TRIM32
entrez
22954
canonical
uniprot
Q13049
canonical
ensembl
ENSG00000119401
resolver
ensp
ENSP00000363095
resolver
ensp
ENSP00000408292
resolver
ensp
ENSP00000552914
resolver
ensp
ENSP00000552915
resolver
ensp
ENSP00000552916
resolver
ensp
ENSP00000552917
resolver
ensp
ENSP00000552918
resolver
ensp
ENSP00000552919
resolver
ensp
ENSP00000599643
resolver
ensp
ENSP00000599644
resolver
ensp
ENSP00000599645
resolver
enst
ENST00000373983
resolver
enst
ENST00000450136
resolver
enst
ENST00000882855
resolver
enst
ENST00000882856
resolver
enst
ENST00000882857
resolver
enst
ENST00000882858
resolver
enst
ENST00000882859
resolver
enst
ENST00000882860
resolver
enst
ENST00000929584
resolver
enst
ENST00000929585
resolver
enst
ENST00000929586
resolver
genesymbol
TRIM32
resolver
genesymbol_syn
HT2A
resolver
hgnc
HGNC:16380
resolver
uniprot
Q9NQP8
resolver
uniprot_entry
TRI32_HUMAN
resolver
uniprot_sec
Q9NQP8
resolver
amino_acid_sequence
MAAAAASHLNLDALREVLECPICMESFTEEQLRPKLLHCGHTICRQCLEKLLASSINGVRCPFCSKITRITSLTQLTDNLTVLKIIDTAGLSEAVGLLMCRSCGRRLPRQFCRSCGLVLCEPCREADHQPPGHCTLPVKEAAEERRRDFGEKLTRLRELMGELQRRKAALEGVSKDLQARYKAVLQEYGHEERRVQDELARSRKFFTGSLAEVEKSNSQVVEEQSYLLNIAEVQAVSRCDYFLAKIKQADVALLEETADEEEPELTASLPRELTLQDVELLKVGHVGPLQIGQAVKKPRTVNVEDSWAMEATASAASTSVTFREMDMSPEEVVASPRASPAKQRGPEAASNIQQCLFLKKMGAKGSTPGMFNLPVSLYVTSQGEVLVADRGNYRIQVFTRKGFLKEIRRSPSGIDSFVLSFLGADLPNLTPLSVAMNCQGLIGVTDSYDNSLKVYTLDGHCVACHRSQLSKPWGITALPSGQFVVTDVEGGKLWCFTVDRGSGVVKYSCLCSAVRPKFVTCDAEGTVYFTQGLGLNLENRQNEHHLEGGFSIGSVGPDGQLGRQISHFFSENEDFRCIAGMCVDARGDLIVADSSRKEILHFPKGGGYSVLIREGLTCPVGIALTPKGQLLVLDCWDHCIKIYSYHLRRYSTP
uniprot
proteins
disease_involvement
DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 8 (LGMDR8) [MIM:254110]: An autosomal recessive degenerative myopathy characterized by pelvic girdle, shoulder girdle and quadriceps muscle weakness. Clinical phenotype and severity are highly variable. Disease progression is slow and most patients remain ambulatory into the sixth decade of life. {ECO:0000269|PubMed:11822024, ECO:0000269|PubMed:17994549}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Bardet-Biedl syndrome 11 (BBS11) [MIM:615988]: A syndrome characterized by usually severe pigmentary retinopathy, early-onset obesity, polydactyly, hypogenitalism, renal malformation and intellectual disability. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease. {ECO:0000269|PubMed:16606853}. Note=The disease is caused by variants affecting the gene represented in this entry. It has been suggested that TRIM32 might be the E3 ubiquitin ligase for BBS2, a component of the BBSome complex involved in ciliogenesis, that is ubiquitinated and degraded by the proteasome (PubMed:22500027). {ECO:0000269|PubMed:22500027}.
