ID XRCC5_HUMAN Reviewed; 732 AA.
AC P13010; A8K3X5; Q0Z7V0; Q4VBQ5; Q53HH7; Q7M4N0; Q9UCQ0; Q9UCQ1;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 249.
DE RecName: Full=X-ray repair cross-complementing protein 5;
DE EC=3.6.4.-;
DE AltName: Full=86 kDa subunit of Ku antigen;
DE AltName: Full=ATP-dependent DNA helicase 2 subunit 2;
DE AltName: Full=ATP-dependent DNA helicase II 80 kDa subunit;
DE AltName: Full=CTC box-binding factor 85 kDa subunit;
DE Short=CTC85;
DE Short=CTCBF;
DE AltName: Full=DNA repair protein XRCC5;
DE AltName: Full=Ku80;
DE AltName: Full=Ku86;
DE AltName: Full=Lupus Ku autoantigen protein p86;
DE AltName: Full=Nuclear factor IV;
DE AltName: Full=Thyroid-lupus autoantigen;
DE Short=TLAA;
DE AltName: Full=X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining);
GN Name=XRCC5; Synonyms=G22P2;
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], AND PROTEIN SEQUENCE OF 4-22.
RX PubMed=2760028; DOI=10.1016/s0021-9258(18)80011-4;
RA Yaneva M., Wen J., Ayala A., Cook R.;
RT "cDNA-derived amino acid sequence of the 86-kDa subunit of the Ku
RT antigen.";
RL J. Biol. Chem. 264:13407-13411(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2308937; DOI=10.1073/pnas.87.5.1777;
RA Mimori T., Ohosone Y., Hama N., Suwa A., Akizuki M., Homma M.,
RA Griffith A.J., Hardin J.A.;
RT "Isolation and characterization of cDNA encoding the 80-kDa subunit protein
RT of the human autoantigen Ku (p70/p80) recognized by autoantibodies from
RT patients with scleroderma-polymyositis overlap syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1777-1781(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neuroblastoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Coronary artery;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thyroid, and Uterus;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-22.
RX PubMed=2211668; DOI=10.1016/s0021-9258(18)38250-4;
RA Knuth M.W., Gunderson S.I., Thompson N.E., Strasheim L.A., Burgess R.R.;
RT "Purification and characterization of proximal sequence element-binding
RT protein 1, a transcription activating protein related to Ku and TREF that
RT binds the proximal sequence element of the human U1 promoter.";
RL J. Biol. Chem. 265:17911-17920(1990).
RN [9]
RP PROTEIN SEQUENCE OF 2-20, FUNCTION, AND INVOLVEMENT IN LUPUS ERYTHEMATOSUS.
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 [10]
RP PROTEIN SEQUENCE OF 2-16; 98-113; 443-461 AND 473-479, AND DEVELOPMENTAL
RP 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 [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 105-732, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2212941; DOI=10.1084/jem.172.4.1049;
RA Stuiver M.H., Coenjaerts F.E.J., van der Vlied P.C.;
RT "The autoantigen Ku is indistinguishable from NF IV, a protein forming
RT multimeric protein-DNA complexes.";
RL J. Exp. Med. 172:1049-1054(1990).
RN [12]
RP PROTEIN SEQUENCE OF 186-193; 317-326; 545-559 AND 656-661.
RX PubMed=8031790; DOI=10.1021/bi00194a021;
RA Cao Q.P., Pitt S., Leszyk J., Baril E.F.;
RT "DNA-dependent ATPase from HeLa cells is related to human Ku autoantigen.";
RL Biochemistry 33:8548-8557(1994).
RN [13]
RP PROTEIN SEQUENCE OF 526-531; 535-542 AND 704-708, FUNCTION, AND INTERACTION
RP WITH 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 [14]
RP PROTEIN SEQUENCE OF 526-565 AND 709-732.
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 [15]
RP PROTEIN SEQUENCE OF 534-542.
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 [16]
RP PHOSPHORYLATION AT SER-577; SER-579; SER-580 AND THR-715.
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH NAA15;
RP MSX2 AND RUNX2.
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 [18]
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 [19]
RP INTERACTION WITH DHX9.
RX PubMed=14704337; DOI=10.1093/nar/gkg933;
RA Zhang S., Schlott B., Goerlach M., Grosse F.;
RT "DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA helicase
RT II/RNA helicase A and hnRNP proteins in an RNA-dependent manner.";
RL Nucleic Acids Res. 32:1-10(2004).
RN [20]
RP SUMOYLATION.
