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E3 ubiquitin-protein ligase RNF8 (hRNF8) (EC 2.3.2.27) (RING finger protein 8) (RING-type E3 ubiquitin transferase RNF8)

 RNF8_HUMAN              Reviewed;         485 AA.
O76064; A6NN24; A8MYC0; B4DPG0; Q53H16; Q5NKW5;
06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
22-NOV-2017, entry version 176.
RecName: Full=E3 ubiquitin-protein ligase RNF8 {ECO:0000255|HAMAP-Rule:MF_03067};
Short=hRNF8;
EC=2.3.2.27 {ECO:0000255|HAMAP-Rule:MF_03067};
AltName: Full=RING finger protein 8 {ECO:0000255|HAMAP-Rule:MF_03067};
AltName: Full=RING-type E3 ubiquitin transferase RNF8 {ECO:0000255|HAMAP-Rule:MF_03067};
Name=RNF8 {ECO:0000255|HAMAP-Rule:MF_03067}; Synonyms=KIAA0646;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=9852682; DOI=10.1007/s100380050088;
Seki N., Hattori A., Sugano S., Suzuki Y., Nakagawara A., Ohhira M.,
Muramatsu M., Hori T., Saito T.;
"Isolation, tissue expression, and chromosomal assignment of a novel
human gene which encodes a protein with RING finger motif.";
J. Hum. Genet. 43:272-274(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, INTERACTION WITH UBE2E2 AND UBE2N, AUTOUBIQUITINATION,
AND MUTAGENESIS OF CYS-403.
TISSUE=Fetal brain;
PubMed=16215985; DOI=10.1002/jcb.20587;
Plans V., Scheper J., Soler M., Loukili N., Okano Y., Thomson T.M.;
"The RING finger protein RNF8 recruits UBC13 for lysine 63-based self
polyubiquitylation.";
J. Cell. Biochem. 97:572-582(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"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 Res. 5:169-176(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hepatoma;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 81-89; 156-173 AND 215-226, FUNCTION, SUBCELLULAR
LOCATION, MASS SPECTROMETRY, AND MUTAGENESIS OF ARG-42.
PubMed=23233665; DOI=10.1074/jbc.M112.423392;
Zhang S., Zhou Y., Sarkeshik A., Yates J.R. III, Thomson T.M.,
Zhang Z., Lee E.Y., Lee M.Y.;
"Identification of RNF8 as a ubiquitin ligase involved in targeting
the p12 subunit of DNA polymerase delta for degradation in response to
DNA damage.";
J. Biol. Chem. 288:2941-2950(2013).
[11]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UBE2E1; UBE2E2 AND
UBE2E3, AND MUTAGENESIS OF CYS-403.
PubMed=11322894; DOI=10.1046/j.1432-1327.2001.02169.x;
Ito K., Adachi S., Iwakami R., Yasuda H., Muto Y., Seki N., Okano Y.;
"N-terminally extended human ubiquitin-conjugating enzymes (E2s)
mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8.";
Eur. J. Biochem. 268:2725-2732(2001).
[12]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RXRA, AND MUTAGENESIS
OF CYS-403.
PubMed=14981089; DOI=10.1074/jbc.M309148200;
Takano Y., Adachi S., Okuno M., Muto Y., Yoshioka T.,
Matsushima-Nishiwaki R., Tsurumi H., Ito K., Friedman S.L.,
Moriwaki H., Kojima S., Okano Y.;
"The RING finger protein, RNF8, interacts with retinoid X receptor
alpha and enhances its transcription-stimulating activity.";
J. Biol. Chem. 279:18926-18934(2004).
[13]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH
MDC1, DOMAIN, AND MUTAGENESIS OF ARG-42 AND CYS-403.
PubMed=18001824; DOI=10.1016/j.cell.2007.09.040;
Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J.,
Lukas C., Lukas J.;
"RNF8 ubiquitylates histones at DNA double-strand breaks and promotes
assembly of repair proteins.";
Cell 131:887-900(2007).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18077395; DOI=10.1073/pnas.0710061104;
Wang B., Elledge S.J.;
"Ubc13/Rnf8 ubiquitin ligases control foci formation of the
Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage.";
Proc. Natl. Acad. Sci. U.S.A. 104:20759-20763(2007).
[15]
FUNCTION, AND INTERACTION WITH MDC1.
PubMed=18006705; DOI=10.1126/science.1150034;
Kolas N.K., Chapman J.R., Nakada S., Ylanko J., Chahwan R.,
Sweeney F.D., Panier S., Mendez M., Wildenhain J., Thomson T.M.,
Pelletier L., Jackson S.P., Durocher D.;
"Orchestration of the DNA-damage response by the RNF8 ubiquitin
ligase.";
Science 318:1637-1640(2007).
