TRIM11
entrez
81559
canonical
uniprot
Q96F44
canonical
ensembl
ENSG00000154370
resolver
ensp
ENSP00000284551
resolver
ensp
ENSP00000524619
resolver
ensp
ENSP00000603065
resolver
genesymbol
TRIM11
resolver
genesymbol_syn
RNF92
resolver
hgnc
HGNC:16281
resolver
uniprot
A6NKE2
resolver
uniprot
B2RB82
resolver
uniprot
B3KUS3
resolver
uniprot
B4DX88
resolver
uniprot
Q5VSU1
resolver
uniprot
Q8NCA6
resolver
uniprot
Q9C022
resolver
uniprot_entry
TRI11_HUMAN
resolver
uniprot_sec
A6NKE2
resolver
uniprot_sec
B2RB82
resolver
uniprot_sec
B3KUS3
resolver
uniprot_sec
B4DX88
resolver
uniprot_sec
Q5VSU1
resolver
uniprot_sec
Q8NCA6
resolver
uniprot_sec
Q9C022
resolver
amino_acid_sequence
MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSPQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCPAHREPLAAFCGDELRLLCAACERSGEHWAHRVRPLQDAAEDLKAKLEKSLEHLRKQMQDALLFQAQADETCVLWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQRLEEEELEVLPRLREGAAHLGQQSAHLAELIAELEGRCQLPALGLLQDIKDALRRVQDVKLQPPEVVPMELRTVCRVPGLVETLRRFRGDVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGSYYNSSERALAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPEIPFSGTLRPLFSPLSSSPTPMTICRPKGGSGDTLAPQ
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
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). {ECO:0000250|UniProtKB:Q99PQ2, ECO:0000269|PubMed:16904669, ECO:0000269|PubMed:18248090, ECO:0000269|PubMed:27498865}.
uniprot
proteins
mass_dalton
52774
uniprot
proteins
mutagenesis
MUTAGEN 53; /note="C->A: Abolished E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:27498865"; MUTAGEN 56; /note="C->A: Abolished E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:27498865"; MUTAGEN 169; /note="K->R: Does not affect autoubiquitination."; /evidence="ECO:0000269|PubMed:27498865"; MUTAGEN 366; /note="K->R: Does not affect autoubiquitination."; /evidence="ECO:0000269|PubMed:27498865"; MUTAGEN 458; /note="K->R: Reduced autoubiquitination, leading to abolish interaction with SQSTM1/p62."; /evidence="ECO:0000269|PubMed:27498865
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:16904669, ECO:0000269|PubMed:27498865}.
uniprot
proteins
post_translational_modification
PTM: Autoubiquitinated upon DNA stimulation; autoubiquitination at Lys-458 promotes interaction with SQSTM1/p62 and recruitment of AIM2 to autophagosomes. {ECO:0000269|PubMed:27498865}.
uniprot
proteins
protein_family
TRIM/RBCC family
uniprot
proteins
pubmed
11331580
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16904669
uniprot
proteins
pubmed
18248090
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27498865
uniprot
proteins
pubmed
40821731
uniprot
proteins
sequence_length
468
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16904669, ECO:0000269|PubMed:18248090}. Nucleus {ECO:0000269|PubMed:16904669}.
uniprot
proteins