RX PubMed=15561718; DOI=10.1074/jbc.m411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-like
RT modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [21]
RP DOMAIN, AND MUTAGENESIS OF 720-GLU-GLU-721 AND 726-ASP-ASP-727.
RX PubMed=15758953; DOI=10.1038/nature03442;
RA Falck J., Coates J., Jackson S.P.;
RT "Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA
RT damage.";
RL Nature 434:605-611(2005).
RN [22]
RP INTERACTION WITH APLF.
RX PubMed=17396150; DOI=10.1038/sj.emboj.7601663;
RA Kanno S., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S., Yasui A.;
RT "A novel human AP endonuclease with conserved zinc-finger-like motifs
RT involved in DNA strand break responses.";
RL EMBO J. 26:2094-2103(2007).
RN [23]
RP INTERACTION WITH APLF.
RX PubMed=17353262; DOI=10.1128/mcb.02269-06;
RA Iles N., Rulten S., El-Khamisy S.F., Caldecott K.W.;
RT "APLF (C2orf13) is a novel human protein involved in the cellular response
RT to chromosomal DNA strand breaks.";
RL Mol. Cell. Biol. 27:3793-3803(2007).
RN [24]
RP IDENTIFICATION BY 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 [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-144; LYS-265; LYS-332; LYS-660
RP AND LYS-665, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [26]
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 [27]
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 [28]
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 [29]
RP FUNCTION.
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 [30]
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 [31]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=22002106; DOI=10.1074/mcp.m111.013680;
RA Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
RT "Systematic analysis of protein pools, isoforms, and modifications
RT affecting turnover and subcellular localization.";
RL Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
RN [32]
RP DNA-BINDING, IDENTIFICATION IN A COMPLEX WITH XRCC6 AND DEAF1, SUBCELLULAR
RP 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 [33]
RP UBIQUITINATION BY RNF8.
RX PubMed=22266820; DOI=10.1038/nsmb.2211;
RA Feng L., Chen J.;
RT "The E3 ligase RNF8 regulates KU80 removal and NHEJ repair.";
RL Nat. Struct. Mol. Biol. 19:201-206(2012).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255; SER-258; SER-318 AND
RP THR-535, AND IDENTIFICATION BY MASS SPECTROMETRY [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 [35]
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 [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-577, AND IDENTIFICATION BY
RP 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 [37]
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 [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-568, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [39]
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 [40]
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 [41]
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 [42]
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 [43]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [44]
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 [45]
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 [46]
RP UBIQUITINATION, AND INTERACTION WITH RNF138.
RX PubMed=26502055; DOI=10.1038/ncb3259;
RA Ismail I.H., Gagne J.P., Genois M.M., Strickfaden H., McDonald D., Xu Z.,
RA Poirier G.G., Masson J.Y., Hendzel M.J.;
RT "The RNF138 E3 ligase displaces Ku to promote DNA end resection and
RT regulate DNA repair pathway choice.";
RL Nat. Cell Biol. 17:1446-1457(2015).
RN [47]
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 [48]
RP FUNCTION, AND INTERACTION WITH PRKDC; HEXIM1; XRCC6; SFPQ; NONO; PSPC1;
RP 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 [49]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-195; LYS-532; LYS-534; LYS-566;
RP LYS-568; LYS-669 AND LYS-688, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [50]
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 [51]
RP INTERACTION WITH HUMAN T-CELL LEUKEMIA VIRUS 1/HTLV-1 PROTEIN HBZ
RP (MICROBIAL INFECTION).
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 [52]
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 [53]
RP INTERACTION WITH APLF.
RX PubMed=31733588; DOI=10.1016/j.dnarep.2019.102739;
RA Kim K., Min J., Kirby T.W., Gabel S.A., Pedersen L.C., London R.E.;
RT "Ligand binding characteristics of the Ku80 von Willebrand domain.";
RL DNA Repair 85:102739-102739(2020).
RN [54]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=32103174; DOI=10.1038/s41586-020-2041-2;
RA Shao Z., Flynn R.A., Crowe J.L., Zhu Y., Liang J., Jiang W., Aryan F.,
RA Aoude P., Bertozzi C.R., Estes V.M., Lee B.J., Bhagat G., Zha S., Calo E.;
RT "DNA-PKcs has KU-dependent function in rRNA processing and
RT haematopoiesis.";
RL Nature 579:291-296(2020).
RN [55]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-565 IN COMPLEX WITH XRCC6, 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 [56] {ECO:0007744|PDB:7NFC, ECO:0007744|PDB:7NFE}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.14 ANGSTROMS) IN COMPLEX WITH THE NHEJ
RP COMPLEX AND DNA, AND IDENTIFICATION IN THE NHEJ COMPLEX.
