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X-ray repair cross-complementing protein 5 (EC 3.6.4.-) (86 kDa subunit of Ku antigen) (ATP-dependent DNA helicase 2 subunit 2) (ATP-dependent DNA helicase II 80 kDa subunit) (CTC box-binding factor 85 kDa subunit) (CTC85) (CTCBF) (DNA repair protein XRCC5) (Ku80) (Ku86) (Lupus Ku autoantigen protein p86) (Nuclear factor IV) (Thyroid-lupus autoantigen) (TLAA) (X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining))

 XRCC5_HUMAN             Reviewed;         732 AA.
P13010; A8K3X5; Q0Z7V0; Q4VBQ5; Q53HH7; Q7M4N0; Q9UCQ0; Q9UCQ1;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 202.
RecName: Full=X-ray repair cross-complementing protein 5;
EC=3.6.4.-;
AltName: Full=86 kDa subunit of Ku antigen;
AltName: Full=ATP-dependent DNA helicase 2 subunit 2;
AltName: Full=ATP-dependent DNA helicase II 80 kDa subunit;
AltName: Full=CTC box-binding factor 85 kDa subunit;
Short=CTC85;
Short=CTCBF;
AltName: Full=DNA repair protein XRCC5;
AltName: Full=Ku80;
AltName: Full=Ku86;
AltName: Full=Lupus Ku autoantigen protein p86;
AltName: Full=Nuclear factor IV;
AltName: Full=Thyroid-lupus autoantigen;
Short=TLAA;
AltName: Full=X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining);
Name=XRCC5; Synonyms=G22P2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 4-22.
PubMed=2760028;
Yaneva M., Wen J., Ayala A., Cook R.;
"cDNA-derived amino acid sequence of the 86-kDa subunit of the Ku
antigen.";
J. Biol. Chem. 264:13407-13411(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2308937; DOI=10.1073/pnas.87.5.1777;
Mimori T., Ohosone Y., Hama N., Suwa A., Akizuki M., Homma M.,
Griffith A.J., Hardin J.A.;
"Isolation and characterization of cDNA encoding the 80-kDa subunit
protein of the human autoantigen Ku (p70/p80) recognized by
autoantibodies from patients with scleroderma-polymyositis overlap
syndrome.";
Proc. Natl. Acad. Sci. U.S.A. 87:1777-1781(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Neuroblastoma;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Coronary artery;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thyroid, and Uterus;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-22.
PubMed=2211668;
Knuth M.W., Gunderson S.I., Thompson N.E., Strasheim L.A.,
Burgess R.R.;
"Purification and characterization of proximal sequence element-
binding protein 1, a transcription activating protein related to Ku
and TREF that binds the proximal sequence element of the human U1
promoter.";
J. Biol. Chem. 265:17911-17920(1990).
[9]
PROTEIN SEQUENCE OF 2-20, FUNCTION, AND INVOLVEMENT IN LUPUS
ERYTHEMATOSUS.
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).
[10]
PROTEIN SEQUENCE OF 2-16; 98-113; 443-461 AND 473-479, 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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 105-732, AND PARTIAL PROTEIN SEQUENCE.
PubMed=2212941; DOI=10.1084/jem.172.4.1049;
Stuiver M.H., Coenjaerts F.E.J., van der Vlied P.C.;
"The autoantigen Ku is indistinguishable from NF IV, a protein forming
multimeric protein-DNA complexes.";
J. Exp. Med. 172:1049-1054(1990).
[12]
PROTEIN SEQUENCE OF 186-193; 317-326; 545-559 AND 656-661.
PubMed=8031790; DOI=10.1021/bi00194a021;
Cao Q.P., Pitt S., Leszyk J., Baril E.F.;
"DNA-dependent ATPase from HeLa cells is related to human Ku
autoantigen.";
Biochemistry 33:8548-8557(1994).
[13]
PROTEIN SEQUENCE OF 526-531; 535-542 AND 704-708, 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).
[14]
PROTEIN SEQUENCE OF 526-565 AND 709-732.
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).
[15]
PROTEIN SEQUENCE OF 534-542.
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).
[16]
PHOSPHORYLATION AT SER-577; SER-579; SER-580 AND THR-715.
