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Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Cell cycle checkpoint kinase) (Checkpoint kinase-1)

 CHK1_HUMAN              Reviewed;         476 AA.
O14757; A8K934; B4DDD0; B4DSK3; B5BTY6; F5H7S4; H2BI51;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
12-AUG-2020, entry version 229.
RecName: Full=Serine/threonine-protein kinase Chk1;
EC=2.7.11.1;
AltName: Full=CHK1 checkpoint homolog;
AltName: Full=Cell cycle checkpoint kinase;
AltName: Full=Checkpoint kinase-1;
Name=CHEK1; Synonyms=CHK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN PHOSPHORYLATION OF
CDC25A; CDC25B AND CDC25C, INTERACTION WITH CDC25A; CDC25B AND CDC25C,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-130, AND
VARIANT VAL-471.
PubMed=9278511; DOI=10.1126/science.277.5331.1497;
Sanchez Y., Wong C., Thoma R.S., Richman R., Wu Z., Piwnica-Worms H.,
Elledge S.J.;
"Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA
damage to Cdk regulation through Cdc25.";
Science 277:1497-1501(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
LOCATION, AND VARIANT VAL-471.
PubMed=9382850; DOI=10.1016/s0960-9822(06)00417-9;
Flaggs G., Plug A.W., Dunks K.M., Mundt K.E., Ford J.C., Quiggle M.R.E.,
Taylor E.M., Westphal C.H., Ashley T., Hoekstra M.F., Carr A.M.;
"Atm-dependent interactions of a mammalian chk1 homolog with meiotic
chromosomes.";
Curr. Biol. 7:977-986(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-471.
PubMed=10717241; DOI=10.3892/ijo.16.4.731;
Semba S., Ouyang H., Han S.-Y., Kato Y., Horii A.;
"Analysis of the candidate target genes for mutation in microsatellite
instability-positive cancers of the colorectum, stomach, and endometrium.";
Int. J. Oncol. 16:731-737(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
TISSUE=Fetal thymus;
PubMed=22184239; DOI=10.1073/pnas.1104767109;
Pabla N., Bhatt K., Dong Z.;
"Checkpoint kinase 1 (Chk1)-short is a splice variant and endogenous
inhibitor of Chk1 that regulates cell cycle and DNA damage checkpoints.";
Proc. Natl. Acad. Sci. U.S.A. 109:197-202(2012).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
VAL-471.
TISSUE=Brain, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-156 AND VAL-471.
NIEHS SNPs program;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-471.
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
Nomura N.;
"Human protein factory for converting the transcriptome into an in vitro-
expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
Hattori M., Rogers J., Lander E.S., Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-471.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-471.
TISSUE=Bone marrow, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
FUNCTION IN PHOSPHORYLATION OF TP53, AND MUTAGENESIS OF ASP-130.
PubMed=10673501;
Shieh S.-Y., Ahn J., Tamai K., Taya Y., Prives C.;
"The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2)
phosphorylate p53 at multiple DNA damage-inducible sites.";
Genes Dev. 14:289-300(2000).
[12]
ERRATUM OF PUBMED:10673501.
Shieh S.-Y., Ahn J., Tamai K., Taya Y., Prives C.;
Genes Dev. 14:750-750(2000).
[13]
PHOSPHORYLATION AT SER-345 BY ATR.
PubMed=10859164;
Liu Q., Guntuku S., Cui X.-S., Matsuoka S., Cortez D., Tamai K., Luo G.,
Carattini-Rivera S., DeMayo F., Bradley A., Donehower L.A., Elledge S.J.;
"Chk1 is an essential kinase that is regulated by Atr and required for the
G(2)/M DNA damage checkpoint.";
Genes Dev. 14:1448-1459(2000).
[14]
FUNCTION IN DNA REPLICATION, PHOSPHORYLATION BY ATR, AND MUTAGENESIS OF
ASP-130.
PubMed=11535615; DOI=10.1083/jcb.200104099;
Feijoo C., Hall-Jackson C., Wu R., Jenkins D., Leitch J., Gilbert D.M.,
Smythe C.;
"Activation of mammalian Chk1 during DNA replication arrest: a role for
Chk1 in the intra-S phase checkpoint monitoring replication origin
firing.";
J. Cell Biol. 154:913-923(2001).
[15]
PHOSPHORYLATION AT SER-317 AND SER-345, AND MUTAGENESIS OF ASP-130;
SER-317; SER-345; SER-357; SER-366 AND SER-468.