RX PubMed=34352203; DOI=10.1016/j.molcel.2021.07.005;
RA Chaplin A.K., Hardwick S.W., Stavridi A.K., Buehl C.J., Goff N.J.,
RA Ropars V., Liang S., De Oliveira T.M., Chirgadze D.Y., Meek K.,
RA Charbonnier J.B., Blundell T.L.;
RT "Cryo-EM of NHEJ supercomplexes provides insights into DNA repair.";
RL Mol. Cell 81:3400-3409(2021).
RN [57] {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). Required for double-strand break repair and V(D)J
CC recombination (PubMed:7957065, PubMed:8621488, PubMed:12145306,
CC PubMed:11493912). Also has a role in chromosome translocation
CC (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912). The
CC DNA helicase II complex binds preferentially to fork-like ends of
CC double-stranded DNA in a cell cycle-dependent manner (PubMed:7957065,
CC PubMed:8621488, PubMed:12145306, PubMed:11493912). It works in the 3'-
CC 5' direction (PubMed:7957065, PubMed:8621488, PubMed:12145306,
CC PubMed:11493912). During NHEJ, the XRCC5-XRRC6 dimer performs the
CC recognition step: it recognizes and binds to the broken ends of the DNA
CC and protects them from further resection (PubMed:7957065,
CC PubMed:8621488, PubMed:12145306, PubMed:11493912). Binding to DNA may
CC be mediated by XRCC6 (PubMed:7957065, PubMed:8621488, PubMed:12145306,
CC PubMed:11493912). The XRCC5-XRRC6 dimer acts as a regulatory subunit of
CC the DNA-dependent protein kinase complex DNA-PK by increasing the
CC affinity of the catalytic subunit PRKDC to DNA by 100-fold
CC (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:20383123,
CC PubMed:11493912). The XRCC5-XRRC6 dimer is probably involved in
CC stabilizing broken DNA ends and bringing them together (PubMed:7957065,
CC PubMed:8621488, PubMed:12145306, PubMed:20383123). 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:20383123). The
CC XRCC5-XRRC6 dimer probably also acts as a 5'-deoxyribose-5-phosphate
CC lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5'
CC deoxyribose-5-phosphate at an abasic site near double-strand breaks
CC (PubMed:20383123). XRCC5 probably acts as the catalytic subunit of 5'-
CC dRP activity, and allows to 'clean' the termini of abasic sites, a
CC class of nucleotide damage commonly associated with strand breaks,
CC before such broken ends can be joined (PubMed:20383123). The XRCC5-
CC XRRC6 dimer together with APEX1 acts as a negative regulator of
CC transcription (PubMed:8621488). In association with NAA15, the XRCC5-
CC XRRC6 dimer binds to the osteocalcin promoter and activates osteocalcin
CC expression (PubMed:12145306). As part of the DNA-PK complex, involved
CC in the early steps of ribosome assembly by promoting the processing of
CC precursor rRNA into mature 18S rRNA in the small-subunit processome
CC (PubMed:32103174). Binding to U3 small nucleolar RNA, recruits PRKDC
CC and XRCC5/Ku86 to the small-subunit processome (PubMed:32103174). Plays
CC a role in the regulation of DNA virus-mediated innate immune response
CC by assembling into the HDP-RNP complex, a complex that serves as a
CC platform for IRF3 phosphorylation and subsequent innate immune response
CC activation through the cGAS-STING pathway (PubMed:28712728).
CC {ECO:0000269|PubMed:11493912, ECO:0000269|PubMed:12145306,
CC ECO:0000269|PubMed:20383123, ECO:0000269|PubMed:28712728,
CC ECO:0000269|PubMed:32103174, ECO:0000269|PubMed:7957065,
CC ECO:0000269|PubMed:8621488}.
CC -!- SUBUNIT: Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70
CC (PubMed:25941166, PubMed:25670504, PubMed:11493912, PubMed:22442688).
CC Component of the core long-range non-homologous end joining (NHEJ)
CC complex (also named DNA-PK complex) composed of PRKDC, LIG4, XRCC4,
CC XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF (PubMed:25941166, PubMed:25670504,
CC PubMed:11493912, PubMed:22442688, PubMed:33854234, PubMed:34352203).
CC Additional component of the NHEJ complex includes PAXX
CC (PubMed:25574025, PubMed:25941166, PubMed:25670504, PubMed:27601299).