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).
[17]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH
NAA15; MSX2 AND RUNX2.
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).
[18]
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).
[19]
INTERACTION WITH DHX9.
PubMed=14704337; DOI=10.1093/nar/gkg933;
Zhang S., Schlott B., Goerlach M., Grosse F.;
"DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA
helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent
manner.";
Nucleic Acids Res. 32:1-10(2004).
[20]
SUMOYLATION.
PubMed=15561718; DOI=10.1074/jbc.M411718200;
Gocke C.B., Yu H., Kang J.;
"Systematic identification and analysis of mammalian small ubiquitin-
like modifier substrates.";
J. Biol. Chem. 280:5004-5012(2005).
[21]
DOMAIN, AND MUTAGENESIS OF 720-GLU-GLU-721 AND 726-ASP-ASP-727.
PubMed=15758953; DOI=10.1038/nature03442;
Falck J., Coates J., Jackson S.P.;
"Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of
DNA damage.";
Nature 434:605-611(2005).
[22]
INTERACTION WITH APLF.
PubMed=17396150; DOI=10.1038/sj.emboj.7601663;
Kanno S., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S.,
Yasui A.;
"A novel human AP endonuclease with conserved zinc-finger-like motifs
involved in DNA strand break responses.";
EMBO J. 26:2094-2103(2007).
[23]
INTERACTION WITH APLF.
PubMed=17353262; DOI=10.1128/MCB.02269-06;
Iles N., Rulten S., El-Khamisy S.F., Caldecott K.W.;
"APLF (C2orf13) is a novel human protein involved in the cellular
response to chromosomal DNA strand breaks.";
Mol. Cell. Biol. 27:3793-3803(2007).
[24]
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).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-144; LYS-265; LYS-332;
LYS-660 AND LYS-665, 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).
[26]
FUNCTION.
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).
[27]
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).
[28]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=22002106; DOI=10.1074/mcp.M111.013680;
Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
"Systematic analysis of protein pools, isoforms, and modifications
affecting turnover and subcellular localization.";
Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
[29]
DNA-BINDING, IDENTIFICATION IN A COMPLEX WITH XRCC6 AND 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).
[30]
UBIQUITINATION BY RNF8.
PubMed=22266820; DOI=10.1038/nsmb.2211;
Feng L., Chen J.;
"The E3 ligase RNF8 regulates KU80 removal and NHEJ repair.";
Nat. Struct. Mol. Biol. 19:201-206(2012).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255; SER-258; SER-318
AND THR-535, 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).
[32]
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).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-577, AND 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).
[34]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-568, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[35]
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).
[36]
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).
[37]
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).
[38]
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).
[39]
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).
[40]
INTERACTION WITH C9ORF142.
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).
[41]
UBIQUITINATION, AND INTERACTION WITH RNF138.
PubMed=26502055; DOI=10.1038/ncb3259;
Ismail I.H., Gagne J.P., Genois M.M., Strickfaden H., McDonald D.,
Xu Z., Poirier G.G., Masson J.Y., Hendzel M.J.;
"The RNF138 E3 ligase displaces Ku to promote DNA end resection and
regulate DNA repair pathway choice.";
Nat. Cell Biol. 17:1446-1457(2015).
[42]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-195; LYS-532; LYS-534;
LYS-566; LYS-568; LYS-669 AND LYS-688, 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).
[43]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-565 IN COMPLEX WITH XRCC6.
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
(PubMed:12145306, PubMed:20383123, PubMed:7957065,
PubMed:8621488). The assembly of the DNA-PK complex to DNA ends is
required for the NHEJ ligation step. In association with NAA15,
the XRCC5/6 dimer binds to the osteocalcin promoter and activates
osteocalcin expression (PubMed:20383123). The XRCC5/6 dimer
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. XRCC5
probably acts as the catalytic subunit of 5'-dRP activity, and
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
(PubMed:8621488). {ECO:0000269|PubMed:12145306,
ECO:0000269|PubMed:20383123, ECO:0000269|PubMed:7957065,
ECO:0000269|PubMed:8621488}.
