RNF8

RNF8
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2CSW, 2PIE, 4AYC, 4ORH, 4WHV
Identifiers
Aliases	RNF8, hring finger protein 8
External IDs	OMIM: 611685; MGI: 1929069; HomoloGene: 2944; GeneCards: RNF8; OMA:RNF8 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6p21.2 Start 37,353,979 bp End 37,394,734 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17|17 A3.3 Start 29,833,764 bp End 29,863,965 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence cerebellar hemisphere left testis right testis ventricular zone islet of Langerhans prefrontal cortex gonad right hemisphere of cerebellum mucosa of esophagus Top expressed in primary oocyte secondary oocyte zygote tail of embryo fetal liver hematopoietic progenitor cell maxillary prominence neural layer of retina endocardial cushion mandibular prominence superior cervical ganglion More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein homodimerization activity histone binding chromatin binding metal ion binding ubiquitin-protein transferase activity protein binding ubiquitin protein ligase binding transferase activity identical protein binding zinc ion binding ubiquitin binding ubiquitin protein ligase activity Cellular component site of double-strand break ubiquitin ligase complex nucleoplasm chromosome telomere midbody nucleus cytosol cytoplasm Biological process response to ionizing radiation histone H2A ubiquitination interstrand cross-link repair ubiquitin-dependent protein catabolic process protein K63-linked ubiquitination positive regulation of DNA repair histone H2A K63-linked ubiquitination negative regulation of transcription elongation from RNA polymerase II promoter cellular response to DNA damage stimulus cell division protein K48-linked ubiquitination isotype switching protein ubiquitination spermatid development cell cycle histone H2B ubiquitination double-strand break repair via nonhomologous end joining histone exchange protein autoubiquitination double-strand break repair DNA repair chromatin organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9025 58230 Ensembl ENSG00000112130 ENSMUSG00000090083 UniProt O76064 Q8VC56 RefSeq (mRNA) NM_003958 NM_183078 NM_021419 RefSeq (protein) NP_003949 NP_898901 NP_067394 Location (UCSC) Chr 6: 37.35 – 37.39 Mb Chr 17: 29.83 – 29.86 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

E3 ubiquitin-protein ligase RNF8 is an enzyme that in humans is encoded by the RNF8 gene.

Function

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 a ubiquitin ligase (E3) in the ubiquitination of certain nuclear proteins. Alternatively spliced transcript variants encoding distinct isoforms have been reported.

Interactions

RNF8 has been shown to interact with Retinoid X receptor alpha.

See also

• RING finger domain

Further reading

• Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Ito K, Adachi S, Iwakami R, Yasuda H, Muto Y, Seki N, Okano Y (May 2001). "N-Terminally extended human ubiquitin-conjugating enzymes (E2s) mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8". European Journal of Biochemistry / FEBS. 268 (9): 2725–32. doi:10.1046/j.1432-1327.2001.02169.x. PMID 11322894.
• Takano Y, Adachi S, Okuno M, Muto Y, Yoshioka T, Matsushima-Nishiwaki R, Tsurumi H, Ito K, Friedman SL, Moriwaki H, Kojima S, Okano Y (Apr 2004). "The RING finger protein, RNF8, interacts with retinoid X receptor alpha and enhances its transcription-stimulating activity". The Journal of Biological Chemistry. 279 (18): 18926–34. doi:10.1074/jbc.M309148200. PMID 14981089.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Lehner B, Sanderson CM (Jul 2004). "A protein interaction framework for human mRNA degradation". Genome Research. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Kolas NK, Chapman JR, Nakada S, Ylanko J, Chahwan R, Sweeney FD, Panier S, Mendez M, Wildenhain J, Thomson TM, Pelletier L, Jackson SP, Durocher D (Dec 2007). "Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase". Science. 318 (5856): 1637–40. doi:10.1126/science.1150034. PMC 2430610. PMID 18006705.

External links

• RNF8+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)