CC Following autophosphorylation, PRKDC dissociates from DNA, leading to
CC formation of the short-range NHEJ complex, composed of LIG4, XRCC4,
CC XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF (PubMed:33854234). The XRCC5-XRCC6
CC dimer also associates with NAA15, and this complex displays DNA binding
CC activity towards the osteocalcin FGF response element (OCFRE)
CC (PubMed:12145306). In addition, XRCC5 binds to the osteoblast-specific
CC transcription factors MSX2 and RUNX2 (PubMed:12145306). Interacts with
CC ELF3 (PubMed:15075319). Interacts with APLF (via KBM motif)
CC (PubMed:17353262, PubMed:17396150, PubMed:23689425, PubMed:27063109,
CC PubMed:31733588). The XRCC5/XRCC6 dimer associates in a DNA-dependent
CC manner with APEX1 (PubMed:8621488). Identified in a complex with DEAF1
CC and XRCC6. 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 RNF138 (PubMed:26502055). Interacts with CYREN isoform 1 (CYREN-1) and
CC isoform 4 (CYREN-2) (via KBM motif) (PubMed:27063109, PubMed:24610814,
CC PubMed:28959974). Interacts with WRN (via KBM motif) (PubMed:27063109).
CC Interacts (via N-terminus) with HSF1 (via N-terminus); this interaction
CC is direct and prevents XRCC5/XRCC6 heterodimeric binding and non-
CC homologous end joining (NHEJ) repair activities induced by ionizing
CC radiation (IR) (PubMed:26359349). Interacts with DHX9; this interaction
CC occurs in a RNA-dependent manner (PubMed:14704337). Part of the HDP-RNP
CC complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle
CC proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA
CC (PubMed:28712728). Interacts with ERCC6 (PubMed:26030138). The XRCC5-
CC XRCC6 dimer associates with ALKBH2. {ECO:0000269|PubMed:11493912,
CC ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:14704337,
CC ECO:0000269|PubMed:15075319, ECO:0000269|PubMed:17353262,
CC ECO:0000269|PubMed:17396150, ECO:0000269|PubMed:22442688,
CC ECO:0000269|PubMed:23689425, ECO:0000269|PubMed:23972994,
CC ECO:0000269|PubMed:24610814, ECO:0000269|PubMed:25574025,
CC ECO:0000269|PubMed:25670504, ECO:0000269|PubMed:25852083,
CC ECO:0000269|PubMed:25941166, ECO:0000269|PubMed:26030138,
CC ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:26502055,
CC ECO:0000269|PubMed:27063109, ECO:0000269|PubMed:27601299,
CC ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:28959974,
CC ECO:0000269|PubMed:29490055, ECO:0000269|PubMed:31733588,
CC ECO:0000269|PubMed:34352203, ECO:0000269|PubMed:8621488}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human T-cell leukemia
CC virus 1/HTLV-1 protein HBZ. {ECO:0000269|PubMed:29769340}.
CC -!- INTERACTION:
CC P13010; Q8IW19: APLF; NbExp=14; IntAct=EBI-357997, EBI-1256044;
CC P13010; P38432: COIL; NbExp=6; IntAct=EBI-357997, EBI-945751;
CC P13010; Q96EV8-1: DTNBP1; NbExp=2; IntAct=EBI-357997, EBI-16749108;
CC P13010; Q9H4A6: GOLPH3; NbExp=2; IntAct=EBI-357997, EBI-2465479;
CC P13010; P09629: HOXB7; NbExp=9; IntAct=EBI-357997, EBI-1248457;
CC P13010; P04792: HSPB1; NbExp=2; IntAct=EBI-357997, EBI-352682;
CC P13010; Q9BUH6: PAXX; NbExp=2; IntAct=EBI-357997, EBI-2839993;
CC P13010; Q9BUH6-1: PAXX; NbExp=5; IntAct=EBI-357997, EBI-16137878;
CC P13010; O15355: PPM1G; NbExp=3; IntAct=EBI-357997, EBI-725702;
CC P13010; P78527: PRKDC; NbExp=8; IntAct=EBI-357997, EBI-352053;
CC P13010; P13693: TPT1; NbExp=4; IntAct=EBI-357997, EBI-1783169;
CC P13010; P12956: XRCC6; NbExp=20; IntAct=EBI-357997, EBI-353208;
CC P13010; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-357997, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22442688,
CC ECO:0000269|PubMed:32103174}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:22002106, ECO:0000269|PubMed:32103174}. Chromosome
CC {ECO:0000269|PubMed:22442688}.