-!- 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 (PubMed:25941166, PubMed:25670504, PubMed:11493912,
PubMed:22442688). Additional components of the NHEJ complex
include NHEJ1/XLF and C9orf142/PAXX (PubMed:25574025,
PubMed:25941166, PubMed:25670504). The dimer also associates with
NAA15, and this complex displays DNA binding activity towards the
osteocalcin FGF response element (OCFRE) (PubMed:12145306). In
addition, XRCC5 binds to the osteoblast-specific transcription
factors MSX2 and RUNX2 (PubMed:12145306). Interacts with ELF3
(PubMed:15075319). May interact with APLF (PubMed:17353262,
PubMed:17396150). The XRCC5/XRCC6 dimer associates in a DNA-
dependent manner with APEX1 (PubMed:8621488). Identified in a
complex with DEAF1 and XRCC6. 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 RNF138
(PubMed:26502055). 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). Interacts with DHX9; this interaction
occurs in a RNA-dependent manner (PubMed:14704337).
{ECO:0000269|PubMed:11493912, ECO:0000269|PubMed:12145306,
ECO:0000269|PubMed:14704337, ECO:0000269|PubMed:15075319,
ECO:0000269|PubMed:17353262, ECO:0000269|PubMed:17396150,
ECO:0000269|PubMed:22442688, ECO:0000269|PubMed:24610814,
ECO:0000269|PubMed:25574025, ECO:0000269|PubMed:25670504,
ECO:0000269|PubMed:25852083, ECO:0000269|PubMed:25941166,
ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:26502055,
ECO:0000269|PubMed:8621488}.
-!- INTERACTION:
Q8IW19:APLF; NbExp=12; IntAct=EBI-357997, EBI-1256044;
P38432:COIL; NbExp=6; IntAct=EBI-357997, EBI-945751;
Q9H4A6:GOLPH3; NbExp=2; IntAct=EBI-357997, EBI-2465479;
P09629:HOXB7; NbExp=9; IntAct=EBI-357997, EBI-1248457;
P04792:HSPB1; NbExp=2; IntAct=EBI-357997, EBI-352682;
O15355:PPM1G; NbExp=3; IntAct=EBI-357997, EBI-725702;
P78527:PRKDC; NbExp=7; IntAct=EBI-357997, EBI-352053;
P12956:XRCC6; NbExp=15; IntAct=EBI-357997, EBI-353208;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22442688}.
Nucleus, nucleolus {ECO:0000269|PubMed:22002106}. Chromosome
{ECO:0000269|PubMed:22442688}.
-!- DEVELOPMENTAL STAGE: Expression increases during promyelocyte
differentiation. {ECO:0000269|PubMed:8605992}.
-!- INDUCTION: In osteoblasts, by FGF2.
-!- DOMAIN: The EEXXXDDL motif is required for the interaction with
catalytic subunit PRKDC and its recruitment to sites of DNA
damage. {ECO:0000269|PubMed:15758953}.
-!- PTM: Phosphorylated on serine residues. Phosphorylation by PRKDC
may enhance helicase activity. {ECO:0000269|PubMed:10026262}.
-!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
-!- PTM: Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination
following DNA damage, leading to its degradation and removal from
DNA damage sites (PubMed:22266820). Ubiquitinated by RNF138,
leading to remove the Ku complex from DNA breaks
(PubMed:26502055). {ECO:0000269|PubMed:22266820,
ECO:0000269|PubMed:26502055}.
-!- MISCELLANEOUS: Individuals with systemic lupus erythematosus (SLE)
and related disorders produce extremely large amounts of
autoantibodies to XRCC6 and XRCC5. {ECO:0000269|PubMed:7957065}.
-!- SIMILARITY: Belongs to the ku80 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS SNPs;
URL="http://egp.gs.washington.edu/data/xrcc5/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/XRCC5ID337ch2q35.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J04977; AAA59475.1; -; mRNA.
EMBL; M30938; AAA36154.1; -; mRNA.
EMBL; AK290740; BAF83429.1; -; mRNA.
EMBL; AK222603; BAD96323.1; -; mRNA.
EMBL; DQ787434; ABG46942.1; -; Genomic_DNA.
EMBL; CH471063; EAW70562.1; -; Genomic_DNA.
