TRIML1
Probable E3 ubiquitin-protein ligase TRIML1
Also known as: FLJ36180, RNF209, TRIML_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q8N9V2
- Gene
- TRIML1
- Ensembl
- ENSG00000184108
- Chromosome
- 4
- Canonical length
- 468 aa
- Protein class
- Enzymes, Predicted intracellular proteins
OverviewNCBI Gene
The protein encoded by this gene is a tripartite motif family protein with similarities to E3 ubiquitin-protein ligases. While the function of the encoded protein has not been determined, the orthologous protein in mouse has been shown to bind ubiquitin-specific protease 5 and is involved in the blastocyst development stage. [provided by RefSeq, Sep 2016]
Canonical amino-acid sequenceUniProt
468 residues, UniProt reviewed canonical sequence.
>Q8N9V2|TRIML1
1 MSTADLMENL REELTCFICL DYFSSPVTTE CGHSFCLVCL LRSWEEHNTP LSCPECWRTL
61 EGPHFQSNER LGRLASIARQ LRSQVLQSED EQGSYGRMPT TAKALSDDEQ GGSAFVAQSH
121 GANRVHLSSE AEEHHREKLQ EILNLLRVRR KEAQAVLTHE KERVKLCQEE TKTCKQVVVS
181 EYMKMHQFLK EEEQLQLQLL EQEEKENMRK LRNNEIKLTQ QIRSLSKMIA QIESSSQSSA
241 FESLEEVRGA LERSEPLLLQ CPEATTTELS LCRITGMKEM LRKFSTEITL DPATANAYLV
301 LSEDLKSVKY GGSRQQLPDN PERFDQSATV LGTQIFTSGR HYWEVEVGNK TEWEVGICKD
361 SVSRKGNLPK PPGDLFSLIG LKIGDDYSLW VSSPLKGQHV REPVCKVGVF LDYESGHIAF
421 YNGTDESLIY SFPQASFQEA LRPIFSPCLP NEGTNTDPLT ICSLNSHVLocalizationUniProt · AlphaFold · HPA
Whether an antibody against TRIML1 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)
- 0.37
- Highest tissue expression
- 11 nTPM
Expression across tissuesHPA
Tissue
- testis: 11 nTPM
- adipose tissue: 0 nTPM
- adrenal gland: 0 nTPM
- amygdala: 0 nTPM
- appendix: 0 nTPM
- basal ganglia: 0 nTPM
Single-cell type
- early spermatids: 190 nCPM
- late primary spermatocytes: 44 nCPM
- late spermatids: 36 nCPM
- migrating cytotrophoblasts: 3.3 nCPM
- cone photoreceptor cells: 2.1 nCPM
- cytotrophoblasts: 1.9 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- amygdala: 0 nTPM
- basal ganglia: 0 nTPM
- cerebellum: 0 nTPM
- cerebral cortex: 0 nTPM
- choroid plexus: 0 nTPM
- hippocampal formation: 0 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)
- 1.37
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.41
- DepMap mean gene effect
- 0.11
- DepMap dependency class
- none
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
- 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
- B30.2/SPRY domain superfamily
- Tripartite motif-containing
- SPRY domain
- SPRY-associated domain
- zinc finger of C3HC4-type, RING
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of TRIML1 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 TRIML1 as an antibody target. Whether an autoantibody or antibody against TRIML1 could matter depends on whether native TRIML1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
TRIML1 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 TRIML1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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