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X-ray repair cross-complementing protein 6 (EC 3.6.4.-) (EC 4.2.99.-) (5'-deoxyribose-5-phosphate lyase Ku70) (5'-dRP lyase Ku70) (70 kDa subunit of Ku antigen) (ATP-dependent DNA helicase 2 subunit 1) (ATP-dependent DNA helicase II 70 kDa subunit) (CTC box-binding factor 75 kDa subunit) (CTC75) (CTCBF) (DNA repair protein XRCC6) (Lupus Ku autoantigen protein p70) (Ku70) (Thyroid-lupus autoantigen) (TLAA) (X-ray repair complementing defective repair in Chinese hamster cells 6)

 XRCC6_HUMAN             Reviewed;         609 AA.
P12956; B1AHC8; Q6FG89; Q9UCQ2; Q9UCQ3;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 213.
RecName: Full=X-ray repair cross-complementing protein 6;
EC=3.6.4.-;
EC=4.2.99.-;
AltName: Full=5'-deoxyribose-5-phosphate lyase Ku70;
Short=5'-dRP lyase Ku70;
AltName: Full=70 kDa subunit of Ku antigen;
AltName: Full=ATP-dependent DNA helicase 2 subunit 1;
AltName: Full=ATP-dependent DNA helicase II 70 kDa subunit;
AltName: Full=CTC box-binding factor 75 kDa subunit;
Short=CTC75;
Short=CTCBF;
AltName: Full=DNA repair protein XRCC6;
AltName: Full=Lupus Ku autoantigen protein p70;
Short=Ku70;
AltName: Full=Thyroid-lupus autoantigen;
Short=TLAA;
AltName: Full=X-ray repair complementing defective repair in Chinese hamster cells 6;
Name=XRCC6; Synonyms=G22P1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2917966;
Chan J.Y., Lerman M.I., Prabhakar B.S., Isozaki O., Santisteban P.,
Kuppers R.C., Oates E.L., Notkins A.L., Kohn L.D.;
"Cloning and characterization of a cDNA that encodes a 70-kDa novel
human thyroid autoantigen.";
J. Biol. Chem. 264:3651-3654(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
ROLE IN LUPUS ERYTHEMATOSUS.
PubMed=2466842;
Reeves W.H., Sthoeger Z.M.;
"Molecular cloning of cDNA encoding the p70 (Ku) lupus autoantigen.";
J. Biol. Chem. 264:5047-5052(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1608402; DOI=10.1007/BF00419754;
Griffith A.J., Craft J., Evans J., Mimori T., Hardin J.A.;
"Nucleotide sequence and genomic structure analyses of the p70 subunit
of the human Ku autoantigen: evidence for a family of genes encoding
Ku (p70)-related polypeptides.";
Mol. Biol. Rep. 16:91-97(1992).
[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).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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=Brain, Kidney, Lung, Placenta, and Skin;
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 10-30 AND 299-317.
PubMed=1537839;
Wedrychowski A., Henzel W., Huston L., Paslidis N., Ellerson D.,
McRae M., Seong D., Howard O.M.Z., Deisseroth A.;
"Identification of proteins binding to interferon-inducible
transcriptional enhancers in hematopoietic cells.";
J. Biol. Chem. 267:4533-4540(1992).
[11]
PROTEIN SEQUENCE OF 101-114 AND 116-125, AND DEVELOPMENTAL STAGE.
TISSUE=Cervix carcinoma;
PubMed=8605992; DOI=10.1016/0014-5793(96)00189-5;
Oderwald H., Hughes M.J., Jost J.-P.;
"Non-histone protein 1 (NHP1) is a member of the Ku protein family
which is upregulated in differentiating mouse myoblasts and human
promyelocytes.";
FEBS Lett. 382:313-318(1996).
[12]
PROTEIN SEQUENCE OF 288-293 AND 300-312, FUNCTION, AND INTERACTION
WITH APEX1.
PubMed=8621488; DOI=10.1074/jbc.271.15.8593;
Chung U., Igarashi T., Nishishita T., Iwanari H., Iwamatsu A.,
Suwa A., Mimori T., Hata K., Ebisu S., Ogata E., Fujita T.,
Okazaki T.;
"The interaction between Ku antigen and REF1 protein mediates negative
gene regulation by extracellular calcium.";
J. Biol. Chem. 271:8593-8598(1996).
[13]
PROTEIN SEQUENCE OF 301-308 AND 556-565.