EMBL; BC019027; AAH19027.1; -; mRNA.
EMBL; BC095442; AAH95442.1; -; mRNA.
EMBL; X57500; CAA40736.1; -; mRNA.
CCDS; CCDS2402.1; -.
PIR; A35051; A32626.
PIR; D42397; D42397.
PIR; S62889; S62889.
RefSeq; NP_066964.1; NM_021141.3.
UniGene; Hs.388739; -.
PDB; 1JEQ; X-ray; 2.70 A; B=1-565.
PDB; 1JEY; X-ray; 2.50 A; B=1-565.
PDB; 1Q2Z; NMR; -; A=590-709.
PDB; 1RW2; NMR; -; A=566-710.
PDB; 3RZ9; X-ray; 2.29 A; B=559-571.
PDBsum; 1JEQ; -.
PDBsum; 1JEY; -.
PDBsum; 1Q2Z; -.
PDBsum; 1RW2; -.
PDBsum; 3RZ9; -.
ProteinModelPortal; P13010; -.
SMR; P13010; -.
BioGrid; 113353; 229.
CORUM; P13010; -.
DIP; DIP-31379N; -.
ELM; P13010; -.
IntAct; P13010; 99.
MINT; MINT-131739; -.
STRING; 9606.ENSP00000375977; -.
iPTMnet; P13010; -.
PhosphoSitePlus; P13010; -.
SwissPalm; P13010; -.
BioMuta; XRCC5; -.
DMDM; 125731; -.
SWISS-2DPAGE; P13010; -.
EPD; P13010; -.
MaxQB; P13010; -.
PaxDb; P13010; -.
PeptideAtlas; P13010; -.
PRIDE; P13010; -.
DNASU; 7520; -.
Ensembl; ENST00000392132; ENSP00000375977; ENSG00000079246.
Ensembl; ENST00000392133; ENSP00000375978; ENSG00000079246.
GeneID; 7520; -.
KEGG; hsa:7520; -.
UCSC; uc002vfy.4; human.
CTD; 7520; -.
DisGeNET; 7520; -.
EuPathDB; HostDB:ENSG00000079246.15; -.
GeneCards; XRCC5; -.
HGNC; HGNC:12833; XRCC5.
HPA; CAB004468; -.
HPA; HPA025813; -.
HPA; HPA064685; -.
MIM; 194364; gene.
neXtProt; NX_P13010; -.
OpenTargets; ENSG00000079246; -.
PharmGKB; PA37425; -.
eggNOG; KOG2326; Eukaryota.
eggNOG; ENOG410YKH9; LUCA.
GeneTree; ENSGT00390000015674; -.
HOVERGEN; HBG006237; -.
InParanoid; P13010; -.
KO; K10885; -.
OMA; DIVPFSK; -.
OrthoDB; EOG091G11VD; -.
PhylomeDB; P13010; -.
TreeFam; TF101205; -.
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; P13010; -.
ChiTaRS; XRCC5; human.
EvolutionaryTrace; P13010; -.
GeneWiki; Ku80; -.
GenomeRNAi; 7520; -.
PMAP-CutDB; P13010; -.
PRO; PR:P13010; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000079246; -.
CleanEx; HS_XRCC5; -.
ExpressionAtlas; P13010; baseline and differential.
Genevisible; P13010; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
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; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc.
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:0008047; F:enzyme activator activity; TAS:BHF-UCL.
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; IDA:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0071475; P:cellular hyperosmotic salinity response; IEA:Ensembl.
GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
GO; GO:0071480; P:cellular response to gamma radiation; IDA:UniProtKB.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0071481; P:cellular response to X-ray; IEA:Ensembl.
GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
GO; GO:0006302; P:double-strand break repair; IMP:BHF-UCL.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
GO; GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome.
GO; GO:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl.
GO; GO:1904430; P:negative regulation of t-circle formation; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0043085; P:positive regulation of catalytic activity; TAS:BHF-UCL.
GO; GO:0050769; P:positive regulation of neurogenesis; IEA:Ensembl.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:CAFA.
