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	MGI: 1929069 HomoloGene: 2944 GeneCards: RNF8
Gene ontology Molecular function • protein homodimerization activity • histone binding • zinc ion binding • chromatin binding • metal ion binding • ubiquitin-protein transferase activity • ligase activity • protein binding • ubiquitin protein ligase binding Cellular component • cytoplasm • site of double-strand break • ubiquitin ligase complex • nucleoplasm • chromosome • chromosome, telomeric region • midbody • nucleus Biological process • response to ionizing radiation • histone H2A ubiquitination • mitotic nuclear division • 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 • covalent chromatin modification Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9025	58230
Ensembl	ENSG00000112130	ENSMUSG00000090083
UniProt	O76064	Q8VC56
RefSeq (mRNA)	NM_003958 NM_183078	NM_021419
RefSeq (protein)	NP_003949.1 NP_898901.1	NP_067394.1
Location (UCSC)	Chr 6: 37.35 – 37.39 Mb	Chr 17: 29.61 – 29.64 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

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E3 ubiquitin-protein ligase RNF8 is an enzyme that in humans is encoded by the RNF8 gene.^[3][4][5]

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.^[5]

Interactions

RNF8 has been shown to interact with Retinoid X receptor alpha.^[6]

See also

• RING finger domain

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Jun 1998). "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Research. 5 (3): 169–76. doi:10.1093/dnares/5.3.169. PMID 9734811.
4. Seki N, Hattori A, Sugano S, Suzuki Y, Nakagawara A, Ohhira M, Muramatsu M, Hori T, Saito T (Jan 1999). "Isolation, tissue expression, and chromosomal assignment of a novel human gene which encodes a protein with RING finger motif". Journal of Human Genetics. 43 (4): 272–4. doi:10.1007/s100380050088. PMID 9852682.
5. "Entrez Gene: RNF8 ring finger protein 8".
6. 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.

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.
• 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 US National Library of Medicine Medical Subject Headings (MeSH)