PubMed=7882982;
Genersch E., Eckerskorn C., Lottspeich F., Herzog C., Kuehn K.,
Poeschl E.;
"Purification of the sequence-specific transcription factor CTCBF,
involved in the control of human collagen IV genes: subunits with
homology to Ku antigen.";
EMBO J. 14:791-800(1995).
[14]
PROTEIN SEQUENCE OF 346-352, AND FUNCTION.
PubMed=7957065;
Tuteja N., Tuteja R., Ochem A., Taneja P., Huang N.W., Simoncsits A.,
Susic S., Rahman K., Marusic L., Chen J., Zhang J., Wang S.,
Pongor S., Falaschi A.;
"Human DNA helicase II: a novel DNA unwinding enzyme identified as the
Ku autoantigen.";
EMBO J. 13:4991-5001(1994).
[15]
PHOSPHORYLATION AT SER-51.
PubMed=9362500; DOI=10.1093/emboj/16.22.6874;
Jin S., Weaver D.T.;
"Double-strand break repair by Ku70 requires heterodimerization with
Ku80 and DNA binding functions.";
EMBO J. 16:6874-6885(1997).
[16]
FUNCTION, AND INTERACTION WITH PRKDC.
PubMed=9742108; DOI=10.1128/MCB.18.10.5908;
West R.B., Yaneva M., Lieber M.R.;
"Productive and nonproductive complexes of Ku and DNA-dependent
protein kinase at DNA termini.";
Mol. Cell. Biol. 18:5908-5920(1998).
[17]
PHOSPHORYLATION AT SER-6.
PubMed=10026262; DOI=10.1021/bi982584b;
Chan D.W., Ye R., Veillette C.J., Lees-Miller S.P.;
"DNA-dependent protein kinase phosphorylation sites in Ku 70/80
heterodimer.";
Biochemistry 38:1819-1828(1999).
[18]
REVIEW.
PubMed=10377944; DOI=10.1016/S0921-8777(99)00006-3;
Featherstone C., Jackson S.P.;
"Ku, a DNA repair protein with multiple cellular functions?";
Mutat. Res. 434:3-15(1999).
[19]
INTERACTION WITH XRCC6BP1.
TISSUE=Liver;
PubMed=10219089; DOI=10.1093/nar/27.10.2165;
Yang C.-R., Yeh S.-Y., Leskov K., Odegaard E., Hsu H.L., Chang C.,
Kinsella T.J., Chen D.J., Boothman D.A.;
"Isolation of Ku70-binding proteins (KUBs).";
Nucleic Acids Res. 27:2165-2174(1999).
[20]
INTERACTION WITH PRKDC.
PubMed=12509254; DOI=10.1016/S1568-7864(01)00018-0;
Hsu H.-L., Yannone S.M., Chen D.J.;
"Defining interactions between DNA-PK and ligase IV/XRCC4.";
DNA Repair 1:225-235(2002).
[21]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH
NAA15; MSX2; RUNX2 AND DLX5.
TISSUE=Heart, and Osteoblast;
PubMed=12145306; DOI=10.1074/jbc.M206482200;
Willis D.M., Loewy A.P., Charlton-Kachigian N., Shao J.-S.,
Ornitz D.M., Towler D.A.;
"Regulation of osteocalcin gene expression by a novel Ku antigen
transcription factor complex.";
J. Biol. Chem. 277:37280-37291(2002).
[22]
IDENTIFICATION IN A COMPLEX WITH G22P2; PRKDC AND XRCC4, AND
PHOSPHORYLATION.
PubMed=12547193; DOI=10.1016/S0022-2836(02)01328-1;
Calsou P., Delteil C., Frit P., Drouet J., Salles B.;
"Coordinated assembly of Ku and p460 subunits of the DNA-dependent
protein kinase on DNA ends is necessary for XRCC4-ligase IV
recruitment.";
J. Mol. Biol. 326:93-103(2003).
[23]
INTERACTION WITH ELF3.
PubMed=15075319; DOI=10.1074/jbc.M401356200;
Wang H., Fang R., Cho J.-Y., Libermann T.A., Oettgen P.;
"Positive and negative modulation of the transcriptional activity of
the ETS factor ESE-1 through interaction with p300, CREB-binding
protein, and Ku 70/86.";
J. Biol. Chem. 279:25241-25250(2004).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, 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).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, 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).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-331; LYS-338 AND
LYS-461, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[28]
FUNCTION IN DNA REPAIR, AND INTERACTION WITH CDK9.