[16]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=17724460; DOI=10.1038/sj.onc.1210782;
Plans V., Guerra-Rebollo M., Thomson T.M.;
"Regulation of mitotic exit by the RNF8 ubiquitin ligase.";
Oncogene 27:1355-1365(2008).
[17]
FUNCTION.
PubMed=18948756; DOI=10.4161/cc.7.21.6949;
Zhang S., Chea J., Meng X., Zhou Y., Lee E.Y.C., Lee M.Y.W.T.;
"PCNA is ubiquitinated by RNF8.";
Cell Cycle 7:3399-3404(2008).
[18]
FUNCTION.
PubMed=18337245; DOI=10.1074/jbc.M710197200;
Sakasai R., Tibbetts R.;
"RNF8-dependent and RNF8-independent regulation of 53BP1 in response
to DNA damage.";
J. Biol. Chem. 283:13549-13555(2008).
[19]
INTERACTION WITH UBE2N.
PubMed=18678647; DOI=10.1128/MCB.00987-08;
Huen M.S.Y., Huang J., Yuan J., Yamamoto M., Akira S., Ashley C.,
Xiao W., Chen J.;
"Noncanonical E2 variant-independent function of UBC13 in promoting
checkpoint protein assembly.";
Mol. Cell. Biol. 28:6104-6112(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
INTERACTION WITH HERC2.
PubMed=20023648; DOI=10.1038/ncb2008;
Bekker-Jensen S., Rendtlew Danielsen J., Fugger K., Gromova I.,
Nerstedt A., Lukas C., Bartek J., Lukas J., Mailand N.;
"HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors
on damaged chromosomes.";
Nat. Cell Biol. 12:80-86(2010).
[23]
FUNCTION.
PubMed=19203578; DOI=10.1016/j.cell.2008.12.042;
Stewart G.S., Panier S., Townsend K., Al-Hakim A.K., Kolas N.K.,
Miller E.S., Nakada S., Ylanko J., Olivarius S., Mendez M.,
Oldreive C., Wildenhain J., Tagliaferro A., Pelletier L.,
Taubenheim N., Durandy A., Byrd P.J., Stankovic T., Taylor A.M.R.,
Durocher D.;
"The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling
cascade at sites of DNA damage.";
Cell 136:420-434(2009).
[24]
FUNCTION.
PubMed=19203579; DOI=10.1016/j.cell.2008.12.041;
Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H.,
Pepperkok R., Ellenberg J., Panier S., Durocher D., Bartek J.,
Lukas J., Lukas C.;
"RNF168 binds and amplifies ubiquitin conjugates on damaged
chromosomes to allow accumulation of repair proteins.";
Cell 136:435-446(2009).
[25]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19124460; DOI=10.1074/jbc.M809158200;
Gong Z., Cho Y.-W., Kim J.-E., Ge K., Chen J.;
"Accumulation of Pax2 transactivation domain interaction protein
(PTIP) at sites of DNA breaks via RNF8-dependent pathway is required
for cell survival after DNA damage.";
J. Biol. Chem. 284:7284-7293(2009).
[26]
FUNCTION.
PubMed=19015238; DOI=10.1128/MCB.01302-08;
Wu J., Huen M.S.Y., Lu L.-Y., Ye L., Dou Y., Ljungman M., Chen J.,
Yu X.;
"Histone ubiquitination associates with BRCA1-dependent DNA damage
response.";
Mol. Cell. Biol. 29:849-860(2009).
[27]
FUNCTION.
PubMed=19202061; DOI=10.1073/pnas.0807485106;
Shao G., Lilli D.R., Patterson-Fortin J., Coleman K.A.,
Morrissey D.E., Greenberg R.A.;
"The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-
Ubc13-dependent ubiquitination events at DNA double strand breaks.";
Proc. Natl. Acad. Sci. U.S.A. 106:3166-3171(2009).
[28]
FUNCTION.
PubMed=20550933; DOI=10.1016/j.cell.2010.04.038;
Shanbhag N.M., Rafalska-Metcalf I.U., Balane-Bolivar C., Janicki S.M.,
Greenberg R.A.;
"ATM-dependent chromatin changes silence transcription in cis to DNA
double-strand breaks.";
Cell 141:970-981(2010).
[29]
FUNCTION.
PubMed=21558560; DOI=10.1074/jbc.M111.232041;
Sy S.M., Jiang J., Dong S.S., Lok G.T., Wu J., Cai H., Yeung E.S.,
Huang J., Chen J., Deng Y., Huen M.S.;
"Critical roles of ring finger protein RNF8 in replication stress
responses.";
J. Biol. Chem. 286:22355-22361(2011).
[30]
FUNCTION, AND MUTAGENESIS OF ARG-42 AND CYS-406.
PubMed=21857671; DOI=10.1038/ncb2326;
Peuscher M.H., Jacobs J.J.;
"DNA-damage response and repair activities at uncapped telomeres
depend on RNF8.";
Nat. Cell Biol. 13:1139-1145(2011).
