XRCC6_HUMAN
ID XRCC6_HUMAN Reviewed; 609 AA.
AC P12956; B1AHC8; Q6FG89; Q9UCQ2; Q9UCQ3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 247.
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 lyase Ku70;
DE AltName: Full=70 kDa subunit of Ku antigen;
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=Lupus Ku autoantigen protein p70;
DE Short=Ku70;
DE AltName: Full=Thyroid-lupus autoantigen;
DE Short=TLAA;
DE AltName: Full=X-ray repair complementing defective repair in Chinese hamster cells 6;
GN Name=XRCC6; Synonyms=G22P1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2917966; DOI=10.1016/s0021-9258(19)84898-6;
RA Chan J.Y., Lerman M.I., Prabhakar B.S., Isozaki O., Santisteban P.,
RA Kuppers R.C., Oates E.L., Notkins A.L., Kohn L.D.;
RT "Cloning and characterization of a cDNA that encodes a 70-kDa novel human
RT thyroid autoantigen.";
RL J. Biol. Chem. 264:3651-3654(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND ROLE
RP IN LUPUS ERYTHEMATOSUS.
RX PubMed=2466842; DOI=10.1016/s0021-9258(18)83697-3;
RA Reeves W.H., Sthoeger Z.M.;
RT "Molecular cloning of cDNA encoding the p70 (Ku) lupus autoantigen.";
RL J. Biol. Chem. 264:5047-5052(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1608402; DOI=10.1007/bf00419754;
RA Griffith A.J., Craft J., Evans J., Mimori T., Hardin J.A.;
RT "Nucleotide sequence and genomic structure analyses of the p70 subunit of
RT the human Ku autoantigen: evidence for a family of genes encoding Ku (p70)-
RT related polypeptides.";
RL Mol. Biol. Rep. 16:91-97(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Kidney, Lung, Placenta, and Skin;
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 [10]
RP PROTEIN SEQUENCE OF 10-30 AND 299-317.
RX PubMed=1537839; DOI=10.1016/s0021-9258(18)42866-9;
RA Wedrychowski A., Henzel W., Huston L., Paslidis N., Ellerson D., McRae M.,
RA Seong D., Howard O.M.Z., Deisseroth A.;
RT "Identification of proteins binding to interferon-inducible transcriptional
RT enhancers in hematopoietic cells.";
RL J. Biol. Chem. 267:4533-4540(1992).
RN [11]
RP PROTEIN SEQUENCE OF 101-114 AND 116-125, AND DEVELOPMENTAL STAGE.
RC TISSUE=Cervix carcinoma;
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 [12]
RP PROTEIN SEQUENCE OF 288-293 AND 300-312, FUNCTION, AND INTERACTION WITH
RP APEX1.
RX PubMed=8621488; DOI=10.1074/jbc.271.15.8593;
RA Chung U., Igarashi T., Nishishita T., Iwanari H., Iwamatsu A., Suwa A.,
RA Mimori T., Hata K., Ebisu S., Ogata E., Fujita T., Okazaki T.;
RT "The interaction between Ku antigen and REF1 protein mediates negative gene
RT regulation by extracellular calcium.";
RL J. Biol. Chem. 271:8593-8598(1996).
RN [13]
RP PROTEIN SEQUENCE OF 301-308 AND 556-565.
RX PubMed=7882982; DOI=10.1002/j.1460-2075.1995.tb07057.x;
RA Genersch E., Eckerskorn C., Lottspeich F., Herzog C., Kuehn K., Poeschl E.;
RT "Purification of the sequence-specific transcription factor CTCBF, involved
RT in the control of human collagen IV genes: subunits with homology to Ku
RT antigen.";
RL EMBO J. 14:791-800(1995).
RN [14]
RP PROTEIN SEQUENCE OF 346-352, AND FUNCTION.
RX PubMed=7957065; DOI=10.1002/j.1460-2075.1994.tb06826.x;
RA Tuteja N., Tuteja R., Ochem A., Taneja P., Huang N.W., Simoncsits A.,
RA Susic S., Rahman K., Marusic L., Chen J., Zhang J., Wang S., Pongor S.,
RA Falaschi A.;
RT "Human DNA helicase II: a novel DNA unwinding enzyme identified as the Ku
RT autoantigen.";
RL EMBO J. 13:4991-5001(1994).
RN [15]
RP PHOSPHORYLATION AT SER-51.
RX PubMed=9362500; DOI=10.1093/emboj/16.22.6874;
RA Jin S., Weaver D.T.;
RT "Double-strand break repair by Ku70 requires heterodimerization with Ku80
RT and DNA binding functions.";
RL EMBO J. 16:6874-6885(1997).
RN [16]
RP FUNCTION, AND INTERACTION WITH PRKDC.
RX PubMed=9742108; DOI=10.1128/mcb.18.10.5908;
RA West R.B., Yaneva M., Lieber M.R.;
RT "Productive and nonproductive complexes of Ku and DNA-dependent protein
RT kinase at DNA termini.";
RL Mol. Cell. Biol. 18:5908-5920(1998).
RN [17]
RP PHOSPHORYLATION AT SER-6.