PubMed=11390642; DOI=10.1128/mcb.21.13.4129-4139.2001;
Zhao H., Piwnica-Worms H.;
"ATR-mediated checkpoint pathways regulate phosphorylation and activation
of human Chk1.";
Mol. Cell. Biol. 21:4129-4139(2001).
[16]
SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF ASP-130.
PubMed=11821419; DOI=10.1074/jbc.m111705200;
O'Neill T., Giarratani L., Chen P., Iyer L., Lee C.-H., Bobiak M.,
Kanai F., Zhou B.-B., Chung J.H., Rathbun G.A.;
"Determination of substrate motifs for human Chk1 and hCds1/Chk2 by the
oriented peptide library approach.";
J. Biol. Chem. 277:16102-16115(2002).
[17]
ERRATUM OF PUBMED:11821419.
O'Neill T., Giarratani L., Chen P., Iyer L., Lee C.-H., Bobiak M.,
Kanai F., Zhou B.-B., Chung J.H., Rathbun G.A.;
J. Biol. Chem. 277:35776-35777(2002).
[18]
FUNCTION IN DNA DAMAGE RESPONSE, PHOSPHORYLATION AT SER-317 AND SER-345,
AND MUTAGENESIS OF LYS-38.
PubMed=12446774; DOI=10.1128/mcb.22.24.8552-8561.2002;
Heffernan T.P., Simpson D.A., Frank A.R., Heinloth A.N., Paules R.S.,
Cordeiro-Stone M., Kaufmann W.K.;
"An ATR- and Chk1-dependent S checkpoint inhibits replicon initiation
following UVC-induced DNA damage.";
Mol. Cell. Biol. 22:8552-8561(2002).
[19]
SUBCELLULAR LOCATION, AND INTERACTION WITH BRCA1.
PubMed=11836499; DOI=10.1038/ng837;
Yarden R.I., Pardo-Reoyo S., Sgagias M., Cowan K.H., Brody L.C.;
"BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon DNA
damage.";
Nat. Genet. 30:285-289(2002).
[20]
FUNCTION IN DNA DAMAGE RESPONSE.
PubMed=12399544; DOI=10.1073/pnas.182557299;
Zhao H., Watkins J.L., Piwnica-Worms H.;
"Disruption of the checkpoint kinase 1/cell division cycle 25A pathway
abrogates ionizing radiation-induced S and G2 checkpoints.";
Proc. Natl. Acad. Sci. U.S.A. 99:14795-14800(2002).
[21]
FUNCTION IN CDC25A TURNOVER, PHOSPHORYLATION AT SER-317 AND SER-345, AND
MUTAGENESIS OF SER-317 AND SER-345.
PubMed=12676583; DOI=10.1016/s1535-6108(03)00048-5;
Soerensen C.S., Syljuaesen R.G., Falck J., Schroeder T., Roennstrand L.,
Khanna K.K., Zhou B.-B., Bartek J., Lukas J.;
"Chk1 regulates the S phase checkpoint by coupling the physiological
turnover and ionizing radiation-induced accelerated proteolysis of
Cdc25A.";
Cancer Cell 3:247-258(2003).
[22]
FUNCTION IN PHOSPHORYLATION OF TLK1, AND PHOSPHORYLATION AT SER-317.
PubMed=12660173; DOI=10.1093/emboj/cdg151;
Groth A., Lukas J., Nigg E.A., Sillje H.H.W., Wernstedt C., Bartek J.,
Hansen K.;
"Human tousled like kinases are targeted by an ATM- and Chk1-dependent DNA
damage checkpoint.";
EMBO J. 22:1676-1687(2003).
[23]
FUNCTION IN CDC25A TURNOVER, AND MUTAGENESIS OF ASP-130.
PubMed=14681206; DOI=10.1101/gad.1157503;
Jin J., Shirogane T., Xu L., Nalepa G., Qin J., Elledge S.J., Harper J.W.;
"SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein
phosphatase.";
Genes Dev. 17:3062-3074(2003).
[24]
PHOSPHORYLATION AT SER-317, AND MUTAGENESIS OF ASP-130; SER-317 AND
SER-345.
