XRCC6_MOUSE
ID XRCC6_MOUSE Reviewed; 608 AA.
AC P23475; O88212; Q3UJL8; Q62027; Q62382; Q62453; Q6GTV8; Q8QZX7;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 5.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=X-ray repair cross-complementing protein 6;
DE EC=3.6.4.-;
DE EC=4.2.99.-;
DE AltName: Full=5'-deoxyribose-5-phosphate lyase Ku70;
DE Short=5'-dRP/AP lyase Ku70;
DE AltName: Full=ATP-dependent DNA helicase 2 subunit 1;
DE AltName: Full=ATP-dependent DNA helicase II 70 kDa subunit;
DE AltName: Full=CTC box-binding factor 75 kDa subunit;
DE Short=CTC75;
DE Short=CTCBF;
DE AltName: Full=DNA repair protein XRCC6;
DE AltName: Full=Ku autoantigen protein p70 homolog;
DE Short=Ku70;
GN Name=Xrcc6; Synonyms=G22p1, Ku70;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=8661113; DOI=10.1006/geno.1996.0331;
RA Takiguchi Y., Kurimasa A., Chen F., Pardington P.E., Kuriyama T.,
RA Okinaka R.T., Moyzis R., Chen D.J.;
RT "Genomic structure and chromosomal assignment of the mouse Ku70 gene.";
RL Genomics 35:129-135(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary carcinoma;
RX PubMed=9582343; DOI=10.1074/jbc.273.21.13058;
RA Fukumura R., Araki R., Fujimori A., Mori M., Saito T., Watanabe F.,
RA Sarashi M., Itsukaichi H., Eguch-Kasai K., Sato K., Tatsumi K., Abe M.;
RT "Murine cell line SX9 bearing a mutation in the DNA-PKcs gene exhibits
RT aberrant V(D)J recombination not only in the coding joint but also in the
RT signal joint.";
RL J. Biol. Chem. 273:13058-13064(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-46.
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RA Baughman G.A., Nemeth J.E., Bourgeois S.;
RT "Nucleotide sequence of the 5' region of the murine p70 Ku autoantigen
RT cDNA.";
RL Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-608.
RX PubMed=1701785;
RA Porges A.J., Ng T., Reeves W.H.;
RT "Antigenic determinants of the Ku (p70/p80) autoantigen are poorly
RT conserved between species.";
RL J. Immunol. 145:4222-4228(1990).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=8605992; DOI=10.1016/0014-5793(96)00189-5;
RA Oderwald H., Hughes M.J., Jost J.-P.;
RT "Non-histone protein 1 (NHP1) is a member of the Ku protein family which is
RT upregulated in differentiating mouse myoblasts and human promyelocytes.";
RL FEBS Lett. 382:313-318(1996).
RN [9]
RP FUNCTION.
RC TISSUE=Osteoblast;
RX PubMed=12145306; DOI=10.1074/jbc.m206482200;
RA Willis D.M., Loewy A.P., Charlton-Kachigian N., Shao J.-S., Ornitz D.M.,
RA Towler D.A.;
RT "Regulation of osteocalcin gene expression by a novel Ku antigen
RT transcription factor complex.";
RL J. Biol. Chem. 277:37280-37291(2002).
RN [10]
RP INTERACTION WITH CLU.
RX PubMed=12551933; DOI=10.1074/jbc.m209233200;
RA Leskov K.S., Klokov D.Y., Li J., Kinsella T.J., Boothman D.A.;
RT "Synthesis and functional analyses of nuclear clusterin, a cell death
RT protein.";
RL J. Biol. Chem. 278:11590-11600(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP INTERACTION WITH CYREN.
RX PubMed=30017584; DOI=10.1016/j.molcel.2018.06.018;
RA Hung P.J., Johnson B., Chen B.R., Byrum A.K., Bredemeyer A.L.,
RA Yewdell W.T., Johnson T.E., Lee B.J., Deivasigamani S., Hindi I.,
RA Amatya P., Gross M.L., Paull T.T., Pisapia D.J., Chaudhuri J.,
RA Petrini J.J.H., Mosammaparast N., Amarasinghe G.K., Zha S., Tyler J.K.,
RA Sleckman B.P.;
RT "MRI is a DNA damage response adaptor during classical non-homologous end
RT joining.";
RL Mol. Cell 71:332-342(2018).