RX PubMed=10026262; DOI=10.1021/bi982584b;
RA Chan D.W., Ye R., Veillette C.J., Lees-Miller S.P.;
RT "DNA-dependent protein kinase phosphorylation sites in Ku 70/80
RT heterodimer.";
RL Biochemistry 38:1819-1828(1999).
RN [18]
RP REVIEW.
RX PubMed=10377944; DOI=10.1016/s0921-8777(99)00006-3;
RA Featherstone C., Jackson S.P.;
RT "Ku, a DNA repair protein with multiple cellular functions?";
RL Mutat. Res. 434:3-15(1999).
RN [19]
RP INTERACTION WITH ATP23.
RC TISSUE=Liver;
RX PubMed=10219089; DOI=10.1093/nar/27.10.2165;
RA Yang C.-R., Yeh S.-Y., Leskov K., Odegaard E., Hsu H.L., Chang C.,
RA Kinsella T.J., Chen D.J., Boothman D.A.;
RT "Isolation of Ku70-binding proteins (KUBs).";
RL Nucleic Acids Res. 27:2165-2174(1999).
RN [20]
RP INTERACTION WITH PRKDC.
RX PubMed=12509254; DOI=10.1016/s1568-7864(01)00018-0;
RA Hsu H.-L., Yannone S.M., Chen D.J.;
RT "Defining interactions between DNA-PK and ligase IV/XRCC4.";
RL DNA Repair 1:225-235(2002).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH NAA15;
RP MSX2; RUNX2 AND DLX5.
RC TISSUE=Heart, and 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 [22]
RP IDENTIFICATION IN A COMPLEX WITH XRCC5; PRKDC AND XRCC4, AND
RP PHOSPHORYLATION.
RX PubMed=12547193; DOI=10.1016/s0022-2836(02)01328-1;
RA Calsou P., Delteil C., Frit P., Drouet J., Salles B.;
RT "Coordinated assembly of Ku and p460 subunits of the DNA-dependent protein
RT kinase on DNA ends is necessary for XRCC4-ligase IV recruitment.";
RL J. Mol. Biol. 326:93-103(2003).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [24]
RP INTERACTION WITH ELF3.
RX PubMed=15075319; DOI=10.1074/jbc.m401356200;
RA Wang H., Fang R., Cho J.-Y., Libermann T.A., Oettgen P.;
RT "Positive and negative modulation of the transcriptional activity of the
RT ETS factor ESE-1 through interaction with p300, CREB-binding protein, and
RT Ku 70/86.";
RL J. Biol. Chem. 279:25241-25250(2004).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-331; LYS-338 AND LYS-461,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [29]
RP FUNCTION IN DNA REPAIR, AND INTERACTION WITH CDK9.
RX PubMed=20493174; DOI=10.1016/j.bbrc.2010.05.092;
RA Liu H., Herrmann C.H., Chiang K., Sung T.L., Moon S.H., Donehower L.A.,
RA Rice A.P.;
RT "55K isoform of CDK9 associates with Ku70 and is involved in DNA repair.";
RL Biochem. Biophys. Res. Commun. 397:245-250(2010).
RN [30]
RP INTERACTION WITH ALKBH2.
RX PubMed=23972994; DOI=10.1016/j.celrep.2013.07.027;
RA Li P., Gao S., Wang L., Yu F., Li J., Wang C., Li J., Wong J.;
RT "ABH2 couples regulation of ribosomal DNA transcription with DNA alkylation
RT repair.";
RL Cell Rep. 4:817-829(2013).
RN [31]
RP INTERACTION WITH APLF.
RX PubMed=23689425; DOI=10.1074/jbc.m112.440388;
RA Shirodkar P., Fenton A.L., Meng L., Koch C.A.;
RT "Identification and functional characterization of a Ku-binding motif in
RT aprataxin polynucleotide kinase/phosphatase-like factor (APLF).";
RL J. Biol. Chem. 288:19604-19613(2013).
RN [32]
RP INTERACTION WITH APLF; WRN AND CYREN.
RX PubMed=27063109; DOI=10.1038/ncomms11242;
RA Grundy G.J., Rulten S.L., Arribas-Bosacoma R., Davidson K., Kozik Z.,
RA Oliver A.W., Pearl L.H., Caldecott K.W.;
RT "The Ku-binding motif is a conserved module for recruitment and stimulation
RT of non-homologous end-joining proteins.";
RL Nat. Commun. 7:11242-11242(2016).
RN [33]
RP FUNCTION AS A 5'-DRP LYASE, AND MUTAGENESIS OF LYS-31; LYS-160 AND LYS-164.
RX PubMed=20383123; DOI=10.1038/nature08926;
RA Roberts S.A., Strande N., Burkhalter M.D., Strom C., Havener J.M.,
RA Hasty P., Ramsden D.A.;
RT "Ku is a 5'-dRP/AP lyase that excises nucleotide damage near broken ends.";
RL Nature 464:1214-1217(2010).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455 AND SER-550, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [37]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [38]
RP DNA-BINDING, IDENTIFICATION IN A COMPLEX WITH DEAF1 AND XRCC5, INTERACTION
RP WITH DEAF1, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22442688; DOI=10.1371/journal.pone.0033404;
RA Jensik P.J., Huggenvik J.I., Collard M.W.;
RT "Deformed epidermal autoregulatory factor-1 (DEAF1) interacts with the Ku70
RT subunit of the DNA-dependent protein kinase complex.";
RL PLoS ONE 7:E33404-E33404(2012).