[31]
FUNCTION.
PubMed=22865450; DOI=10.1158/0008-5472.CAN-12-1057;
Nakada S., Yonamine R.M., Matsuo K.;
"RNF8 regulates assembly of RAD51 at DNA double-strand breaks in the
absence of BRCA1 and 53BP1.";
Cancer Res. 72:4974-4983(2012).
[32]
FUNCTION IN UBIQUITINATION OF KDM4A, AND MUTAGENESIS OF ILE-405.
PubMed=22373579; DOI=10.1038/emboj.2012.47;
Mallette F.A., Mattiroli F., Cui G., Young L.C., Hendzel M.J., Mer G.,
Sixma T.K., Richard S.;
"RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1
recruitment to DNA damage sites.";
EMBO J. 31:1865-1878(2012).
[33]
FUNCTION.
PubMed=22531782; DOI=10.1038/emboj.2012.104;
Luijsterburg M.S., Acs K., Ackermann L., Wiegant W.W.,
Bekker-Jensen S., Larsen D.H., Khanna K.K., van Attikum H.,
Mailand N., Dantuma N.P.;
"A new non-catalytic role for ubiquitin ligase RNF8 in unfolding
higher-order chromatin structure.";
EMBO J. 31:2511-2527(2012).
[34]
INTERACTION WITH HUMAN HERPESVIRUS 1 ICP0 (MICROBIAL INFECTION), AND
MUTAGENESIS OF ARG-42.
PubMed=22405594; DOI=10.1016/j.molcel.2012.02.004;
Chaurushiya M.S., Lilley C.E., Aslanian A., Meisenhelder J.,
Scott D.C., Landry S., Ticau S., Boutell C., Yates J.R. III,
Schulman B.A., Hunter T., Weitzman M.D.;
"Viral E3 ubiquitin ligase-mediated degradation of a cellular E3:
viral mimicry of a cellular phosphorylation mark targets the RNF8 FHA
domain.";
Mol. Cell 46:79-90(2012).
[35]
FUNCTION.
PubMed=22705371; DOI=10.1016/j.molcel.2012.05.026;
Yan Z., Guo R., Paramasivam M., Shen W., Ling C., Fox D. III, Wang Y.,
Oostra A.B., Kuehl J., Lee D.Y., Takata M., Hoatlin M.E.,
Schindler D., Joenje H., de Winter J.P., Li L., Seidman M.M., Wang W.;
"A ubiquitin-binding protein, FAAP20, links RNF8-mediated
ubiquitination to the Fanconi anemia DNA repair network.";
Mol. Cell 47:61-75(2012).
[36]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UBE2N.
PubMed=22266820; DOI=10.1038/nsmb.2211;
Feng L., Chen J.;
"The E3 ligase RNF8 regulates KU80 removal and NHEJ repair.";
Nat. Struct. Mol. Biol. 19:201-206(2012).
[37]
FUNCTION, AND MUTAGENESIS OF ILE-405.
PubMed=21911360; DOI=10.1093/nar/gkr655;
Lok G.T., Sy S.M., Dong S.S., Ching Y.P., Tsao S.W., Thomson T.M.,
Huen M.S.;
"Differential regulation of RNF8-mediated Lys48- and Lys63-based poly-
ubiquitylation.";
Nucleic Acids Res. 40:196-205(2012).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[39]
STRUCTURE BY NMR OF 8-139.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the FHA domain of human ubiquitin ligase
protein RNF8.";
Submitted (NOV-2005) to the PDB data bank.
[40]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 13-146 IN COMPLEX WITH
PHOSPHOPEPTIDE, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
LOCATION.
PubMed=18001825; DOI=10.1016/j.cell.2007.09.041;
Huen M.S.Y., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J.;
"RNF8 transduces the DNA-damage signal via histone ubiquitylation and
checkpoint protein assembly.";
Cell 131:901-914(2007).
[41]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 351-483 IN COMPLEX WITH ZINC,
SUBUNIT, FUNCTION, AND MUTAGENESIS OF ASP-443.
PubMed=22980979; DOI=10.1016/j.cell.2012.08.005;
Mattiroli F., Vissers J.H., van Dijk W.J., Ikpa P., Citterio E.,
Vermeulen W., Marteijn J.A., Sixma T.K.;
"RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage
signaling.";
Cell 150:1182-1195(2012).
[42]
X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS) OF 345-485 IN COMPLEX WITH
UBE2N, AND MUTAGENESIS OF ILE-405.
