TRIM32
E3 ubiquitin-protein ligase TRIM32
Also known as: BBS11, HT2A, LGMD2H, TATIP, TRI32_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q13049
- Gene
- TRIM32
- Ensembl
- ENSG00000119401
- Chromosome
- 9
- Canonical length
- 653 aa
- Protein class
- Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins
- Subcellular location
- Intermediate filaments
OverviewNCBI Gene
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies. The protein has also been localized to the nucleus, where it interacts with the activation domain of the HIV-1 Tat protein. The Tat protein activates transcription of HIV-1 genes. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
653 residues, UniProt reviewed canonical sequence.
>Q13049|TRIM32
1 MAAAAASHLN LDALREVLEC PICMESFTEE QLRPKLLHCG HTICRQCLEK LLASSINGVR
61 CPFCSKITRI TSLTQLTDNL TVLKIIDTAG LSEAVGLLMC RSCGRRLPRQ FCRSCGLVLC
121 EPCREADHQP PGHCTLPVKE AAEERRRDFG EKLTRLRELM GELQRRKAAL EGVSKDLQAR
181 YKAVLQEYGH EERRVQDELA RSRKFFTGSL AEVEKSNSQV VEEQSYLLNI AEVQAVSRCD
241 YFLAKIKQAD VALLEETADE EEPELTASLP RELTLQDVEL LKVGHVGPLQ IGQAVKKPRT
301 VNVEDSWAME ATASAASTSV TFREMDMSPE EVVASPRASP AKQRGPEAAS NIQQCLFLKK
361 MGAKGSTPGM FNLPVSLYVT SQGEVLVADR GNYRIQVFTR KGFLKEIRRS PSGIDSFVLS
421 FLGADLPNLT PLSVAMNCQG LIGVTDSYDN SLKVYTLDGH CVACHRSQLS KPWGITALPS
481 GQFVVTDVEG GKLWCFTVDR GSGVVKYSCL CSAVRPKFVT CDAEGTVYFT QGLGLNLENR
541 QNEHHLEGGF SIGSVGPDGQ LGRQISHFFS ENEDFRCIAG MCVDARGDLI VADSSRKEIL
601 HFPKGGGYSV LIREGLTCPV GIALTPKGQL LVLDCWDHCI KIYSYHLRRY STPLocalizationUniProt · AlphaFold · HPA
Whether an antibody against TRIM32 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.36
- Highest tissue expression
- 17 nTPM
Expression across tissuesHPA
Tissue
- skeletal muscle: 17 nTPM
- cerebellum: 13 nTPM
- fallopian tube: 12 nTPM
- tongue: 12 nTPM
- smooth muscle: 10 nTPM
- cervix: 9.5 nTPM
Single-cell type
- thymic myoid cells: 35 nCPM
- decidual stromal cells: 29 nCPM
- choroid plexus epithelial cells: 27 nCPM
- early primary spermatocytes: 23 nCPM
- respiratory ciliated cells: 23 nCPM
- fallopian tube ciliated cells: 20 nCPM
Immune cell
- T-reg: 21 nTPM
- gdT-cell: 11 nTPM
- naive CD8 T-cell: 9.8 nTPM
- naive CD4 T-cell: 9.6 nTPM
- memory CD4 T-cell: 9.5 nTPM
- memory CD8 T-cell: 8.7 nTPM
Brain region
- cerebellum: 46 nTPM
- choroid plexus: 45 nTPM
- hypothalamus: 25 nTPM
- cerebral cortex: 23 nTPM
- hippocampal formation: 22 nTPM
- basal ganglia: 22 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about TRIM32.
Disease | AllUniProt
Conditions TRIM32 is implicated in, by any mechanism.
- Muscular dystrophy, limb-girdle, autosomal recessive 8 (LGMDR8) MIM:254110
- Bardet-Biedl syndrome 11 (BBS11) MIM:615988
Disease | GeneticClinVar
70 pathogenic / likely-pathogenic of 761 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Bardet-Biedl syndrome
- Sarcotubular myopathy
- Bardet-Biedl syndrome 11
- TRIM32-related disorder
- Autosomal recessive limb-girdle muscular dystrophy
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.86
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.83
- DepMap mean gene effect
- 0.08
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- autophagosome assembly
- axon development
- cellular response to amino acid starvation
- cellular response to stress
- fat cell differentiation
- free ubiquitin chain polymerization
- innate immune response
- muscle cell cellular homeostasis
- negative regulation of cilium assembly
- negative regulation of fibroblast proliferation
- negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage
- negative regulation of toll-like receptor 4 signaling pathway
- negative regulation of viral transcription
- positive regulation of autophagosome assembly
- positive regulation of autophagy
- positive regulation of canonical NF-kappaB signal transduction
- positive regulation of cell cycle
- positive regulation of cell growth
- positive regulation of cell migration
- positive regulation of cell motility
- positive regulation of neurogenesis
- positive regulation of neuron differentiation
- positive regulation of protein catabolic process
- positive regulation of proteolysis
- positive regulation of striated muscle cell differentiation
- positive regulation of tumor necrosis factor-mediated signaling pathway
- protein K63-linked ubiquitination
- protein polyubiquitination
- protein ubiquitination
- response to oxidative stress
- response to starvation
- response to tumor necrosis factor
- response to UV
- suppression of viral release by host
- tissue homeostasis
- ubiquitin-dependent protein catabolic process
- actin ubiquitination
- positive regulation of chemokine (C-C motif) ligand 20 production
- positive regulation of interleukin-17-mediated signaling pathway
Molecular functions
- identical protein binding
- myosin binding
- protein-macromolecule adaptor activity
- RNA binding
- Tat protein binding
- transcription coactivator activity
- translation initiation factor binding
- ubiquitin binding
- ubiquitin protein ligase activity
- ubiquitin-protein transferase activity
- zinc ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of TRIM32 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads TRIM32 as an antibody target. Whether an autoantibody or antibody against TRIM32 could matter depends on whether native TRIM32 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
TRIM32 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label TRIM32 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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