RN [39]
RP INTERACTION WITH HMBOX1.
RX PubMed=23685356; DOI=10.1038/emboj.2013.105;
RA Kappei D., Butter F., Benda C., Scheibe M., Draskovic I., Stevense M.,
RA Novo C.L., Basquin C., Araki M., Araki K., Krastev D.B., Kittler R.,
RA Jessberger R., Londono-Vallejo J.A., Mann M., Buchholz F.;
RT "HOT1 is a mammalian direct telomere repeat-binding protein contributing to
RT telomerase recruitment.";
RL EMBO J. 32:1681-1701(2013).
RN [40]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-27; SER-306; THR-455;
RP SER-477; SER-520 AND SER-560, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [41]
RP INTERACTION WITH CYREN.
RX PubMed=24610814; DOI=10.1074/jbc.c113.533968;
RA Slavoff S.A., Heo J., Budnik B.A., Hanakahi L.A., Saghatelian A.;
RT "A human short open reading frame (sORF)-encoded polypeptide that
RT stimulates DNA end joining.";
RL J. Biol. Chem. 289:10950-10957(2014).
RN [42]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [43]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-556, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [44]
RP ADP-RIBOSYLATION.
RX PubMed=24598253; DOI=10.1093/nar/gku174;
RA Beck C., Boehler C., Guirouilh Barbat J., Bonnet M.E., Illuzzi G.,
RA Ronde P., Gauthier L.R., Magroun N., Rajendran A., Lopez B.S., Scully R.,
RA Boussin F.D., Schreiber V., Dantzer F.;
RT "PARP3 affects the relative contribution of homologous recombination and
RT nonhomologous end-joining pathways.";
RL Nucleic Acids Res. 42:5616-5632(2014).
RN [45]
RP INTERACTION WITH NR4A3.
RX PubMed=25852083; DOI=10.1093/cvr/cvv126;
RA Medunjanin S., Daniel J.M., Weinert S., Dutzmann J., Burgbacher F.,
RA Brecht S., Bruemmer D., Kaehne T., Naumann M., Sedding D.G.,
RA Zuschratter W., Braun-Dullaeus R.C.;
RT "DNA-dependent protein kinase (DNA-PK) permits vascular smooth muscle cell
RT proliferation through phosphorylation of the orphan nuclear receptor
RT NOR1.";
RL Cardiovasc. Res. 106:488-497(2015).
RN [46]
RP SUBUNIT.
RX PubMed=25941166; DOI=10.1038/cdd.2015.22;
RA Craxton A., Somers J., Munnur D., Jukes-Jones R., Cain K., Malewicz M.;
RT "XLS (c9orf142) is a new component of mammalian DNA double-stranded break
RT repair.";
RL Cell Death Differ. 22:890-897(2015).
RN [47]
RP SUBUNIT.
RX PubMed=25670504; DOI=10.1038/ncomms7233;
RA Xing M., Yang M., Huo W., Feng F., Wei L., Jiang W., Ning S., Yan Z.,
RA Li W., Wang Q., Hou M., Dong C., Guo R., Gao G., Ji J., Zha S., Lan L.,
RA Liang H., Xu D.;
RT "Interactome analysis identifies a new paralogue of XRCC4 in non-homologous
RT end joining DNA repair pathway.";
RL Nat. Commun. 6:6233-6233(2015).
RN [48]
RP INTERACTION WITH HSF1.
RX PubMed=26359349; DOI=10.18632/oncotarget.5073;
RA Kang G.Y., Kim E.H., Lee H.J., Gil N.Y., Cha H.J., Lee Y.S.;
RT "Heat shock factor 1, an inhibitor of non-homologous end joining repair.";
RL Oncotarget 6:29712-29724(2015).
RN [49]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [50]
RP INTERACTION WITH PAXX.
RX PubMed=25574025; DOI=10.1126/science.1261971;
RA Ochi T., Blackford A.N., Coates J., Jhujh S., Mehmood S., Tamura N.,
RA Travers J., Wu Q., Draviam V.M., Robinson C.V., Blundell T.L.,
RA Jackson S.P.;
RT "DNA repair. PAXX, a paralog of XRCC4 and XLF, interacts with Ku to promote
RT DNA double-strand break repair.";
RL Science 347:185-188(2015).
RN [51]
RP INTERACTION WITH PAXX.
RX PubMed=27601299; DOI=10.1016/j.celrep.2016.08.069;
RA Lescale C., Lenden Hasse H., Blackford A.N., Balmus G., Bianchi J.J.,
RA Yu W., Bacoccina L., Jarade A., Clouin C., Sivapalan R.,
RA Reina-San-Martin B., Jackson S.P., Deriano L.;
RT "Specific roles of XRCC4 paralogs PAXX and XLF during V(D)J
RT recombination.";
RL Cell Rep. 16:2967-2979(2016).
RN [52]
RP INTERACTION WITH PAXX.
RX PubMed=27705800; DOI=10.1016/j.celrep.2016.09.026;
RA Tadi S.K., Tellier-Lebegue C., Nemoz C., Drevet P., Audebert S., Roy S.,
RA Meek K., Charbonnier J.B., Modesti M.;
RT "PAXX is an accessory c-NHEJ factor that associates with Ku70 and has
RT overlapping functions with XLF.";
RL Cell Rep. 17:541-555(2016).
