ID A0A2K5HSS4_COLAP Unreviewed; 486 AA. AC A0A2K5HSS4; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 18-JUL-2018, entry version 5. DE RecName: Full=E3 ubiquitin-protein ligase RNF8 {ECO:0000256|HAMAP-Rule:MF_03067, ECO:0000256|PIRNR:PIRNR037950}; DE EC=2.3.2.27 {ECO:0000256|HAMAP-Rule:MF_03067, ECO:0000256|PIRNR:PIRNR037950}; DE AltName: Full=RING finger protein 8 {ECO:0000256|HAMAP-Rule:MF_03067}; DE AltName: Full=RING-type E3 ubiquitin transferase RNF8 {ECO:0000256|HAMAP-Rule:MF_03067}; GN Name=RNF8 {ECO:0000256|HAMAP-Rule:MF_03067, GN ECO:0000313|Ensembl:ENSCANP00000007391}; OS Colobus angolensis palliatus (Peters' Angolan colobus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Colobinae; Colobus. OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000007391, ECO:0000313|Proteomes:UP000233080}; RN [1] {ECO:0000313|Ensembl:ENSCANP00000007391, ECO:0000313|Proteomes:UP000233080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Hughes D.S., Murali S., Raveendran M., Korchina V., Bandaranaike D., RA Bellair M., Blankenburg K., Chao H., Dahdouli M., Dinh H., RA Doddapaneni H., Gnanaolivu R., Gross S., Jayaseelan J., Jones J., RA Khan Z., Kovar C., Kurapati P., Le B., Lee S., Mathew T., RA Narasimhan A., Okwuonu G., Ongeri F., Osuji N., Qu C., Quiroz J., RA Rajbhandari K., Reid J.G., Santibanez J., Skinner E., Wang Y., Xin Y., RA Han Y., Muzny D.M., Richards S., Worley K.C., Rogers J., Gibbs R.A.; RT "Black and white colobus reference genome project."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCANP00000007391} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2018) to UniProtKB. CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating CC enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin- CC conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor CC protein]-L-lysine. {ECO:0000256|HAMAP-Rule:MF_03067}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000256|HAMAP-Rule:MF_03067, ECO:0000256|PIRNR:PIRNR037950}. CC -!- DOMAIN: The FHA domain specifically recognizes and binds ATM- CC phosphorylated MDC1 and phosphorylated HERC2. {ECO:0000256|HAMAP- CC Rule:MF_03067}. CC -!- PTM: Autoubiquitinated through 'Lys-48' and 'Lys-63' of ubiquitin. CC 'Lys-63' polyubiquitination is mediated by UBE2N. 'Lys-29'-type CC polyubiquitination is also observed, but it doesn't require its CC own functional RING-type zinc finger. {ECO:0000256|HAMAP- CC Rule:MF_03067}. CC -!- SIMILARITY: Belongs to the RNF8 family. {ECO:0000256|HAMAP- CC Rule:MF_03067, ECO:0000256|PIRNR:PIRNR037950}. CC -!- CAUTION: According to a well-established model, RNF8 initiate H2A CC 'Lys-63'-linked ubiquitination leading to recruitment of RNF168 to CC amplify H2A 'Lys-63'-linked ubiquitination. However, other data CC suggest that RNF168 is the priming ubiquitin ligase by mediating CC monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone CC H2A (H2AK13Ub and H2AK15Ub respectively). These data suggest that CC RNF168 might be recruited to DSBs sites in a RNF8-dependent manner CC by binding to non-histone proteins ubiquitinated via 'Lys-63'- CC linked and initiates monoubiquitination of H2A, which is then CC amplified by RNF8. Additional evidences are however required to CC confirm these data. {ECO:0000256|HAMAP-Rule:MF_03067}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_011799916.1; XM_011944526.1. DR Ensembl; ENSCANT00000027385; ENSCANP00000007391; ENSCANG00000024187. DR GeneID; 105513611; -. DR CTD; 9025; -. DR GeneTree; ENSGT00400000022349; -. DR UniPathway; UPA00143; -. DR Proteomes; UP000233080; Whole Genome Shotgun Assembly. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-KW. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule. DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:UniProtKB-UniRule. DR GO; GO:0003682; F:chromatin binding; IEA:UniProtKB-UniRule. DR GO; GO:0042393; F:histone binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-UniRule. DR GO; GO:0043130; F:ubiquitin binding; IEA:UniProtKB-UniRule. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0006302; P:double-strand break repair; IEA:UniProtKB-UniRule. DR GO; GO:0033522; P:histone H2A ubiquitination; IEA:UniProtKB-UniRule. DR GO; GO:0033523; P:histone H2B ubiquitination; IEA:UniProtKB-UniRule. DR GO; GO:0045739; P:positive regulation of DNA repair; IEA:UniProtKB-UniRule. DR GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:UniProtKB-UniRule. DR GO; GO:0010212; P:response to ionizing radiation; IEA:UniProtKB-UniRule. DR CDD; cd00060; FHA; 1. DR Gene3D; 3.30.40.10; -; 1. DR HAMAP; MF_03067; RNF8; 1. DR InterPro; IPR000253; FHA_dom. DR InterPro; IPR017335; RNF8. DR InterPro; IPR008984; SMAD_FHA_dom_sf. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR Pfam; PF00498; FHA; 1. DR PIRSF; PIRSF037950; E3_ubiquit_lig_RNF8; 1. DR SMART; SM00240; FHA; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF49879; SSF49879; 1. DR PROSITE; PS50006; FHA_DOMAIN; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_03067}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_03067}; KW Chromatin regulator {ECO:0000256|HAMAP-Rule:MF_03067, KW ECO:0000256|PIRNR:PIRNR037950}; KW Chromosome {ECO:0000256|HAMAP-Rule:MF_03067}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000233080}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03067}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_03067, KW ECO:0000256|PIRNR:PIRNR037950}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_03067, KW ECO:0000256|PIRNR:PIRNR037950}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03067}; KW Mitosis {ECO:0000256|HAMAP-Rule:MF_03067}; KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03067, KW ECO:0000256|PIRNR:PIRNR037950}; KW Reference proteome {ECO:0000313|Proteomes:UP000233080}; KW Telomere {ECO:0000256|HAMAP-Rule:MF_03067}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03067}; KW Ubl conjugation {ECO:0000256|HAMAP-Rule:MF_03067}; KW Ubl conjugation pathway {ECO:0000256|HAMAP-Rule:MF_03067, KW ECO:0000256|PIRNR:PIRNR037950}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_03067}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_03067, ECO:0000256|PROSITE- KW ProRule:PRU00175}. FT DOMAIN 38 92 FHA. {ECO:0000259|PROSITE:PS50006}. FT DOMAIN 404 442 RING-type. {ECO:0000259|PROSITE:PS50089}. FT REGION 68 72 Required for interaction with PIWIL1. FT {ECO:0000256|HAMAP-Rule:MF_03067}. FT COILED 279 299 {ECO:0000256|SAM:Coils}. FT COILED 302 331 {ECO:0000256|SAM:Coils}. FT COILED 334 393 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 486 AA; 55611 MW; 2F1FD22E84B1F59A CRC64; MGEPGFFVTG DRAGGRSWCL RRVGMSAGWL LLEDGLEVTV GRGFGVTYQL VSKICPLMIS RNHCVLKQNP EGQWTIMDNK SLNGVWLNRA RLEPLRVYSI QQGDYIQLGV PLENKENAEY EYEVTEEDWE TIYPCLSPKN DQMIEKNKEL RTKRKFSLDQ LGGPGAEGPS NLKSKINKVS YESGQSVKSQ GKGEVASTPS ENLDPKLTAL EPSKNTTGAP IYSGFPIVTE VHHEQKASNS SASQRSLQMF KVTMSRILRL KIQMQEKHEA VTNVKKQTQK GNSKKIVQME QELQDLQSQL CAEQAQQQAR VEQLEKTFQE EEQHLEGLEI AQGEEDLKQQ LAQALQEHWA LMEELNRSKK DFEAIIQAKN KELEQTKEEK EKVQAQKEEV LSHMNDVLEN ELQCIICSEY FIEAVTLNCA HSFCSYCINE WMKRKIECPI CRKDIESKTY SLVLDNCINK MVNNLSSEVK ERRIVLIRER KAKRLF //