PRKDC_HUMAN
ID PRKDC_HUMAN Reviewed; 4128 AA.
AC P78527; P78528; Q13327; Q13337; Q14175; Q59H99; Q7Z611; Q96SE6; Q9UME3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 3.
DT 03-AUG-2022, entry version 229.
DE RecName: Full=DNA-dependent protein kinase catalytic subunit;
DE Short=DNA-PK catalytic subunit;
DE Short=DNA-PKcs;
DE EC=2.7.11.1 {ECO:0000269|PubMed:26237645, ECO:0000269|PubMed:32103174};
DE AltName: Full=DNPK1;
DE AltName: Full=p460;
GN Name=PRKDC; Synonyms=HYRC, HYRC1;
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].
RC TISSUE=Cervix carcinoma;
RX PubMed=7671312; DOI=10.1016/0092-8674(95)90482-4;
RA Hartley K.O., Gell D., Smith G.C.M., Zhang H., Divecha N., Connelly M.A.,
RA Admon A., Lees-Miller S.P., Anderson C.W., Jackson S.P.;
RT "DNA-dependent protein kinase catalytic subunit: a relative of
RT phosphatidylinositol 3-kinase and the ataxia telangiectasia gene product.";
RL Cell 82:849-856(1995).
RN [2]
RP SEQUENCE REVISION, AND ALTERNATIVE SPLICING.
RA Gell D., Anderson C.W.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-6; ILE-333; SER-605;
RP MET-680; SER-695; SER-1071; VAL-1314; VAL-1588; HIS-1603; VAL-2095;
RP GLU-2702; CYS-2899; ASP-3149; SER-3201; GLU-3404; THR-3434; SER-3459;
RP MET-3562; LEU-3836 AND VAL-3932.
RG NIEHS SNPs program;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1689.
RX PubMed=11418067; DOI=10.1667/0033-7587(2001)156[0002:fmiptg]2.0.co;2;
RA Anderson C.W., Dunn J.J., Freimuth P.I., Galloway A.M.,
RA Allalunis-Turner M.J.;
RT "Frameshift mutation in PRKDC, the gene for DNA-PKcs, in the DNA repair-
RT defective, human, glioma-derived cell line M059J.";
RL Radiat. Res. 156:2-9(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
RX PubMed=9284934; DOI=10.1159/000134594;
RA Ladenburger E.M., Fackelmayer F.O., Hameister H., Knippers R.;
RT "MCM4 and PRKDC, human genes encoding proteins MCM4 and DNA-PKcs, are close
RT neighbours located on chromosome 8q12-->q13.";
RL Cytogenet. Cell Genet. 77:268-270(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1789-2203.
RC TISSUE=Placenta;
RX PubMed=7638222; DOI=10.1073/pnas.92.16.7515;
RA Sipley J.D., Menninger J.C., Hartley K.O., Ward D.C., Jackson S.P.,
RA Anderson C.W.;
RT "Gene for the catalytic subunit of the human DNA-activated protein kinase
RT maps to the site of the XRCC7 gene on chromosome 8.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7515-7519(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2255-2335.
RC TISSUE=Placenta;
RA Abe M.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3199-4128 (ISOFORM 1).
RC TISSUE=Fetal lung;
RX PubMed=7594449;
RA Poltoratsky V.P., Shi X., York J.D., Lieber M.R., Carter T.H.;
RT "Human DNA-activated protein kinase (DNA-PK) is homologous to
RT phosphatidylinositol kinases.";
RL J. Immunol. 155:4529-4533(1995).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3250-4128 (ISOFORM 1).
RA Anderson C.W., Dunn J.J., Freimuth P.I.;
RT "Sequence of the 3' segment (exons 70-86) of PRKDC, the gene for human DNA-
RT PKcs.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3372-4128 (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno F.R.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP FUNCTION, AND PHOSPHORYLATION OF HSPCA.
RX PubMed=2507541; DOI=10.1016/s0021-9258(18)71488-9;
RA Lees-Miller S.P., Anderson C.W.;
RT "The human double-stranded DNA-activated protein kinase phosphorylates the
RT 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine
RT residues.";
RL J. Biol. Chem. 264:17275-17280(1989).
RN [12]
RP FUNCTION, AND PHOSPHORYLATION OF H1.
RX PubMed=2247066; DOI=10.1128/mcb.10.12.6460-6471.1990;
RA Carter T., Vancurova I., Sun I., Lou W., DeLeon S.;
RT "A DNA-activated protein kinase from HeLa cell nuclei.";
RL Mol. Cell. Biol. 10:6460-6471(1990).
RN [13]
RP FUNCTION, AND PHOSPHORYLATION OF MYC.
RX PubMed=1597196; DOI=10.1111/j.1432-1033.1992.tb16964.x;
RA Iijima S., Teraoka H., Date T., Tsukada K.;
RT "DNA-activated protein kinase in Raji Burkitt's lymphoma cells.
RT Phosphorylation of c-Myc oncoprotein.";
RL Eur. J. Biochem. 206:595-603(1992).
RN [14]
RP FUNCTION, AND PHOSPHORYLATION OF SRF.
RX PubMed=8407951; DOI=10.1016/s0021-9258(19)36904-2;
RA Liu S.-H., Ma J.-T., Yueh A.Y., Lees-Miller S.P., Anderson C.W., Ng S.-Y.;
RT "The carboxyl-terminal transactivation domain of human serum response
RT factor contains DNA-activated protein kinase phosphorylation sites.";
RL J. Biol. Chem. 268:21147-21154(1993).
RN [15]
RP FUNCTION, AND PHOSPHORYLATION OF JUN.
RX PubMed=8464713; DOI=10.1093/nar/21.5.1289;
RA Bannister A.J., Gottlieb T.M., Kouzarides T., Jackson S.P.;
RT "c-Jun is phosphorylated by the DNA-dependent protein kinase in vitro;
RT definition of the minimal kinase recognition motif.";
RL Nucleic Acids Res. 21:1289-1295(1993).
RN [16]
RP CLEAVAGE BY CASPASE-3.
RX PubMed=8804412; DOI=10.1016/0014-5793(96)00842-3;
RA Teraoka H., Yumoto Y., Watanabe F., Tsukada K., Suwa A., Enari M.,
RA Nagata S.;
RT "CPP32/Yama/apopain cleaves the catalytic component of DNA-dependent
RT protein kinase in the holoenzyme.";
RL FEBS Lett. 393:1-6(1996).
RN [17]
RP ALTERNATIVE SPLICING.
RX PubMed=8917110; DOI=10.1016/0378-1119(96)00135-7;
RA Connelly M.A., Zhang H., Kieleczawa J., Anderson C.W.;
RT "Alternate splice-site utilization in the gene for the catalytic subunit of
RT the DNA-activated protein kinase, DNA-PKcs.";
RL Gene 175:271-273(1996).
RN [18]
RP FUNCTION, AND PHOSPHORYLATION OF TP53.
RX PubMed=9363941; DOI=10.1016/s0092-8674(00)80416-x;
RA Shieh S.-Y., Ikeda M., Taya Y., Prives C.;
RT "DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2.";
RL Cell 91:325-334(1997).
RN [19]
RP CHARACTERIZATION, AND INTERACTION WITH CIB1.
RX PubMed=9372844; DOI=10.1016/s0921-8777(97)00035-9;
RA Wu X., Lieber M.R.;
RT "Interaction between DNA-dependent protein kinase and a novel protein,
RT KIP.";
RL Mutat. Res. 385:13-20(1997).
RN [20]
RP FUNCTION, AND PHOSPHORYLATION OF XRCC6.
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 [21]
RP FUNCTION, AND PHOSPHORYLATION OF RFA2.
RX PubMed=9139719; DOI=10.1074/jbc.272.19.12634;
RA Niu H., Erdjument-Bromage H., Pan Z.-Q., Lee S.-H., Tempst P., Hurwitz J.;
RT "Mapping of amino acid residues in the p34 subunit of human single-stranded
RT DNA-binding protein phosphorylated by DNA-dependent protein kinase and Cdc2
RT kinase in vitro.";
RL J. Biol. Chem. 272:12634-12641(1997).
RN [22]
RP ACTIVITY REGULATION.
RX PubMed=9766667;
RA Sarkaria J.N., Tibbetts R.S., Busby E.C., Kennedy A.P., Hill D.E.,
RA Abraham R.T.;
RT "Inhibition of phosphoinositide 3-kinase related kinases by the
RT radiosensitizing agent wortmannin.";
RL Cancer Res. 58:4375-4382(1998).
RN [23]
RP FUNCTION, INTERACTION WITH C1D, AND MUTAGENESIS OF LEU-1510 AND
RP 1516-GLU-LEU-1517.
RX PubMed=9679063; DOI=10.1101/gad.12.14.2188;
RA Yavuzer U., Smith G.C.M., Bliss T., Werner D., Jackson S.P.;
RT "DNA end-independent activation of DNA-PK mediated via association with the
RT DNA-binding protein C1D.";
RL Genes Dev. 12:2188-2199(1998).
RN [24]
RP INTERACTION WITH ILF3.
RX PubMed=9442054; DOI=10.1074/jbc.273.4.2136;
RA Ting N.S.Y., Kao P.N., Chan D.W., Lintott L.G., Lees-Miller S.P.;
RT "DNA-dependent protein kinase interacts with antigen receptor response
RT element binding proteins NF90 and NF45.";
RL J. Biol. Chem. 273:2136-2145(1998).
RN [25]
RP DNA-BINDING.
RX PubMed=9435225; DOI=10.1073/pnas.95.2.525;
RA Hammarsten O., Chu G.;
RT "DNA-dependent protein kinase: DNA binding and activation in the absence of
RT Ku.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:525-530(1998).
RN [26]
RP FUNCTION, AND PHOSPHORYLATION OF XRCC5 AND XRCC6.
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 [27]
RP FUNCTION, AND PHOSPHORYLATION OF PARP1.