PubMed=22589545; DOI=10.1074/jbc.M112.359653;
Campbell S.J., Edwards R.A., Leung C.C., Neculai D., Hodge C.D.,
Dhe-Paganon S., Glover J.N.;
"Molecular insights into the function of RING Finger (RNF)-containing
proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation.";
J. Biol. Chem. 287:23900-23910(2012).
-!- FUNCTION: E3 ubiquitin-protein ligase that plays a key role in DNA
damage signaling via 2 distinct roles: by mediating the 'Lys-63'-
linked ubiquitination of histones H2A and H2AX and promoting the
recruitment of DNA repair proteins at double-strand breaks (DSBs)
sites, and by catalyzing 'Lys-48'-linked ubiquitination to remove
target proteins from DNA damage sites. Following DNA DSBs, it is
recruited to the sites of damage by ATM-phosphorylated MDC1 and
catalyzes the 'Lys-63'-linked ubiquitination of histones H2A and
H2AX, thereby promoting the formation of TP53BP1 and BRCA1
ionizing radiation-induced foci (IRIF). Also controls the
recruitment of UIMC1-BRCC3 (RAP80-BRCC36) and PAXIP1/PTIP to DNA
damage sites. Also recruited at DNA interstrand cross-links (ICLs)
sites and catalyzes 'Lys-63'-linked ubiquitination of histones H2A
and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi
anemia (FA) complex, followed by interstrand cross-link repair.
H2A ubiquitination also mediates the ATM-dependent transcriptional
silencing at regions flanking DSBs in cis, a mechanism to avoid
collision between transcription and repair intermediates. Promotes
the formation of 'Lys-63'-linked polyubiquitin chains via
interactions with the specific ubiquitin-conjugating UBE2N/UBC13
and ubiquitinates non-histone substrates such as PCNA. Substrates
that are polyubiquitinated at 'Lys-63' are usually not targeted
for degradation. Also catalyzes the formation of 'Lys-48'-linked
polyubiquitin chains via interaction with the ubiquitin-
conjugating UBE2L6/UBCH8, leading to degradation of substrate
proteins such as CHEK2, JMJD2A/KDM4A and KU80/XRCC5: it is still
unclear how the preference toward 'Lys-48'- versus 'Lys-63'-linked
ubiquitination is regulated but it could be due to RNF8 ability to
interact with specific E2 specific ligases. For instance,
interaction with phosphorylated HERC2 promotes the association
between RNF8 and UBE2N/UBC13 and favors the specific formation of
'Lys-63'-linked ubiquitin chains. Promotes non-homologous end
joining (NHEJ) by promoting the 'Lys-48'-linked ubiquitination and
degradation the of KU80/XRCC5. Following DNA damage, mediates the
ubiquitination and degradation of JMJD2A/KDM4A in collaboration
with RNF168, leading to unmask H4K20me2 mark and promote the
recruitment of TP53BP1 at DNA damage sites (PubMed:11322894,
PubMed:14981089, PubMed:17724460, PubMed:18001824,
PubMed:18001825, PubMed:18006705, PubMed:18077395,
PubMed:18337245, PubMed:18948756, PubMed:19015238,
PubMed:19124460, PubMed:19202061, PubMed:19203578,
PubMed:19203579, PubMed:20550933, PubMed:21558560,
PubMed:21857671, PubMed:21911360, PubMed:22266820,
PubMed:22373579, PubMed:22531782, PubMed:22705371,
PubMed:22865450, PubMed:22980979). Following DNA damage, mediates
the ubiquitination and degradation of POLD4/p12, a subunit of DNA
polymerase delta. In the absence of POLD4, DNA polymerase delta
complex exhibits higher proofreading activity (PubMed:23233665).
In addition to its function in damage signaling, also plays a role
in higher-order chromatin structure by mediating extensive
chromatin decondensation. Involved in the activation of ATM by
promoting histone H2B ubiquitination, which indirectly triggers
histone H4 'Lys-16' acetylation (H4K16ac), establishing a
chromatin environment that promotes efficient activation of ATM
kinase. Required in the testis, where it plays a role in the
replacement of histones during spermatogenesis. At uncapped
telomeres, promotes the joining of deprotected chromosome ends by
inducing H2A ubiquitination and TP53BP1 recruitment, suggesting
that it may enhance cancer development by aggravating telomere-
induced genome instability in case of telomeric crisis. Promotes
the assembly of RAD51 at DNA DSBs in the absence of BRCA1 and
TP53BP1 Also involved in class switch recombination in immune
system, via its role in regulation of DSBs repair. May be required
for proper exit from mitosis after spindle checkpoint activation
and may regulate cytokinesis. May play a role in the regulation of
RXRA-mediated transcriptional activity. Not involved in RXRA
ubiquitination by UBE2E2 (PubMed:11322894, PubMed:14981089,
PubMed:17724460, PubMed:18001824, PubMed:18001825,
PubMed:18006705, PubMed:18077395, PubMed:18337245,
PubMed:18948756, PubMed:19015238, PubMed:19124460,
PubMed:19202061, PubMed:19203578, PubMed:19203579,
PubMed:20550933, PubMed:21558560, PubMed:21857671,
PubMed:21911360, PubMed:22266820, PubMed:22373579,
PubMed:22531782, PubMed:22705371, PubMed:22865450,
PubMed:22980979). {ECO:0000269|PubMed:11322894,
ECO:0000269|PubMed:14981089, ECO:0000269|PubMed:17724460,
ECO:0000269|PubMed:18001824, ECO:0000269|PubMed:18001825,
ECO:0000269|PubMed:18006705, ECO:0000269|PubMed:18077395,
ECO:0000269|PubMed:18337245, ECO:0000269|PubMed:18948756,
ECO:0000269|PubMed:19015238, ECO:0000269|PubMed:19124460,
ECO:0000269|PubMed:19202061, ECO:0000269|PubMed:19203578,
ECO:0000269|PubMed:19203579, ECO:0000269|PubMed:20550933,
ECO:0000269|PubMed:21558560, ECO:0000269|PubMed:21857671,
ECO:0000269|PubMed:21911360, ECO:0000269|PubMed:22266820,
ECO:0000269|PubMed:22373579, ECO:0000269|PubMed:22531782,
ECO:0000269|PubMed:22705371, ECO:0000269|PubMed:22865450,
ECO:0000269|PubMed:22980979, ECO:0000269|PubMed:23233665}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000255|HAMAP-Rule:MF_03067}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|HAMAP-Rule:MF_03067}.