CC -!- DEVELOPMENTAL STAGE: Expression increases during promyelocyte
CC differentiation. {ECO:0000269|PubMed:8605992}.
CC -!- INDUCTION: In osteoblasts, by FGF2.
CC -!- DOMAIN: The EEXXXDDL motif is required for the interaction with
CC catalytic subunit PRKDC and its recruitment to sites of DNA damage.
CC {ECO:0000269|PubMed:15758953}.
CC -!- DOMAIN: The VWFA domain interacts with the KBM (Ku-binding motif) found
CC in a number of DNA repair proteins. {ECO:0000250|UniProtKB:Q6DDS9}.
CC -!- DOMAIN: The N-terminal and C-terminal regions are not required for
CC binding to DNA or for degradation of the protein with only the central
CC region being required for these processes.
CC {ECO:0000250|UniProtKB:Q6DDS9}.
CC -!- PTM: ADP-ribosylated by PARP3. {ECO:0000269|PubMed:24598253}.
CC -!- PTM: Phosphorylated on serine residues. Phosphorylation by PRKDC may
CC enhance helicase activity. {ECO:0000269|PubMed:10026262}.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
CC -!- PTM: Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination following
CC DNA damage, leading to its degradation and removal from DNA damage
CC sites (PubMed:22266820). Ubiquitinated by RNF138, leading to remove the
CC Ku complex from DNA breaks (PubMed:26502055).
CC {ECO:0000269|PubMed:22266820, ECO:0000269|PubMed:26502055}.
CC -!- MISCELLANEOUS: Individuals with systemic lupus erythematosus (SLE) and
CC related disorders produce extremely large amounts of autoantibodies to
CC XRCC6 and XRCC5. {ECO:0000269|PubMed:7957065}.
CC -!- SIMILARITY: Belongs to the ku80 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS SNPs;
CC URL="http://egp.gs.washington.edu/data/xrcc5/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/337/XRCC5";
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DR EMBL; J04977; AAA59475.1; -; mRNA.
DR EMBL; M30938; AAA36154.1; -; mRNA.
DR EMBL; AK290740; BAF83429.1; -; mRNA.
DR EMBL; AK222603; BAD96323.1; -; mRNA.
DR EMBL; DQ787434; ABG46942.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70562.1; -; Genomic_DNA.
DR EMBL; BC019027; AAH19027.1; -; mRNA.
DR EMBL; BC095442; AAH95442.1; -; mRNA.
DR EMBL; X57500; CAA40736.1; -; mRNA.
DR CCDS; CCDS2402.1; -.
DR PIR; A35051; A32626.
DR PIR; D42397; D42397.
DR PIR; S62889; S62889.
DR RefSeq; NP_066964.1; NM_021141.3.
DR PDB; 1JEQ; X-ray; 2.70 A; B=1-565.
DR PDB; 1JEY; X-ray; 2.50 A; B=1-565.
DR PDB; 1Q2Z; NMR; -; A=590-709.
DR PDB; 1RW2; NMR; -; A=566-710.
DR PDB; 3RZ9; X-ray; 2.29 A; B=559-571.
DR PDB; 5Y3R; EM; 6.60 A; B=6-541.
DR PDB; 6ERF; X-ray; 3.01 A; B/D/F/H=2-555.
DR PDB; 6ERG; X-ray; 2.90 A; B/E=2-555.
DR PDB; 6ERH; X-ray; 2.80 A; B/D=2-555.
DR PDB; 6ZH6; EM; 3.93 A; B=541-732.
DR PDB; 6ZHA; EM; 3.91 A; C=1-732.
DR PDB; 6ZHE; EM; 7.24 A; C/H=1-732.
DR PDB; 7AXZ; EM; 3.20 A; B=1-732.
DR PDB; 7K0Y; EM; 3.70 A; C=1-732.
DR PDB; 7K17; X-ray; 4.30 A; C/D=541-732.
DR PDB; 7K1J; EM; 3.90 A; C=1-732.
DR PDB; 7K1K; EM; 4.10 A; C=1-732.
DR PDB; 7K1N; EM; 3.90 A; C=1-732.
DR PDB; 7LSY; EM; 8.40 A; B/K=1-732.
DR PDB; 7LT3; EM; 4.60 A; B/K=1-732.
DR PDB; 7NFC; EM; 4.14 A; C/H=1-732.
DR PDB; 7NFE; EM; 4.29 A; C=1-732.
DR PDB; 7SGL; EM; 3.00 A; C=1-732.
DR PDB; 7SU3; EM; 3.30 A; C=1-732.