RX PubMed=10467406; DOI=10.1038/sj.onc.1202823;
RA Ariumi Y., Masutani M., Copeland T.D., Mimori T., Sugimura T.,
RA Shimotohno K., Ueda K., Hatanaka M., Noda M.;
RT "Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent
RT protein kinase in vitro.";
RL Oncogene 18:4616-4625(1999).
RN [28]
RP PHOSPHORYLATION AT THR-2609; SER-2612; THR-2638 AND THR-2647.
RX PubMed=12186630; DOI=10.1042/bj20020973;
RA Douglas P., Sapkota G.P., Morrice N., Yu Y., Goodarzi A.A., Merkle D.,
RA Meek K., Alessi D.R., Lees-Miller S.P.;
RT "Identification of in vitro and in vivo phosphorylation sites in the
RT catalytic subunit of the DNA-dependent protein kinase.";
RL Biochem. J. 368:243-251(2002).
RN [29]
RP FUNCTION, AND INTERACTION WITH DCLRE1C.
RX PubMed=11955432; DOI=10.1016/s0092-8674(02)00671-2;
RA Ma Y., Pannicke U., Schwarz K., Lieber M.R.;
RT "Hairpin opening and overhang processing by an Artemis/DNA-dependent
RT protein kinase complex in nonhomologous end joining and V(D)J
RT recombination.";
RL Cell 108:781-794(2002).
RN [30]
RP FUNCTION, AND PHOSPHORYLATION OF XRCC4.
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 [31]
RP PHOSPHORYLATION AT THR-2609, MUTAGENESIS OF THR-2609, SUBCELLULAR LOCATION,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12231622; DOI=10.1101/gad.1015202;
RA Chan D.W., Chen B.P., Prithivirajsingh S., Kurimasa A., Story M.D., Qin J.,
RA Chen D.J.;
RT "Autophosphorylation of the DNA-dependent protein kinase catalytic subunit
RT is required for rejoining of DNA double-strand breaks.";
RL Genes Dev. 16:2333-2338(2002).
RN [32]
RP FUNCTION, AND PHOSPHORYLATION OF WRN.
RX PubMed=11889123; DOI=10.1074/jbc.m111523200;
RA Karmakar P., Piotrowski J., Brosh R.M. Jr., Sommers J.A., Miller S.P.,
RA Cheng W.H., Snowden C.M., Ramsden D.A., Bohr V.A.;
RT "Werner protein is a target of DNA-dependent protein kinase in vivo and in
RT vitro, and its catalytic activities are regulated by phosphorylation.";
RL J. Biol. Chem. 277:18291-18302(2002).
RN [33]
RP FUNCTION, AND MUTAGENESIS OF THR-2638 AND THR-2647.
RX PubMed=12649176;
RA Soubeyrand S., Pope L., Pakuts B., Hache R.J.;
RT "Threonines 2638/2647 in DNA-PK are essential for cellular resistance to
RT ionizing radiation.";
RL Cancer Res. 63:1198-1201(2003).
RN [34]
RP FUNCTION, AND PHOSPHORYLATION OF POU2F1.
RX PubMed=14612514;
RA Schild-Poulter C., Shih A., Yarymowich N.C., Hache R.J.G.;
RT "Down-regulation of histone H2B by DNA-dependent protein kinase in response
RT to DNA damage through modulation of octamer transcription factor 1.";
RL Cancer Res. 63:7197-7205(2003).
RN [35]
RP FUNCTION IN PHOSPHORYLATION OF XRCC4.
RX PubMed=14599745; DOI=10.1016/s1568-7864(03)00143-5;
RA Yu Y., Wang W., Ding Q., Ye R., Chen D., Merkle D., Schriemer D., Meek K.,
RA Lees-Miller S.P.;
RT "DNA-PK phosphorylation sites in XRCC4 are not required for survival after
RT radiation or for V(D)J recombination.";
RL DNA Repair 2:1239-1252(2003).
RN [36]
RP FUNCTION, AND PHOSPHORYLATION OF H2AX.
RX PubMed=14627815; DOI=10.1093/nar/gkg921;
RA Park E.-J., Chan D.W., Park J.-H., Oettinger M.A., Kwon J.;
RT "DNA-PK is activated by nucleosomes and phosphorylates H2AX within the
RT nucleosomes in an acetylation-dependent manner.";
RL Nucleic Acids Res. 31:6819-6827(2003).
RN [37]
RP FUNCTION IN PHOSPHORYLATION OF XRCC4.
RX PubMed=15177042; DOI=10.1016/j.dnarep.2003.11.005;
RA Lee K.J., Jovanovic M., Udayakumar D., Bladen C.L., Dynan W.S.;
RT "Identification of DNA-PKcs phosphorylation sites in XRCC4 and effects of
RT mutations at these sites on DNA end joining in a cell-free system.";
RL DNA Repair 3:267-276(2004).
RN [38]
RP FUNCTION IN PHOSPHORYLATION OF NHEJ1.
RX PubMed=18644470; DOI=10.1016/j.dnarep.2008.06.015;
RA Yu Y., Mahaney B.L., Yano K., Ye R., Fang S., Douglas P., Chen D.J.,
RA Lees-Miller S.P.;
RT "DNA-PK and ATM phosphorylation sites in XLF/Cernunnos are not required for
RT repair of DNA double strand breaks.";
RL DNA Repair 7:1680-1692(2008).
RN [39]
RP FUNCTION IN PHOSPHORYLATION OF XRCC4.
RX PubMed=26666690; DOI=10.1093/jrr/rrv086;
RA Sharma M.K., Imamichi S., Fukuchi M., Samarth R.M., Tomita M.,
RA Matsumoto Y.;
RT "In cellulo phosphorylation of XRCC4 Ser320 by DNA-PK induced by DNA
RT damage.";
RL J. Radiat. Res. 57:115-120(2016).
RN [40]
RP FUNCTION IN PHOSPHORYLATION OF XRCC4.
RX PubMed=30247612; DOI=10.1093/jrr/rry072;
RA Amiri Moghani A.R., Sharma M.K., Matsumoto Y.;
RT "In cellulo phosphorylation of DNA double-strand break repair protein XRCC4
RT on Ser260 by DNA-PK.";
RL J. Radiat. Res. 59:700-708(2018).
RN [41]
RP INTERACTION WITH DCLRE1C.
RX PubMed=15071507; DOI=10.1038/sj.emboj.7600206;
RA Pannicke U., Ma Y., Hopfner K.-P., Niewolik D., Lieber M.R., Schwarz K.;
RT "Functional and biochemical dissection of the structure-specific nuclease
RT ARTEMIS.";
RL EMBO J. 23:1987-1997(2004).
RN [42]
RP INTERACTION WITH DCLRE1C.
RX PubMed=14744996; DOI=10.1084/jem.20031142;
RA Poinsignon C., Moshous D., Callebaut I., de Chasseval R., Villey I.,
RA de Villartay J.-P.;
RT "The metallo-beta-lactamase/beta-CASP domain of Artemis constitutes the
RT catalytic core for V(D)J recombination.";
RL J. Exp. Med. 199:315-321(2004).
RN [43]
RP FUNCTION, AND INTERACTION WITH DCLRE1C.
RX PubMed=15574326; DOI=10.1016/j.molcel.2004.11.017;
RA Ma Y., Lu H., Tippin B., Goodman M.F., Shimazaki N., Koiwai O.,
RA Hsieh C.-L., Schwarz K., Lieber M.R.;
RT "A biochemically defined system for mammalian nonhomologous DNA end
RT joining.";
RL Mol. Cell 16:701-713(2004).
RN [44]
RP INTERACTION WITH DCLRE1C.
RX PubMed=15456891; DOI=10.1128/mcb.24.20.9207-9220.2004;
RA Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D.,
RA Legerski R.J.;
RT "Artemis is a phosphorylation target of ATM and ATR and is involved in the
RT G2/M DNA damage checkpoint response.";
RL Mol. Cell. Biol. 24:9207-9220(2004).
RN [45]
RP FUNCTION, AND PHOSPHORYLATION OF 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 [46]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2056 AND THR-2609,
RP AND DEPHOSPHORYLATION AT SER-2056 AND THR-2609.
RX PubMed=14734805; DOI=10.1073/pnas.0307765100;
RA Wechsler T., Chen B.P., Harper R., Morotomi-Yano K., Huang B.C., Meek K.,
RA Cleaver J.E., Chen D.J., Wabl M.;
RT "DNA-PKcs function regulated specifically by protein phosphatase 5.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1247-1252(2004).
RN [47]
RP FUNCTION, AND PHOSPHORYLATION OF H2AX.
RX PubMed=16046194; DOI=10.1016/j.dnarep.2005.06.005;
RA Reitsema T., Klokov D., Banath J.P., Olive P.L.;
RT "DNA-PK is responsible for enhanced phosphorylation of histone H2AX under
RT hypertonic conditions.";
RL DNA Repair 4:1172-1181(2005).
RN [48]
RP INTERACTION WITH DCLRE1C.
RX PubMed=15811628; DOI=10.1016/j.dnarep.2005.02.001;
RA Wang J., Pluth J.M., Cooper P.K., Cowan M.J., Chen D.J., Yannone S.M.;
RT "Artemis deficiency confers a DNA double-strand break repair defect and
RT Artemis phosphorylation status is altered by DNA damage and cell cycle
RT progression.";
RL DNA Repair 4:556-570(2005).
RN [49]
RP INTERACTION WITH DCLRE1C.
RX PubMed=15936993; DOI=10.1016/j.dnarep.2005.04.013;
RA Ma Y., Schwarz K., Lieber M.R.;
RT "The Artemis:DNA-PKcs endonuclease cleaves DNA loops, flaps, and gaps.";
RL DNA Repair 4:845-851(2005).
RN [50]
RP INTERACTION WITH XRCC5.
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 [51]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3205, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [52]
RP FUNCTION, AND PHOSPHORYLATION OF XRCC1.