-!- SUBUNIT: Homodimer. Forms a E2-E3 ubiquitin ligase complex
composed of the RNF8 homodimer and a E2 heterodimer of UBE2N and
UBE2V2. Interacts with class III E2s, including UBE2E1, UBE2E2,
and UBE2E3 and with UBE2N. Interacts with RXRA. Interacts (via FHA
domain) with ATM-phosphorylated MDC1. Interacts (via FHA domain)
with 'Thr-4827' phosphorylated HERC2 (via C-terminus). Interacts
with PIWIL1; leading to sequester RNF8 in the cytoplasm (By
similarity). {ECO:0000250|UniProtKB:Q8VC56,
ECO:0000269|PubMed:11322894, ECO:0000269|PubMed:14981089,
ECO:0000269|PubMed:16215985, ECO:0000269|PubMed:18001824,
ECO:0000269|PubMed:18001825, ECO:0000269|PubMed:18006705,
ECO:0000269|PubMed:18678647, ECO:0000269|PubMed:20023648,
ECO:0000269|PubMed:22266820, ECO:0000269|PubMed:22589545,
ECO:0000269|PubMed:22980979}.
-!- SUBUNIT: (Microbial infection) Interacts (via FHA domain) with
phosphorylated human herpesvirus 1 ICP0 protein; leading to RNF8
degradation by the proteasome. {ECO:0000269|PubMed:22405594}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-373337, EBI-373337;
Q9C0F1:CEP44; NbExp=3; IntAct=EBI-373337, EBI-744115;
V9HW80:HEL-S-70; NbExp=3; IntAct=EBI-373337, EBI-10175326;
Q8IX15-3:HOMEZ; NbExp=3; IntAct=EBI-373337, EBI-10172004;
Q5T7B8-2:KIF24; NbExp=4; IntAct=EBI-373337, EBI-10213781;
P61968:LMO4; NbExp=4; IntAct=EBI-373337, EBI-2798728;
Q9Y6D9:MAD1L1; NbExp=5; IntAct=EBI-373337, EBI-742610;
Q14676:MDC1; NbExp=11; IntAct=EBI-373337, EBI-495644;
Q9UL42:PNMA2; NbExp=8; IntAct=EBI-373337, EBI-302355;
O43251:RBFOX2; NbExp=3; IntAct=EBI-373337, EBI-746056;
Q9UH03:SEPT3; NbExp=5; IntAct=EBI-373337, EBI-727037;
O75558:STX11; NbExp=4; IntAct=EBI-373337, EBI-714135;
Q9BSE2:TMEM79; NbExp=5; IntAct=EBI-373337, EBI-8649725;
Q99986:VRK1; NbExp=2; IntAct=EBI-373337, EBI-1769146;
Q9Y3C0:WASHC3; NbExp=4; IntAct=EBI-373337, EBI-712969;
O00401:WASL; NbExp=6; IntAct=EBI-373337, EBI-957615;
Q96IT1:ZNF496; NbExp=4; IntAct=EBI-373337, EBI-743906;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03067,
ECO:0000269|PubMed:11322894, ECO:0000269|PubMed:14981089,
ECO:0000269|PubMed:16215985, ECO:0000269|PubMed:23233665}.