RN [53]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRKDC; XRCC5; HEXIM1;
RP SFPQ; NONO; PSPC1; RBM14 AND MATR3.
RX PubMed=28712728; DOI=10.1016/j.molcel.2017.06.020;
RA Morchikh M., Cribier A., Raffel R., Amraoui S., Cau J., Severac D.,
RA Dubois E., Schwartz O., Bennasser Y., Benkirane M.;
RT "HEXIM1 and NEAT1 Long non-coding RNA form a multi-subunit complex that
RT regulates DNA-mediated innate immune response.";
RL Mol. Cell 67:387-399(2017).
RN [54]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-287; LYS-317 AND LYS-556, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [55]
RP INTERACTION WITH CYREN.
RX PubMed=28959974; DOI=10.1038/nature24023;
RA Arnoult N., Correia A., Ma J., Merlo A., Garcia-Gomez S., Maric M.,
RA Tognetti M., Benner C.W., Boulton S.J., Saghatelian A., Karlseder J.;
RT "Regulation of DNA repair pathway choice in S and G2 phases by the NHEJ
RT inhibitor CYREN.";
RL Nature 549:548-552(2017).
RN [56]
RP INTERACTION WITH HUMAN T-CELL LEUKEMIA VIRUS 1/HTLV-1 PROTEIN HBZ.
RX PubMed=29769340; DOI=10.1128/jvi.00672-18;
RA Rushing A.W., Hoang K., Polakowski N., Lemasson I.;
RT "non-homologous end joining (NHEJ).";
RL J. Virol. 0:0-0(2018).
RN [57]
RP INTERACTION WITH ATF7.
RX PubMed=29490055; DOI=10.1093/nar/gky155;
RA Maekawa T., Liu B., Nakai D., Yoshida K., Nakamura K.I., Yasukawa M.,
RA Koike M., Takubo K., Chatton B., Ishikawa F., Masutomi K., Ishii S.;
RT "ATF7 mediates TNF-alpha-induced telomere shortening.";
RL Nucleic Acids Res. 46:4487-4504(2018).
RN [58]
RP STRUCTURE BY NMR OF 557-610.
RX PubMed=11457852; DOI=10.1074/jbc.m105238200;
RA Zhang Z., Zhu L., Lin D., Chen F., Chen D.J., Chen Y.;
RT "The three-dimensional structure of the C-terminal DNA-binding domain of
RT human Ku70.";
RL J. Biol. Chem. 276:38231-38236(2001).
RN [59]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 36-609 IN COMPLEX WITH XRCC5, AND
RP FUNCTION.
RX PubMed=11493912; DOI=10.1038/35088000;
RA Walker J.R., Corpina R.A., Goldberg J.;
RT "Structure of the Ku heterodimer bound to DNA and its implications for
RT double-strand break repair.";
RL Nature 412:607-614(2001).
RN [60] {ECO:0007744|PDB:7LSY, ECO:0007744|PDB:7LT3}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.6 ANGSTROMS) IN COMPLEX WITH THE NHEJ
RP COMPLEX, AND IDENTIFICATION IN THE NHEJ COMPLEX.
RX PubMed=33854234; DOI=10.1038/s41586-021-03458-7;
RA Chen S., Lee L., Naila T., Fishbain S., Wang A., Tomkinson A.E.,
RA Lees-Miller S.P., He Y.;
RT "Structural basis of long-range to short-range synaptic transition in
RT NHEJ.";
RL Nature 593:294-298(2021).
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 (PubMed:7957065, PubMed:8621488, PubMed:12145306,
CC PubMed:11493912, PubMed:20493174, PubMed:2466842, PubMed:9742108).
CC Required for double-strand break repair and V(D)J recombination
CC (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912,
CC PubMed:20493174, PubMed:2466842, PubMed:9742108). Also has a role in
CC chromosome translocation (PubMed:7957065, PubMed:8621488,
CC PubMed:12145306, PubMed:11493912, PubMed:20493174, PubMed:2466842,
CC PubMed:9742108). Has a role in chromosome translocation
CC (PubMed:7957065, PubMed:20493174, PubMed:2466842, PubMed:9742108,
CC PubMed:8621488, PubMed:12145306, PubMed:11493912). The DNA helicase II
CC complex binds preferentially to fork-like ends of double-stranded DNA
CC in a cell cycle-dependent manner (PubMed:7957065, PubMed:8621488,
CC PubMed:20493174, PubMed:2466842, PubMed:9742108, PubMed:12145306,
CC PubMed:11493912). It works in the 3'-5' direction (PubMed:20493174,
CC PubMed:2466842, PubMed:9742108, PubMed:7957065, PubMed:8621488,
CC PubMed:12145306, PubMed:11493912). During NHEJ, the XRCC5-XRRC6 dimer
CC performs the recognition step: it recognizes and binds to the broken
CC ends of the DNA and protects them from further resection
CC (PubMed:7957065, PubMed:8621488, PubMed:20493174, PubMed:2466842,
CC PubMed:9742108, PubMed:12145306, PubMed:11493912). Binding to DNA may
CC be mediated by XRCC6 (PubMed:20493174, PubMed:2466842, PubMed:9742108,
CC PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912). The
CC XRCC5-XRRC6 dimer acts as regulatory subunit of the DNA-dependent
CC protein kinase complex DNA-PK by increasing the affinity of the
CC catalytic subunit PRKDC to DNA by 100-fold (PubMed:7957065,
CC PubMed:8621488, PubMed:12145306, PubMed:11493912, PubMed:20493174,
CC PubMed:2466842, PubMed:9742108). The XRCC5-XRRC6 dimer is probably
CC involved in stabilizing broken DNA ends and bringing them together
CC (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912,
CC PubMed:20493174, PubMed:2466842, PubMed:9742108). The assembly of the
CC DNA-PK complex to DNA ends is required for the NHEJ ligation step
CC (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912,
CC PubMed:20493174, PubMed:2466842, PubMed:9742108). Probably also acts as
CC a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the
CC beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site
CC near double-strand breaks (PubMed:20383123). 5'-dRP lyase activity
CC allows to 'clean' the termini of abasic sites, a class of nucleotide
CC damage commonly associated with strand breaks, before such broken ends
CC can be joined (PubMed:20383123). The XRCC5-XRRC6 dimer together with
CC APEX1 acts as a negative regulator of transcription (PubMed:8621488).