PubMed=20493174; DOI=10.1016/j.bbrc.2010.05.092;
Liu H., Herrmann C.H., Chiang K., Sung T.L., Moon S.H.,
Donehower L.A., Rice A.P.;
"55K isoform of CDK9 associates with Ku70 and is involved in DNA
repair.";
Biochem. Biophys. Res. Commun. 397:245-250(2010).
[29]
FUNCTION AS A 5'-DRP LYASE, AND MUTAGENESIS OF LYS-31; LYS-160 AND
LYS-164.
PubMed=20383123; DOI=10.1038/nature08926;
Roberts S.A., Strande N., Burkhalter M.D., Strom C., Havener J.M.,
Hasty P., Ramsden D.A.;
"Ku is a 5'-dRP/AP lyase that excises nucleotide damage near broken
ends.";
Nature 464:1214-1217(2010).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455 AND SER-550, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[33]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[34]
DNA-BINDING, IDENTIFICATION IN A COMPLEX WITH DEAF1 AND XRCC5,
INTERACTION WITH DEAF1, SUBCELLULAR LOCATION, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=22442688; DOI=10.1371/journal.pone.0033404;
Jensik P.J., Huggenvik J.I., Collard M.W.;
"Deformed epidermal autoregulatory factor-1 (DEAF1) interacts with the
Ku70 subunit of the DNA-dependent protein kinase complex.";
PLoS ONE 7:E33404-E33404(2012).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-27; SER-306;
THR-455; SER-477; SER-520 AND SER-560, 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).
[36]
INTERACTION WITH MRI.
PubMed=24610814; DOI=10.1074/jbc.C113.533968;
Slavoff S.A., Heo J., Budnik B.A., Hanakahi L.A., Saghatelian A.;
"A human short open reading frame (sORF)-encoded polypeptide that
stimulates DNA end joining.";
J. Biol. Chem. 289:10950-10957(2014).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-556, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[39]
INTERACTION WITH NR4A3.
PubMed=25852083; DOI=10.1093/cvr/cvv126;
Medunjanin S., Daniel J.M., Weinert S., Dutzmann J., Burgbacher F.,
Brecht S., Bruemmer D., Kaehne T., Naumann M., Sedding D.G.,
Zuschratter W., Braun-Dullaeus R.C.;
"DNA-dependent protein kinase (DNA-PK) permits vascular smooth muscle
cell proliferation through phosphorylation of the orphan nuclear
receptor NOR1.";
Cardiovasc. Res. 106:488-497(2015).
[40]
SUBUNIT.
PubMed=25941166; DOI=10.1038/cdd.2015.22;
Craxton A., Somers J., Munnur D., Jukes-Jones R., Cain K.,
Malewicz M.;
"XLS (c9orf142) is a new component of mammalian DNA double-stranded
break repair.";
Cell Death Differ. 22:890-897(2015).
[41]
SUBUNIT.
PubMed=25670504; DOI=10.1038/ncomms7233;
Xing M., Yang M., Huo W., Feng F., Wei L., Jiang W., Ning S., Yan Z.,
Li W., Wang Q., Hou M., Dong C., Guo R., Gao G., Ji J., Zha S.,
Lan L., Liang H., Xu D.;
"Interactome analysis identifies a new paralogue of XRCC4 in non-
homologous end joining DNA repair pathway.";
Nat. Commun. 6:6233-6233(2015).
[42]
INTERACTION WITH HSF1.
PubMed=26359349; DOI=10.18632/oncotarget.5073;
Kang G.Y., Kim E.H., Lee H.J., Gil N.Y., Cha H.J., Lee Y.S.;
"Heat shock factor 1, an inhibitor of non-homologous end joining
repair.";
Oncotarget 6:29712-29724(2015).
[43]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[44]
INTERACTION WITH PAXX.
PubMed=25574025; DOI=10.1126/science.1261971;
Ochi T., Blackford A.N., Coates J., Jhujh S., Mehmood S., Tamura N.,
Travers J., Wu Q., Draviam V.M., Robinson C.V., Blundell T.L.,
Jackson S.P.;
"DNA repair. PAXX, a paralog of XRCC4 and XLF, interacts with Ku to
promote DNA double-strand break repair.";
Science 347:185-188(2015).
[45]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRKDC; XRCC5;
HEXIM1; SFPQ; NONO; PSPC1; RBM14 AND MATR3.