RX PubMed=16397295; DOI=10.1093/nar/gkj409;
RA Levy N., Martz A., Bresson A., Spenlehauer C., de Murcia G.,
RA Menissier-de Murcia J.;
RT "XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA
RT damage.";
RL Nucleic Acids Res. 34:32-41(2006).
RN [53]
RP REVIEW.
RX PubMed=15592499; DOI=10.1038/sj.onc.1208332;
RA Collis S.J., DeWeese T.L., Jeggo P.A., Parker A.R.;
RT "The life and death of DNA-PK.";
RL Oncogene 24:949-961(2005).
RN [54]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [55]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3205 AND SER-4026, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [56]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3205, 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 [57]
RP INVOLVEMENT IN IMD26, AND VARIANT IMD26 ARG-3062.
RX PubMed=19075392; DOI=10.1172/jci37141;
RA van der Burg M., Ijspeert H., Verkaik N.S., Turul T., Wiegant W.W.,
RA Morotomi-Yano K., Mari P.O., Tezcan I., Chen D.J., Zdzienicka M.Z.,
RA van Dongen J.J., van Gent D.C.;
RT "A DNA-PKcs mutation in a radiosensitive T-B- SCID patient inhibits Artemis
RT activation and nonhomologous end-joining.";
RL J. Clin. Invest. 119:91-98(2009).
RN [58]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-893; SER-2612; SER-3205 AND
RP SER-4026, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [59]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3205, 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 [60]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117; LYS-828; LYS-1209; LYS-1970;
RP LYS-2259; LYS-3241; LYS-3260; LYS-3621; LYS-3638 AND LYS-3642, AND
RP 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 [61]
RP INTERACTION WITH TTI1.
RX PubMed=20810650; DOI=10.1101/gad.1934210;
RA Hurov K.E., Cotta-Ramusino C., Elledge S.J.;
RT "A genetic screen identifies the Triple T complex required for DNA damage
RT signaling and ATM and ATR stability.";
RL Genes Dev. 24:1939-1950(2010).
RN [62]
RP INTERACTION WITH TELO2.
RX PubMed=20801936; DOI=10.1101/gad.1956410;
RA Takai H., Xie Y., de Lange T., Pavletich N.P.;
RT "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and
RT ATR complexes.";
RL Genes Dev. 24:2019-2030(2010).
RN [63]
RP INTERACTION WITH TELO2 AND TTI1.
RX PubMed=20427287; DOI=10.1074/jbc.m110.121699;
RA Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K.,
RA Iemura S., Natsume T., Mizushima N.;
RT "Tti1 and Tel2 are critical factors in mammalian target of rapamycin
RT complex assembly.";
RL J. Biol. Chem. 285:20109-20116(2010).
RN [64]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3205 AND SER-4026, 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 [65]
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 [66]
RP INTERACTION WITH BRAT1, AND PHOSPHORYLATION AT SER-2056.
RX PubMed=22977523; DOI=10.3892/etm.2011.232;
RA So E.Y., Ouchi T.;
RT "Functional interaction of BRCA1/ATM-associated BAAT1 with the DNA-PK
RT catalytic subunit.";
RL Exp. Ther. Med. 2:443-447(2011).
RN [67]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2612 AND SER-3205, AND
RP IDENTIFICATION BY 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 [68]
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 [69]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511; SER-687; SER-841;
RP SER-1065; THR-2535; SER-2612; THR-2638; THR-2647; SER-2789; SER-3205;
RP SER-3731; SER-3821 AND SER-4026, 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 [70]
RP INTERACTION WITH SETX.
RX PubMed=23149945; DOI=10.1128/mcb.01195-12;
RA Yuce O., West S.C.;
RT "Senataxin, defective in the neurodegenerative disorder ataxia with
RT oculomotor apraxia 2, lies at the interface of transcription and the DNA
RT damage response.";
RL Mol. Cell. Biol. 33:406-417(2013).
RN [71]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2612, 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 [72]
RP UBIQUITINATION BY RNF144A.
RX PubMed=24979766; DOI=10.1073/pnas.1323107111;
RA Ho S.R., Mahanic C.S., Lee Y.J., Lin W.C.;
RT "RNF144A, an E3 ubiquitin ligase for DNA-PKcs, promotes apoptosis during
RT DNA damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E2646-E2655(2014).
RN [73]
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 [74]
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 [75]
RP FUNCTION IN PHOSPHORYLATION OF FH, AND CATALYTIC ACTIVITY.
RX PubMed=26237645; DOI=10.1038/ncb3209;
RA Jiang Y., Qian X., Shen J., Wang Y., Li X., Liu R., Xia Y., Chen Q.,
RA Peng G., Lin S.Y., Lu Z.;
RT "Local generation of fumarate promotes DNA repair through inhibition of
RT histone H3 demethylation.";
RL Nat. Cell Biol. 17:1158-1168(2015).
RN [76]
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 [77]
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 [78]
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 [79]
RP FUNCTION, AND INTERACTION WITH HEXIM1; XRCC5; 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 [80]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29478807; DOI=10.1016/j.molcel.2018.01.031;
RA Huang T.H., Fowler F., Chen C.C., Shen Z.J., Sleckman B., Tyler J.K.;
RT "The histone chaperones ASF1 and CAF-1 promote MMS22L-TONSL-mediated Rad51
RT loading onto ssDNA during homologous recombination in human cells.";
RL Mol. Cell 69:879-892(2018).
RN [81]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT
RP THR-2609.
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 [82]
RP FUNCTION.
RX PubMed=33273464; DOI=10.1038/s41467-020-19941-0;
RA Sun X., Liu T., Zhao J., Xia H., Xie J., Guo Y., Zhong L., Li M., Yang Q.,
RA Peng C., Rouvet I., Belot A., Shu H.B., Feng P., Zhang J.;
RT "DNA-PK deficiency potentiates cGAS-mediated antiviral innate immunity.";
RL Nat. Commun. 11:6182-6182(2020).
RN [83]
RP INTERACTION WITH KAT5.
RX PubMed=32832608; DOI=10.1126/sciadv.aba7822;
RA Gao S.S., Guan H., Yan S., Hu S., Song M., Guo Z.P., Xie D.F., Liu Y.,
RA Liu X., Zhang S., Zhou P.K.;
RT "TIP60 K430 SUMOylation attenuates its interaction with DNA-PKcs in S-phase
RT cells: Facilitating homologous recombination and emerging target for cancer
RT therapy.";
RL Sci. Adv. 6:eaba7822-eaba7822(2020).
RN [84] {ECO:0007744|PDB:7LT3}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.6 ANGSTROMS) IN COMPLEX WITH THE NHEJ
RP COMPLEX, FUNCTION, IDENTIFICATION IN THE NHEJ COMPLEX, AND
RP AUTOPHOSPHORYLATION.
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).
RN [85]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-6; ASN-263; ILE-333; ILE-420; SER-500;
RP SER-605; LEU-649; SER-695; HIS-1136; VAL-1190; THR-1237; PHE-1279;
RP MET-1447; GLY-1619; VAL-1680; VAL-1680; PRO-2023; GLN-2598; ASN-2810;
RP CYS-2899; ALA-2941; ASP-3085; ASP-3149; SER-3198; SER-3201; GLU-3404;
RP THR-3434; MET-3562; PHE-3584; ILE-3800; LEU-3836; SER-3936 AND MET-3937.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [86]
RP VARIANT IMD26 VAL-3574, AND CHARACTERIZATION OF VARIANT IMD26 VAL-3574.
RX PubMed=23722905; DOI=10.1172/jci67349;
RA Woodbine L., Neal J.A., Sasi N.K., Shimada M., Deem K., Coleman H.,
RA Dobyns W.B., Ogi T., Meek K., Davies E.G., Jeggo P.A.;
RT "PRKDC mutations in a SCID patient with profound neurological
RT abnormalities.";
RL J. Clin. Invest. 123:2969-2980(2013).
CC -!- FUNCTION: Serine/threonine-protein kinase that acts as a molecular
CC sensor for DNA damage (PubMed:11955432, PubMed:12649176,
CC PubMed:14734805, PubMed:33854234). Involved in DNA non-homologous end
CC joining (NHEJ) required for double-strand break (DSB) repair and V(D)J
CC recombination (PubMed:11955432, PubMed:12649176, PubMed:14734805,
CC PubMed:33854234). Must be bound to DNA to express its catalytic
CC properties (PubMed:11955432). Promotes processing of hairpin DNA
CC structures in V(D)J recombination by activation of the hairpin
CC endonuclease artemis (DCLRE1C) (PubMed:11955432). Recruited by XRCC5
CC and XRCC6 to DNA ends and is required to (1) protect and align broken
CC ends of DNA, thereby preventing their degradation, (2) and sequester
CC the DSB for repair by NHEJ (PubMed:15574326, PubMed:11955432,
CC PubMed:12649176, PubMed:14734805, PubMed:33854234). Act as a scaffold
CC protein to aid the localization of DNA repair proteins to the site of
CC damage (PubMed:15574326, PubMed:11955432, PubMed:12649176,
CC PubMed:14734805). The assembly of the DNA-PK complex at DNA ends is
CC also required for the NHEJ ligation step (PubMed:15574326,
CC PubMed:11955432, PubMed:12649176, PubMed:14734805). Found at the ends
CC of chromosomes, suggesting a further role in the maintenance of
CC telomeric stability and the prevention of chromosomal end fusion (By
CC similarity). Also involved in modulation of transcription
CC (PubMed:15574326, PubMed:11955432, PubMed:12649176, PubMed:14734805).