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03067}. Midbody
{ECO:0000255|HAMAP-Rule:MF_03067}. Chromosome, telomere
{ECO:0000255|HAMAP-Rule:MF_03067}. Note=Recruited at uncapped
telomeres (By similarity). Following DNA damage, such as double-
strand breaks, recruited to the sites of damage (PubMed:18001824,
PubMed:18077395, PubMed:22266820, PubMed:23233665). During
prophase, concomitant with nuclear envelope breakdown, localizes
throughout the cell, with a dotted pattern. In telophase, again in
the nucleus and also with a discrete dotted pattern in the
cytoplasm. In late telophase and during cytokinesis, localizes in
the midbody of the tubulin bridge joining the daughter cells. Does
not seem to be associated with condensed chromosomes at any time
during the cell cycle. During spermatogenesis, sequestered in the
cytoplasm by PIWIL1: RNF8 is released following ubiquitination and
degradation of PIWIL1. {ECO:0000255|HAMAP-Rule:MF_03067,
ECO:0000269|PubMed:18001824, ECO:0000269|PubMed:18077395,
ECO:0000269|PubMed:22266820, ECO:0000269|PubMed:23233665}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O76064-1; Sequence=Displayed;
Name=2;
IsoId=O76064-2; Sequence=VSP_036671, VSP_037831;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay. No
experimental confirmation available.;
Name=3;
IsoId=O76064-3; Sequence=VSP_054037, VSP_054038;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- TISSUE SPECIFICITY: Ubiquitous. In fetal tissues, highest
expression in brain, thymus and liver. In adult tissues, highest
levels in brain and testis, lowest levels in peripheral blood
cells. {ECO:0000269|PubMed:16215985, ECO:0000269|PubMed:9852682}.
-!- DEVELOPMENTAL STAGE: Low levels at the G1-S boundary increase in
intensity during S phase and until the end of the G2 phase.
Abruptly decreases in late mitosis (at protein level). Barely
detectable in anaphase. {ECO:0000269|PubMed:17724460}.
-!- DOMAIN: The FHA domain specifically recognizes and binds ATM-
phosphorylated MDC1 and 'Thr-4827' phosphorylated HERC2
(PubMed:18001824). This domain is required for proper recruitment
to DNA damage sites after UV irradiation, ionizing radiation, or
treatment with an alkylating agent (PubMed:23233665).
{ECO:0000269|PubMed:18001824, ECO:0000269|PubMed:23233665}.
-!- PTM: Autoubiquitinated through 'Lys-48' and 'Lys-63' of ubiquitin.
'Lys-63' polyubiquitination is mediated by UBE2N. 'Lys-29'-type
polyubiquitination is also observed, but it doesn't require its
own functional RING-type zinc finger. {ECO:0000255|HAMAP-
Rule:MF_03067, ECO:0000269|PubMed:16215985}.
-!- SIMILARITY: Belongs to the RNF8 family. {ECO:0000255|HAMAP-
Rule:MF_03067}.
-!- CAUTION: According to a well-established model, RNF8 initiate H2A
'Lys-63'-linked ubiquitination leading to recruitment of RNF168 to
amplify H2A 'Lys-63'-linked ubiquitination (PubMed:19203578 and
PubMed:19203579). However, other data suggest that RNF168 is the
priming ubiquitin ligase by mediating monoubiquitination of 'Lys-
13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub
respectively) (PubMed:22980979). These data suggest that RNF168
might be recruited to DSBs sites in a RNF8-dependent manner by
binding to non-histone proteins ubiquitinated via 'Lys-63'-linked
and initiates monoubiquitination of H2A, which is then amplified
by RNF8 (PubMed:22980979). Additional evidences are however
required to confirm these data. {ECO:0000255|HAMAP-Rule:MF_03067,
ECO:0000305|PubMed:22980979}.
-!- SEQUENCE CAUTION:
Sequence=BAA31621.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG60572.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
Sequence=EAX03945.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB012770; BAA33557.1; -; Genomic_DNA.
EMBL; AF334675; AAQ14887.1; -; mRNA.
EMBL; AB014546; BAA31621.2; ALT_INIT; mRNA.
EMBL; AK298319; BAG60572.1; ALT_SEQ; mRNA.
EMBL; BT007446; AAP36114.1; -; mRNA.
EMBL; AK222765; BAD96485.1; -; mRNA.
EMBL; AL096712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX03944.1; -; Genomic_DNA.
EMBL; CH471081; EAX03945.1; ALT_SEQ; Genomic_DNA.
EMBL; BC007517; AAH07517.1; -; mRNA.
CCDS; CCDS4833.1; -. [O76064-3]
CCDS; CCDS4834.1; -. [O76064-1]
RefSeq; NP_003949.1; NM_003958.3. [O76064-1]
RefSeq; NP_898901.1; NM_183078.2. [O76064-3]
UniGene; Hs.485278; -.
PDB; 2CSW; NMR; -; A=8-139.
PDB; 2PIE; X-ray; 1.35 A; A=13-146.
PDB; 4AYC; X-ray; 1.90 A; A/B=351-485.
PDB; 4ORH; X-ray; 4.80 A; C/G/H/K/L=345-485.