PubMed=28712728; DOI=10.1016/j.molcel.2017.06.020;
Morchikh M., Cribier A., Raffel R., Amraoui S., Cau J., Severac D.,
Dubois E., Schwartz O., Bennasser Y., Benkirane M.;
"HEXIM1 and NEAT1 Long non-coding RNA form a multi-subunit complex
that regulates DNA-mediated innate immune response.";
Mol. Cell 67:387-399(2017).
[46]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-287; LYS-317 AND LYS-556,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[47]
STRUCTURE BY NMR OF 557-610.
PubMed=11457852; DOI=10.1074/jbc.M105238200;
Zhang Z., Zhu L., Lin D., Chen F., Chen D.J., Chen Y.;
"The three-dimensional structure of the C-terminal DNA-binding domain
of human Ku70.";
J. Biol. Chem. 276:38231-38236(2001).
[48]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 36-609 IN COMPLEX WITH G22P2.
PubMed=11493912; DOI=10.1038/35088000;
Walker J.R., Corpina R.A., Goldberg J.;
"Structure of the Ku heterodimer bound to DNA and its implications for
double-strand break repair.";
Nature 412:607-614(2001).
-!- FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase.
Has a role in chromosome translocation. The DNA helicase II
complex binds preferentially to fork-like ends of double-stranded
DNA in a cell cycle-dependent manner. It works in the 3'-5'
direction. Binding to DNA may be mediated by XRCC6. Involved in
DNA non-homologous end joining (NHEJ) required for double-strand
break repair and V(D)J recombination. The XRCC5/6 dimer acts as
regulatory subunit of the DNA-dependent protein kinase complex
DNA-PK by increasing the affinity of the catalytic subunit PRKDC
to DNA by 100-fold. The XRCC5/6 dimer is probably involved in
stabilizing broken DNA ends and bringing them together. The
assembly of the DNA-PK complex to DNA ends is required for the
NHEJ ligation step. Required for osteocalcin gene expression.
Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP
lyase), by catalyzing the beta-elimination of the 5' deoxyribose-
5-phosphate at an abasic site near double-strand breaks. 5'-dRP
lyase activity allows to 'clean' the termini of abasic sites, a
class of nucleotide damage commonly associated with strand breaks,
before such broken ends can be joined. The XRCC5/6 dimer together
with APEX1 acts as a negative regulator of transcription. Plays a
role in the regulation of DNA virus-mediated innate immune
response by assembling into the HDP-RNP complex, a complex that
serves as a platform for IRF3 phosphorylation and subsequent
innate immune response activation through the cGAS-STING pathway.
{ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:20383123,
ECO:0000269|PubMed:20493174, ECO:0000269|PubMed:2466842,
ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:7957065,
ECO:0000269|PubMed:8621488, ECO:0000269|PubMed:9742108}.
-!- SUBUNIT: Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70. The
dimer associates in a DNA-dependent manner with PRKDC to form the
DNA-dependent protein kinase complex DNA-PK, and with the LIG4-
XRCC4 complex to form the core of the non-homologous end joining
(NHEJ) complex. Additional components of the NHEJ complex include
NHEJ1/XLF and PAXX (PubMed:25574025, PubMed:25941166,
PubMed:25670504). The dimer also associates with NAA15, and this
complex binds to the osteocalcin promoter and activates
osteocalcin expression. In addition, XRCC6 interacts with the
osteoblast-specific transcription factors MSX2, RUNX2 and DLX5.
Interacts with ELF3. Interacts with ATP23. The XRCC5/6 dimer
associates in a DNA-dependent manner with APEX1. Binds to CDK9
isoform 2. Identified in a complex with DEAF1 and XRCC5. Interacts
with DEAF1 (via the SAND domain); the interaction is direct and
may be inhibited by DNA-binding (PubMed:10219089, PubMed:11493912,
PubMed:12145306, PubMed:12509254, PubMed:12547193,
PubMed:15075319, PubMed:20493174, PubMed:22442688, PubMed:8621488,
PubMed:9742108). Interacts with CLU (By similarity). Interacts
with NR4A3; the DNA-dependent protein kinase complex DNA-PK
phosphorylates and activates NR4A3 and prevents NR4A3
ubiquitinylation and degradation (PubMed:25852083). Interacts with
MRI isoform 1 (MRI-1) and isoform 4 (MRI-2) (PubMed:24610814).
