TRAIP
E3 ubiquitin-protein ligase TRAIP
Also known as: RNF206, TRAIP_HUMAN, TRIP
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9BWF2
- Gene
- TRAIP
- Ensembl
- ENSG00000183763
- Chromosome
- 3
- Canonical length
- 469 aa
- Protein class
- Disease related genes, Enzymes, Human disease related genes, Potential drug targets, Predicted intracellular proteins
- Subcellular location
- Plasma membrane,Cytosol
OverviewNCBI Gene
This gene encodes a protein that contains an N-terminal RING finger motif and a putative coiled-coil domain. A similar murine protein interacts with TNFR-associated factor 1 (TRAF1), TNFR-associated factor 2 (TRAF2), and cylindromatosis. The interaction with TRAF2 inhibits TRAF2-mediated nuclear factor kappa-B, subunit 1 activation that is required for cell activation and protection against apoptosis. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
469 residues, UniProt reviewed canonical sequence.
>Q9BWF2|TRAIP
1 MPIRALCTIC SDFFDHSRDV AAIHCGHTFH LQCLIQWFET APSRTCPQCR IQVGKRTIIN
61 KLFFDLAQEE ENVLDAEFLK NELDNVRAQL SQKDKEKRDS QVIIDTLRDT LEERNATVVS
121 LQQALGKAEM LCSTLKKQMK YLEQQQDETK QAQEEARRLR SKMKTMEQIE LLLQSQRPEV
181 EEMIRDMGVG QSAVEQLAVY CVSLKKEYEN LKEARKASGE VADKLRKDLF SSRSKLQTVY
241 SELDQAKLEL KSAQKDLQSA DKEIMSLKKK LTMLQETLNL PPVASETVDR LVLESPAPVE
301 VNLKLRRPSF RDDIDLNATF DVDTPPARPS SSQHGYYEKL CLEKSHSPIQ DVPKKICKGP
361 RKESQLSLGG QSCAGEPDEE LVGAFPIFVR NAILGQKQPK RPRSESSCSK DVVRTGFDGL
421 GGRTKFIQPT DTVMIRPLPV KPKTKVKQRV RVKTVPSLFQ AKLDTFLWSLocalizationUniProt · AlphaFold · HPA
Whether an antibody against TRAIP 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)
- 0.54
- Highest tissue expression
- 7.6 nTPM
Expression across tissuesHPA
Tissue
- testis: 7.6 nTPM
- bone marrow: 6.4 nTPM
- basal ganglia: 6 nTPM
- thymus: 5 nTPM
- lymph node: 4.3 nTPM
- tonsil: 4.1 nTPM
Single-cell type
- oocytes: 41 nCPM
- early primary spermatocytes: 18 nCPM
- differentiating spermatogonia: 14 nCPM
- monocyte progenitors: 14 nCPM
- late primary spermatocytes: 13 nCPM
- retinal amacrine cells: 12 nCPM
Immune cell
- memory B-cell: 2.9 nTPM
- memory CD8 T-cell: 2.1 nTPM
- naive B-cell: 1.5 nTPM
- non-classical monocyte: 1.3 nTPM
- NK-cell: 1.2 nTPM
- naive CD8 T-cell: 1.1 nTPM
Brain region
- basal ganglia: 5.1 nTPM
- hippocampal formation: 3.2 nTPM
- amygdala: 2.6 nTPM
- hypothalamus: 2.5 nTPM
- cerebral cortex: 2.1 nTPM
- thalamus: 2.1 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about TRAIP.
Disease | AllUniProt
Conditions TRAIP is implicated in, by any mechanism.
- Seckel syndrome 9 (SCKL9) MIM:616777
Disease | GeneticClinVar
13 pathogenic / likely-pathogenic of 230 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Seckel syndrome 9
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)
- 0.71
- gnomAD pLI
- 0
- gnomAD missense Z
- 1.32
- DepMap mean gene effect
- -0.62
- DepMap dependency class
- common
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
- apoptotic process
- DNA damage response
- negative regulation of interferon-beta production
- negative regulation of tumor necrosis factor-mediated signaling pathway
- protein ubiquitination
- protein-DNA covalent cross-linking repair
- replication fork processing
- signal transduction
Molecular functions
- identical protein binding
- ubiquitin protein ligase activity
- ubiquitin-protein transferase activity
- zinc ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Zinc finger, RING-type
- Zinc finger, RING/FYVE/PHD-type
- Ring finger domain
- TRAIP E3 ubiquitin-protein ligase
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of TRAIP 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 TRAIP as an antibody target. Whether an autoantibody or antibody against TRAIP could matter depends on whether native TRAIP is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
TRAIP 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 TRAIP as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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