Seroatlas · Human Serome Atlas

TRIM23

E3 ubiquitin-protein ligase TRIM23

Also known as: ARD1, ARFD1, RNF46, TRI23_HUMAN

Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene

Protein identityUniProt · HPA

UniProt accession
P36406
Gene
TRIM23
Ensembl
ENSG00000113595
Chromosome
5
Canonical length
574 aa
Protein class
Cancer-related genes, Enzymes, Predicted intracellular proteins
Quaternary structure
Homodimer

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. This protein is also a member of the ADP ribosylation factor family of guanine nucleotide-binding family of proteins. Its carboxy terminus contains an ADP-ribosylation factor domain and a guanine nucleotide binding site, while the amino terminus contains a GTPase activating protein domain which acts on the guanine nucleotide binding site. The protein localizes to lysosomes and the Golgi apparatus. It plays a role in the formation of intracellular transport vesicles, their movement from one compartment to another, and phopholipase D activation. Three alternatively spliced transcript variants for this gene have been described. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

574 residues, UniProt reviewed canonical sequence.

>P36406|TRIM23
     1  MATLVVNKLG AGVDSGRQGS RGTAVVKVLE CGVCEDVFSL QGDKVPRLLL CGHTVCHDCL
    61  TRLPLHGRAI RCPFDRQVTD LGDSGVWGLK KNFALLELLE RLQNGPIGQY GAAEESIGIS
   121  GESIIRCDED EAHLASVYCT VCATHLCSEC SQVTHSTKTL AKHRRVPLAD KPHEKTMCSQ
   181  HQVHAIEFVC LEEGCQTSPL MCCVCKEYGK HQGHKHSVLE PEANQIRASI LDMAHCIRTF
   241  TEEISDYSRK LVGIVQHIEG GEQIVEDGIG MAHTEHVPGT AENARSCIRA YFYDLHETLC
   301  RQEEMALSVV DAHVREKLIW LRQQQEDMTI LLSEVSAACL HCEKTLQQDD CRVVLAKQEI
   361  TRLLETLQKQ QQQFTEVADH IQLDASIPVT FTKDNRVHIG PKMEIRVVTL GLDGAGKTTI
   421  LFKLKQDEFM QPIPTIGFNV ETVEYKNLKF TIWDVGGKHK LRPLWKHYYL NTQAVVFVVD
   481  SSHRDRISEA HSELAKLLTE KELRDALLLI FANKQDVAGA LSVEEITELL SLHKLCCGRS
   541  WYIQGCDARS GMGLYEGLDW LSRQLVAAGV LDVA

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against TRIM23 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)
0.38
Highest tissue expression
27 nTPM

Expression across tissuesHPA

Tissue

  • cerebral cortex: 27 nTPM
  • tongue: 16 nTPM
  • cerebellum: 16 nTPM
  • retina: 14 nTPM
  • skeletal muscle: 12 nTPM
  • ovary: 11 nTPM

Single-cell type

  • corticotrophs: 61 nCPM
  • brain excitatory neurons: 58 nCPM
  • brain inhibitory neurons: 58 nCPM
  • somatotrophs: 56 nCPM
  • thyrotrophs: 56 nCPM
  • other brain neurons: 52 nCPM

Immune cell

  • basophil: 20 nTPM
  • neutrophil: 9.2 nTPM
  • eosinophil: 8.9 nTPM
  • naive CD4 T-cell: 8.1 nTPM
  • T-reg: 6.4 nTPM
  • naive CD8 T-cell: 6.1 nTPM

Brain region

  • white matter: 50 nTPM
  • cerebellum: 48 nTPM
  • cerebral cortex: 44 nTPM
  • basal ganglia: 38 nTPM
  • pons: 37 nTPM
  • spinal cord: 37 nTPM

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)
0.58
gnomAD pLI
0
gnomAD missense Z
2.5
DepMap mean gene effect
-0.08
DepMap dependency class
selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% 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 TRIM23 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 TRIM23 as an antibody target. Whether an autoantibody or antibody against TRIM23 could matter depends on whether native TRIM23 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.

TRIM23 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 TRIM23 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.

Canonical record: https://seroatlas.com/gene/TRIM23. 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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