Q96F44 · TRI11_HUMAN
- ProteinE3 ubiquitin-protein ligase TRIM11
- GeneTRIM11
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids468 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX (By similarity).
Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis (By similarity).
May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences (By similarity).
May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway (By similarity).
Mediates MED15 ubiquitination leading to proteasomal degradation (PubMed:16904669).
May contribute to the innate restriction of retroviruses (PubMed:18248090).
Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression (PubMed:18248090).
Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain (PubMed:18248090).
May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle (PubMed:18248090).
Acts as an inhibitor of the AIM2 inflammasome by promoting autophagy-dependent degradation of AIM2 (PubMed:27498865).
Mechanistically, undergoes autoubiquitination upon DNA stimulation, promoting interaction with AIM2 and SQSTM1/p62, leading to AIM2 recruitment to autophagosomes (PubMed:27498865).
Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis (By similarity).
May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences (By similarity).
May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway (By similarity).
Mediates MED15 ubiquitination leading to proteasomal degradation (PubMed:16904669).
May contribute to the innate restriction of retroviruses (PubMed:18248090).
Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression (PubMed:18248090).
Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain (PubMed:18248090).
May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle (PubMed:18248090).
Acts as an inhibitor of the AIM2 inflammasome by promoting autophagy-dependent degradation of AIM2 (PubMed:27498865).
Mechanistically, undergoes autoubiquitination upon DNA stimulation, promoting interaction with AIM2 and SQSTM1/p62, leading to AIM2 recruitment to autophagosomes (PubMed:27498865).
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 | nucleoplasm | |
Molecular Function | protein domain specific binding | |
Molecular Function | protein-macromolecule adaptor activity | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin-protein transferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | innate immune response | |
Biological Process | negative regulation of AIM2 inflammasome complex assembly | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | negative regulation of neurogenesis | |
Biological Process | negative regulation of viral entry into host cell | |
Biological Process | negative regulation of viral transcription | |
Biological Process | positive regulation of viral entry into host cell | |
Biological Process | protein autoubiquitination | |
Biological Process | protein ubiquitination | |
Biological Process | regulation of gene expression | |
Biological Process | suppression of viral release by host |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase TRIM11
- 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 accessionQ96F44
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 53 | Abolished E3 ubiquitin-protein ligase activity. | ||||
Sequence: C → A | ||||||
Mutagenesis | 56 | Abolished E3 ubiquitin-protein ligase activity. | ||||
Sequence: C → A | ||||||
Mutagenesis | 169 | Does not affect autoubiquitination. | ||||
Sequence: K → R | ||||||
Mutagenesis | 366 | Does not affect autoubiquitination. | ||||
Sequence: K → R | ||||||
Mutagenesis | 458 | Reduced autoubiquitination, leading to abolish interaction with SQSTM1/p62. | ||||
Sequence: K → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 438 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, modified residue, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000056215 | 1-468 | UniProt | E3 ubiquitin-protein ligase TRIM11 | |||
Sequence: MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSPQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCPAHREPLAAFCGDELRLLCAACERSGEHWAHRVRPLQDAAEDLKAKLEKSLEHLRKQMQDALLFQAQADETCVLWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQRLEEEELEVLPRLREGAAHLGQQSAHLAELIAELEGRCQLPALGLLQDIKDALRRVQDVKLQPPEVVPMELRTVCRVPGLVETLRRFRGDVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGSYYNSSERALAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPEIPFSGTLRPLFSPLSSSPTPMTICRPKGGSGDTLAPQ | |||||||
Modified residue | 85 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 458 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Autoubiquitinated upon DNA stimulation; autoubiquitination at Lys-458 promotes interaction with SQSTM1/p62 and recruitment of AIM2 to autophagosomes.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binds cytoplasmic tail of integrin alpha-1 (PubMed:11331580).
Interacts with the HN peptide (By similarity).