PDB; 4WHV; X-ray; 8.30 A; C/D/I/J=345-485.
PDBsum; 2CSW; -.
PDBsum; 2PIE; -.
PDBsum; 4AYC; -.
PDBsum; 4ORH; -.
PDBsum; 4WHV; -.
ProteinModelPortal; O76064; -.
SMR; O76064; -.
BioGrid; 114492; 57.
DIP; DIP-31265N; -.
IntAct; O76064; 60.
MINT; MINT-1459889; -.
STRING; 9606.ENSP00000362578; -.
iPTMnet; O76064; -.
PhosphoSitePlus; O76064; -.
BioMuta; RNF8; -.
EPD; O76064; -.
MaxQB; O76064; -.
PaxDb; O76064; -.
PeptideAtlas; O76064; -.
PRIDE; O76064; -.
DNASU; 9025; -.
Ensembl; ENST00000229866; ENSP00000229866; ENSG00000112130. [O76064-2]
Ensembl; ENST00000373479; ENSP00000362578; ENSG00000112130. [O76064-1]
Ensembl; ENST00000469731; ENSP00000418879; ENSG00000112130. [O76064-3]
GeneID; 9025; -.
KEGG; hsa:9025; -.
UCSC; uc003onq.4; human. [O76064-1]
CTD; 9025; -.
DisGeNET; 9025; -.
EuPathDB; HostDB:ENSG00000112130.16; -.
GeneCards; RNF8; -.
HGNC; HGNC:10071; RNF8.
HPA; HPA050731; -.
HPA; HPA064925; -.
MIM; 611685; gene.
neXtProt; NX_O76064; -.
OpenTargets; ENSG00000112130; -.
PharmGKB; PA34445; -.
eggNOG; ENOG410INBI; Eukaryota.
eggNOG; ENOG410Z9IW; LUCA.
GeneTree; ENSGT00400000022349; -.
HOGENOM; HOG000154169; -.
HOVERGEN; HBG023954; -.
InParanoid; O76064; -.
KO; K10667; -.
OMA; IHKGDHI; -.
OrthoDB; EOG091G0I40; -.
PhylomeDB; O76064; -.
TreeFam; TF330957; -.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
SIGNOR; O76064; -.
UniPathway; UPA00143; -.
ChiTaRS; RNF8; human.
EvolutionaryTrace; O76064; -.
GeneWiki; RNF8; -.
GenomeRNAi; 9025; -.
PRO; PR:O76064; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112130; -.
CleanEx; HS_RNF8; -.
ExpressionAtlas; O76064; baseline and differential.
Genevisible; O76064; HS.
GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0006302; P:double-strand break repair; IDA:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
GO; GO:0043486; P:histone exchange; ISS:UniProtKB.
GO; GO:0070535; P:histone H2A K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:0033522; P:histone H2A ubiquitination; IDA:UniProtKB.
GO; GO:0033523; P:histone H2B ubiquitination; ISS:UniProtKB.
GO; GO:0036297; P:interstrand cross-link repair; TAS:UniProtKB.
GO; GO:0045190; P:isotype switching; ISS:UniProtKB.
GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0045739; P:positive regulation of DNA repair; IDA:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; ISS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
CDD; cd00060; FHA; 1.
Gene3D; 3.30.40.10; -; 1.
HAMAP; MF_03067; RNF8; 1.
InterPro; IPR000253; FHA_dom.
InterPro; IPR017335; RNF8.
InterPro; IPR008984; SMAD_FHA_dom_sf.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00498; FHA; 1.
PIRSF; PIRSF037950; E3_ubiquit_lig_RNF8; 1.
SMART; SM00240; FHA; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF49879; SSF49879; 1.
PROSITE; PS50006; FHA_DOMAIN; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Chromatin regulator; Chromosome; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA damage; DNA repair; Metal-binding;
Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Telomere; Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 485 E3 ubiquitin-protein ligase RNF8.
/FTId=PRO_0000056048.
DOMAIN 38 92 FHA. {ECO:0000255|HAMAP-Rule:MF_03067}.
ZN_FING 403 441 RING-type. {ECO:0000255|HAMAP-
Rule:MF_03067}.
REGION 68 72 Required for interaction with PIWIL1.
{ECO:0000255|HAMAP-Rule:MF_03067}.
COMPBIAS 276 345 Gln-rich.
MOD_RES 157 157 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 81 98 SLNGVWLNRARLEPLRVY -> SFPSEKAEDFTAAGERFL
(in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036671.
VAR_SEQ 99 485 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037831.
VAR_SEQ 413 448 AVTLNCAHSFCSYCINEWMKRKIECPICRKDIKSKT -> Q
RDCSEDRALRAFERLPGSASLRWSGGFSLAVTPLL (in
isoform 3). {ECO:0000305}.
/FTId=VSP_054037.
VAR_SEQ 449 485 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_054038.
