RNF34
E3 ubiquitin-protein ligase RNF34
Also known as: FLJ21786, RIF, RIFF, RNF34_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q969K3
- Gene
- RNF34
- Ensembl
- ENSG00000170633
- Chromosome
- 12
- Canonical length
- 372 aa
- Protein class
- Enzymes, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Nuclear bodies
OverviewNCBI Gene
The protein encoded by this gene contains a RINF finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein interacts with DNAJA3/hTid-1, which is a DnaJ protein reported to function as a modulator of apoptosis. Overexpression of this gene in Hela cells was shown to confer the resistance to TNF-alpha induced apoptosis, suggesting an anti-apoptotic function of this protein. This protein can be cleaved by caspase-3 during the induction of apoptosis. This protein also targets p53 and phospho-p53 for degradation. Alternatively splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Feb 2012]
Canonical amino-acid sequenceUniProt
372 residues, UniProt reviewed canonical sequence.
>Q969K3|RNF34
1 MKAGATSMWA SCCGLLNEVM GTGAVRGQQS AFAGATGPFR FTPNPEFSTY PPAATEGPNI
61 VCKACGLSFS VFRKKHVCCD CKKDFCSVCS VLQENLRRCS TCHLLQETAF QRPQLMRLKV
121 KDLRQYLILR NIPIDTCREK EDLVDLVLCH HGLGSEDDMD TSSLNSSRSQ TSSFFTRSFF
181 SNYTAPSATM SSFQGELMDG DQTSRSGVPA QVQSEITSAN TEDDDDDDDE DDDDEEENAE
241 DRNPGLSKER VRASLSDLSS LDDVEGMSVR QLKEILARNF VNYSGCCEKW ELVEKVNRLY
301 KENEENQKSY GERLQLQDEE DDSLCRICMD AVIDCVLLEC GHMVTCTKCG KRMSECPICR
361 QYVVRAVHVF KSLocalizationUniProt · AlphaFold · HPA
Whether an antibody against RNF34 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
- Cell surface
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.51
- Highest tissue expression
- 56 nTPM
Expression across tissuesHPA
Tissue
- skeletal muscle: 56 nTPM
- tongue: 35 nTPM
- lymph node: 33 nTPM
- thymus: 26 nTPM
- tonsil: 26 nTPM
- cerebellum: 25 nTPM
Single-cell type
- early primary spermatocytes: 258 nCPM
- myonuclei: 197 nCPM
- oocytes: 134 nCPM
- enterocytes: 126 nCPM
- epididymal clear cells: 114 nCPM
- cholangiocytes: 107 nCPM
Immune cell
- T-reg: 109 nTPM
- eosinophil: 94 nTPM
- basophil: 87 nTPM
- memory CD4 T-cell: 86 nTPM
- memory B-cell: 79 nTPM
- NK-cell: 79 nTPM
Brain region
- white matter: 56 nTPM
- cerebellum: 56 nTPM
- basal ganglia: 51 nTPM
- cerebral cortex: 50 nTPM
- hypothalamus: 49 nTPM
- midbrain: 45 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)
- 0.49
- gnomAD pLI
- 0.61
- gnomAD missense Z
- 1.44
- DepMap mean gene effect
- -0.05
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 7% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- apoptotic process
- cellular response to cold
- negative regulation of extrinsic apoptotic signaling pathway via death domain receptors
- negative regulation of signal transduction by p53 class mediator
- nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway
- proteasome-mediated ubiquitin-dependent protein catabolic process
- protein K48-linked ubiquitination
- protein ubiquitination
- regulation of signal transduction by p53 class mediator
- ubiquitin-dependent protein catabolic process
- regulation of oxygen metabolic process
Molecular functions
- p53 binding
- phosphatidylinositol phosphate binding
- ubiquitin protein ligase activity
- ubiquitin protein ligase binding
- zinc ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Zinc finger, RING-type
- Zinc finger, FYVE/PHD-type
- Zinc finger, RING/FYVE/PHD-type
- SAP domain superfamily
- E3 ubiquitin-protein ligase CARP1/2, FYVE/PHD zinc finger
- RING-FYVE domain-containing E3 ubiquitin-protein ligase
- RNF34/RFFL, HeH domain
- RNF34/RFFL, SAP domain
- Zinc finger, C3HC4 type (RING finger)
- E3 ubiquitin-protein ligase CARP1/2, FYVE/PHD zinc finger
- E3 ubiquitin-protein ligase rififylin-like domain
- RNF34/RFFL SAP domain
- E3 ubiquitin-protein ligase CARP1, FYVE/PHD zinc finger
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of RNF34 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 RNF34 as an antibody target. Whether an autoantibody or antibody against RNF34 could matter depends on whether native RNF34 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
RNF34 is annotated at the cell surface, where native RNF34 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label RNF34 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
Loading the interactive Seroatlas protein explorer...