CC As part of the DNA-PK complex, involved in the early steps of ribosome
CC assembly by promoting the processing of precursor rRNA into mature 18S
CC rRNA in the small-subunit processome (PubMed:32103174). Binding to U3
CC small nucleolar RNA, recruits PRKDC and XRCC5/Ku86 to the small-subunit
CC processome (PubMed:32103174). Recognizes the substrate consensus
CC sequence [ST]-Q (PubMed:15574326, PubMed:11955432, PubMed:12649176,
CC PubMed:14734805). Phosphorylates 'Ser-139' of histone variant H2AX,
CC thereby regulating DNA damage response mechanism (PubMed:14627815,
CC PubMed:16046194). Phosphorylates ASF1A, DCLRE1C, c-Abl/ABL1, histone
CC H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, FH, SRF,
CC NHEJ1/XLF, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2
CC (PubMed:2507541, PubMed:2247066, PubMed:1597196, PubMed:8407951,
CC PubMed:8464713, PubMed:9362500, PubMed:9139719, PubMed:10026262,
CC PubMed:10467406, PubMed:12509254, PubMed:11889123, PubMed:14612514,
CC PubMed:14599745, PubMed:15177042, PubMed:18644470, PubMed:26666690,
CC PubMed:30247612, PubMed:14704337, PubMed:16397295, PubMed:26237645,
CC PubMed:28712728, PubMed:29478807). Can phosphorylate C1D not only in
CC the presence of linear DNA but also in the presence of supercoiled DNA
CC (PubMed:9679063). Ability to phosphorylate p53/TP53 in the presence of
CC supercoiled DNA is dependent on C1D (PubMed:9363941). Contributes to
CC the determination of the circadian period length by antagonizing
CC phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein
CC stability, most likely through an indirect mechanism (By similarity).
CC Plays a role in the regulation of DNA virus-mediated innate immune
CC response by assembling into the HDP-RNP complex, a complex that serves
CC as a platform for IRF3 phosphorylation and subsequent innate immune
CC response activation through the cGAS-STING pathway (PubMed:28712728).
CC Also regulates the cGAS-STING pathway by catalyzing phosphorylation of
CC CGAS, thereby impairing CGAS oligomerization and activation
CC (PubMed:33273464). {ECO:0000250|UniProtKB:P97313,
CC ECO:0000269|PubMed:10026262, ECO:0000269|PubMed:10467406,
CC ECO:0000269|PubMed:11889123, ECO:0000269|PubMed:11955432,
CC ECO:0000269|PubMed:12509254, ECO:0000269|PubMed:12649176,
CC ECO:0000269|PubMed:14599745, ECO:0000269|PubMed:14612514,
CC ECO:0000269|PubMed:14627815, ECO:0000269|PubMed:14704337,
CC ECO:0000269|PubMed:14734805, ECO:0000269|PubMed:15177042,
CC ECO:0000269|PubMed:15574326, ECO:0000269|PubMed:1597196,
CC ECO:0000269|PubMed:16046194, ECO:0000269|PubMed:16397295,
CC ECO:0000269|PubMed:18644470, ECO:0000269|PubMed:2247066,
CC ECO:0000269|PubMed:2507541, ECO:0000269|PubMed:26237645,
CC ECO:0000269|PubMed:26666690, ECO:0000269|PubMed:28712728,
CC ECO:0000269|PubMed:29478807, ECO:0000269|PubMed:30247612,
CC ECO:0000269|PubMed:32103174, ECO:0000269|PubMed:33273464,
CC ECO:0000269|PubMed:33854234, ECO:0000269|PubMed:8407951,
CC ECO:0000269|PubMed:8464713, ECO:0000269|PubMed:9139719,
CC ECO:0000269|PubMed:9362500, ECO:0000269|PubMed:9363941,
CC ECO:0000269|PubMed:9679063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:29478807, ECO:0000269|PubMed:32103174};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:26237645,
CC ECO:0000269|PubMed:32103174};
CC -!- ACTIVITY REGULATION: Activity seems to be attenuated by
CC autophosphorylation. Binding to the SL1 region of U3 small nucleolar
CC RNA promotes auto-phosphorylation activity (PubMed:32103174). Inhibited
CC by wortmannin (PubMed:9766667). {ECO:0000269|PubMed:32103174,
CC ECO:0000269|PubMed:9766667}.
CC -!- SUBUNIT: DNA-PK is a heterotrimer of PRKDC and the Ku dimer (composed
CC of XRCC6/Ku70 and XRCC5/Ku86) (PubMed:15758953, PubMed:25670504).
CC Formation of this complex may be promoted by interaction with ILF3
CC (PubMed:9442054). 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:15758953,
CC PubMed:25670504, PubMed:33854234). Additional component of the NHEJ
CC complex includes PAXX (PubMed:25574025, PubMed:25941166). Following
CC autophosphorylation, PRKDC dissociates from DNA (PubMed:33854234).
CC Interacts with DNA-PKcs-interacting protein (KIP) with the region
CC upstream the kinase domain (PubMed:9372844). PRKDC alone also interacts
CC with and phosphorylates DCLRE1C, thereby activating the latent
CC endonuclease activity of this protein (PubMed:11955432,
CC PubMed:15071507, PubMed:14744996, PubMed:15456891, PubMed:15574326,
CC PubMed:15811628, PubMed:15936993). Interacts with C1D (PubMed:9679063).
CC Interacts with TTI1 and TELO2 (PubMed:20801936, PubMed:20427287,
CC PubMed:20810650). Interacts with CIB1 (PubMed:9372844). Interacts with
CC SETX (PubMed:23149945). Interacts with NR4A3; the DNA-dependent protein
CC kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents
CC NR4A3 ubiquitination and degradation (PubMed:25852083). Interacts with
CC BRAT1 (PubMed:22977523). Part of the HDP-RNP complex composed of at
CC least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO,
CC PSPC1, RBM14, and MATR3) and NEAT1 RNA (PubMed:28712728). Interacts
CC with KAT5 (PubMed:32832608). {ECO:0000269|PubMed:11955432,
CC ECO:0000269|PubMed:14744996, ECO:0000269|PubMed:15071507,
CC ECO:0000269|PubMed:15456891, ECO:0000269|PubMed:15574326,
CC ECO:0000269|PubMed:15758953, ECO:0000269|PubMed:15811628,
CC ECO:0000269|PubMed:15936993, ECO:0000269|PubMed:20427287,
CC ECO:0000269|PubMed:20801936, ECO:0000269|PubMed:20810650,
CC ECO:0000269|PubMed:22977523, ECO:0000269|PubMed:23149945,
CC ECO:0000269|PubMed:25574025, ECO:0000269|PubMed:25670504,
CC ECO:0000269|PubMed:25852083, ECO:0000269|PubMed:25941166,
CC ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:32832608,
CC ECO:0000269|PubMed:33854234, ECO:0000269|PubMed:9372844,
CC ECO:0000269|PubMed:9442054, ECO:0000269|PubMed:9679063}.
CC -!- INTERACTION:
CC P78527; O43918: AIRE; NbExp=2; IntAct=EBI-352053, EBI-1753081;
CC P78527; P10275: AR; NbExp=3; IntAct=EBI-352053, EBI-608057;
CC P78527; Q96SD1: DCLRE1C; NbExp=4; IntAct=EBI-352053, EBI-11694104;
CC P78527; P14921: ETS1; NbExp=2; IntAct=EBI-352053, EBI-913209;
CC P78527; P50549: ETV1; NbExp=2; IntAct=EBI-352053, EBI-3905068;
CC P78527; P09629: HOXB7; NbExp=2; IntAct=EBI-352053, EBI-1248457;
CC P78527; Q9BPZ7: MAPKAP1; NbExp=2; IntAct=EBI-352053, EBI-749938;
CC P78527; Q96RI1-2: NR1H4; NbExp=4; IntAct=EBI-352053, EBI-9640524;
CC P78527; P10276: RARA; NbExp=3; IntAct=EBI-352053, EBI-413374;
CC P78527; P17947: SPI1; NbExp=2; IntAct=EBI-352053, EBI-2293548;
CC P78527; P13010: XRCC5; NbExp=8; IntAct=EBI-352053, EBI-357997;
CC P78527; P12956: XRCC6; NbExp=7; IntAct=EBI-352053, EBI-353208;
CC P78527; P25490: YY1; NbExp=2; IntAct=EBI-352053, EBI-765538;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12231622,
CC ECO:0000269|PubMed:14734805, ECO:0000269|PubMed:22002106}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:22002106, ECO:0000269|PubMed:32103174}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P78527-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P78527-2; Sequence=VSP_004708;
CC -!- PTM: Autophosphorylated at two clusters, the T2609 cluster and the
CC S2056 cluster (PubMed:33854234). Autophosphorylated on Ser-2056, Thr-
CC 2609, Thr-2638 and Thr-2647 (PubMed:14734805, PubMed:12186630,
CC PubMed:12231622, PubMed:33854234). Ser-2056 and Thr-2609 are DNA
CC damage-inducible phosphorylation sites (inducible with ionizing
CC radiation, IR) dephosphorylated by PPP5C (PubMed:14734805,
CC PubMed:12186630, PubMed:12231622). Autophosphorylation induces a
CC conformational change that leads to remodeling of the DNA-PK complex,
CC requisite for efficient end processing and DNA repair (PubMed:14734805,
CC PubMed:12186630, PubMed:12231622). Autophosphorylation in trans within
CC DNA-PK complexes loaded on DNA ends leads to the dissociation of PRKDC
CC from DNA and the transition into the short-range NHEJ complex
CC (PubMed:33854234). Autophosphorylation of the T2609 cluster is required
CC for hematopoietic development and protein synthesis in erythrocytes
CC precursors (By similarity). {ECO:0000250|UniProtKB:P97313,
CC ECO:0000269|PubMed:12186630, ECO:0000269|PubMed:12231622,
CC ECO:0000269|PubMed:14734805, ECO:0000269|PubMed:33854234}.
CC -!- PTM: S-nitrosylated by GAPDH. {ECO:0000250|UniProtKB:P97313}.
CC -!- PTM: Polyubiquitinated by RNF144A, leading to proteasomal degradation.
CC {ECO:0000269|PubMed:24979766}.