Interacts (via N-terminus) with HSF1 (via N-terminus); this
interaction is direct and prevents XRCC5/XRCC6 heterodimeric
binding and non-homologous end joining (NHEJ) repair activities
induced by ionizing radiation (IR) (PubMed:26359349). Part of the
HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6,
paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and
NEAT1 RNA (PubMed:28712728). {ECO:0000250|UniProtKB:P23475,
ECO:0000269|PubMed:10219089, ECO:0000269|PubMed:11493912,
ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:12509254,
ECO:0000269|PubMed:12547193, ECO:0000269|PubMed:15075319,
ECO:0000269|PubMed:20493174, ECO:0000269|PubMed:22442688,
ECO:0000269|PubMed:24610814, ECO:0000269|PubMed:25574025,
ECO:0000269|PubMed:25852083, ECO:0000269|PubMed:26359349,
ECO:0000269|PubMed:8621488, ECO:0000269|PubMed:9742108}.
-!- INTERACTION:
Q96P48:ARAP1; NbExp=2; IntAct=EBI-353208, EBI-710003;
Q07812:BAX; NbExp=2; IntAct=EBI-353208, EBI-516580;
P38432:COIL; NbExp=3; IntAct=EBI-353208, EBI-945751;
Q6NT76:HMBOX1; NbExp=2; IntAct=EBI-353208, EBI-2549423;
P42858:HTT; NbExp=3; IntAct=EBI-353208, EBI-466029;
Q92597:NDRG1; NbExp=2; IntAct=EBI-353208, EBI-716486;
Q08752:PPID; NbExp=4; IntAct=EBI-353208, EBI-716596;
O15355:PPM1G; NbExp=3; IntAct=EBI-353208, EBI-725702;
P78527:PRKDC; NbExp=7; IntAct=EBI-353208, EBI-352053;
Q96EB6:SIRT1; NbExp=7; IntAct=EBI-353208, EBI-1802965;
Q9NQB0:TCF7L2; NbExp=9; IntAct=EBI-353208, EBI-924724;
Q9NYB0:TERF2IP; NbExp=3; IntAct=EBI-353208, EBI-750109;
P04637:TP53; NbExp=2; IntAct=EBI-353208, EBI-366083;
P13693:TPT1; NbExp=4; IntAct=EBI-353208, EBI-1783169;
Q14191:WRN; NbExp=5; IntAct=EBI-353208, EBI-368417;
Q13426:XRCC4; NbExp=3; IntAct=EBI-353208, EBI-717592;
P13010:XRCC5; NbExp=16; IntAct=EBI-353208, EBI-357997;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22442688}.
Chromosome {ECO:0000269|PubMed:22442688}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P12956-1; Sequence=Displayed;
Name=2;
IsoId=P12956-2; Sequence=VSP_056030;
Note=No experimental confirmation available.;
-!- DEVELOPMENTAL STAGE: Expression does not increase during
promyelocyte differentiation. {ECO:0000269|PubMed:8605992}.
-!- INDUCTION: In osteoblasts, by FGF2.
-!- PTM: Phosphorylation by PRKDC may enhance helicase activity.
Phosphorylation of Ser-51 does not affect DNA repair.
{ECO:0000269|PubMed:10026262, ECO:0000269|PubMed:12547193,
ECO:0000269|PubMed:9362500}.
-!- MISCELLANEOUS: Individuals with systemic lupus erythematosus (SLE)
and related disorders produce extremely large amounts of
autoantibodies to XRCC5 and XRCC6. Existence of a major
autoantigenic epitope or epitopes on the C-terminal 190 amino
acids of XRCC6 containing the leucine repeat. The majority of
autoantibodies to XRCC6 in most sera from patients with SLE seem
to be reactive with this region.
-!- SIMILARITY: Belongs to the ku70 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/g22p1/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/XRCC6ID246ch22q13.html";
-----------------------------------------------------------------------
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EMBL; J04607; AAA61177.1; -; mRNA.
EMBL; J04611; AAA51733.1; -; mRNA.
EMBL; M32865; AAA36155.1; -; mRNA.
EMBL; S38729; AAB22381.1; -; mRNA.
EMBL; AK055786; BAG51575.1; -; mRNA.
EMBL; CR542219; CAG47015.1; -; mRNA.
EMBL; AY870329; AAW34364.1; -; Genomic_DNA.
EMBL; Z83840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW60448.1; -; Genomic_DNA.
EMBL; BC008343; AAH08343.1; -; mRNA.
EMBL; BC010034; AAH10034.1; -; mRNA.
EMBL; BC012154; AAH12154.1; -; mRNA.