DR PDB; 7SUD; EM; 3.60 A; C=1-732.
DR PDB; 7Z6O; X-ray; 3.70 A; B=1-732.
DR PDB; 7Z87; EM; 2.91 A; C=1-732.
DR PDB; 7Z88; EM; 3.33 A; C=1-732.
DR PDB; 7ZT6; EM; 3.50 A; B=1-732.
DR PDB; 7ZVT; EM; 2.74 A; B=1-732.
DR PDB; 7ZWA; EM; 2.80 A; B=1-732.
DR PDB; 7ZYG; EM; 2.68 A; B=1-732.
DR PDB; 8AG4; EM; 2.46 A; B=1-732.
DR PDB; 8AG5; EM; 3.47 A; B=1-732.
DR PDB; 8ASC; X-ray; 2.95 A; B/F/L/P=2-555.
DR PDB; 8BH3; EM; 4.55 A; C/L=1-732.
DR PDB; 8BHV; EM; 4.51 A; b/j=1-732.
DR PDB; 8BHY; EM; 5.33 A; C/L=1-732.
DR PDB; 8BOT; EM; 7.76 A; C/H/U=1-732.
DR PDB; 8EZA; EM; 4.39 A; B/K=1-732.
DR PDB; 8EZB; EM; 8.90 A; B/K=1-732.
DR PDBsum; 1JEQ; -.
DR PDBsum; 1JEY; -.
DR PDBsum; 1Q2Z; -.
DR PDBsum; 1RW2; -.
DR PDBsum; 3RZ9; -.
DR PDBsum; 5Y3R; -.
DR PDBsum; 6ERF; -.
DR PDBsum; 6ERG; -.
DR PDBsum; 6ERH; -.
DR PDBsum; 6ZH6; -.
DR PDBsum; 6ZHA; -.
DR PDBsum; 6ZHE; -.
DR PDBsum; 7AXZ; -.
DR PDBsum; 7K0Y; -.
DR PDBsum; 7K17; -.
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 PDBsum; 7SUD; -.
DR PDBsum; 7Z6O; -.
DR PDBsum; 7Z87; -.
DR PDBsum; 7Z88; -.
DR PDBsum; 7ZT6; -.
DR PDBsum; 7ZVT; -.
DR PDBsum; 7ZWA; -.
DR PDBsum; 7ZYG; -.
DR PDBsum; 8AG4; -.
DR PDBsum; 8AG5; -.
DR PDBsum; 8ASC; -.
DR PDBsum; 8BH3; -.
DR PDBsum; 8BHV; -.
DR PDBsum; 8BHY; -.
DR PDBsum; 8BOT; -.
DR PDBsum; 8EZA; -.
DR PDBsum; 8EZB; -.
DR AlphaFoldDB; P13010; -.
DR BMRB; P13010; -.
DR EMDB; EMD-11215; -.
DR EMDB; EMD-14545; -.
DR EMDB; EMD-14546; -.
DR EMDB; EMD-14955; -.
DR EMDB; EMD-14986; -.
DR EMDB; EMD-14995; -.
DR EMDB; EMD-15022; -.
DR EMDB; EMD-16044; -.
DR EMDB; EMD-16070; -.
DR EMDB; EMD-16074; -.
DR EMDB; EMD-16145; -.
DR EMDB; EMD-23509; -.
DR EMDB; EMD-23511; -.
DR EMDB; EMD-23513; -.
DR EMDB; EMD-23514; -.
DR EMDB; EMD-25114; -.
DR EMDB; EMD-25115; -.
DR EMDB; EMD-25440; -.
DR EMDB; EMD-28732; -.
DR EMDB; EMD-28733; -.
DR EMDB; EMD-28735; -.
DR EMDB; EMD-28738; -.
DR EMDB; EMD-5833; -.
DR SASBDB; P13010; -.
DR SMR; P13010; -.
DR BioGRID; 113353; 487.
DR ComplexPortal; CPX-1993; Ku70:Ku80 complex.
DR CORUM; P13010; -.
DR DIP; DIP-31379N; -.
DR ELM; P13010; -.
DR IntAct; P13010; 158.
DR MINT; P13010; -.
DR STRING; 9606.ENSP00000375978; -.
DR ChEMBL; CHEMBL4106136; -.
DR MoonDB; P13010; Curated.
DR GlyGen; P13010; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P13010; -.
DR MetOSite; P13010; -.
DR PhosphoSitePlus; P13010; -.
DR SwissPalm; P13010; -.
DR BioMuta; XRCC5; -.
DR DMDM; 125731; -.