CC -!- DISEASE: Immunodeficiency 26 with or without neurologic abnormalities
CC (IMD26) [MIM:615966]: A form of severe combined immunodeficiency
CC characterized by reduced or absent T and B cells, recurrent
CC candidiasis, and lower respiratory tract infections. Some patients show
CC dysmorphic features, severe growth failure, microcephaly, seizures, and
CC impaired neurological functions. {ECO:0000269|PubMed:19075392,
CC ECO:0000269|PubMed:23722905}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/prkdc/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U47077; AAB39925.5; -; mRNA.
DR EMBL; U34994; AAC50210.3; -; mRNA.
DR EMBL; AY316117; AAP69525.1; -; Genomic_DNA.
DR EMBL; U63630; AAC52019.2; -; Genomic_DNA.
DR EMBL; U90415; AAB51722.1; -; Genomic_DNA.
DR EMBL; L27425; AAA79244.1; -; Genomic_DNA.
DR EMBL; AB052953; BAB79635.1; -; Genomic_DNA.
DR EMBL; U35835; AAA79184.1; -; mRNA.
DR EMBL; AY030284; AAK40350.1; -; Genomic_DNA.
DR EMBL; AB208860; BAD92097.1; -; mRNA.
DR CCDS; CCDS75734.1; -. [P78527-2]
DR CCDS; CCDS75735.1; -. [P78527-1]
DR PIR; A57099; A57099.
DR PIR; G02083; G02083.
DR RefSeq; NP_001075109.1; NM_001081640.1. [P78527-2]
DR RefSeq; NP_008835.5; NM_006904.6. [P78527-1]
DR PDB; 5LUQ; X-ray; 4.30 A; A/B=2-2575, A/B=2774-4127.
DR PDB; 5W1R; EM; 4.40 A; A=1-4128.
DR PDB; 5Y3R; EM; 6.60 A; C=10-4128.
DR PDB; 6ZFP; EM; 3.24 A; A=1-4128.
DR PDB; 6ZH2; EM; 3.92 A; A=1-4128.
DR PDB; 6ZH4; EM; 3.62 A; A=1-4128.
DR PDB; 6ZH6; EM; 3.93 A; A=1-4128.
DR PDB; 6ZH8; EM; 4.14 A; A=1-4128.
DR PDB; 6ZHA; EM; 3.91 A; A=1-4128.
DR PDB; 6ZHE; EM; 7.24 A; A/F=1-4128.
DR PDB; 7K0Y; EM; 3.70 A; A=1-4128.
DR PDB; 7K10; EM; 3.30 A; A=1-4128.
DR PDB; 7K11; EM; 3.21 A; A=1-4128.
DR PDB; 7K19; EM; 4.30 A; A=1-4128.
DR PDB; 7K1B; EM; 4.30 A; A=1-4128.
DR PDB; 7K1J; EM; 3.90 A; A=1-4128.
DR PDB; 7K1K; EM; 4.10 A; A=1-4128.
DR PDB; 7K1N; EM; 3.90 A; A=1-4128.
DR PDB; 7LT3; EM; 4.60 A; C/L=1-4128.
DR PDB; 7NFC; EM; 4.14 A; A/F=1-4128.
DR PDB; 7NFE; EM; 4.29 A; A=1-4128.
DR PDB; 7OTM; EM; 3.33 A; A=1-4128.
DR PDB; 7OTP; EM; 3.40 A; A=1-4128.
DR PDB; 7OTV; EM; 3.24 A; A=1-4128.
DR PDB; 7OTW; EM; 2.99 A; A=1-4128.
DR PDB; 7OTY; EM; 2.96 A; A=1-4128.
DR PDB; 7SGL; EM; 3.00 A; A=1-4128.
DR PDB; 7SU3; EM; 3.30 A; A=1-4128.
DR PDB; 7SUD; EM; 3.60 A; A=1-4128.
DR PDBsum; 5LUQ; -.
DR PDBsum; 5W1R; -.
DR PDBsum; 5Y3R; -.
DR PDBsum; 6ZFP; -.
DR PDBsum; 6ZH2; -.
DR PDBsum; 6ZH4; -.
DR PDBsum; 6ZH6; -.
DR PDBsum; 6ZH8; -.
DR PDBsum; 6ZHA; -.
DR PDBsum; 6ZHE; -.
DR PDBsum; 7K0Y; -.
DR PDBsum; 7K10; -.
DR PDBsum; 7K11; -.
DR PDBsum; 7K19; -.
DR PDBsum; 7K1B; -.
DR PDBsum; 7K1J; -.
DR PDBsum; 7K1K; -.
DR PDBsum; 7K1N; -.
DR PDBsum; 7LT3; -.
DR PDBsum; 7NFC; -.
DR PDBsum; 7NFE; -.
DR PDBsum; 7OTM; -.
DR PDBsum; 7OTP; -.
DR PDBsum; 7OTV; -.
DR PDBsum; 7OTW; -.
DR PDBsum; 7OTY; -.
DR PDBsum; 7SGL; -.
DR PDBsum; 7SU3; -.
DR PDBsum; 7SUD; -.
DR SASBDB; P78527; -.
DR SMR; P78527; -.
DR BioGRID; 111577; 547.
DR ComplexPortal; CPX-3403; DNA-dependent protein kinase complex.
DR CORUM; P78527; -.
DR DIP; DIP-24186N; -.
DR ELM; P78527; -.
DR IntAct; P78527; 208.
DR MINT; P78527; -.
DR STRING; 9606.ENSP00000313420; -.
DR BindingDB; P78527; -.
DR ChEMBL; CHEMBL3142; -.
DR DrugBank; DB00201; Caffeine.
DR DrugBank; DB05210; SF1126.
DR DrugCentral; P78527; -.
DR GuidetoPHARMACOLOGY; 2800; -.
DR CarbonylDB; P78527; -.
DR GlyConnect; 1183; 1 N-Linked glycan (1 site).
DR GlyGen; P78527; 9 sites, 1 N-linked glycan (1 site), 2 O-linked glycans (8 sites).
DR iPTMnet; P78527; -.
DR MetOSite; P78527; -.
DR PhosphoSitePlus; P78527; -.
DR SwissPalm; P78527; -.
DR BioMuta; PRKDC; -.
DR DMDM; 38258929; -.
DR SWISS-2DPAGE; P78527; -.
DR EPD; P78527; -.
DR jPOST; P78527; -.
DR MassIVE; P78527; -.
DR MaxQB; P78527; -.
DR PaxDb; P78527; -.
DR PeptideAtlas; P78527; -.
DR PRIDE; P78527; -.
DR ProteomicsDB; 57634; -. [P78527-1]
DR ProteomicsDB; 57635; -. [P78527-2]
DR Antibodypedia; 52433; 1594 antibodies from 44 providers.
DR DNASU; 5591; -.
DR Ensembl; ENST00000314191.7; ENSP00000313420.3; ENSG00000253729.8. [P78527-1]
DR Ensembl; ENST00000338368.7; ENSP00000345182.4; ENSG00000253729.8. [P78527-2]
DR GeneID; 5591; -.
DR KEGG; hsa:5591; -.
DR MANE-Select; ENST00000314191.7; ENSP00000313420.3; NM_006904.7; NP_008835.5.
DR UCSC; uc033bkh.1; human. [P78527-1]
DR CTD; 5591; -.
DR DisGeNET; 5591; -.
DR GeneCards; PRKDC; -.
DR HGNC; HGNC:9413; PRKDC.
DR HPA; ENSG00000253729; Low tissue specificity.
DR MalaCards; PRKDC; -.
DR MIM; 600899; gene.
DR MIM; 615966; phenotype.
DR neXtProt; NX_P78527; -.
DR OpenTargets; ENSG00000253729; -.
DR Orphanet; 317425; Severe combined immunodeficiency due to DNA-PKcs deficiency.
DR PharmGKB; PA33776; -.
DR VEuPathDB; HostDB:ENSG00000253729; -.
DR eggNOG; KOG0891; Eukaryota.
DR GeneTree; ENSGT00940000155633; -.
DR HOGENOM; CLU_224534_0_0_1; -.
DR InParanoid; P78527; -.
DR OMA; GIQIFMQ; -.
DR OrthoDB; 26975at2759; -.
DR PhylomeDB; P78527; -.
DR TreeFam; TF324494; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; P78527; -.
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-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR SignaLink; P78527; -.
DR SIGNOR; P78527; -.
DR BioGRID-ORCS; 5591; 63 hits in 314 CRISPR screens.
DR ChiTaRS; PRKDC; human.
DR GeneWiki; DNA-PKcs; -.
DR GenomeRNAi; 5591; -.
DR Pharos; P78527; Tchem.
DR PRO; PR:P78527; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P78527; protein.
DR Bgee; ENSG00000253729; Expressed in ventricular zone and 204 other tissues.
DR ExpressionAtlas; P78527; baseline and differential.
DR Genevisible; P78527; 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:0005958; C:DNA-dependent protein kinase-DNA ligase 4 complex; IDA:MGI.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0070419; C:nonhomologous end joining complex; IDA:UniProtKB.
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:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004677; F:DNA-dependent protein kinase activity; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:CAFA.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0004672; F:protein kinase activity; IDA:CACAO.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0034511; F:U3 snoRNA binding; IDA:UniProtKB.
DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
DR GO; GO:0002326; P:B cell lineage commitment; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
DR GO; GO:0006302; P:double-strand break repair; IMP:BHF-UCL.
DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; TAS:BHF-UCL.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0002327; P:immature B cell differentiation; IEA:Ensembl.
DR GO; GO:0033152; P:immunoglobulin V(D)J recombination; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IDA:UniProtKB.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CACAO.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045621; P:positive regulation of lymphocyte differentiation; ISS:UniProtKB.
DR GO; GO:1905221; P:positive regulation of platelet formation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0002328; P:pro-B cell differentiation; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; IMP:UniProtKB.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0034462; P:small-subunit processome assembly; IDA:UniProtKB.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0002360; P:T cell lineage commitment; IEA:Ensembl.
DR GO; GO:0033153; P:T cell receptor V(D)J recombination; IEA:Ensembl.