EMBL; BC018259; AAH18259.1; -; mRNA.
EMBL; BC072449; AAH72449.1; -; mRNA.
CCDS; CCDS14021.1; -. [P12956-1]
CCDS; CCDS74870.1; -. [P12956-2]
PIR; A30299; A30894.
RefSeq; NP_001275905.1; NM_001288976.1. [P12956-1]
RefSeq; NP_001275906.1; NM_001288977.1. [P12956-2]
RefSeq; NP_001460.1; NM_001469.4. [P12956-1]
UniGene; Hs.292493; -.
UniGene; Hs.730702; -.
PDB; 1JEQ; X-ray; 2.70 A; A=1-609.
PDB; 1JEY; X-ray; 2.50 A; A=1-609.
PDB; 1JJR; NMR; -; A=556-609.
PDB; 3RZX; X-ray; 2.61 A; B=537-558.
PDB; 5Y3R; EM; 6.60 A; A=34-534.
PDBsum; 1JEQ; -.
PDBsum; 1JEY; -.
PDBsum; 1JJR; -.
PDBsum; 3RZX; -.
PDBsum; 5Y3R; -.
ProteinModelPortal; P12956; -.
SMR; P12956; -.
BioGrid; 108822; 283.
CORUM; P12956; -.
DIP; DIP-24188N; -.
ELM; P12956; -.
IntAct; P12956; 157.
MINT; MINT-1416738; -.
STRING; 9606.ENSP00000352257; -.
iPTMnet; P12956; -.
PhosphoSitePlus; P12956; -.
SwissPalm; P12956; -.
DMDM; 125729; -.
SWISS-2DPAGE; P12956; -.
EPD; P12956; -.
MaxQB; P12956; -.
PaxDb; P12956; -.
PeptideAtlas; P12956; -.
PRIDE; P12956; -.
DNASU; 2547; -.
Ensembl; ENST00000359308; ENSP00000352257; ENSG00000196419. [P12956-1]
Ensembl; ENST00000360079; ENSP00000353192; ENSG00000196419. [P12956-1]
Ensembl; ENST00000402580; ENSP00000384941; ENSG00000196419. [P12956-2]
Ensembl; ENST00000405878; ENSP00000384257; ENSG00000196419. [P12956-1]
GeneID; 2547; -.
KEGG; hsa:2547; -.
UCSC; uc003bao.3; human. [P12956-1]
CTD; 2547; -.
DisGeNET; 2547; -.
EuPathDB; HostDB:ENSG00000196419.12; -.
GeneCards; XRCC6; -.
HGNC; HGNC:4055; XRCC6.
HPA; CAB004254; -.
HPA; HPA047549; -.
HPA; HPA062226; -.
MIM; 152690; gene.
neXtProt; NX_P12956; -.
OpenTargets; ENSG00000196419; -.
PharmGKB; PA28467; -.
eggNOG; KOG2327; Eukaryota.
eggNOG; ENOG410XNXU; LUCA.
GeneTree; ENSGT00390000001422; -.
HOGENOM; HOG000006588; -.
HOVERGEN; HBG006236; -.
InParanoid; P12956; -.
KO; K10884; -.
OMA; DVFTSCN; -.
OrthoDB; EOG091G04AI; -.
PhylomeDB; P12956; -.
TreeFam; TF315101; -.
Reactome; R-HSA-164843; 2-LTR circle formation.
Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
Reactome; R-HSA-3270619; IRF3-mediated induction of type I IFN.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; P12956; -.
ChiTaRS; XRCC6; human.
EvolutionaryTrace; P12956; -.
GeneWiki; Ku70; -.
GenomeRNAi; 2547; -.
PMAP-CutDB; P12956; -.
PRO; PR:P12956; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000196419; -.
CleanEx; HS_XRCC6; -.
ExpressionAtlas; P12956; baseline and differential.
Genevisible; P12956; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0043564; C:Ku70:Ku80 complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0070419; C:nonhomologous end joining complex; IDA:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0000783; C:nuclear telomere cap complex; TAS:BHF-UCL.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0043234; C:protein complex; IDA:CAFA.
GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0005667; C:transcription factor complex; IDA:UniProtKB.
GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IMP:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc.
GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; TAS:ProtInc.
GO; GO:0044877; F:macromolecular complex binding; IPI:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0042162; F:telomeric DNA binding; IEA:InterPro.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0071475; P:cellular hyperosmotic salinity response; IEA:Ensembl.