CC In association with NAA15, the XRCC5-XRRC6 dimer binds to the
CC osteocalcin promoter and activates osteocalcin expression
CC (PubMed:12145306). Plays a role in the regulation of DNA virus-mediated
CC innate immune response by assembling into the HDP-RNP complex, a
CC complex that serves as a platform for IRF3 phosphorylation and
CC subsequent innate immune response activation through the cGAS-STING
CC pathway (PubMed:28712728). {ECO:0000269|PubMed:11493912,
CC ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:20383123,
CC ECO:0000269|PubMed:20493174, ECO:0000269|PubMed:2466842,
CC ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:7957065,
CC ECO:0000269|PubMed:8621488, ECO:0000269|PubMed:9742108}.
CC -!- SUBUNIT: Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70
CC (PubMed:11493912). 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 (PubMed:12509254,
CC PubMed:9742108, PubMed:12547193, PubMed:25941166, PubMed:25670504,
CC PubMed:33854234). Additional component of the NHEJ complex includes
CC PAXX (PubMed:25574025, PubMed:27601299, PubMed:27705800). Following
CC autophosphorylation, PRKDC dissociates from DNA, leading to formation
CC of the short-range NHEJ complex, composed of LIG4, XRCC4, XRCC6/Ku70,
CC XRCC5/Ku86 and NHEJ1/XLF (PubMed:33854234). The XRCC5-XRCC6 dimer also
CC associates with NAA15, and this complex binds to the osteocalcin
CC promoter and activates osteocalcin expression (PubMed:12145306). In
CC addition, XRCC6 interacts with the osteoblast-specific transcription
CC factors MSX2, RUNX2 and DLX5 (PubMed:12145306). Interacts with ELF3
CC (PubMed:15075319). Interacts with ATP23 (PubMed:10219089). The XRCC5-
CC XRRC6 dimer associates in a DNA-dependent manner with APEX1
CC (PubMed:8621488). Binds to CDK9 isoform 2 (PubMed:20493174). Identified
CC in a complex with DEAF1 and XRCC5 (PubMed:22442688). Interacts with
CC DEAF1 (via the SAND domain); the interaction is direct and may be
CC inhibited by DNA-binding (PubMed:22442688). Interacts with CLU (By
CC similarity). Interacts with NR4A3; the DNA-dependent protein kinase
CC complex DNA-PK phosphorylates and activates NR4A3 and prevents NR4A3
CC ubiquitinylation and degradation (PubMed:25852083). Interacts with
CC CYREN isoform 1 (CYREN-1) and isoform 4 (CYREN-2) (via KBM motif)
CC (PubMed:27063109, PubMed:24610814, PubMed:28959974). Interacts (via N-
CC terminus) with HSF1 (via N-terminus); this interaction is direct and
CC prevents XRCC5/XRCC6 heterodimeric binding and non-homologous end
CC joining (NHEJ) repair activities induced by ionizing radiation (IR)
CC (PubMed:26359349). Part of the HDP-RNP complex composed of at least
CC HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1,
CC RBM14, and MATR3) and NEAT1 RNA (PubMed:28712728). Interacts with
CC HMBOX1 (PubMed:23685356). Interacts with ATF7 (PubMed:29490055).
CC Interacts with APLF (via KBM motif) (PubMed:23689425, PubMed:27063109).