DR GO; GO:0016233; P:telomere capping; IMP:BHF-UCL.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR CDD; cd05172; PIKKc_DNA-PK; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR037706; DNA-PK_dom.
DR InterPro; IPR012582; DNAPKcs_CC3.
DR InterPro; IPR045581; DNAPKcs_CC5.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR Pfam; PF19704; DNAPKcs_CC5; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08163; NUC194; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM01344; NUC194; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Biological rhythms; Disease variant; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Immunity; Innate immunity; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribosome biogenesis; SCID; Serine/threonine-protein kinase; TPR repeat;
KW Transferase; Ubl conjugation.
FT CHAIN 1..4128
FT /note="DNA-dependent protein kinase catalytic subunit"
FT /id="PRO_0000225598"
FT REPEAT 288..323
FT /note="HEAT 1"
FT REPEAT 1004..1040
FT /note="HEAT 2"
FT REPEAT 1723..1756
FT /note="TPR 1"
FT DOMAIN 2906..3539
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT REPEAT 2920..2948
FT /note="TPR 2"
FT REPEAT 2949..2982
FT /note="TPR 3"
FT DOMAIN 3722..4053
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 4096..4128
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 1503..1538
FT /note="Interaction with C1D"
FT /evidence="ECO:0000269|PubMed:9679063"
FT REGION 1503..1538
FT /note="Leucine-zipper"
FT REGION 2050..2073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2436..3212
FT /note="KIP-binding"
FT /evidence="ECO:0000269|PubMed:9372844"
FT REGION 3200..3222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3728..3734
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3919..3927
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3939..3964
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT SITE 2020..2021
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000269|PubMed:8804412"
FT MOD_RES 117
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 828
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 841
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1209
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1970
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2056
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:14734805,
FT ECO:0000269|PubMed:22977523"
FT MOD_RES 2259
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2535
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2609
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12186630,
FT ECO:0000269|PubMed:12231622, ECO:0000269|PubMed:14734805,
FT ECO:0000269|PubMed:32103174"
FT MOD_RES 2612
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12186630,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2638
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12186630,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2647
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12186630,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 3205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 3241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 3260
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 3621
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 3638
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 3642
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 3731
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 3821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 4026
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 3799..3829
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.10"
FT /id="VSP_004708"
FT VARIANT 6
FT /note="A -> S (in dbSNP:rs8177999)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_019179"
FT VARIANT 263
FT /note="K -> N (in a lung adenocarcinoma sample; somatic
FT mutation; dbSNP:rs758032015)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041602"
FT VARIANT 333
FT /note="M -> I (in dbSNP:rs8178017)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_019180"
FT VARIANT 420
FT /note="V -> I (in dbSNP:rs55925466)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041603"
FT VARIANT 500
FT /note="G -> S (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041604"
FT VARIANT 605
FT /note="T -> S (in dbSNP:rs8178033)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_019181"
FT VARIANT 649
FT /note="F -> L (in dbSNP:rs55811715)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041605"
FT VARIANT 680
FT /note="I -> M (in dbSNP:rs8178040)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019182"
FT VARIANT 695
FT /note="P -> S (in dbSNP:rs8178046)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_019183"
FT VARIANT 1071
FT /note="N -> S (in dbSNP:rs8178070)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019184"
FT VARIANT 1136
FT /note="R -> H (in a colorectal adenocarcinoma sample;
FT somatic mutation; dbSNP:rs781401034)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041606"
FT VARIANT 1190
FT /note="L -> V (in dbSNP:rs34598508)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041607"
FT VARIANT 1237
FT /note="A -> T (in dbSNP:rs191531119)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041608"
FT VARIANT 1279
FT /note="L -> F"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041609"
FT VARIANT 1314
FT /note="G -> V (in dbSNP:rs8178090)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019185"
FT VARIANT 1447
FT /note="R -> M (in a lung squamous cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041610"
FT VARIANT 1588
FT /note="D -> V (in dbSNP:rs8178104)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019186"
FT VARIANT 1603
FT /note="Q -> H (in dbSNP:rs8178106)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019187"
FT VARIANT 1619
FT /note="A -> G (in dbSNP:rs56182356)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041611"
FT VARIANT 1680
FT /note="A -> V (in a metastatic melanoma sample; somatic
FT mutation; dbSNP:rs55735910)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041612"
FT VARIANT 2023
FT /note="S -> P (in dbSNP:rs56042895)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041613"
FT VARIANT 2095
FT /note="A -> V (in dbSNP:rs8178147)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019188"
FT VARIANT 2598
FT /note="R -> Q (in dbSNP:rs55923149)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041614"
FT VARIANT 2702
FT /note="K -> E (in dbSNP:rs8178178)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019189"
FT VARIANT 2810
FT /note="S -> N (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041615"
FT VARIANT 2899
FT /note="R -> C (in dbSNP:rs4278157)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_019190"
FT VARIANT 2941
FT /note="G -> A (in a lung neuroendocrine carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041616"
FT VARIANT 3062
FT /note="L -> R (in IMD26; shows increased long palindromic
FT (P)-nucleotide stretches in the immunoglobulin coding
FT joints indicating a defect in hairpin opening and
FT insufficient DCLRE1C activation; dbSNP:rs587777685)"
FT /evidence="ECO:0000269|PubMed:19075392"
FT /id="VAR_072569"
FT VARIANT 3085
FT /note="E -> D (in dbSNP:rs56135402)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041617"
FT VARIANT 3149
FT /note="G -> D (in dbSNP:rs8178208)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_019191"
FT VARIANT 3198
FT /note="T -> S (in dbSNP:rs55793951)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041618"
FT VARIANT 3201
FT /note="P -> S (in dbSNP:rs8178216)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_019192"
FT VARIANT 3404
FT /note="G -> E (in dbSNP:rs8178225)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_019193"
FT VARIANT 3434
FT /note="I -> T (in dbSNP:rs7830743)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_019194"
FT VARIANT 3459
FT /note="N -> S (in dbSNP:rs8178228)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019195"
FT VARIANT 3562
FT /note="L -> M (in dbSNP:rs8178232)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_019196"
FT VARIANT 3574
FT /note="A -> V (in IMD26; shows impaired function in
FT response to irradiation and a less severe defect in V(D)J
FT end-joining suggesting that the missense mutation retained
FT some functional capacity; consistent with a loss of
FT function mutation; dbSNP:rs587777686)"
FT /evidence="ECO:0000269|PubMed:23722905"
FT /id="VAR_072570"
FT VARIANT 3584
FT /note="L -> F (in dbSNP:rs55866966)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041619"
FT VARIANT 3702
FT /note="P -> L (in dbSNP:rs8178236)"
FT /id="VAR_050534"
FT VARIANT 3800
FT /note="L -> I (in dbSNP:rs56216442)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041620"
FT VARIANT 3836
FT /note="P -> L (in dbSNP:rs8178245)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_019197"
FT VARIANT 3932
FT /note="M -> V (in dbSNP:rs8178248)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019198"
FT VARIANT 3936
FT /note="G -> S (in dbSNP:rs55670423)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041621"
FT VARIANT 3937
FT /note="V -> M (in dbSNP:rs56090750)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041622"
FT MUTAGEN 1510
FT /note="L->P: Loss of interaction with C1D."
FT /evidence="ECO:0000269|PubMed:9679063"
FT MUTAGEN 1516..1517
FT /note="EL->PD: Loss of interaction with C1D."
FT /evidence="ECO:0000269|PubMed:9679063"
FT MUTAGEN 2609
FT /note="T->A: Leads to radiation sensitivity and impaired
FT DSB joining. Gives rise to reduced phosphorylation; when
FT associated with A-2612."
FT /evidence="ECO:0000269|PubMed:12231622"
FT MUTAGEN 2612
FT /note="S->A: Reduced phosphorylation; when associated with
FT A-2609."
FT MUTAGEN 2638
FT /note="T->A: Alleviates phosphorylation, leaves a fully
FT active enzyme with compromised cellular resistance to
FT ionizing radiation without affecting DNA end joining; when
FT associated with A-2647."
FT /evidence="ECO:0000269|PubMed:12649176"
FT MUTAGEN 2647
FT /note="T->A: Alleviates phosphorylation, leaves a fully
FT active enzyme with compromised cellular resistance to
FT ionizing radiation without affecting DNA end joining; when
FT associated with A-2638."