GO; GO:0051973; P:positive regulation of telomerase activity; TAS:BHF-UCL.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
GO; GO:0070198; P:protein localization to chromosome, telomeric region; TAS:BHF-UCL.
GO; GO:0048660; P:regulation of smooth muscle cell proliferation; IMP:UniProtKB.
GO; GO:0032204; P:regulation of telomere maintenance; TAS:BHF-UCL.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.40.290.10; -; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
InterPro; IPR024193; Ku80.
InterPro; IPR005160; Ku_C.
InterPro; IPR005161; Ku_N.
InterPro; IPR014893; Ku_PK_bind.
InterPro; IPR016194; SPOC-like_C_dom.
InterPro; IPR002035; VWF_A.
PANTHER; PTHR12604:SF7; PTHR12604:SF7; 1.
Pfam; PF02735; Ku; 1.
Pfam; PF03730; Ku_C; 1.
Pfam; PF03731; Ku_N; 1.
Pfam; PF08785; Ku_PK_bind; 1.
PIRSF; PIRSF016570; Ku80; 1.
SMART; SM00559; Ku78; 1.
SMART; SM00327; VWA; 1.
SUPFAM; SSF100939; SSF100939; 1.
SUPFAM; SSF101420; SSF101420; 1.
SUPFAM; SSF53300; SSF53300; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; ATP-binding; Chromosome;
Complete proteome; Direct protein sequencing; DNA damage;
DNA recombination; DNA repair; DNA-binding; Helicase; Hydrolase;
Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Systemic lupus erythematosus;
Transcription; Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7957065,
ECO:0000269|PubMed:8605992}.
CHAIN 2 732 X-ray repair cross-complementing protein
5.
/FTId=PRO_0000084340.
DOMAIN 251 460 Ku.
REGION 138 165 Leucine-zipper.
MOTIF 720 728 EEXXXDL motif.
COMPBIAS 478 519 Pro-rich.
MOD_RES 144 144 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 265 265 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 332 332 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 535 535 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 577 577 Phosphoserine; by PRKDC.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:10026262}.
MOD_RES 579 579 Phosphoserine; by PRKDC.
{ECO:0000305|PubMed:10026262}.
MOD_RES 580 580 Phosphoserine; by PRKDC.
{ECO:0000269|PubMed:10026262}.
MOD_RES 660 660 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 665 665 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 715 715 Phosphothreonine; by PRKDC.
{ECO:0000305|PubMed:10026262}.
CROSSLNK 195 195 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 532 532 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 534 534 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 566 566 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 568 568 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:28112733}.
CROSSLNK 669 669 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 688 688 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 463 463 L -> F (in dbSNP:rs1805380).
/FTId=VAR_014724.
VARIANT 508 508 I -> V (in dbSNP:rs2287558).
/FTId=VAR_053784.
MUTAGEN 720 721 EE->AA: Abolishes interaction with PRKDC
and its recruitment to sites of DNA
damage. {ECO:0000269|PubMed:15758953}.
MUTAGEN 726 727 DD->AA: Abolishes interaction with PRKDC
and its recruitment to sites of DNA
damage. {ECO:0000269|PubMed:15758953}.
CONFLICT 14 16 MDV -> YSY (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 117 117 V -> A (in Ref. 3; BAF83429).
{ECO:0000305}.
CONFLICT 134 134 I -> V (in Ref. 4; BAD96323).
{ECO:0000305}.
CONFLICT 178 178 R -> S (in Ref. 4; BAD96323).
{ECO:0000305}.
CONFLICT 315 315 R -> L (in Ref. 11; CAA40736).
{ECO:0000305}.
CONFLICT 461 461 M -> R (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 479 479 T -> G (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 540 540 I -> T (in Ref. 3; BAF83429).
{ECO:0000305}.
STRAND 8 15 {ECO:0000244|PDB:1JEY}.
HELIX 18 21 {ECO:0000244|PDB:1JEY}.
HELIX 30 47 {ECO:0000244|PDB:1JEY}.
STRAND 53 60 {ECO:0000244|PDB:1JEY}.
TURN 70 72 {ECO:0000244|PDB:1JEY}.
STRAND 77 84 {ECO:0000244|PDB:1JEY}.
HELIX 88 95 {ECO:0000244|PDB:1JEY}.
