TRIM25
E3 ubiquitin/ISG15 ligase TRIM25
Also known as: EFP, RNF147, TRI25_HUMAN, ZNF147
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q14258
- Gene
- TRIM25
- Ensembl
- ENSG00000121060
- Chromosome
- 17
- Canonical length
- 630 aa
- Protein class
- Cancer-related genes, Enzymes, Plasma proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Nuclear bodies,Cytosol
- 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. The protein is an RNA binding protein, functions as a ubiquitin E3 ligase and is involved in multiple cellular processes, including regulation of antiviral innate immunity. [provided by RefSeq, Sep 2021]
Canonical amino-acid sequenceUniProt
630 residues, UniProt reviewed canonical sequence.
>Q14258|TRIM25
1 MAELCPLAEE LSCSICLEPF KEPVTTPCGH NFCGSCLNET WAVQGSPYLC PQCRAVYQAR
61 PQLHKNTVLC NVVEQFLQAD LAREPPADVW TPPARASAPS PNAQVACDHC LKEAAVKTCL
121 VCMASFCQEH LQPHFDSPAF QDHPLQPPVR DLLRRKCSQH NRLREFFCPE HSECICHICL
181 VEHKTCSPAS LSQASADLEA TLRHKLTVMY SQINGASRAL DDVRNRQQDV RMTANRKVEQ
241 LQQEYTEMKA LLDASETTST RKIKEEEKRV NSKFDTIYQI LLKKKSEIQT LKEEIEQSLT
301 KRDEFEFLEK ASKLRGISTK PVYIPEVELN HKLIKGIHQS TIDLKNELKQ CIGRLQEPTP
361 SSGDPGEHDP ASTHKSTRPV KKVSKEEKKS KKPPPVPALP SKLPTFGAPE QLVDLKQAGL
421 EAAAKATSSH PNSTSLKAKV LETFLAKSRP ELLEYYIKVI LDYNTAHNKV ALSECYTVAS
481 VAEMPQNYRP HPQRFTYCSQ VLGLHCYKKG IHYWEVELQK NNFCGVGICY GSMNRQGPES
541 RLGRNSASWC VEWFNTKISA WHNNVEKTLP STKATRVGVL LNCDHGFVIF FAVADKVHLM
601 YKFRVDFTEA LYPAFWVFSA GATLSICSPKLocalizationUniProt · AlphaFold · HPA
Whether an antibody against TRIM25 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)
- 0.4
- Highest tissue expression
- 46 nTPM
Expression across tissuesHPA
Tissue
- bone marrow: 46 nTPM
- spleen: 40 nTPM
- liver: 28 nTPM
- skin: 28 nTPM
- lung: 24 nTPM
- esophagus: 19 nTPM
Single-cell type
- neutrophils: 452 nCPM
- endometrial luminal cells: 260 nCPM
- endometrial glandular cells: 182 nCPM
- monocytes: 135 nCPM
- epicardial cells: 89 nCPM
- retinal bipolar cells: 85 nCPM
Immune cell
- neutrophil: 8.7 nTPM
- myeloid DC: 2.9 nTPM
- intermediate monocyte: 2.4 nTPM
- basophil: 2.3 nTPM
- classical monocyte: 2.3 nTPM
- memory B-cell: 2.1 nTPM
Brain region
- cerebral cortex: 27 nTPM
- hypothalamus: 15 nTPM
- spinal cord: 13 nTPM
- thalamus: 13 nTPM
- choroid plexus: 12 nTPM
- medulla oblongata: 12 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)
- 0.59
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.86
- DepMap mean gene effect
- -0.09
- 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
- antiviral innate immune response
- cellular response to leukemia inhibitory factor
- cytoplasmic pattern recognition receptor signaling pathway
- ERAD pathway
- host-mediated suppression of symbiont invasion
- innate immune response
- positive regulation of canonical NF-kappaB signal transduction
- protein K48-linked ubiquitination
- protein monoubiquitination
- regulation of protein localization
- regulation of viral entry into host cell
- response to estrogen
- response to oxidative stress
- response to vitamin D
- suppression of viral release by host
- ubiquitin-dependent protein catabolic process
- viral release from host cell
Molecular functions
- cadherin binding
- ligase activity
- RIG-I binding
- RNA binding
- transcription coactivator activity
- ubiquitin protein ligase activity
- ubiquitin-protein transferase activity
- zinc ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Zinc finger, RING-type
- B30.2/SPRY domain
- SPRY domain
- Butyrophylin-like, SPRY domain
- SPRY-associated
- Zinc finger, RING/FYVE/PHD-type
- Concanavalin A-like lectin/glucanase domain superfamily
- Zinc finger, RING-type, conserved site
- Zinc finger, RING-type, eukaryotic
- B30.2/SPRY domain superfamily
- E3 ubiquitin-protein ligase TRIM/RNF
- TRIM8/14/16/25/29/45/65, coiled-coil region
- SPRY domain
- RING-type zinc-finger
- SPRY-associated domain
- TRIM protein coiled-coil region
- TRIM25, PRY/SPRY domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of TRIM25 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 TRIM25 as an antibody target. Whether an autoantibody or antibody against TRIM25 could matter depends on whether native TRIM25 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
TRIM25 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 TRIM25 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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