RN [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=32103174; DOI=10.1038/s41586-020-2041-2;
RA Shao Z., Flynn R.A., Crowe J.L., Zhu Y., Liang J., Jiang W., Aryan F.,
RA Aoude P., Bertozzi C.R., Estes V.M., Lee B.J., Bhagat G., Zha S., Calo E.;
RT "DNA-PKcs has KU-dependent function in rRNA processing and
RT haematopoiesis.";
RL Nature 579:291-296(2020).
CC -!- FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase that
CC plays a key role in DNA non-homologous end joining (NHEJ) by recruiting
CC DNA-PK to DNA (By similarity). Required for double-strand break repair
CC and V(D)J recombination (By similarity). Also has a role in chromosome
CC translocation (By similarity). Has a role in chromosome translocation
CC (By similarity). The DNA helicase II complex binds preferentially to
CC fork-like ends of double-stranded DNA in a cell cycle-dependent manner
CC (By similarity). It works in the 3'-5' direction (By similarity).
CC During NHEJ, the XRCC5-XRRC6 dimer performs the recognition step: it
CC recognizes and binds to the broken ends of the DNA and protects them
CC from further resection (By similarity). Binding to DNA may be mediated
CC by XRCC6 (By similarity). The XRCC5-XRRC6 dimer acts as regulatory
CC subunit of the DNA-dependent protein kinase complex DNA-PK by
CC increasing the affinity of the catalytic subunit PRKDC to DNA by 100-
CC fold (By similarity). The XRCC5-XRRC6 dimer is probably involved in
CC stabilizing broken DNA ends and bringing them together (By similarity).
CC The assembly of the DNA-PK complex to DNA ends is required for the NHEJ
CC ligation step (By similarity). Probably also acts as a 5'-deoxyribose-
CC 5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of
CC the 5' deoxyribose-5-phosphate at an abasic site near double-strand
CC breaks (By similarity). 5'-dRP lyase activity allows to 'clean' the
CC termini of abasic sites, a class of nucleotide damage commonly
CC associated with strand breaks, before such broken ends can be joined
CC (By similarity). The XRCC5-XRRC6 dimer together with APEX1 acts as a
CC negative regulator of transcription (By similarity). In association
CC with NAA15, the XRCC5-XRRC6 dimer binds to the osteocalcin promoter and
CC activates osteocalcin expression (PubMed:12145306). Plays a role in the
CC regulation of DNA virus-mediated innate immune response by assembling
CC into the HDP-RNP complex, a complex that serves as a platform for IRF3
CC phosphorylation and subsequent innate immune response activation
CC through the cGAS-STING pathway (By similarity).
CC {ECO:0000250|UniProtKB:P12956, ECO:0000269|PubMed:12145306}.
CC -!- SUBUNIT: Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70 (By
CC similarity). Component of the core long-range non-homologous end
CC joining (NHEJ) complex (also named DNA-PK complex) composed of PRKDC,
CC LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF (By similarity).
CC Additional component of the NHEJ complex includes PAXX (By similarity).
CC Following autophosphorylation, PRKDC dissociates from DNA, leading to
CC formation of the short-range NHEJ complex, composed of LIG4, XRCC4,
CC XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF (By similarity). The XRCC5-XRCC6
CC dimer also associates with NAA15, and this complex binds to the
CC osteocalcin promoter and activates osteocalcin expression (By
CC similarity). In addition, XRCC6 interacts with the osteoblast-specific
CC transcription factors MSX2, RUNX2 and DLX5 (By similarity). Interacts
CC with ELF3 (By similarity). Interacts with ATP23 (By similarity). The
CC XRCC5-XRRC6 dimer associates in a DNA-dependent manner with APEX1 (By
CC similarity). Binds to CDK9 (By similarity). Identified in a complex
CC with DEAF1 and XRCC5 (By similarity). Interacts with DEAF1 (via the
CC SAND domain); the interaction is direct and may be inhibited by DNA-
CC binding (By similarity). Interacts with CLU (PubMed:12551933).
CC Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK
CC phosphorylates and activates NR4A3 and prevents NR4A3 ubiquitinylation
CC and degradation (By similarity). Interacts with CYREN (via KBM motif)
CC (PubMed:30017584). Interacts (via N-terminus) with HSF1 (via N-
CC terminus); this interaction is direct and prevents XRCC5/XRCC6
CC heterodimeric binding and non-homologous end joining (NHEJ) repair
CC activities induced by ionizing radiation (IR) (By similarity). Part of
CC the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6,
CC paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1
CC RNA (By similarity). Interacts with HMBOX1 (By similarity). Interacts
CC with ATF7 (By similarity). Interacts with APLF (via KBM motif) (By
CC similarity). Interacts with WRN (via KBM motif) (By similarity). The
CC XRCC5-XRCC6 dimer associates with ALKBH2.