CC Interacts with WRN (via KBM motif) (PubMed:27063109). The XRCC5-XRCC6
CC dimer associates with ALKBH2. {ECO:0000250|UniProtKB:P23475,
CC ECO:0000269|PubMed:10219089, ECO:0000269|PubMed:11493912,
CC ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:12509254,
CC ECO:0000269|PubMed:12547193, ECO:0000269|PubMed:15075319,
CC ECO:0000269|PubMed:20493174, ECO:0000269|PubMed:22442688,
CC ECO:0000269|PubMed:23685356, ECO:0000269|PubMed:23689425,
CC ECO:0000269|PubMed:23972994, ECO:0000269|PubMed:24610814,
CC ECO:0000269|PubMed:25574025, ECO:0000269|PubMed:25670504,
CC ECO:0000269|PubMed:25852083, ECO:0000269|PubMed:25941166,
CC ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:27063109,
CC ECO:0000269|PubMed:27601299, ECO:0000269|PubMed:27705800,
CC ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:28959974,
CC ECO:0000269|PubMed:29490055, ECO:0000269|PubMed:33854234,
CC ECO:0000269|PubMed:8621488, ECO:0000269|PubMed:9742108}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human T-cell leukemia
CC virus 1/HTLV-1 protein HBZ. {ECO:0000269|PubMed:29769340}.
CC -!- INTERACTION:
CC P12956; Q96P48: ARAP1; NbExp=2; IntAct=EBI-353208, EBI-710003;
CC P12956; Q07812: BAX; NbExp=2; IntAct=EBI-353208, EBI-516580;
CC P12956; P38432: COIL; NbExp=3; IntAct=EBI-353208, EBI-945751;
CC P12956; O75398: DEAF1; NbExp=7; IntAct=EBI-353208, EBI-718185;
CC P12956; Q6NT76: HMBOX1; NbExp=2; IntAct=EBI-353208, EBI-2549423;
CC P12956; P42858: HTT; NbExp=21; IntAct=EBI-353208, EBI-466029;
CC P12956; Q92597: NDRG1; NbExp=2; IntAct=EBI-353208, EBI-716486;
CC P12956; Q08752: PPID; NbExp=4; IntAct=EBI-353208, EBI-716596;
CC P12956; O15355: PPM1G; NbExp=3; IntAct=EBI-353208, EBI-725702;
CC P12956; P78527: PRKDC; NbExp=7; IntAct=EBI-353208, EBI-352053;
CC P12956; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-353208, EBI-396669;
CC P12956; Q96EB6: SIRT1; NbExp=7; IntAct=EBI-353208, EBI-1802965;
CC P12956; Q9NQB0: TCF7L2; NbExp=10; IntAct=EBI-353208, EBI-924724;
CC P12956; Q9NYB0: TERF2IP; NbExp=3; IntAct=EBI-353208, EBI-750109;
CC P12956; P04637: TP53; NbExp=2; IntAct=EBI-353208, EBI-366083;
CC P12956; P13693: TPT1; NbExp=8; IntAct=EBI-353208, EBI-1783169;
CC P12956; O76024: WFS1; NbExp=3; IntAct=EBI-353208, EBI-720609;
CC P12956; Q14191: WRN; NbExp=6; IntAct=EBI-353208, EBI-368417;
CC P12956; Q13426: XRCC4; NbExp=3; IntAct=EBI-353208, EBI-717592;
CC P12956; P13010: XRCC5; NbExp=20; IntAct=EBI-353208, EBI-357997;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22442688}. Chromosome
CC {ECO:0000269|PubMed:22442688}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P12956-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P12956-2; Sequence=VSP_056030;
CC -!- DEVELOPMENTAL STAGE: Expression does not increase during promyelocyte
CC differentiation. {ECO:0000269|PubMed:8605992}.
CC -!- INDUCTION: In osteoblasts, by FGF2.
CC -!- PTM: Phosphorylation by PRKDC may enhance helicase activity.
CC Phosphorylation of Ser-51 does not affect DNA repair.
CC {ECO:0000269|PubMed:10026262, ECO:0000269|PubMed:12547193,
CC ECO:0000269|PubMed:9362500}.
CC -!- PTM: ADP-ribosylated by PARP3. {ECO:0000269|PubMed:24598253}.
CC -!- MISCELLANEOUS: Individuals with systemic lupus erythematosus (SLE) and
CC related disorders produce extremely large amounts of autoantibodies to
CC XRCC5 and XRCC6. Existence of a major autoantigenic epitope or epitopes
CC on the C-terminal 190 amino acids of XRCC6 containing the leucine
CC repeat. The majority of autoantibodies to XRCC6 in most sera from
CC patients with SLE seem to be reactive with this region.
CC -!- SIMILARITY: Belongs to the ku70 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/g22p1/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/XRCC6ID246ch22q13.html";
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DR EMBL; J04607; AAA61177.1; -; mRNA.
DR EMBL; J04611; AAA51733.1; -; mRNA.
DR EMBL; M32865; AAA36155.1; -; mRNA.
DR EMBL; S38729; AAB22381.1; -; mRNA.
DR EMBL; AK055786; BAG51575.1; -; mRNA.
DR EMBL; CR542219; CAG47015.1; -; mRNA.
DR EMBL; AY870329; AAW34364.1; -; Genomic_DNA.
DR EMBL; Z83840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60448.1; -; Genomic_DNA.
DR EMBL; BC008343; AAH08343.1; -; mRNA.
DR EMBL; BC010034; AAH10034.1; -; mRNA.
DR EMBL; BC012154; AAH12154.1; -; mRNA.
DR EMBL; BC018259; AAH18259.1; -; mRNA.
DR EMBL; BC072449; AAH72449.1; -; mRNA.
DR CCDS; CCDS14021.1; -. [P12956-1]
DR CCDS; CCDS74870.1; -. [P12956-2]
DR PIR; A30299; A30894.
