TRIM2
Tripartite motif-containing protein 2
Also known as: CMT2R, KIAA0517, RNF86, TRIM2_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9C040
- Gene
- TRIM2
- Ensembl
- ENSG00000109654
- Chromosome
- 4
- Canonical length
- 744 aa
- Protein class
- Disease related genes, Enzymes, Human disease related genes, Potential drug targets, Predicted intracellular proteins
- Subcellular location
- Centrosome
- Quaternary structure
- Homooligomer
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 filaments. It plays a neuroprotective role and functions as an E3-ubiquitin ligase in proteasome-mediated degradation of target proteins. Mutations in this gene can cause early-onset axonal neuropathy. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2014]
Canonical amino-acid sequenceUniProt
744 residues, UniProt reviewed canonical sequence.
>Q9C040|TRIM2
1 MASEGTNIPS PVVRQIDKQF LICSICLERY KNPKVLPCLH TFCERCLQNY IPAHSLTLSC
61 PVCRQTSILP EKGVAALQNN FFITNLMDVL QRTPGSNAEE SSILETVTAV AAGKPLSCPN
121 HDGNVMEFYC QSCETAMCRE CTEGEHAEHP TVPLKDVVEQ HKASLQVQLD AVNKRLPEID
181 SALQFISEII HQLTNQKASI VDDIHSTFDE LQKTLNVRKS VLLMELEVNY GLKHKVLQSQ
241 LDTLLQGQES IKSCSNFTAQ ALNHGTETEV LLVKKQMSEK LNELADQDFP LHPRENDQLD
301 FIVETEGLKK SIHNLGTILT TNAVASETVA TGEGLRQTII GQPMSVTITT KDKDGELCKT
361 GNAYLTAELS TPDGSVADGE ILDNKNGTYE FLYTVQKEGD FTLSLRLYDQ HIRGSPFKLK
421 VIRSADVSPT TEGVKRRVKS PGSGHVKQKA VKRPASMYST GKRKENPIED DLIFRVGTKG
481 RNKGEFTNLQ GVAASTNGKI LIADSNNQCV QIFSNDGQFK SRFGIRGRSP GQLQRPTGVA
541 VHPSGDIIIA DYDNKWVSIF SSDGKFKTKI GSGKLMGPKG VSVDRNGHII VVDNKACCVF
601 IFQPNGKIVT RFGSRGNGDR QFAGPHFAAV NSNNEIIITD FHNHSVKVFN QEGEFMLKFG
661 SNGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDGSG SFLSYINTSA DPLYGPQGLA
721 LTSDGHVVVA DSGNHCFKVY RYLQLocalizationUniProt · AlphaFold · HPA
Whether an antibody against TRIM2 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)
- 0.34
- Highest tissue expression
- 63 nTPM
Expression across tissuesHPA
Tissue
- cerebral cortex: 63 nTPM
- thyroid gland: 47 nTPM
- salivary gland: 40 nTPM
- spinal cord: 31 nTPM
- cerebellum: 31 nTPM
- stomach: 26 nTPM
Single-cell type
- oligodendrocytes: 1,616 nCPM
- renal collecting duct intercalated cells: 509 nCPM
- ependymal cells: 492 nCPM
- distal convoluted tubule cells: 414 nCPM
- loop of henle epithelial cells: 370 nCPM
- oligodendrocyte progenitor cells: 363 nCPM
Immune cell
- memory CD4 T-cell: 1 nTPM
- T-reg: 0.8 nTPM
- memory B-cell: 0.3 nTPM
- myeloid DC: 0.1 nTPM
- naive B-cell: 0.1 nTPM
- naive CD4 T-cell: 0.1 nTPM
Brain region
- white matter: 333 nTPM
- basal ganglia: 232 nTPM
- pons: 219 nTPM
- cerebral cortex: 219 nTPM
- hippocampal formation: 203 nTPM
- cerebellum: 183 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about TRIM2.
Disease | AllUniProt
Conditions TRIM2 is implicated in, by any mechanism.
- Charcot-Marie-Tooth disease, axonal, type 2R (CMT2R) MIM:615490
Disease | GeneticClinVar
6 pathogenic / likely-pathogenic of 561 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Charcot-Marie-Tooth disease type 2R
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)
- 0.27
- gnomAD pLI
- 1
- gnomAD missense Z
- 3.57
- DepMap mean gene effect
- 0.03
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cellular response to leukemia inhibitory factor
- proteasome-mediated ubiquitin-dependent protein catabolic process
- protein polyubiquitination
- regulation of neuron apoptotic process
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
- B-box-type zinc finger
- NHL repeat
- Filamin/ABP280 repeat
- Zinc finger, RING-type
- B-box, C-terminal
- Six-bladed beta-propeller, TolB-like
- Zinc finger, RING/FYVE/PHD-type
- Immunoglobulin-like fold
- Immunoglobulin E-set
- Filamin/ABP280 repeat-like
- Zinc finger, RING-type, conserved site
- Zinc finger, RING-type, eukaryotic
- Tripartite Motif and NHL Repeat Containing E3 Ligases
- Tripartite motif-containing protein 2/3, C-terminal domain
- Filamin/ABP280 repeat
- B-box zinc finger
- NHL repeat
- RING-type zinc-finger
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of TRIM2 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 TRIM2 as an antibody target. Whether an autoantibody or antibody against TRIM2 could matter depends on whether native TRIM2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
TRIM2 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 TRIM2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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