VARIANT 162 162 A -> T (in dbSNP:rs34338974).
/FTId=VAR_052096.
VARIANT 473 473 I -> V (in dbSNP:rs1139944).
/FTId=VAR_052097.
MUTAGEN 42 42 R->A: Abolishes interaction with ATM-
phosphorylated MDC1. Abolishes
interaction with human herpesvirus 1
ICP0. Abolishes recruitment to DNA damage
sites after UV irradiation, ionizing
radiation, or treatment with an
alkylating agent.
{ECO:0000269|PubMed:18001824,
ECO:0000269|PubMed:21857671,
ECO:0000269|PubMed:22405594,
ECO:0000269|PubMed:23233665}.
MUTAGEN 403 403 C->S: Marked reduction of E2-dependent
ubiquitination of histone H2A. Loss of
UBE2E2- and UBE2N-binding. Loss of
nuclear localization.
{ECO:0000269|PubMed:11322894,
ECO:0000269|PubMed:14981089,
ECO:0000269|PubMed:16215985,
ECO:0000269|PubMed:18001824}.
MUTAGEN 405 405 I->A: Impairs interaction with
UBE2L6/UBCH8 and ability to mediate 'Lys-
48'-linked ubiquitination E3 ligase
activity, while it still catalyzes 'Lys-
63'-linked ubiquitination and still
interacts with UBE2N/UBC13.
{ECO:0000269|PubMed:21911360,
ECO:0000269|PubMed:22373579,
ECO:0000269|PubMed:22589545}.
MUTAGEN 406 406 C->S: Abolishes ubiquitin-ligase
activity. {ECO:0000269|PubMed:21857671}.
MUTAGEN 443 443 D->R: Does not affect the monomeric
structure but abolishes ability to
monoubiquitinate H2A in nucleosomes.
{ECO:0000269|PubMed:22980979}.
CONFLICT 230 230 V -> A (in Ref. 6; BAD96485).
{ECO:0000305}.
CONFLICT 334 334 K -> R (in Ref. 6; BAD96485).
{ECO:0000305}.
STRAND 16 22 {ECO:0000244|PDB:2PIE}.
STRAND 29 32 {ECO:0000244|PDB:2PIE}.
STRAND 38 49 {ECO:0000244|PDB:2PIE}.
HELIX 56 58 {ECO:0000244|PDB:2CSW}.
STRAND 64 68 {ECO:0000244|PDB:2PIE}.
STRAND 74 78 {ECO:0000244|PDB:2PIE}.
STRAND 85 87 {ECO:0000244|PDB:2PIE}.
STRAND 105 109 {ECO:0000244|PDB:2PIE}.
STRAND 119 128 {ECO:0000244|PDB:2PIE}.
HELIX 129 132 {ECO:0000244|PDB:2PIE}.
HELIX 133 135 {ECO:0000244|PDB:2PIE}.
HELIX 351 400 {ECO:0000244|PDB:4AYC}.
TURN 404 406 {ECO:0000244|PDB:4AYC}.
STRAND 411 416 {ECO:0000244|PDB:4AYC}.
STRAND 421 423 {ECO:0000244|PDB:4AYC}.
HELIX 424 430 {ECO:0000244|PDB:4AYC}.
TURN 431 433 {ECO:0000244|PDB:4AYC}.
TURN 438 440 {ECO:0000244|PDB:4AYC}.
STRAND 447 449 {ECO:0000244|PDB:4AYC}.
HELIX 451 461 {ECO:0000244|PDB:4AYC}.
HELIX 466 480 {ECO:0000244|PDB:4AYC}.
SEQUENCE 485 AA; 55518 MW; 54650B2FFC9948B1 CRC64;
MGEPGFFVTG DRAGGRSWCL RRVGMSAGWL LLEDGCEVTV GRGFGVTYQL VSKICPLMIS
RNHCVLKQNP EGQWTIMDNK SLNGVWLNRA RLEPLRVYSI HQGDYIQLGV PLENKENAEY
EYEVTEEDWE TIYPCLSPKN DQMIEKNKEL RTKRKFSLDE LAGPGAEGPS NLKSKINKVS
CESGQPVKSQ GKGEVASTPS DNLDPKLTAL EPSKTTGAPI YPGFPKVTEV HHEQKASNSS
ASQRSLQMFK VTMSRILRLK IQMQEKHEAV MNVKKQTQKG NSKKVVQMEQ ELQDLQSQLC
AEQAQQQARV EQLEKTFQEE EQHLQGLEIA QGEKDLKQQL AQALQEHWAL MEELNRSKKD
FEAIIQAKNK ELEQTKEEKE KMQAQKEEVL SHMNDVLENE LQCIICSEYF IEAVTLNCAH
SFCSYCINEW MKRKIECPIC RKDIKSKTYS LVLDNCINKM VNNLSSEVKE RRIVLIRERK
AKRLF


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