HELIX 107 121 {ECO:0000244|PDB:1JEY}.
STRAND 122 125 {ECO:0000244|PDB:1JEY}.
STRAND 128 135 {ECO:0000244|PDB:1JEY}.
HELIX 144 146 {ECO:0000244|PDB:1JEQ}.
HELIX 147 156 {ECO:0000244|PDB:1JEY}.
STRAND 159 167 {ECO:0000244|PDB:1JEY}.
TURN 194 196 {ECO:0000244|PDB:1JEY}.
HELIX 199 216 {ECO:0000244|PDB:1JEY}.
HELIX 218 223 {ECO:0000244|PDB:1JEY}.
STRAND 224 226 {ECO:0000244|PDB:1JEY}.
HELIX 227 230 {ECO:0000244|PDB:1JEY}.
TURN 235 237 {ECO:0000244|PDB:1JEY}.
HELIX 238 240 {ECO:0000244|PDB:1JEY}.
STRAND 247 253 {ECO:0000244|PDB:1JEY}.
TURN 254 256 {ECO:0000244|PDB:1JEY}.
STRAND 257 267 {ECO:0000244|PDB:1JEY}.
STRAND 277 280 {ECO:0000244|PDB:1JEY}.
TURN 281 283 {ECO:0000244|PDB:1JEY}.
STRAND 289 301 {ECO:0000244|PDB:1JEY}.
HELIX 307 309 {ECO:0000244|PDB:1JEY}.
STRAND 310 316 {ECO:0000244|PDB:1JEY}.
STRAND 319 322 {ECO:0000244|PDB:1JEY}.
HELIX 325 331 {ECO:0000244|PDB:1JEY}.
STRAND 338 347 {ECO:0000244|PDB:1JEY}.
HELIX 348 350 {ECO:0000244|PDB:1JEY}.
HELIX 353 355 {ECO:0000244|PDB:1JEY}.
STRAND 357 366 {ECO:0000244|PDB:1JEY}.
HELIX 371 386 {ECO:0000244|PDB:1JEY}.
STRAND 389 401 {ECO:0000244|PDB:1JEY}.
STRAND 404 412 {ECO:0000244|PDB:1JEY}.
STRAND 417 423 {ECO:0000244|PDB:1JEY}.
HELIX 427 429 {ECO:0000244|PDB:1JEY}.
STRAND 438 440 {ECO:0000244|PDB:1JEQ}.
STRAND 442 444 {ECO:0000244|PDB:1JEY}.
HELIX 448 460 {ECO:0000244|PDB:1JEY}.
STRAND 464 467 {ECO:0000244|PDB:1JEQ}.
TURN 468 471 {ECO:0000244|PDB:1JEQ}.
STRAND 474 476 {ECO:0000244|PDB:1JEY}.
HELIX 479 481 {ECO:0000244|PDB:1JEY}.
HELIX 485 499 {ECO:0000244|PDB:1JEY}.
STRAND 501 503 {ECO:0000244|PDB:1JEQ}.
HELIX 510 516 {ECO:0000244|PDB:1JEY}.
HELIX 520 536 {ECO:0000244|PDB:1JEY}.
STRAND 581 586 {ECO:0000244|PDB:1RW2}.
STRAND 588 592 {ECO:0000244|PDB:1RW2}.
HELIX 594 601 {ECO:0000244|PDB:1Q2Z}.
STRAND 603 605 {ECO:0000244|PDB:1Q2Z}.
TURN 608 610 {ECO:0000244|PDB:1Q2Z}.
HELIX 611 626 {ECO:0000244|PDB:1Q2Z}.
HELIX 629 649 {ECO:0000244|PDB:1Q2Z}.
HELIX 652 667 {ECO:0000244|PDB:1Q2Z}.
HELIX 673 680 {ECO:0000244|PDB:1Q2Z}.
STRAND 691 693 {ECO:0000244|PDB:1Q2Z}.
HELIX 698 701 {ECO:0000244|PDB:1Q2Z}.
TURN 702 704 {ECO:0000244|PDB:1Q2Z}.
