Trim11
entrez
94091
canonical
uniprot
Q99PQ2
canonical
ensembl
ENSMUSG00000020455
resolver
ensp
ENSMUSP00000090749
resolver
ensp
ENSMUSP00000104438
resolver
ensp
ENSMUSP00000322697
resolver
ensp
ENSMUSP00000322705
resolver
genesymbol
Trim11
resolver
uniprot
A2A868
resolver
uniprot
A2AB84
resolver
uniprot
Q3TCL5
resolver
uniprot
Q8VDX5
resolver
uniprot_entry
TRI11_MOUSE
resolver
uniprot_sec
A2A868
resolver
uniprot_sec
A2AB84
resolver
uniprot_sec
Q3TCL5
resolver
uniprot_sec
Q8VDX5
resolver
amino_acid_sequence
MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSAQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCAAHREPLTTFCGDDLSLLCPICERSEHWTHRVRPLQEAADDLKGRLEKSLEHLRKQMEDAMLFQAQAEETCALWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQKLEEEELEVLPRLREGAARLGQQSTQLAALISELESRCQLPALGLLQDIKDALCRVQDVKLQPPAVVPMELRTVCRVPGLVETLRRFRGDITLDPDTANPELVLSEDRRSVQRGEQRQALPDNPERFDPGPCVLGQERITSGRHYWEVEVGDQTSWALGVCKETANRKEKGELSAGNGFWILVFLGSFYNSNEPAFSPLRDPPKRVGIFLDYEAGHLSFYSATDGSLLFIFPETLFSGTLRPLFSPLSSSPTPMTICRLIGVSGDTLGPQ
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 (PubMed:18628401). Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis (PubMed:18628401). May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences (PubMed:18628401). May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway (PubMed:12670303). Mediates MED15 ubiquitination leading to proteasomal degradation (By similarity). 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 (By similarity). Mechanistically, undergoes autoubiquitination upon DNA stimulation, promoting interaction with AIM2 and SQSTM1/p62, leading to AIM2 recruitment to autophagosomes (By similarity). {ECO:0000250|UniProtKB:Q96F44, ECO:0000269|PubMed:12670303, ECO:0000269|PubMed:18248090, ECO:0000269|PubMed:18628401}.
uniprot
proteins
mass_dalton
52580
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:18628401}.
uniprot
proteins
post_translational_modification
PTM: Autoubiquitinated upon DNA stimulation; autoubiquitination promotes interaction with SQSTM1/p62 and recruitment of AIM2 to autophagosomes. {ECO:0000250|UniProtKB:Q96F44}.
uniprot
proteins
protein_family
TRIM/RBCC family
uniprot
proteins
pubmed
11331580
uniprot
proteins
pubmed
12670303
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18248090
uniprot
proteins
pubmed
18275850
uniprot
proteins
pubmed
18628401
uniprot
proteins
pubmed
19468303
uniprot
proteins
sequence_length
467
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18628401}. Nucleus {ECO:0000269|PubMed:18628401}. Note=In the nucleus, colocalizes with PAX6. {ECO:0000269|PubMed:18628401}.
uniprot
proteins