DR RefSeq; NP_001275905.1; NM_001288976.1. [P12956-1]
DR RefSeq; NP_001275906.1; NM_001288977.1. [P12956-2]
DR RefSeq; NP_001460.1; NM_001469.4. [P12956-1]
DR PDB; 1JEQ; X-ray; 2.70 A; A=1-609.
DR PDB; 1JEY; X-ray; 2.50 A; A=1-609.
DR PDB; 1JJR; NMR; -; A=556-609.
DR PDB; 3RZX; X-ray; 2.61 A; B=537-558.
DR PDB; 5Y3R; EM; 6.60 A; A=34-534.
DR PDB; 6ERF; X-ray; 3.01 A; A/C/E/G=1-544.
DR PDB; 6ERG; X-ray; 2.90 A; A/D=1-544.
DR PDB; 6ERH; X-ray; 2.80 A; A/C=1-544.
DR PDB; 6ZHA; EM; 3.91 A; B=1-609.
DR PDB; 6ZHE; EM; 7.24 A; B/G=1-609.
DR PDB; 7AXZ; EM; 3.20 A; A=1-609.
DR PDB; 7K0Y; EM; 3.70 A; B=1-609.
DR PDB; 7K1J; EM; 3.90 A; B=1-609.
DR PDB; 7K1K; EM; 4.10 A; B=1-609.
DR PDB; 7K1N; EM; 3.90 A; B=1-609.
DR PDB; 7LSY; EM; 8.40 A; A/J=1-600.
DR PDB; 7LT3; EM; 4.60 A; A/J=1-609.
DR PDB; 7NFC; EM; 4.14 A; B/G=1-609.
DR PDB; 7NFE; EM; 4.29 A; B=1-609.
DR PDB; 7SGL; EM; 3.00 A; B=1-609.
DR PDB; 7SU3; EM; 3.30 A; B=1-609.
DR PDBsum; 1JEQ; -.
DR PDBsum; 1JEY; -.
DR PDBsum; 1JJR; -.
DR PDBsum; 3RZX; -.
DR PDBsum; 5Y3R; -.
DR PDBsum; 6ERF; -.
DR PDBsum; 6ERG; -.
DR PDBsum; 6ERH; -.
DR PDBsum; 6ZHA; -.
DR PDBsum; 6ZHE; -.
DR PDBsum; 7AXZ; -.
DR PDBsum; 7K0Y; -.
DR PDBsum; 7K1J; -.
DR PDBsum; 7K1K; -.
DR PDBsum; 7K1N; -.
DR PDBsum; 7LSY; -.
DR PDBsum; 7LT3; -.
DR PDBsum; 7NFC; -.
DR PDBsum; 7NFE; -.
DR PDBsum; 7SGL; -.
DR PDBsum; 7SU3; -.
DR AlphaFoldDB; P12956; -.
DR BMRB; P12956; -.
DR SASBDB; P12956; -.
DR SMR; P12956; -.
DR BioGRID; 108822; 715.
DR ComplexPortal; CPX-1993; Ku70:Ku80 complex.
DR CORUM; P12956; -.
DR DIP; DIP-24188N; -.
DR ELM; P12956; -.
DR IntAct; P12956; 212.
DR MINT; P12956; -.
DR STRING; 9606.ENSP00000352257; -.
DR ChEMBL; CHEMBL4106136; -.
DR MoonDB; P12956; Curated.
DR GlyGen; P12956; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P12956; -.
DR MetOSite; P12956; -.
DR PhosphoSitePlus; P12956; -.
DR SwissPalm; P12956; -.
DR BioMuta; XRCC6; -.
DR DMDM; 125729; -.
DR SWISS-2DPAGE; P12956; -.
DR EPD; P12956; -.
DR jPOST; P12956; -.
DR MassIVE; P12956; -.
DR MaxQB; P12956; -.
DR PaxDb; P12956; -.
DR PeptideAtlas; P12956; -.
DR PRIDE; P12956; -.
DR ProteomicsDB; 2929; -.
DR ProteomicsDB; 52888; -. [P12956-1]
DR Antibodypedia; 3790; 1341 antibodies from 43 providers.
DR DNASU; 2547; -.
DR Ensembl; ENST00000359308.8; ENSP00000352257.4; ENSG00000196419.13. [P12956-1]
DR Ensembl; ENST00000360079.8; ENSP00000353192.3; ENSG00000196419.13. [P12956-1]
DR Ensembl; ENST00000402580.7; ENSP00000384941.3; ENSG00000196419.13. [P12956-2]
DR Ensembl; ENST00000405878.5; ENSP00000384257.1; ENSG00000196419.13. [P12956-1]
DR GeneID; 2547; -.
DR KEGG; hsa:2547; -.
DR MANE-Select; ENST00000360079.8; ENSP00000353192.3; NM_001469.5; NP_001460.1.
DR UCSC; uc003bao.3; human. [P12956-1]
DR CTD; 2547; -.
DR DisGeNET; 2547; -.
DR GeneCards; XRCC6; -.
DR HGNC; HGNC:4055; XRCC6.
DR HPA; ENSG00000196419; Low tissue specificity.
DR MIM; 152690; gene.
DR neXtProt; NX_P12956; -.