Interacts with PHOX2B (By similarity).
Interacts (when autoubiquitinated) with SQSTM1/p62; promoting AIM2 recruitment to autophagosomes (PubMed:27498865).
Interacts with AIM2; promoting its autophagy-dependent degradation (PubMed:27498865).
Interacts with the HN peptide (By similarity).
Interacts with PHOX2B (By similarity).
Interacts (when autoubiquitinated) with SQSTM1/p62; promoting AIM2 recruitment to autophagosomes (PubMed:27498865).
Interacts with AIM2; promoting its autophagy-dependent degradation (PubMed:27498865).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q96F44 | MED15 Q96RN5 | 5 | EBI-851809, EBI-394506 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 16-57 | RING-type | ||||
Sequence: CAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECR | ||||||
Zinc finger | 87-128 | B box-type | ||||
Sequence: VPQGVCPAHREPLAAFCGDELRLLCAACERSGEHWAHRVRPL | ||||||
Coiled coil | 129-208 | |||||
Sequence: QDAAEDLKAKLEKSLEHLRKQMQDALLFQAQADETCVLWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQRLEEEELEVL | ||||||
Domain | 268-461 | B30.2/SPRY | ||||
Sequence: ELRTVCRVPGLVETLRRFRGDVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGSYYNSSERALAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPEIPFSGTLRPLFSPLSSSPTPMTICRPKGGS |
Domain
The coiled-coil domain and the B30.2 domain are both necessary for interaction with HN and PAX6 (By similarity).
They are also involved in MED15-binding (PubMed:16904669).
They are also involved in MED15-binding (PubMed:16904669).
The B30.2 domain may be involved cellular protein quality control by promoting the degradation of insoluble ubiquitinated proteins.
Sequence similarities
Belongs to the TRIM/RBCC family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q96F44-1
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
- Length468
- Mass (Da)52,774
- Last updated2002-12-06 v2
- Checksum8DE4BDF79F221739
Q96F44-2
- Name2
Q96F44-3
- Name3
- NoteMay be due to competing acceptor splice site.
- Differences from canonical
- 169-169: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_039628 | 169 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 234 | in Ref. 2; BAG53535 | ||||
Sequence: G → D | ||||||
Sequence conflict | 260 | in Ref. 2; BAG37129 | ||||
Sequence: Q → R | ||||||
Alternative sequence | VSP_012057 | 288-385 | in isoform 2 | |||
Sequence: DVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGS → RCGGPRWGDDSRRGPAKDLGSQPRVLCPATASSKLTVSWWWVVGKTSSAHTSDISCVGIFTPNNSSTSGNELGIQGFHSALNRIASADTTGVSTDPTD | ||||||
Sequence conflict | 289 | in Ref. 2; BAG53535 | ||||
Sequence: V → M | ||||||
Sequence conflict | 319 | in Ref. 2; BAG53535 | ||||
Sequence: P → S | ||||||
Alternative sequence | VSP_012058 | 386-468 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 395-398 | in Ref. 5; AAG53498 | ||||
Sequence: APLR → GSIP | ||||||
Sequence conflict | 467 | in Ref. 5; AAG53498 | ||||
Sequence: P → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF327056 EMBL· GenBank· DDBJ | AAM63957.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074866 EMBL· GenBank· DDBJ | BAC11254.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314539 EMBL· GenBank· DDBJ | BAG37129.1 EMBL· GenBank· DDBJ | mRNA | ||
AK097825 EMBL· GenBank· DDBJ | BAG53535.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK301859 EMBL· GenBank· DDBJ | BAG63300.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL670729 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC011629 EMBL· GenBank· DDBJ | AAH11629.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC069227 EMBL· GenBank· DDBJ | AAH69227.1 EMBL· GenBank· DDBJ | mRNA | ||
AF220125 EMBL· GenBank· DDBJ | AAG53498.1 EMBL· GenBank· DDBJ | mRNA |