GO; GO:0071480; P:cellular response to gamma radiation; IDA:UniProtKB.
GO; GO:0071481; P:cellular response to X-ray; IEA:Ensembl.
GO; GO:0006266; P:DNA ligation; TAS:ProtInc.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IDA:BHF-UCL.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
GO; GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:CAFA.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
GO; GO:0051290; P:protein heterotetramerization; IDA:BHF-UCL.
GO; GO:0048660; P:regulation of smooth muscle cell proliferation; IMP:UniProtKB.
GO; GO:0000723; P:telomere maintenance; TAS:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.720.30; -; 1.
Gene3D; 2.40.290.10; -; 1.
Gene3D; 3.40.50.410; -; 1.
Gene3D; 4.10.970.10; -; 1.
InterPro; IPR006165; Ku70.
InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
InterPro; IPR027388; Ku70_bridge/pillars_dom.
InterPro; IPR005160; Ku_C.
InterPro; IPR005161; Ku_N.
InterPro; IPR003034; SAP_dom.
InterPro; IPR036361; SAP_dom_sf.
InterPro; IPR016194; SPOC-like_C_dom.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR12604:SF2; PTHR12604:SF2; 1.
Pfam; PF02735; Ku; 1.
Pfam; PF03730; Ku_C; 1.
Pfam; PF03731; Ku_N; 1.
Pfam; PF02037; SAP; 1.
PIRSF; PIRSF003033; Ku70; 1.
SMART; SM00559; Ku78; 1.
SMART; SM00513; SAP; 1.
SUPFAM; SSF100939; SSF100939; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF68906; SSF68906; 1.
TIGRFAMs; TIGR00578; ku70; 1.
PROSITE; PS50800; SAP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
ATP-binding; Chromosome; Complete proteome; Direct protein sequencing;
DNA damage; DNA recombination; DNA repair; DNA-binding; Helicase;
Hydrolase; Immunity; Innate immunity; Isopeptide bond; Lyase;
Multifunctional enzyme; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Systemic lupus erythematosus; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
CHAIN 2 609 X-ray repair cross-complementing protein
6.
/FTId=PRO_0000210179.
DOMAIN 261 468 Ku.
DOMAIN 573 607 SAP. {ECO:0000255|PROSITE-
ProRule:PRU00186}.
REGION 550 609 Interaction with DEAF1.
{ECO:0000269|PubMed:22442688}.
COMPBIAS 2 61 Ser-rich (potentially targets for
phosphorylation).
COMPBIAS 11 29 Asp/Glu-rich (acidic).
COMPBIAS 330 342 Asp/Glu-rich (acidic).
ACT_SITE 31 31 Schiff-base intermediate with DNA; for
5'-deoxyribose-5-phosphate lyase
activity. {ECO:0000305}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 6 6 Phosphoserine; by PRKDC.
{ECO:0000269|PubMed:10026262}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 31 31 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 51 51 Phosphoserine; by PRKDC.
{ECO:0000269|PubMed:9362500}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 331 331 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 338 338 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 455 455 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 461 461 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 477 477 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 520 520 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 550 550 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 560 560 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 287 287 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 317 317 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 556 556 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 65 105 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056030.
MUTAGEN 31 31 K->A: Diminishes the ability to form a
Schiff base. Abolishes adduct formation;
when associated with A-160 and A-164.
{ECO:0000269|PubMed:20383123}.
MUTAGEN 160 160 K->A: Abolishes adduct formation; when
associated with A-31 and A-160.
{ECO:0000269|PubMed:20383123}.
MUTAGEN 164 164 K->A: Abolishes adduct formation; when
associated with A-31 and A-164.
{ECO:0000269|PubMed:20383123}.
CONFLICT 20 20 Q -> D (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 101 101 N -> K (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 103 103 Y -> L (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 116 116 I -> S (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 125 125 Q -> S (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 181 181 A -> T (in Ref. 5; CAG47015).
{ECO:0000305}.
STRAND 35 43 {ECO:0000244|PDB:1JEY}.
HELIX 46 49 {ECO:0000244|PDB:1JEY}.
STRAND 53 56 {ECO:0000244|PDB:1JEY}.
HELIX 59 76 {ECO:0000244|PDB:1JEY}.
STRAND 82 89 {ECO:0000244|PDB:1JEY}.
STRAND 102 109 {ECO:0000244|PDB:1JEY}.
HELIX 113 120 {ECO:0000244|PDB:1JEY}.