CC {ECO:0000250|UniProtKB:P12956, ECO:0000269|PubMed:12551933,
CC ECO:0000269|PubMed:30017584}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12956}.
CC Chromosome {ECO:0000250|UniProtKB:P12956}.
CC -!- DEVELOPMENTAL STAGE: Expression increases during promyelocyte
CC differentiation. {ECO:0000269|PubMed:8605992}.
CC -!- PTM: Phosphorylation by PRKDC may enhance helicase activity.
CC Phosphorylation of Ser-49 does not affect DNA repair.
CC {ECO:0000250|UniProtKB:P12956}.
CC -!- PTM: ADP-ribosylated by PARP3. {ECO:0000250|UniProtKB:P12956}.
CC -!- DISRUPTION PHENOTYPE: Viable. Reduced number of peripheral lymphocytes,
CC however number of erythrocytes, platelets and neutrophils are normal.
CC Translation levels in erythrocyte precursors are normal.
CC {ECO:0000269|PubMed:32103174}.
CC -!- SIMILARITY: Belongs to the ku70 family. {ECO:0000305}.
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DR EMBL; U50378; AAC52675.1; -; Genomic_DNA.
DR EMBL; U50367; AAC52675.1; JOINED; Genomic_DNA.
DR EMBL; U50368; AAC52675.1; JOINED; Genomic_DNA.
DR EMBL; U50369; AAC52675.1; JOINED; Genomic_DNA.
DR EMBL; U50370; AAC52675.1; JOINED; Genomic_DNA.
DR EMBL; U50371; AAC52675.1; JOINED; Genomic_DNA.
DR EMBL; U50372; AAC52675.1; JOINED; Genomic_DNA.
DR EMBL; U50373; AAC52675.1; JOINED; Genomic_DNA.
DR EMBL; U50374; AAC52675.1; JOINED; Genomic_DNA.
DR EMBL; U50375; AAC52675.1; JOINED; Genomic_DNA.
DR EMBL; U50376; AAC52675.1; JOINED; Genomic_DNA.
DR EMBL; U50377; AAC52675.1; JOINED; Genomic_DNA.
DR EMBL; U34878; AAC53575.1; -; Genomic_DNA.
DR EMBL; AB010282; BAA28874.1; -; mRNA.
DR EMBL; AF483500; AAL90774.1; -; mRNA.
DR EMBL; AF483501; AAL90775.1; -; mRNA.
DR EMBL; AK143570; BAE25441.1; -; mRNA.
DR EMBL; AK146392; BAE27135.1; -; mRNA.
DR EMBL; AK146394; BAE27137.1; -; mRNA.
DR EMBL; AK146396; BAE27139.1; -; mRNA.
DR EMBL; BC031422; AAH31422.1; -; mRNA.
DR EMBL; Z14157; CAA78526.1; -; mRNA.
DR EMBL; M38700; AAA39396.1; -; mRNA.
DR CCDS; CCDS37153.1; -.
DR PIR; A43534; A43534.
DR PIR; S25149; S25149.
DR RefSeq; NP_034377.2; NM_010247.2.
DR RefSeq; XP_006520505.1; XM_006520442.3.
DR RefSeq; XP_006520506.1; XM_006520443.3.
DR RefSeq; XP_011243758.1; XM_011245456.2.
DR AlphaFoldDB; P23475; -.
DR SMR; P23475; -.
DR BioGRID; 199785; 22.
DR ComplexPortal; CPX-2047; Ku70:Ku80 complex.
DR CORUM; P23475; -.
DR IntAct; P23475; 7.
DR MINT; P23475; -.
DR STRING; 10090.ENSMUSP00000068559; -.
DR iPTMnet; P23475; -.
DR PhosphoSitePlus; P23475; -.
DR EPD; P23475; -.
DR jPOST; P23475; -.
DR MaxQB; P23475; -.
DR PaxDb; P23475; -.
DR PeptideAtlas; P23475; -.
DR PRIDE; P23475; -.
DR ProteomicsDB; 299724; -.
DR DNASU; 14375; -.
DR GeneID; 14375; -.
DR KEGG; mmu:14375; -.
DR UCSC; uc007wxy.1; mouse.
DR CTD; 2547; -.
DR MGI; MGI:95606; Xrcc6.
DR eggNOG; KOG2327; Eukaryota.
DR InParanoid; P23475; -.
DR OrthoDB; 402798at2759; -.
DR TreeFam; TF315101; -.
DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 14375; 28 hits in 110 CRISPR screens.
DR ChiTaRS; Xrcc6; mouse.
DR PRO; PR:P23475; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P23475; protein.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0070418; C:DNA-dependent protein kinase complex; ISO:MGI.
DR GO; GO:0043564; C:Ku70:Ku80 complex; ISS:UniProtKB.
DR GO; GO:0070419; C:nonhomologous end joining complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:MGI.
DR GO; GO:0030332; F:cyclin binding; ISO:MGI.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0045027; F:DNA end binding; ISO:MGI.
DR GO; GO:0003678; F:DNA helicase activity; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; ISO:MGI.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0002218; P:activation of innate immune response; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISS:UniProtKB.
DR GO; GO:0071481; P:cellular response to X-ray; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IMP:MGI.
DR GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; ISO:MGI.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:0045621; P:positive regulation of lymphocyte differentiation; IMP:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IMP:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0000725; P:recombinational repair; IC:ComplexPortal.
DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:MGI.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR GO; GO:0033151; P:V(D)J recombination; IMP:MGI.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR Gene3D; 4.10.970.10; -; 1.
DR InterPro; IPR006165; Ku70.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR027388; Ku70_bridge/pillars_dom_sf.
DR InterPro; IPR005160; Ku_C.
DR InterPro; IPR005161; Ku_N.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF02735; Ku; 1.
DR Pfam; PF03730; Ku_C; 1.
DR Pfam; PF03731; Ku_N; 1.
DR Pfam; PF02037; SAP; 1.
DR PIRSF; PIRSF003033; Ku70; 1.
DR SMART; SM00559; Ku78; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR TIGRFAMs; TIGR00578; ku70; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; ADP-ribosylation; ATP-binding; Chromosome;
KW DNA damage; DNA recombination; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Immunity; Innate immunity; Isopeptide bond; Lyase;
KW Multifunctional enzyme; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT CHAIN 2..608
FT /note="X-ray repair cross-complementing protein 6"
FT /id="PRO_0000210180"
FT DOMAIN 259..466
FT /note="Ku"
FT DOMAIN 571..605
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..607
FT /note="Interaction with DEAF1"
FT /evidence="ECO:0000250"
FT COMPBIAS 9..23
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 29
FT /note="Schiff-base intermediate with DNA; for 5'-
FT deoxyribose-5-phosphate lyase activity"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT MOD_RES 6
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT MOD_RES 29
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT MOD_RES 49
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT MOD_RES 329
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT MOD_RES 336
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT MOD_RES 459
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT CROSSLNK 315
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P12956"
FT CONFLICT 225
FT /note="E -> G (in Ref. 4; BAE27139/BAE27137/BAE27135)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="K -> E (in Ref. 3; BAE25441/AAL90775/AAL90774)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="P -> H (in Ref. 7; AAA39396)"
FT /evidence="ECO:0000305"
FT CONFLICT 466..467
FT /note="KL -> NV (in Ref. 1; AAC52675 and 7; AAA39396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 69484 MW; 1C27DBF1DB7A1154 CRC64;
MSEWESYYKT EGEEEEEEEE SPDTGGEYKY SGRDSLIFLV DASRAMFESQ GEDELTPFDM
SIQCIQSVYT SKIISSDRDL LAVVFYGTEK DKNSVNFKNI YVLQDLDNPG AKRVLELDQF
KGQQGKKHFR DTVGHGSDYS LSEVLWVCAN LFSDVQLKMS HKRIMLFTNE DDPHGRDSAK
ASRARTKASD LRDTGIFLDL MHLKKPGGFD VSVFYRDIIT TAEDEDLGVH FEESSKLEDL
LRKVRAKETK KRVLSRLKFK LGEDVVLMVG IYNLVQKANK PFPVRLYRET NEPVKTKTRT
FNVNTGSLLL PSDTKRSLTY GTRQIVLEKE ETEELKRFDE PGLILMGFKP TVMLKKQHYL
RPSLFVYPEE SLVSGSSTLF SALLTKCVEK KVIAVCRYTP RKNVSPYFVA LVPQEEELDD
QNIQVTPGGF QLVFLPYADD KRKVPFTEKV TANQEQIDKM KAIVQKLRFT YRSDSFENPV
LQQHFRNLEA LALDMMESEQ VVDLTLPKVE AIKKRLGSLA DEFKELVYPP GYNPEGKVAK
RKQDDEGSTS KKPKVELSEE ELKAHFRKGT LGKLTVPTLK DICKAHGLKS GPKKQELLDA
LIRHLEKN