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin ligase that plays a role in various biological processes including neural stem cell differentiation, innate immunity, inflammatory resonse and autophagy (PubMed:19349376, PubMed:31123703, PubMed:40793792). Plays a role in virus-triggered induction of IFN-beta and TNF by mediating the ubiquitination of STING1. Mechanistically, targets STING1 for 'Lys-63'-linked ubiquitination which promotes the interaction of STING1 with TBK1 (PubMed:22745133). Regulates bacterial clearance and promotes autophagy in Mycobacterium tuberculosis-infected macrophages (PubMed:37543647). Negatively regulates TLR3/4-mediated innate immune and inflammatory response by triggering the autophagic degradation of TICAM1 in an E3 activity-independent manner (PubMed:28898289). Plays an essential role in oxidative stress induced cell death by inducing loss of transmembrane potential and enhancing mitochondrial reactive oxygen species (ROS) production during oxidative stress conditions (PubMed:32918979). Ubiquitinates XIAP and targets it for proteasomal degradation (PubMed:21628460). Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation (PubMed:19349376). May ubiquitinate BBS2 (PubMed:22500027). Ubiquitinates PIAS4/PIASY and promotes its degradation in keratinocytes treated with UVB and TNF (By similarity). Also acts as a regulator of autophagy by mediating formation of unanchored 'Lys-63'-linked polyubiquitin chains that activate ULK1: interaction with AMBRA1 is required for ULK1 activation (PubMed:31123703). Positively regulates dendritic branching by promoting ubiquitination and subsequent degradation of the epigenetic factor CDYL (PubMed:34888944). Under metabolic stress and phosphorylation by CHK2, mediates 'Lys-63'-linked ubiquitination of ATG7 at 'Lys-45' to initiate autophagy (PubMed:37943659). {ECO:0000250|UniProtKB:Q8CH72, ECO:0000269|PubMed:19349376, ECO:0000269|PubMed:21628460, ECO:0000269|PubMed:22500027, ECO:0000269|PubMed:22745133, ECO:0000269|PubMed:28898289, ECO:0000269|PubMed:31123703, ECO:0000269|PubMed:32918979, ECO:0000269|PubMed:34888944, ECO:0000269|PubMed:37543647, ECO:0000269|PubMed:37943659, ECO:0000269|PubMed:40793792}.; FUNCTION: (Microbial infection) May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo (PubMed:7778269). Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo (PubMed:7778269). {ECO:0000269|PubMed:7778269}.
uniprot
proteins
mass_dalton
71989
uniprot
proteins
mutagenesis
MUTAGEN 39; /note="C->S: Abolished E3 ubiquitin ligase activity and ability to activate ULK1. Impairs ATG7 ubiquitination."; /evidence="ECO:0000269|PubMed:31123703, ECO:0000269|PubMed:37543647, ECO:0000269|PubMed:37943659"; MUTAGEN 55; /note="S->A: Increases the apoptotic cell death induced by glucose starvation."; /evidence="ECO:0000269|PubMed:37943659"; MUTAGEN 55; /note="S->D: Decreases the apoptotic cell death induced by glucose starvation."; /evidence="ECO:0000269|PubMed:37943659
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:19349376, ECO:0000269|PubMed:31123703, ECO:0000269|PubMed:37943659}.
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated. {ECO:0000269|PubMed:19349376}.; PTM: Phosphorylation at Ser-55 by CHEK2 under oxidative stress, activates the E3 ligase activity and promotes ATG7 ubiquitination leading to positive regulation of the autophagosme assembly. {ECO:0000269|PubMed:37943659}.; PTM: (Microbial infection) Cleaved at Glu-331 by Seneca Valley virus protease 3C, resulting in loss of E3 ligase and antiviral activities. {ECO:0000269|PubMed:40793792}.
uniprot
proteins
protein_family
TRIM/RBCC family
uniprot
proteins
pubmed
11822024
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16606853
uniprot
proteins
pubmed
17994549
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19349376
uniprot
proteins
pubmed
21344540
uniprot
proteins
pubmed
21628460
uniprot
proteins
pubmed
22500027
uniprot
proteins
pubmed
22745133
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
26394407
uniprot
proteins
pubmed
28898289
uniprot
proteins
pubmed
31123703
uniprot
proteins
pubmed
32918979
uniprot
proteins
pubmed
34888944
uniprot
proteins
pubmed
37543647
uniprot
proteins
pubmed
37943659
uniprot
proteins
pubmed
40793792
uniprot
proteins
pubmed
7778269
uniprot
proteins
sequence_length
653
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19349376, ECO:0000269|PubMed:37543647, ECO:0000269|PubMed:40793792}. Mitochondrion {ECO:0000269|PubMed:22745133, ECO:0000269|PubMed:32918979}. Endoplasmic reticulum {ECO:0000269|PubMed:22745133}. Note=Localized in cytoplasmic bodies, often located around the nucleus. {ECO:0000269|PubMed:19349376}.
uniprot
proteins