TRIM3
Tripartite motif-containing protein 3
Also known as: BERP, HAC1, RNF22, RNF97, TRIM3_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- O75382
- Gene
- TRIM3
- Ensembl
- ENSG00000110171
- Chromosome
- 11
- Canonical length
- 744 aa
- Protein class
- Predicted intracellular proteins
- Subcellular location
- Mitochondria
- Quaternary structure
- Homooligomer
OverviewNCBI Gene
The protein encoded by this gene is a member of the tripartite motif (TRIM) family, also called the 'RING-B-box-coiled-coil' (RBCC) subgroup of RING finger proteins. 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 localizes to cytoplasmic filaments. It is similar to a rat protein which is a specific partner for the tail domain of myosin V, a class of myosins which are involved in the targeted transport of organelles. The rat protein can also interact with alpha-actinin-4. Thus it is suggested that this human protein may play a role in myosin V-mediated cargo transport. Alternatively spliced transcript variants encoding the same isoform have been identified. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
744 residues, UniProt reviewed canonical sequence.
>O75382|TRIM3
1 MAKREDSPGP EVQPMDKQFL VCSICLDRYQ CPKVLPCLHT FCERCLQNYI PAQSLTLSCP
61 VCRQTSILPE QGVSALQNNF FISSLMEAMQ QAPDGAHDPE DPHPLSVVAG RPLSCPNHEG
121 KTMEFYCEAC ETAMCGECRA GEHREHGTVL LRDVVEQHKA ALQRQLEAVR GRLPQLSAAI
181 ALVGGISQQL QERKAEALAQ ISAAFEDLEQ ALQQRKQALV SDLETICGAK QKVLQSQLDT
241 LRQGQEHIGS SCSFAEQALR LGSAPEVLLV RKHMRERLAA LAAQAFPERP HENAQLELVL
301 EVDGLRRSVL NLGALLTTSA TAHETVATGE GLRQALVGQP ASLTVTTKDK DGRLVRTGSA
361 ELRAEITGPD GTRLPVPVVD HKNGTYELVY TARTEGELLL SVLLYGQPVR GSPFRVRALR
421 PGDLPPSPDD VKRRVKSPGG PGSHVRQKAV RRPSSMYSTG GKRKDNPIED ELVFRVGSRG
481 REKGEFTNLQ GVSAASSGRI VVADSNNQCI QVFSNEGQFK FRFGVRGRSP GQLQRPTGVA
541 VDTNGDIIVA DYDNRWVSIF SPEGKFKTKI GAGRLMGPKG VAVDRNGHII VVDNKSCCVF
601 TFQPNGKLVG RFGGRGATDR HFAGPHFVAV NNKNEIVVTD FHNHSVKVYS ADGEFLFKFG
661 SHGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDSSG SFLSYINTSA EPLYGPQGLA
721 LTSDGHVVVA DAGNHCFKAY RYLQLocalizationUniProt · AlphaFold · HPA
Whether an antibody against TRIM3 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)
- 0.35
- Highest tissue expression
- 49 nTPM
Expression across tissuesHPA
Tissue
- cerebellum: 49 nTPM
- duodenum: 16 nTPM
- cerebral cortex: 16 nTPM
- blood vessel: 15 nTPM
- small intestine: 14 nTPM
- endometrium: 13 nTPM
Single-cell type
- enterocytes: 37 nCPM
- goblet cells: 27 nCPM
- retinal ganglion cells: 23 nCPM
- rod photoreceptor cells: 23 nCPM
- brain excitatory neurons: 23 nCPM
- colonocytes: 21 nCPM
Immune cell
- myeloid DC: 1.2 nTPM
- classical monocyte: 1 nTPM
- intermediate monocyte: 0.9 nTPM
- NK-cell: 0.6 nTPM
- eosinophil: 0.5 nTPM
- gdT-cell: 0.5 nTPM
Brain region
- cerebellum: 39 nTPM
- pons: 35 nTPM
- cerebral cortex: 30 nTPM
- basal ganglia: 29 nTPM
- thalamus: 28 nTPM
- white matter: 27 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)
- 0.29
- gnomAD pLI
- 0.99
- gnomAD missense Z
- 3.71
- DepMap mean gene effect
- 0.18
- DepMap dependency class
- none
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
- nervous system development
- neural precursor cell proliferation
- positive regulation of toll-like receptor 3 signaling pathway
- proteasome-mediated ubiquitin-dependent protein catabolic process
- protein K63-linked ubiquitination
- protein polyubiquitination
- protein transport
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, C3HC4 RING-type
- Tripartite Motif and NHL Repeat Containing E3 Ligases
- Tripartite motif-containing protein 2/3, C-terminal domain
- Zinc finger, C3HC4 type (RING finger)
- Filamin/ABP280 repeat
- B-box zinc finger
- NHL repeat
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of TRIM3 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 TRIM3 as an antibody target. Whether an autoantibody or antibody against TRIM3 could matter depends on whether native TRIM3 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
TRIM3 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 TRIM3 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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