DR SWISS-2DPAGE; P13010; -.
DR CPTAC; CPTAC-606; -.
DR CPTAC; CPTAC-607; -.
DR EPD; P13010; -.
DR jPOST; P13010; -.
DR MassIVE; P13010; -.
DR MaxQB; P13010; -.
DR PaxDb; 9606-ENSP00000375978; -.
DR PeptideAtlas; P13010; -.
DR ProteomicsDB; 52890; -.
DR Pumba; P13010; -.
DR Antibodypedia; 3849; 1300 antibodies from 47 providers.
DR CPTC; P13010; 1 antibody.
DR DNASU; 7520; -.
DR Ensembl; ENST00000392132.7; ENSP00000375977.2; ENSG00000079246.16.
DR Ensembl; ENST00000392133.7; ENSP00000375978.3; ENSG00000079246.16.
DR GeneID; 7520; -.
DR KEGG; hsa:7520; -.
DR MANE-Select; ENST00000392132.7; ENSP00000375977.2; NM_021141.4; NP_066964.1.
DR UCSC; uc002vfy.4; human.
DR AGR; HGNC:12833; -.
DR CTD; 7520; -.
DR DisGeNET; 7520; -.
DR GeneCards; XRCC5; -.
DR HGNC; HGNC:12833; XRCC5.
DR HPA; ENSG00000079246; Low tissue specificity.
DR MIM; 194364; gene.
DR neXtProt; NX_P13010; -.
DR OpenTargets; ENSG00000079246; -.
DR PharmGKB; PA37425; -.
DR VEuPathDB; HostDB:ENSG00000079246; -.
DR eggNOG; KOG2326; Eukaryota.
DR GeneTree; ENSGT00940000153239; -.
DR HOGENOM; CLU_010975_2_1_1; -.
DR InParanoid; P13010; -.
DR OMA; WAMQYVW; -.
DR OrthoDB; 5884at2759; -.
DR PhylomeDB; P13010; -.
DR TreeFam; TF101205; -.
DR PathwayCommons; P13010; -.
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; P13010; -.
DR SIGNOR; P13010; -.
DR BioGRID-ORCS; 7520; 758 hits in 1171 CRISPR screens.
DR ChiTaRS; XRCC5; human.
DR EvolutionaryTrace; P13010; -.
DR GeneWiki; Ku80; -.
DR GenomeRNAi; 7520; -.
DR Pharos; P13010; Tbio.
DR PRO; PR:P13010; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P13010; Protein.
DR Bgee; ENSG00000079246; Expressed in embryo and 217 other cell types or tissues.
DR ExpressionAtlas; P13010; baseline and differential.
DR Genevisible; P13010; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA: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:0005958; C:DNA-dependent protein kinase-DNA ligase 4 complex; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; 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; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0090734; C:site of DNA damage; IMP:UniProtKB.
DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:FlyBase.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:FlyBase.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0045027; F:DNA end binding; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; TAS:ProtInc.
DR GO; GO:0003690; F:double-stranded DNA binding; TAS:ProtInc.
DR GO; GO:0008047; F:enzyme activator activity; TAS:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0034511; F:U3 snoRNA binding; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
DR GO; GO:0071475; P:cellular hyperosmotic salinity response; IEA:Ensembl.
DR GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
DR GO; GO:0071480; P:cellular response to gamma radiation; IDA:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0071481; P:cellular response to X-ray; IEA:Ensembl.
DR GO; GO:0006974; P:DNA damage response; IMP:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
DR GO; GO:0006302; P:double-strand break repair; IMP:BHF-UCL.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:UniProtKB.
DR GO; GO:1904430; P:negative regulation of t-circle formation; IMP:BHF-UCL.
DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR GO; GO:0043085; P:positive regulation of catalytic activity; TAS:BHF-UCL.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:CAFA.
DR GO; GO:0051973; P:positive regulation of telomerase activity; TAS:BHF-UCL.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; TAS:BHF-UCL.
DR GO; GO:0000725; P:recombinational repair; NAS:ComplexPortal.
DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; IMP:UniProtKB.
DR GO; GO:0032204; P:regulation of telomere maintenance; TAS:BHF-UCL.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0034462; P:small-subunit processome assembly; IDA:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR CDD; cd00873; KU80; 1.
DR CDD; cd01458; vWA_ku; 1.
DR DisProt; DP01255; -.
DR Gene3D; 1.10.1600.10; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 1.25.40.240; Ku, C-terminal domain; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR IDEAL; IID00024; -.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR024193; Ku80.
DR InterPro; IPR005160; Ku_C.