HELIX 124 135 {ECO:0000244|PDB:1JEY}.
HELIX 143 155 {ECO:0000244|PDB:1JEY}.
STRAND 161 171 {ECO:0000244|PDB:1JEY}.
TURN 175 178 {ECO:0000244|PDB:1JEY}.
HELIX 180 196 {ECO:0000244|PDB:1JEY}.
STRAND 198 205 {ECO:0000244|PDB:1JEY}.
TURN 213 216 {ECO:0000244|PDB:1JEY}.
HELIX 217 219 {ECO:0000244|PDB:1JEY}.
HELIX 239 250 {ECO:0000244|PDB:1JEY}.
STRAND 256 266 {ECO:0000244|PDB:1JEY}.
STRAND 268 274 {ECO:0000244|PDB:1JEY}.
STRAND 286 289 {ECO:0000244|PDB:1JEY}.
TURN 290 292 {ECO:0000244|PDB:1JEY}.
STRAND 295 304 {ECO:0000244|PDB:1JEY}.
TURN 305 307 {ECO:0000244|PDB:1JEY}.
HELIX 313 315 {ECO:0000244|PDB:1JEY}.
STRAND 316 322 {ECO:0000244|PDB:1JEY}.
STRAND 325 329 {ECO:0000244|PDB:1JEY}.
HELIX 331 336 {ECO:0000244|PDB:1JEY}.
STRAND 343 352 {ECO:0000244|PDB:1JEY}.
HELIX 353 355 {ECO:0000244|PDB:1JEY}.
HELIX 358 360 {ECO:0000244|PDB:1JEY}.
STRAND 366 370 {ECO:0000244|PDB:1JEY}.
TURN 372 374 {ECO:0000244|PDB:1JEY}.
HELIX 378 391 {ECO:0000244|PDB:1JEY}.
STRAND 394 401 {ECO:0000244|PDB:1JEY}.
STRAND 403 405 {ECO:0000244|PDB:1JEY}.
STRAND 409 416 {ECO:0000244|PDB:1JEY}.
STRAND 426 428 {ECO:0000244|PDB:1JEY}.
STRAND 430 436 {ECO:0000244|PDB:1JEY}.
HELIX 440 442 {ECO:0000244|PDB:1JEY}.
HELIX 456 468 {ECO:0000244|PDB:1JEY}.
HELIX 481 494 {ECO:0000244|PDB:1JEY}.
HELIX 511 518 {ECO:0000244|PDB:1JEY}.
HELIX 521 529 {ECO:0000244|PDB:1JEY}.
HELIX 561 569 {ECO:0000244|PDB:1JEQ}.
HELIX 573 575 {ECO:0000244|PDB:1JEQ}.
HELIX 578 587 {ECO:0000244|PDB:1JEQ}.
HELIX 596 607 {ECO:0000244|PDB:1JEQ}.
SEQUENCE 609 AA; 69843 MW; BBD3CD434526DFCB CRC64;
MSGWESYYKT EGDEEAEEEQ EENLEASGDY KYSGRDSLIF LVDASKAMFE SQSEDELTPF
DMSIQCIQSV YISKIISSDR DLLAVVFYGT EKDKNSVNFK NIYVLQELDN PGAKRILELD
QFKGQQGQKR FQDMMGHGSD YSLSEVLWVC ANLFSDVQFK MSHKRIMLFT NEDNPHGNDS
AKASRARTKA GDLRDTGIFL DLMHLKKPGG FDISLFYRDI ISIAEDEDLR VHFEESSKLE
DLLRKVRAKE TRKRALSRLK LKLNKDIVIS VGIYNLVQKA LKPPPIKLYR ETNEPVKTKT
RTFNTSTGGL LLPSDTKRSQ IYGSRQIILE KEETEELKRF DDPGLMLMGF KPLVLLKKHH
YLRPSLFVYP EESLVIGSST LFSALLIKCL EKEVAALCRY TPRRNIPPYF VALVPQEEEL
DDQKIQVTPP GFQLVFLPFA DDKRKMPFTE KIMATPEQVG KMKAIVEKLR FTYRSDSFEN
PVLQQHFRNL EALALDLMEP EQAVDLTLPK VEAMNKRLGS LVDEFKELVY PPDYNPEGKV
TKRKHDNEGS GSKRPKVEYS EEELKTHISK GTLGKFTVPM LKEACRAYGL KSGLKKQELL
EALTKHFQD


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