SEQUENCE 732 AA; 82705 MW; 2363CA84834E74A3 CRC64;
MVRSGNKAAV VLCMDVGFTM SNSIPGIESP FEQAKKVITM FVQRQVFAEN KDEIALVLFG
TDGTDNPLSG GDQYQNITVH RHLMLPDFDL LEDIESKIQP GSQQADFLDA LIVSMDVIQH
ETIGKKFEKR HIEIFTDLSS RFSKSQLDII IHSLKKCDIS LQFFLPFSLG KEDGSGDRGD
GPFRLGGHGP SFPLKGITEQ QKEGLEIVKM VMISLEGEDG LDEIYSFSES LRKLCVFKKI
ERHSIHWPCR LTIGSNLSIR IAAYKSILQE RVKKTWTVVD AKTLKKEDIQ KETVYCLNDD
DETEVLKEDI IQGFRYGSDI VPFSKVDEEQ MKYKSEGKCF SVLGFCKSSQ VQRRFFMGNQ
VLKVFAARDD EAAAVALSSL IHALDDLDMV AIVRYAYDKR ANPQVGVAFP HIKHNYECLV
YVQLPFMEDL RQYMFSSLKN SKKYAPTEAQ LNAVDALIDS MSLAKKDEKT DTLEDLFPTT
KIPNPRFQRL FQCLLHRALH PREPLPPIQQ HIWNMLNPPA EVTTKSQIPL SKIKTLFPLI
EAKKKDQVTA QEIFQDNHED GPTAKKLKTE QGGAHFSVSS LAEGSVTSVG SVNPAENFRV
LVKQKKASFE EASNQLINHI EQFLDTNETP YFMKSIDCIR AFREEAIKFS EEQRFNNFLK
ALQEKVEIKQ LNHFWEIVVQ DGITLITKEE ASGSSVTAEE AKKFLAPKDK PSGDTAAVFE
EGGDVDDLLD MI


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18-003-42479 ATP-dependent DNA helicase 2 subunit 1 - EC 3.6.1.-; ATP-dependent DNA helicase II 70 kDa subunit; Lupus Ku autoantigen protein p70; Ku70; 70 kDa subunit of Ku antigen; Thyroid-lupus autoantigen; TLAA 0.1 mg Protein A
60300 IgG,X_ray repair complementing defective repair in Chinese hamster cells 5 (double_strand_break rejoining; Ku autoantigen, 80kDa) (X 0.1 mg
CSB-PA026233GA01HU Rabbit anti-human X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA026233GA01HU Rabbit anti-human X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
GWB-208DC7 X-ray repair complementing defective repair in Chinese hamster cells 6 (Ku autoantigen 70kDa), Antibody
60301 IgG,X_ray repair complementing defective repair in Chinese hamster cells 6 (Ku autoantigen, 70kDa) 0.1 mg
EIAAB13174 Bos taurus,Bovine,CXPD,DNA excision repair protein ERCC-2,DNA repair protein complementing XP-D cells,ERCC2,TFIIH basal transcription factor complex helicase XPD subunit,Xeroderma pigmentosum group D-
EIAAB13176 CXPD,DNA excision repair protein ERCC-2,DNA repair protein complementing XP-D cells,Ercc2,Mouse,Mus musculus,TFIIH basal transcription factor complex helicase XPD subunit,Xeroderma pigmentosum group D
EIAAB13178 Basic transcription factor 2 89 kDa subunit,BTF2 p89,DNA excision repair protein ERCC-3,DNA repair protein complementing XP-B cells,Ercc3,Mouse,Mus musculus,TFIIH 89 kDa subunit,TFIIH basal transcript
EIAAB13181 Basic transcription factor 2 89 kDa subunit,BTF2 p89,DNA excision repair protein ERCC-3,DNA repair protein complementing XP-B cells,ERCC3,Homo sapiens,Human,TFIIH 89 kDa subunit,TFIIH basal transcript
EIAAB13175 Basic transcription factor 2 80 kDa subunit,BTF2 p80,CXPD,DNA excision repair protein ERCC-2,DNA repair protein complementing XP-D cells,ERCC2,Homo sapiens,Human,TFIIH 80 kDa subunit,TFIIH basal trans


 

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