DR OpenTargets; ENSG00000196419; -.
DR PharmGKB; PA28467; -.
DR VEuPathDB; HostDB:ENSG00000196419; -.
DR eggNOG; KOG2327; Eukaryota.
DR GeneTree; ENSGT00940000153239; -.
DR HOGENOM; CLU_014815_2_0_1; -.
DR InParanoid; P12956; -.
DR OMA; PNDMMGI; -.
DR PhylomeDB; P12956; -.
DR TreeFam; TF315101; -.
DR PathwayCommons; P12956; -.
DR Reactome; R-HSA-164843; 2-LTR circle formation.
DR Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
DR Reactome; R-HSA-3270619; IRF3-mediated induction of type I IFN.
DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P12956; -.
DR SIGNOR; P12956; -.
DR BioGRID-ORCS; 2547; 808 hits in 1060 CRISPR screens.
DR ChiTaRS; XRCC6; human.
DR EvolutionaryTrace; P12956; -.
DR GeneWiki; Ku70; -.
DR GenomeRNAi; 2547; -.
DR Pharos; P12956; Tbio.
DR PRO; PR:P12956; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P12956; protein.
DR Bgee; ENSG00000196419; Expressed in right testis and 212 other tissues.
DR ExpressionAtlas; P12956; baseline and differential.
DR Genevisible; P12956; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070418; C:DNA-dependent protein kinase complex; IPI:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0043564; C:Ku70:Ku80 complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0070419; C:nonhomologous end joining complex; IDA:UniProtKB.
DR GO; GO:0000783; C:nuclear telomere cap complex; TAS:BHF-UCL.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0005667; C:transcription regulator complex; IDA:UniProtKB.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:FlyBase.
DR GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IDA:FlyBase.
DR GO; GO:0003690; F:double-stranded DNA binding; TAS:ProtInc.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; IPI:ARUK-UCL.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
DR GO; GO:0071480; P:cellular response to gamma radiation; IDA:UniProtKB.
DR GO; GO:0071481; P:cellular response to X-ray; IBA:GO_Central.
DR GO; GO:0006266; P:DNA ligation; TAS:ProtInc.
DR GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IDA:BHF-UCL.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0045621; P:positive regulation of lymphocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:CAFA.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0000725; P:recombinational repair; IC:ComplexPortal.
DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; IMP:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR DisProt; DP01254; -.
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 IDEAL; IID00023; -.
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 3D-structure; Acetylation; Activator; ADP-ribosylation;
KW Alternative splicing; ATP-binding; Chromosome; Direct protein sequencing;
KW DNA damage; DNA recombination; DNA repair; DNA-binding; Helicase;
KW Host-virus interaction; Hydrolase; Immunity; Innate immunity;
KW Isopeptide bond; Lyase; Multifunctional enzyme; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Systemic lupus erythematosus;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..609
FT /note="X-ray repair cross-complementing protein 6"
FT /id="PRO_0000210179"
FT DOMAIN 261..468
FT /note="Ku"
FT DOMAIN 573..607
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..609
FT /note="Interaction with DEAF1"
FT /evidence="ECO:0000269|PubMed:22442688"
FT COMPBIAS 537..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 31
FT /note="Schiff-base intermediate with DNA; for 5'-
FT deoxyribose-5-phosphate lyase activity"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 6
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000269|PubMed:10026262"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 31
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 51
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000269|PubMed:9362500"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 331
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 338
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 455
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 461
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 317
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 556
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 65..105
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056030"
FT MUTAGEN 31
FT /note="K->A: Diminishes the ability to form a Schiff base.
FT Abolishes adduct formation; when associated with A-160 and
FT A-164."
FT /evidence="ECO:0000269|PubMed:20383123"
FT MUTAGEN 160
FT /note="K->A: Abolishes adduct formation; when associated
FT with A-31 and A-160."
FT /evidence="ECO:0000269|PubMed:20383123"
FT MUTAGEN 164
FT /note="K->A: Abolishes adduct formation; when associated
FT with A-31 and A-164."
FT /evidence="ECO:0000269|PubMed:20383123"
FT CONFLICT 20
FT /note="Q -> D (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="N -> K (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="Y -> L (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="I -> S (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="Q -> S (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="A -> T (in Ref. 5; CAG47015)"
FT /evidence="ECO:0000305"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 59..76
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:7AXZ"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:1JEY"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 161..171
FT /evidence="ECO:0007829|PDB:1JEY"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 180..196
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:1JEY"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:7SGL"
FT TURN 225..229
FT /evidence="ECO:0007829|PDB:6ERG"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 239..250
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 256..266
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:1JEY"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 295..304
FT /evidence="ECO:0007829|PDB:1JEY"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 343..352
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:1JEY"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 378..391
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 394..401
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 409..416
FT /evidence="ECO:0007829|PDB:1JEY"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:7SGL"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 430..436
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 456..468
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 481..494
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:7AXZ"
FT HELIX 511..518
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 521..529
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 561..569
FT /evidence="ECO:0007829|PDB:1JEQ"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:1JEQ"
FT HELIX 578..587
FT /evidence="ECO:0007829|PDB:1JEQ"
FT HELIX 596..607
FT /evidence="ECO:0007829|PDB:1JEQ"
SQ 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
