TRIM69
entrez
140691
canonical
uniprot
Q86WT6
canonical
ensembl
ENSG00000185880
resolver
ensembl
ENSG00000278211
resolver
ensp
ENSP00000332284
resolver
ensp
ENSP00000342922
resolver
ensp
ENSP00000453077
resolver
ensp
ENSP00000453332
resolver
ensp
ENSP00000453549
resolver
ensp
ENSP00000487832
resolver
enst
ENST00000561043
resolver
enst
ENST00000633859
resolver
genesymbol
TRIM69
resolver
genesymbol_syn
RNF36
resolver
hgnc
HGNC:17857
resolver
uniprot
A8MX03
resolver
uniprot
H0YL66
resolver
uniprot
Q309B0
resolver
uniprot
Q4G1A5
resolver
uniprot
Q6W897
resolver
uniprot
Q8IYY3
resolver
uniprot
Q8WY16
resolver
uniprot
Q8WY17
resolver
uniprot_entry
H0YL66_HUMAN
resolver
uniprot_entry
TRI69_HUMAN
resolver
uniprot_sec
A8MX03
resolver
uniprot_sec
Q309B0
resolver
uniprot_sec
Q4G1A5
resolver
uniprot_sec
Q6W897
resolver
uniprot_sec
Q8IYY3
resolver
uniprot_sec
Q8WY16
resolver
uniprot_sec
Q8WY17
resolver
amino_acid_sequence
MEVSTNPSSNIDPGDYVEMNDSITHLPSKVVIQDITMELHCPLCNDWFRDPLMLSCGHNFCEACIQDFWRLQAKETFCPECKMLCQYNNCTFNPVLDKLVEKIKKLPLLKGHPQCPEHGENLKLFSKPDGKLICFQCKDARLSVGQSKEFLQISDAVHFFTEELAIQQGQLETTLKELQTLRNMQKEAIAAHKENKLHLQQHVSMEFLKLHQFLHSKEKDILTELREEGKALNEEMELNLSQLQEQCLLAKDMLVSIQAKTEQQNSFDFLKDITTLLHSLEQGMKVLATRELISRKLNLGQYKGPIQYMVWREMQDTLCPGLSPLTLDPKTAHPNLVLSKSQTSVWHGDIKKIMPDDPERFDSSVAVLGSRGFTSGKWYWEVEVAKKTKWTVGVVRESIIRKGSCPLTPEQGFWLLRLRNQTDLKALDLPSFSLTLTNNLDKVGIYLDYEGGQLSFYNAKTMTHIYTFSNTFMEKLYPYFCPCLNDGGENKEPLHILHPQ
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase that plays an important role in antiviral immunity by restricting different viral infections including dengue virus or vesicular stomatitis indiana virus (PubMed:23131556, PubMed:30142214, PubMed:31375575, PubMed:31578292). Ubiquitinates viral proteins such as dengue virus NS3 thereby limiting infection (PubMed:30844644). Also involved in antiviral immunity by mediating 'Lys-63'-linked ubiquitination of STING1, thereby promoting STING1 dimerization and downstream activation of cGAS-STING signaling (PubMed:41865946). In addition, acts as a key mediator of type I interferon induced microtubule stabilization by directly associating to microtubules independently of its E3 ligase activity (PubMed:36251989). Also plays a role in cataract formation together with TP53 (PubMed:30844644). Mechanistically, inhibits UVB-induced cell apoptosis and reactive oxygen species (ROS) production by inducing TP53 ubiquitination (PubMed:30844644). Regulates centrosome dynamics and mitotic progression by ubiquitinating STK3/MST2; leading to its redistribution to the perinuclear cytoskeleton and subsequent phosphorylation by PLK1 (PubMed:37739411). {ECO:0000269|PubMed:23131556, ECO:0000269|PubMed:30142214, ECO:0000269|PubMed:30844644, ECO:0000269|PubMed:31375575, ECO:0000269|PubMed:31578292, ECO:0000269|PubMed:36251989, ECO:0000269|PubMed:37739411, ECO:0000269|PubMed:41865946}.
uniprot
proteins
mass_dalton
57419
uniprot
proteins
mutagenesis
MUTAGEN 61..64; /note="CEAC->AEAA: Abolished E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:41865946"; MUTAGEN 61; /note="C->A: Loss of E3 ubiquitin-protein ligase activity; when associated with A-64."; /evidence="ECO:0000269|PubMed:23131556, ECO:0000269|PubMed:30142214, ECO:0000269|PubMed:36251989"; MUTAGEN 64; /note="C->A: Loss of E3 ubiquitin-protein ligase activity; when associated with A-61."; /evidence="ECO:0000269|PubMed:23131556, ECO:0000269|PubMed:30142214, ECO:0000269|PubMed:36251989"; MUTAGEN 95; /note="V->A: Loss of antiviral activity; able to form dimers but not higher-order multimers; when associated with A-96."; /evidence="ECO:0000269|PubMed:31578292"; MUTAGEN 96; /note="L->A: Loss of antiviral activity; able to form dimers but not higher-order multimers; when associated with A-91."; /evidence="ECO:0000269|PubMed:31578292"; MUTAGEN 99; /note="L->A: Loss of antiviral activity; able to form dimers but not higher-order multimers."; /evidence="ECO:0000269|PubMed:31578292
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:30142214, ECO:0000269|PubMed:37739411, ECO:0000269|PubMed:41865946}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Phosphorylation is necessary for nuclear localization. {ECO:0000250|UniProtKB:Q80X56}.
uniprot
proteins
protein_family
TRIM/RBCC family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
23131556
uniprot
proteins
pubmed
30142214
uniprot
proteins
pubmed
30844644
uniprot
proteins
pubmed
31375575
uniprot
proteins
pubmed
31578292
uniprot
proteins
pubmed
33021497
uniprot
proteins
pubmed
36251989
uniprot
proteins
pubmed
37739411
uniprot
proteins
pubmed
41865946
uniprot
proteins
sequence_length
500
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23131556, ECO:0000269|PubMed:31578292, ECO:0000269|PubMed:36251989}. Nucleus {ECO:0000269|PubMed:23131556}. Nucleus speckle {ECO:0000269|PubMed:23131556}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:37739411}. Note=Adopts a filamentous distribution in the cell cytoplasm where it strongly colocalizes with stable microtubules. {ECO:0000269|PubMed:36251989}.
uniprot
proteins