TRIM37
E3 ubiquitin-protein ligase TRIM37
Also known as: KIAA0898, MUL, POB1, TEF3, TRI37_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- O94972
- Gene
- TRIM37
- Ensembl
- ENSG00000108395
- Chromosome
- 17
- Canonical length
- 964 aa
- Protein class
- Disease related genes, Enzymes, Human disease related genes, Potential drug targets, Predicted intracellular proteins
OverviewNCBI Gene
This gene encodes a member of the tripartite motif (TRIM) family, whose members are involved in diverse cellular functions such as developmental patterning and oncogenesis. The TRIM motif includes zinc-binding domains, a RING finger region, a B-box motif and a coiled-coil domain. The RING finger and B-box domains chelate zinc and might be involved in protein-protein and/or protein-nucleic acid interactions. Mutations in this gene are associated with mulibrey (muscle-liver-brain-eye) nanism, an autosomal recessive disorder that involves several tissues of mesodermal origin. TRIM37 localizes in peroxisomal membranes, and has been implicated in human peroxisomal biogenesis disorders. [provided by RefSeq, Jul 2020]
Canonical amino-acid sequenceUniProt
964 residues, UniProt reviewed canonical sequence.
>O94972|TRIM37
1 MDEQSVESIA EVFRCFICME KLRDARLCPH CSKLCCFSCI RRWLTEQRAQ CPHCRAPLQL
61 RELVNCRWAE EVTQQLDTLQ LCSLTKHEEN EKDKCENHHE KLSVFCWTCK KCICHQCALW
121 GGMHGGHTFK PLAEIYEQHV TKVNEEVAKL RRRLMELISL VQEVERNVEA VRNAKDERVR
181 EIRNAVEMMI ARLDTQLKNK LITLMGQKTS LTQETELLES LLQEVEHQLR SCSKSELISK
241 SSEILMMFQQ VHRKPMASFV TTPVPPDFTS ELVPSYDSAT FVLENFSTLR QRADPVYSPP
301 LQVSGLCWRL KVYPDGNGVV RGYYLSVFLE LSAGLPETSK YEYRVEMVHQ SCNDPTKNII
361 REFASDFEVG ECWGYNRFFR LDLLANEGYL NPQNDTVILR FQVRSPTFFQ KSRDQHWYIT
421 QLEAAQTSYI QQINNLKERL TIELSRTQKS RDLSPPDNHL SPQNDDALET RAKKSACSDM
481 LLEGGPTTAS VREAKEDEED EEKIQNEDYH HELSDGDLDL DLVYEDEVNQ LDGSSSSASS
541 TATSNTEEND IDEETMSGEN DVEYNNMELE EGELMEDAAA AGPAGSSHGY VGSSSRISRR
601 THLCSAATSS LLDIDPLILI HLLDLKDRSS IENLWGLQPR PPASLLQPTA SYSRKDKDQR
661 KQQAMWRVPS DLKMLKRLKT QMAEVRCMKT DVKNTLSEIK SSSAASGDMQ TSLFSADQAA
721 LAACGTENSG RLQDLGMELL AKSSVANCYI RNSTNKKSNS PKPARSSVAG SLSLRRAVDP
781 GENSRSKGDC QTLSEGSPGS SQSGSRHSSP RALIHGSIGD ILPKTEDRQC KALDSDAVVV
841 AVFSGLPAVE KRRKMVTLGA NAKGGHLEGL QMTDLENNSE TGELQPVLPE GASAAPEEGM
901 SSDSDIECDT ENEEQEEHTS VGGFHDSFMV MTQPPDEDTH SSFPDGEQIG PEDLSFNTDE
961 NSGRLocalizationUniProt · AlphaFold · HPA
Whether an antibody against TRIM37 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
- Other membrane
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.54
- Highest tissue expression
- 58 nTPM
Expression across tissuesHPA
Tissue
- testis: 58 nTPM
- cerebellum: 39 nTPM
- cerebral cortex: 39 nTPM
- retina: 30 nTPM
- hypothalamus: 21 nTPM
- basal ganglia: 19 nTPM
Single-cell type
- cone photoreceptor cells: 226 nCPM
- late primary spermatocytes: 193 nCPM
- rod photoreceptor cells: 161 nCPM
- sertoli cells: 148 nCPM
- retinal ganglion cells: 139 nCPM
- early primary spermatocytes: 131 nCPM
Immune cell
- basophil: 31 nTPM
- T-reg: 8.3 nTPM
- gdT-cell: 7.2 nTPM
- MAIT T-cell: 6.8 nTPM
- naive CD8 T-cell: 5.4 nTPM
- neutrophil: 5.4 nTPM
Brain region
- cerebral cortex: 87 nTPM
- cerebellum: 76 nTPM
- pons: 73 nTPM
- thalamus: 63 nTPM
- white matter: 62 nTPM
- medulla oblongata: 60 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about TRIM37.
Disease | AllUniProt
Conditions TRIM37 is implicated in, by any mechanism.
- Mulibrey nanism (MUL) MIM:253250
Disease | GeneticClinVar
113 pathogenic / likely-pathogenic of 866 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Mulibrey nanism syndrome
- Inborn genetic diseases
- See cases
- TRIM37-related disorder
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)
- 0.64
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.82
- DepMap mean gene effect
- -0.57
- DepMap dependency class
- common
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 8% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- aggresome assembly
- negative regulation of centriole replication
- negative regulation of gene expression, epigenetic
- negative regulation of transcription by RNA polymerase II
- protein autoubiquitination
- protein import into peroxisome matrix
- protein monoubiquitination
- protein stabilization
Molecular functions
- chromatin binding
- histone H2AK119 ubiquitin ligase activity
- protein homodimerization activity
- transcription coactivator activity
- tumor necrosis factor receptor binding
- ubiquitin protein ligase activity
- ubiquitin protein ligase binding
- ubiquitin-protein transferase activity
- zinc ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- B-box-type zinc finger
- Zinc finger, RING-type
- MATH/TRAF domain
- B-box, C-terminal
- TRAF-like
- Zinc finger, RING/FYVE/PHD-type
- B-box zinc finger
- MATH domain
- TRIM37, MATH domain
- TRIM/RBCC E3 ubiquitin-protein ligases
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of TRIM37 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 TRIM37 as an antibody target. Whether an autoantibody or antibody against TRIM37 could matter depends on whether native TRIM37 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
TRIM37 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 TRIM37 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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