoes extremely rapid proteolytic degradation by the proteasome (PubMed:31133683).
Polyubiquitinated (PubMed:20596523, PubMed:27667714).
Undergoes extremely rapid proteolytic degradation by the proteasome (PubMed:31133683).
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for zinc finger, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 20-62 | RING-type; degenerate | ||||
Sequence: CAICLDYFKDPVSISCGHNFCRGCVTQLWSKEDEEDQNEEEDE | ||||||
Region | 72-167 | Important for rapid proteolytic degradation by the proteasome | ||||
Sequence: VGAMDGWDGSIREVLYRGNADEELFQDQDDDELWLGDSGITNWDNVDYMWDEEEEEEEEDQDYYLGGLRPDLRIDVYREEEILEAYDEDEDEELYP | ||||||
Zinc finger | 222-263 | B box-type | ||||
Sequence: NDQGMCFKHQEALKLFCEVDKEAICVVCRESRSHKQHSVLPL |
Domain
The RING-type zinc finger domain is essential for its E3 ubiquitin-protein ligase activity, ability to positively regulate the NF-kappa-B signaling pathway and its antiviral activity.
Sequence similarities
Belongs to the TRIM/RBCC family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q96A61-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length297
- Mass (Da)34,653
- Last updated2001-12-01 v1
- Checksum13381ED57BDCC6AB
Q96A61-2
- Name2
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5KRY2 | A0A8I5KRY2_HUMAN | TRIM52 | 272 | ||
A0A8I5KQM7 | A0A8I5KQM7_HUMAN | TRIM52 | 287 | ||
A0A8I5KW90 | A0A8I5KW90_HUMAN | TRIM52 | 277 | ||
A0A8I5KYD8 | A0A8I5KYD8_HUMAN | TRIM52 | 285 | ||
A0A8I5KXP2 | A0A8I5KXP2_HUMAN | TRIM52 | 307 | ||
A0A8I5KXQ2 | A0A8I5KXQ2_HUMAN | TRIM52 | 331 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JX896146 EMBL· GenBank· DDBJ | AGA17664.1 EMBL· GenBank· DDBJ | mRNA | ||
AK054802 EMBL· GenBank· DDBJ | BAB70809.1 EMBL· GenBank· DDBJ | mRNA | ||
AB209243 EMBL· GenBank· DDBJ | BAD92480.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC008443 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471165 EMBL· GenBank· DDBJ | EAW53704.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC007372 EMBL· GenBank· DDBJ | AAH07372.1 EMBL· GenBank· DDBJ | mRNA |