FT /evidence="ECO:0000269|PubMed:12649176"
FT CONFLICT 405
FT /note="D -> Y (in Ref. 2; AAC50210)"
FT /evidence="ECO:0000305"
FT CONFLICT 1008
FT /note="A -> S (in Ref. 2; AAC50210)"
FT /evidence="ECO:0000305"
FT CONFLICT 3660
FT /note="N -> T (in Ref. 8; AAA79184)"
FT /evidence="ECO:0000305"
FT CONFLICT 3817
FT /note="L -> W (in Ref. 8; AAA79184)"
FT /evidence="ECO:0000305"
FT CONFLICT 3862
FT /note="A -> P (in Ref. 8; AAA79184)"
FT /evidence="ECO:0000305"
FT CONFLICT 4031
FT /note="I -> V (in Ref. 9; AAK40350)"
FT /evidence="ECO:0000305"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:7SU3"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 64..70
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 76..96
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6ZFP"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 154..161
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:7OTW"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 192..206
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:7SU3"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:7SGL"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:7OTM"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 290..301
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 308..329
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 335..350
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 357..368
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 371..376
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:6ZFP"
FT HELIX 380..395
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:7OTW"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 410..423
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 432..444
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:7SGL"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 454..468
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 473..492
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:7SGL"
FT STRAND 513..518
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 528..534
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 540..544
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:7OTW"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 560..577
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 608..611
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 612..616
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 617..633
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 634..636
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 639..642
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 643..645
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 646..659
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 664..678
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 679..685
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 698..717
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 718..720
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 725..733
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 738..758
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 759..761
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 763..779
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 782..785
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 786..788
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 789..792
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 793..795
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 797..799
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 800..804
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 815..821
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 828..837
FT /evidence="ECO:0007829|PDB:7SU3"
FT HELIX 848..861
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 864..866
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 867..872
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 873..876
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 877..879
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 881..883
FT /evidence="ECO:0007829|PDB:7OTW"
FT STRAND 886..889
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 893..895
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 904..907
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 908..910
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 911..920
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 923..925
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 926..944
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 950..952
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 959..973
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 978..996
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1000..1002
FT /evidence="ECO:0007829|PDB:7SGL"
FT TURN 1003..1007
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1008..1014
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 1015..1017
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1019..1021
FT /evidence="ECO:0007829|PDB:6ZFP"
FT HELIX 1024..1043
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1046..1049
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1056..1067
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1072..1085
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 1086..1091
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1093..1113
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1114..1116
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 1119..1121
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 1123..1140
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1142..1145
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1165..1174
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1175..1177
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1181..1194
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1195..1197
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1198..1200
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 1204..1214
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1218..1225
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1228..1232
FT /evidence="ECO:0007829|PDB:7OTW"
FT TURN 1235..1237
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1239..1243
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1245..1247
FT /evidence="ECO:0007829|PDB:7SU3"
FT STRAND 1248..1250
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 1253..1272
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1274..1276
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1278..1281
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1282..1286
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1290..1298
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1300..1303
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 1309..1311
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1317..1319
FT /evidence="ECO:0007829|PDB:7OTW"
FT TURN 1324..1326
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1327..1350
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1355..1358
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 1359..1362
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1365..1377
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1379..1382
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1391..1408
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 1409..1411
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 1412..1420
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1425..1432
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1437..1440
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1442..1461
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1464..1467
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1472..1475
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1477..1480
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1482..1486
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1488..1490
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1494..1496
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1504..1506
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1507..1519
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1521..1523
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1525..1532
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1555..1573
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1575..1584
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 1585..1589
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1592..1606
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 1607..1610
FT /evidence="ECO:0007829|PDB:7SU3"
FT HELIX 1612..1624
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1626..1629
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 1630..1632
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1634..1637
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 1639..1655
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1658..1660
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1662..1667
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1668..1679
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1682..1684
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 1686..1692
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1693..1695
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 1696..1698
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 1699..1701
FT /evidence="ECO:0007829|PDB:7SU3"
FT TURN 1703..1706
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1707..1721
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1724..1726
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1734..1753
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1756..1766
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1769..1771
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1775..1785
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 1786..1788
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1791..1805
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1814..1821
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1824..1828
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 1832..1834
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1835..1852
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 1856..1861
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 1863..1881
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1882..1884
FT /evidence="ECO:0007829|PDB:6ZFP"
FT HELIX 1886..1889
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1890..1893
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1894..1897
FT /evidence="ECO:0007829|PDB:7SU3"
FT TURN 1899..1901
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1906..1908
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 1911..1924
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1931..1933
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1934..1955
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1959..1966
FT /evidence="ECO:0007829|PDB:7SGL"
FT STRAND 1967..1969
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 1971..1973
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 1974..1976
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 1978..1980
FT /evidence="ECO:0007829|PDB:7SGL"
FT STRAND 1984..1986
FT /evidence="ECO:0007829|PDB:7SGL"
FT STRAND 1992..1996
FT /evidence="ECO:0007829|PDB:7SU3"
FT HELIX 1999..2013
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 2026..2028
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 2036..2044
FT /evidence="ECO:0007829|PDB:7SGL"
FT STRAND 2087..2090
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 2091..2093
FT /evidence="ECO:0007829|PDB:7SU3"
FT HELIX 2094..2105
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2124..2134
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2140..2152
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 2153..2157
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2158..2160
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 2161..2171
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 2173..2182
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2184..2195
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 2196..2199
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2206..2221
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2228..2244
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 2245..2248
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2255..2260
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2269..2282
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 2292..2294
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 2297..2305
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2306..2308
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2313..2332
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 2335..2337
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 2338..2353
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 2354..2356
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 2358..2368
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2372..2377
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2379..2385
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2386..2388
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2392..2403
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 2404..2407
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2413..2417
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2420..2424
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2430..2442
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2443..2445
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2448..2458
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2459..2461
FT /evidence="ECO:0007829|PDB:7OTW"
FT STRAND 2467..2469
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2470..2483
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 2487..2490
FT /evidence="ECO:0007829|PDB:7OTW"
FT STRAND 2492..2494
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 2495..2508
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2509..2511
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2515..2525
