Seroatlas · Human Serome Atlas

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 RYLQ

LocalizationUniProt · 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.

Disease | GeneticClinVar

6 pathogenic / likely-pathogenic of 561 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

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

Molecular functions

Cellular components

Protein domainsUniProt · Pfam · InterPro

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.

Canonical record: https://seroatlas.com/gene/TRIM2. Study-independent annotations aggregated from UniProt, Human Protein Atlas, PubMed, IEDB, Pfam, InterPro, Gene Ontology, AlphaFold, gnomAD, DepMap, ClinVar, TCGA. Catalog release seroatlas-reviewed-human-uniprot-20260313.

Seroatlas is the reference for exploring autoantibody and antibody serology at the human-protein level: the autoreactome and human serome, multiplex serology (HuProt, HuScan, VirScan, PhIP-Seq).

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