RNF8
E3 ubiquitin-protein ligase RNF8
Also known as: KIAA0646, RNF8_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- O76064
- Gene
- RNF8
- Ensembl
- ENSG00000112130
- Chromosome
- 6
- Canonical length
- 485 aa
- Protein class
- Enzymes, Metabolic proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Cytosol
- Quaternary structure
- Homodimer
OverviewNCBI Gene
The protein encoded by this gene contains a RING finger motif and an FHA domain. This protein has been shown to interact with several class II ubiquitin-conjugating enzymes (E2), including UBE2E1/UBCH6, UBE2E2, and UBE2E3, and may act as an ubiquitin ligase (E3) in the ubiquitination of certain nuclear proteins. This protein is also known to play a role in the DNA damage response and depletion of this protein causes cell growth inhibition and cell cycle arrest. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2012]
Canonical amino-acid sequenceUniProt
485 residues, UniProt reviewed canonical sequence.
>O76064|RNF8
1 MGEPGFFVTG DRAGGRSWCL RRVGMSAGWL LLEDGCEVTV GRGFGVTYQL VSKICPLMIS
61 RNHCVLKQNP EGQWTIMDNK SLNGVWLNRA RLEPLRVYSI HQGDYIQLGV PLENKENAEY
121 EYEVTEEDWE TIYPCLSPKN DQMIEKNKEL RTKRKFSLDE LAGPGAEGPS NLKSKINKVS
181 CESGQPVKSQ GKGEVASTPS DNLDPKLTAL EPSKTTGAPI YPGFPKVTEV HHEQKASNSS
241 ASQRSLQMFK VTMSRILRLK IQMQEKHEAV MNVKKQTQKG NSKKVVQMEQ ELQDLQSQLC
301 AEQAQQQARV EQLEKTFQEE EQHLQGLEIA QGEKDLKQQL AQALQEHWAL MEELNRSKKD
361 FEAIIQAKNK ELEQTKEEKE KMQAQKEEVL SHMNDVLENE LQCIICSEYF IEAVTLNCAH
421 SFCSYCINEW MKRKIECPIC RKDIKSKTYS LVLDNCINKM VNNLSSEVKE RRIVLIRERK
481 AKRLFLocalizationUniProt · AlphaFold · HPA
Whether an antibody against RNF8 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)
- 0.45
- Highest tissue expression
- 14 nTPM
Expression across tissuesHPA
Tissue
- choroid plexus: 14 nTPM
- cerebellum: 14 nTPM
- testis: 11 nTPM
- esophagus: 10 nTPM
- cerebral cortex: 10 nTPM
- tongue: 9.9 nTPM
Single-cell type
- sertoli cells: 117 nCPM
- esophageal apical cells: 99 nCPM
- megakaryocytes: 99 nCPM
- esophageal suprabasal cells: 81 nCPM
- endometrial luminal cells: 74 nCPM
- platelets: 73 nCPM
Immune cell
- gdT-cell: 9.5 nTPM
- T-reg: 9.2 nTPM
- memory CD8 T-cell: 9.1 nTPM
- MAIT T-cell: 8.8 nTPM
- non-classical monocyte: 8.8 nTPM
- memory B-cell: 8.1 nTPM
Brain region
- cerebellum: 18 nTPM
- cerebral cortex: 17 nTPM
- thalamus: 16 nTPM
- midbrain: 15 nTPM
- hypothalamus: 15 nTPM
- pons: 15 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)
- 0.18
- gnomAD pLI
- 1
- gnomAD missense Z
- 2.16
- DepMap mean gene effect
- -0.57
- DepMap dependency class
- common
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 8% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cell division
- DNA damage response
- DNA repair-dependent chromatin remodeling
- double-strand break repair
- double-strand break repair via nonhomologous end joining
- epigenetic regulation of gene expression
- interstrand cross-link repair
- isotype switching
- negative regulation of transcription elongation by RNA polymerase II
- positive regulation of DNA repair
- positive regulation of double-strand break repair via homologous recombination
- protein autoubiquitination
- protein K48-linked ubiquitination
- protein K6-linked ubiquitination
- protein K63-linked ubiquitination
- response to ionizing radiation
- signal transduction in response to DNA damage
- sperm DNA condensation
- ubiquitin-dependent protein catabolic process
Molecular functions
- chromatin binding
- histone binding
- identical protein binding
- protein homodimerization activity
- ubiquitin binding
- ubiquitin protein ligase activity
- ubiquitin protein ligase binding
- zinc ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of RNF8 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 RNF8 as an antibody target. Whether an autoantibody or antibody against RNF8 could matter depends on whether native RNF8 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
RNF8 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 RNF8 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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