DR InterPro; IPR036494; Ku_C_sf.
DR InterPro; IPR005161; Ku_N.
DR InterPro; IPR014893; Ku_PK_bind.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR12604; KU AUTOANTIGEN DNA HELICASE; 1.
DR PANTHER; PTHR12604:SF4; X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 5; 1.
DR Pfam; PF02735; Ku; 1.
DR Pfam; PF03730; Ku_C; 1.
DR Pfam; PF03731; Ku_N; 1.
DR Pfam; PF08785; Ku_PK_bind; 1.
DR PIRSF; PIRSF016570; Ku80; 1.
DR SMART; SM00559; Ku78; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF101420; C-terminal domain of Ku80; 1.
DR SUPFAM; SSF100939; SPOC domain-like; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; ADP-ribosylation; ATP-binding;
KW Chromosome; Direct protein sequencing; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Helicase; Host-virus interaction; Hydrolase;
KW Immunity; Innate immunity; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis;
KW Systemic lupus erythematosus; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7957065,
FT ECO:0000269|PubMed:8605992"
FT CHAIN 2..732
FT /note="X-ray repair cross-complementing protein 5"
FT /id="PRO_0000084340"
FT DOMAIN 9..231
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 253..452
FT /note="Ku"
FT /evidence="ECO:0000255"
FT REGION 138..165
FT /note="Leucine-zipper"
FT MOTIF 720..728
FT /note="EEXXXDL motif"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 265
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 332
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 535
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 577
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000269|PubMed:10026262,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 579
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000305|PubMed:10026262"
FT MOD_RES 580
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000269|PubMed:10026262"
FT MOD_RES 660
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 665
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 715
FT /note="Phosphothreonine; by PRKDC"
FT /evidence="ECO:0000305|PubMed:10026262"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 532
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 534
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 566
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 568
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 669
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 688
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 463
FT /note="L -> F (in dbSNP:rs1805380)"
FT /id="VAR_014724"
FT VARIANT 508
FT /note="I -> V (in dbSNP:rs2287558)"
FT /id="VAR_053784"
FT MUTAGEN 720..721
FT /note="EE->AA: Abolishes interaction with PRKDC and its
FT recruitment to sites of DNA damage."
FT /evidence="ECO:0000269|PubMed:15758953"
FT MUTAGEN 726..727
FT /note="DD->AA: Abolishes interaction with PRKDC and its
FT recruitment to sites of DNA damage."
FT /evidence="ECO:0000269|PubMed:15758953"
FT CONFLICT 14..16
FT /note="MDV -> YSY (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="V -> A (in Ref. 3; BAF83429)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="I -> V (in Ref. 4; BAD96323)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="R -> S (in Ref. 4; BAD96323)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="R -> L (in Ref. 11; CAA40736)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="M -> R (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="T -> G (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="I -> T (in Ref. 3; BAF83429)"
FT /evidence="ECO:0000305"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:7Z87"
FT HELIX 30..48
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1JEQ"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:7SGL"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 199..215
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1JEY"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 258..267
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:8AG4"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:7Z88"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:8AG4"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 338..347
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 357..366
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:7Z88"
FT HELIX 371..387
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 389..401
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 404..412
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 417..424
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:1JEQ"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:1JEY"
FT HELIX 448..460
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:7ZVT"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 485..499
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:1JEQ"
FT HELIX 510..515
FT /evidence="ECO:0007829|PDB:8AG4"
FT HELIX 520..536
FT /evidence="ECO:0007829|PDB:8AG4"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 550..553
FT /evidence="ECO:0007829|PDB:7Z87"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:7SU3"
FT STRAND 581..586
FT /evidence="ECO:0007829|PDB:1RW2"
FT STRAND 588..592
FT /evidence="ECO:0007829|PDB:1RW2"
FT HELIX 597..604
FT /evidence="ECO:0007829|PDB:7Z87"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:7Z87"
FT HELIX 613..625
FT /evidence="ECO:0007829|PDB:7Z87"
FT HELIX 629..648
FT /evidence="ECO:0007829|PDB:7Z87"
FT HELIX 652..668
FT /evidence="ECO:0007829|PDB:7Z87"
FT HELIX 673..681
FT /evidence="ECO:0007829|PDB:7Z87"
FT STRAND 688..692
FT /evidence="ECO:0007829|PDB:7Z87"
FT HELIX 700..704
FT /evidence="ECO:0007829|PDB:7Z87"
FT HELIX 725..730
FT /evidence="ECO:0007829|PDB:7Z87"
SQ 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
//