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 2528..2530
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2535..2543
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2548..2550
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2551..2563
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2564..2567
FT /evidence="ECO:0007829|PDB:7SGL"
FT TURN 2570..2573
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2581..2583
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 2594..2602
FT /evidence="ECO:0007829|PDB:7SGL"
FT STRAND 2634..2636
FT /evidence="ECO:0007829|PDB:7SGL"
FT STRAND 2658..2660
FT /evidence="ECO:0007829|PDB:7SU3"
FT STRAND 2721..2723
FT /evidence="ECO:0007829|PDB:7SU3"
FT HELIX 2736..2763
FT /evidence="ECO:0007829|PDB:7SU3"
FT TURN 2764..2766
FT /evidence="ECO:0007829|PDB:7SU3"
FT STRAND 2772..2774
FT /evidence="ECO:0007829|PDB:7SGL"
FT TURN 2777..2779
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 2788..2798
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2802..2823
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2826..2846
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2852..2864
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 2868..2871
FT /evidence="ECO:0007829|PDB:7K11"
FT HELIX 2873..2883
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2886..2898
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2918..2932
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2936..2946
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2952..2961
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2965..2976
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 2982..2984
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 2988..3004
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3008..3013
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3014..3016
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3019..3024
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3027..3031
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3032..3036
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3038..3040
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3041..3054
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3060..3069
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3072..3074
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3075..3079
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3083..3092
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3096..3116
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3122..3130
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3133..3145
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3147..3149
FT /evidence="ECO:0007829|PDB:7SU3"
FT STRAND 3151..3153
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3154..3166
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3171..3173
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3176..3193
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3194..3196
FT /evidence="ECO:0007829|PDB:7OTM"
FT TURN 3227..3229
FT /evidence="ECO:0007829|PDB:6ZFP"
FT HELIX 3231..3248
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3252..3260
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3263..3265
FT /evidence="ECO:0007829|PDB:7OTW"
FT STRAND 3266..3271
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3272..3286
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3288..3290
FT /evidence="ECO:0007829|PDB:7SU3"
FT TURN 3291..3293
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3294..3306
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3308..3310
FT /evidence="ECO:0007829|PDB:7SU3"
FT TURN 3314..3316
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3319..3322
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3323..3343
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3346..3351
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3354..3363
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3364..3366
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3370..3392
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3403..3405
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 3407..3428
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3434..3439
FT /evidence="ECO:0007829|PDB:7SU3"
FT HELIX 3442..3455
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3459..3462
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3465..3471
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3472..3474
FT /evidence="ECO:0007829|PDB:7SU3"
FT HELIX 3476..3479
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3481..3487
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3488..3490
FT /evidence="ECO:0007829|PDB:7K11"
FT HELIX 3494..3498
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3499..3505
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3507..3510
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3512..3514
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3515..3524
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3526..3528
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 3530..3537
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3545..3547
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3548..3562
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3564..3566
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 3567..3575
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3576..3578
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3581..3593
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3595..3599
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3602..3604
FT /evidence="ECO:0007829|PDB:7K10"
FT TURN 3605..3608
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3609..3616
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3617..3619
FT /evidence="ECO:0007829|PDB:7K11"
FT HELIX 3621..3626
FT /evidence="ECO:0007829|PDB:7K11"
FT HELIX 3627..3635
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3636..3639
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3640..3643
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3647..3649
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3650..3652
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 3658..3670
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3671..3673
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3681..3683
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3687..3689
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3694..3696
FT /evidence="ECO:0007829|PDB:7OTW"
FT STRAND 3707..3711
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3713..3715
FT /evidence="ECO:0007829|PDB:7SGL"
FT STRAND 3718..3722
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3730..3733
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3736..3742
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3743..3745
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3746..3752
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3759..3777
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3779..3783
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3793..3797
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3800..3804
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3807..3811
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3812..3817
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3822..3829
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3835..3845
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3847..3849
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3854..3861
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3864..3875
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3876..3878
FT /evidence="ECO:0007829|PDB:7K11"
FT HELIX 3882..3889
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3890..3893
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 3894..3918
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3927..3931
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3932..3934
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3937..3939
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3945..3947
FT /evidence="ECO:0007829|PDB:7SU3"
FT HELIX 3948..3951
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 3952..3955
FT /evidence="ECO:0007829|PDB:7OTW"
FT STRAND 3959..3961
FT /evidence="ECO:0007829|PDB:6ZFP"
FT HELIX 3965..3970
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 3971..3973
FT /evidence="ECO:0007829|PDB:7SGL"
FT TURN 3976..3978
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3979..3993
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 3995..4007
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 4009..4011
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 4013..4021
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 4027..4029
FT /evidence="ECO:0007829|PDB:7SU3"
FT STRAND 4030..4032
FT /evidence="ECO:0007829|PDB:7SGL"
FT HELIX 4034..4036
FT /evidence="ECO:0007829|PDB:7K11"
FT HELIX 4041..4050
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 4051..4053
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 4056..4067
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 4068..4070
FT /evidence="ECO:0007829|PDB:7OTW"
FT HELIX 4074..4082
FT /evidence="ECO:0007829|PDB:7OTY"
FT TURN 4085..4087
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 4091..4093
FT /evidence="ECO:0007829|PDB:7OTY"
FT STRAND 4095..4097
FT /evidence="ECO:0007829|PDB:7K11"
FT HELIX 4100..4112
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 4114..4117
FT /evidence="ECO:0007829|PDB:7OTY"
FT HELIX 4122..4124
FT /evidence="ECO:0007829|PDB:7OTW"
SQ SEQUENCE 4128 AA; 469089 MW; AC6E747FEB09F3E5 CRC64;
MAGSGAGVRC SLLRLQETLS AADRCGAALA GHQLIRGLGQ ECVLSSSPAV LALQTSLVFS
RDFGLLVFVR KSLNSIEFRE CREEILKFLC IFLEKMGQKI APYSVEIKNT CTSVYTKDRA
AKCKIPALDL LIKLLQTFRS SRLMDEFKIG ELFSKFYGEL ALKKKIPDTV LEKVYELLGL
LGEVHPSEMI NNAENLFRAF LGELKTQMTS AVREPKLPVL AGCLKGLSSL LCNFTKSMEE
DPQTSREIFN FVLKAIRPQI DLKRYAVPSA GLRLFALHAS QFSTCLLDNY VSLFEVLLKW
CAHTNVELKK AALSALESFL KQVSNMVAKN AEMHKNKLQY FMEQFYGIIR NVDSNNKELS
IAIRGYGLFA GPCKVINAKD VDFMYVELIQ RCKQMFLTQT DTGDDRVYQM PSFLQSVASV
LLYLDTVPEV YTPVLEHLVV MQIDSFPQYS PKMQLVCCRA IVKVFLALAA KGPVLRNCIS
TVVHQGLIRI CSKPVVLPKG PESESEDHRA SGEVRTGKWK VPTYKDYVDL FRHLLSSDQM
MDSILADEAF FSVNSSSESL NHLLYDEFVK SVLKIVEKLD LTLEIQTVGE QENGDEAPGV
WMIPTSDPAA NLHPAKPKDF SAFINLVEFC REILPEKQAE FFEPWVYSFS YELILQSTRL
PLISGFYKLL SITVRNAKKI KYFEGVSPKS LKHSPEDPEK YSCFALFVKF GKEVAVKMKQ
YKDELLASCL TFLLSLPHNI IELDVRAYVP ALQMAFKLGL SYTPLAEVGL NALEEWSIYI
DRHVMQPYYK DILPCLDGYL KTSALSDETK NNWEVSALSR AAQKGFNKVV LKHLKKTKNL
SSNEAISLEE IRIRVVQMLG SLGGQINKNL LTVTSSDEMM KSYVAWDREK RLSFAVPFRE
MKPVIFLDVF LPRVTELALT ASDRQTKVAA CELLHSMVMF MLGKATQMPE GGQGAPPMYQ
LYKRTFPVLL RLACDVDQVT RQLYEPLVMQ LIHWFTNNKK FESQDTVALL EAILDGIVDP
VDSTLRDFCG RCIREFLKWS IKQITPQQQE KSPVNTKSLF KRLYSLALHP NAFKRLGASL
AFNNIYREFR EEESLVEQFV FEALVIYMES LALAHADEKS LGTIQQCCDA IDHLCRIIEK
KHVSLNKAKK RRLPRGFPPS ASLCLLDLVK WLLAHCGRPQ TECRHKSIEL FYKFVPLLPG
NRSPNLWLKD VLKEEGVSFL INTFEGGGCG QPSGILAQPT LLYLRGPFSL QATLCWLDLL
LAALECYNTF IGERTVGALQ VLGTEAQSSL LKAVAFFLES IAMHDIIAAE KCFGTGAAGN
RTSPQEGERY NYSKCTVVVR IMEFTTTLLN TSPEGWKLLK KDLCNTHLMR VLVQTLCEPA
SIGFNIGDVQ VMAHLPDVCV NLMKALKMSP YKDILETHLR EKITAQSIEE LCAVNLYGPD
AQVDRSRLAA VVSACKQLHR AGLLHNILPS QSTDLHHSVG TELLSLVYKG IAPGDERQCL
PSLDLSCKQL ASGLLELAFA FGGLCERLVS LLLNPAVLST ASLGSSQGSV IHFSHGEYFY
SLFSETINTE LLKNLDLAVL ELMQSSVDNT KMVSAVLNGM LDQSFRERAN QKHQGLKLAT
TILQHWKKCD SWWAKDSPLE TKMAVLALLA KILQIDSSVS FNTSHGSFPE VFTTYISLLA
DTKLDLHLKG QAVTLLPFFT SLTGGSLEEL RRVLEQLIVA HFPMQSREFP PGTPRFNNYV
DCMKKFLDAL ELSQSPMLLE LMTEVLCREQ QHVMEELFQS SFRRIARRGS CVTQVGLLES
VYEMFRKDDP RLSFTRQSFV DRSLLTLLWH CSLDALREFF STIVVDAIDV LKSRFTKLNE
STFDTQITKK MGYYKILDVM YSRLPKDDVH AKESKINQVF HGSCITEGNE LTKTLIKLCY
DAFTENMAGE NQLLERRRLY HCAAYNCAIS VICCVFNELK FYQGFLFSEK PEKNLLIFEN
LIDLKRRYNF PVEVEVPMER KKKYIEIRKE AREAANGDSD GPSYMSSLSY LADSTLSEEM
SQFDFSTGVQ SYSYSSQDPR PATGRFRRRE QRDPTVHDDV LELEMDELNR HECMAPLTAL
VKHMHRSLGP PQGEEDSVPR DLPSWMKFLH GKLGNPIVPL NIRLFLAKLV INTEEVFRPY
AKHWLSPLLQ LAASENNGGE GIHYMVVEIV ATILSWTGLA TPTGVPKDEV LANRLLNFLM
KHVFHPKRAV FRHNLEIIKT LVECWKDCLS IPYRLIFEKF SGKDPNSKDN SVGIQLLGIV
MANDLPPYDP QCGIQSSEYF QALVNNMSFV RYKEVYAAAA EVLGLILRYV MERKNILEES
LCELVAKQLK QHQNTMEDKF IVCLNKVTKS FPPLADRFMN AVFFLLPKFH GVLKTLCLEV
VLCRVEGMTE LYFQLKSKDF VQVMRHRDDE RQKVCLDIIY KMMPKLKPVE LRELLNPVVE
FVSHPSTTCR EQMYNILMWI HDNYRDPESE TDNDSQEIFK LAKDVLIQGL IDENPGLQLI
IRNFWSHETR LPSNTLDRLL ALNSLYSPKI EVHFLSLATN FLLEMTSMSP DYPNPMFEHP
LSECEFQEYT IDSDWRFRST VLTPMFVETQ ASQGTLQTRT QEGSLSARWP VAGQIRATQQ
QHDFTLTQTA DGRSSFDWLT GSSTDPLVDH TSPSSDSLLF AHKRSERLQR APLKSVGPDF
GKKRLGLPGD EVDNKVKGAA GRTDLLRLRR RFMRDQEKLS LMYARKGVAE QKREKEIKSE
LKMKQDAQVV LYRSYRHGDL PDIQIKHSSL ITPLQAVAQR DPIIAKQLFS SLFSGILKEM
DKFKTLSEKN NITQKLLQDF NRFLNTTFSF FPPFVSCIQD ISCQHAALLS LDPAAVSAGC
LASLQQPVGI RLLEEALLRL LPAELPAKRV RGKARLPPDV LRWVELAKLY RSIGEYDVLR
GIFTSEIGTK QITQSALLAE ARSDYSEAAK QYDEALNKQD WVDGEPTEAE KDFWELASLD
CYNHLAEWKS LEYCSTASID SENPPDLNKI WSEPFYQETY LPYMIRSKLK LLLQGEADQS
LLTFIDKAMH GELQKAILEL HYSQELSLLY LLQDDVDRAK YYIQNGIQSF MQNYSSIDVL
LHQSRLTKLQ SVQALTEIQE FISFISKQGN LSSQVPLKRL LNTWTNRYPD AKMDPMNIWD
DIITNRCFFL SKIEEKLTPL PEDNSMNVDQ DGDPSDRMEV QEQEEDISSL IRSCKFSMKM
KMIDSARKQN NFSLAMKLLK ELHKESKTRD DWLVSWVQSY CRLSHCRSRS QGCSEQVLTV
LKTVSLLDEN NVSSYLSKNI LAFRDQNILL GTTYRIIANA LSSEPACLAE IEEDKARRIL
ELSGSSSEDS EKVIAGLYQR AFQHLSEAVQ AAEEEAQPPS WSCGPAAGVI DAYMTLADFC
DQQLRKEEEN ASVIDSAELQ AYPALVVEKM LKALKLNSNE ARLKFPRLLQ IIERYPEETL
SLMTKEISSV PCWQFISWIS HMVALLDKDQ AVAVQHSVEE ITDNYPQAIV YPFIISSESY
SFKDTSTGHK NKEFVARIKS KLDQGGVIQD FINALDQLSN PELLFKDWSN DVRAELAKTP
VNKKNIEKMY ERMYAALGDP KAPGLGAFRR KFIQTFGKEF DKHFGKGGSK LLRMKLSDFN
DITNMLLLKM NKDSKPPGNL KECSPWMSDF KVEFLRNELE IPGQYDGRGK PLPEYHVRIA
GFDERVTVMA SLRRPKRIII RGHDEREHPF LVKGGEDLRQ DQRVEQLFQV MNGILAQDSA
CSQRALQLRT YSVVPMTSRL GLIEWLENTV TLKDLLLNTM SQEEKAAYLS DPRAPPCEYK
DWLTKMSGKH DVGAYMLMYK GANRTETVTS FRKRESKVPA DLLKRAFVRM STSPEAFLAL
RSHFASSHAL ICISHWILGI GDRHLNNFMV AMETGGVIGI DFGHAFGSAT QFLPVPELMP
FRLTRQFINL MLPMKETGLM YSIMVHALRA FRSDPGLLTN TMDVFVKEPS FDWKNFEQKM
LKKGGSWIQE INVAEKNWYP RQKICYAKRK LAGANPAVIT CDELLLGHEK APAFRDYVAV
ARGSKDHNIR AQEPESGLSE ETQVKCLMDQ ATDPNILGRT WEGWEPWM