PubMed=12588868; DOI=10.1074/jbc.m210862200;
Gatei M., Sloper K., Soerensen C., Syljuaesen R., Falck J., Hobson K.,
Savage K., Lukas J., Zhou B.-B., Bartek J., Khanna K.K.;
"Ataxia-telangiectasia-mutated (ATM) and NBS1-dependent phosphorylation of
Chk1 on ser-317 in response to ionizing radiation.";
J. Biol. Chem. 278:14806-14811(2003).
[25]
FUNCTION IN CDC25A TURNOVER, AND PHOSPHORYLATION AT SER-345.
PubMed=12676925; DOI=10.1074/jbc.m300229200;
Xiao Z., Chen Z., Gunasekera A.H., Sowin T.J., Rosenberg S.H., Fesik S.,
Zhang H.;
"Chk1 mediates S and G2 arrests through Cdc25A degradation in response to
DNA-damaging agents.";
J. Biol. Chem. 278:21767-21773(2003).
[26]
INTERACTION WITH YWHAZ AND XPO1, SUBCELLULAR LOCATION, ASSOCIATION WITH
CHROMATIN, PHOSPHORYLATION AT SER-317 AND SER-345, AND MUTAGENESIS OF
SER-317; PHE-344; SER-345 AND MET-353.
PubMed=12676962; DOI=10.1074/jbc.m300070200;
Jiang K., Pereira E., Maxfield M., Russell B., Goudelock D.M., Sanchez Y.;
"Regulation of Chk1 includes chromatin association and 14-3-3 binding
following phosphorylation on ser-345.";
J. Biol. Chem. 278:25207-25217(2003).
[27]
FUNCTION IN CDC25A TURNOVER.
PubMed=12759351; DOI=10.1074/jbc.m302704200;
Hassepass I., Voit R., Hoffmann I.;
"Phosphorylation at serine 75 is required for UV-mediated degradation of
human Cdc25A phosphatase at the S-phase checkpoint.";
J. Biol. Chem. 278:29824-29829(2003).
[28]
INTERACTION WITH CLSPN.
PubMed=12766152; DOI=10.1074/jbc.m301136200;
Chini C.C.S., Chen J.;
"Human claspin is required for replication checkpoint control.";
J. Biol. Chem. 278:30057-30062(2003).
[29]
FUNCTION IN MITOSIS, AND FUNCTION IN PHOSPHORYLATION OF CDC25A.
PubMed=14559997; DOI=10.1128/mcb.23.21.7488-7497.2003;
Chen M.-S., Ryan C.E., Piwnica-Worms H.;
"Chk1 kinase negatively regulates mitotic function of Cdc25A phosphatase
through 14-3-3 binding.";
Mol. Cell. Biol. 23:7488-7497(2003).
[30]
REGULATION OF TLK1.
PubMed=12955071; DOI=10.1038/sj.onc.1206691;
Krause D.R., Jonnalagadda J.C., Gatei M.H., Sillje H.H.W., Zhou B.-B.,
Nigg E.A., Khanna K.;
"Suppression of tousled-like kinase activity after DNA damage or
replication block requires ATM, NBS1 and Chk1.";
Oncogene 22:5927-5937(2003).
[31]
PHOSPHORYLATION AT SER-317.
PubMed=14657349; DOI=10.1073/pnas.2536810100;
Wang Y., Qin J.;
"MSH2 and ATR form a signaling module and regulate two branches of the
damage response to DNA methylation.";
Proc. Natl. Acad. Sci. U.S.A. 100:15387-15392(2003).
[32]
FUNCTION, AND PHOSPHORYLATION AT SER-345.
PubMed=14988723; DOI=10.1038/sj.emboj.7600113;
Pichierri P., Rosselli F.;
"The DNA crosslink-induced S-phase checkpoint depends on ATR-CHK1 and ATR-
NBS1-FANCD2 pathways.";
EMBO J. 23:1178-1187(2004).
[33]
DOMAIN, MITOTIC PHOSPHORYLATION, PHOSPHORYLATION AT SER-345, AND
MUTAGENESIS OF LYS-38.
PubMed=14681223; DOI=10.1074/jbc.m312215200;
Ng C.-P., Lee H.C., Ho C.W., Arooz T., Siu W.Y., Lau A., Poon R.Y.C.;
"Differential mode of regulation of the checkpoint kinases CHK1 and CHK2 by
their regulatory domains.";
J. Biol. Chem. 279:8808-8819(2004).
[34]
FUNCTION IN MITOSIS, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-130.
PubMed=15311285; DOI=10.1038/ncb1165;
Kraemer A., Mailand N., Lukas C., Syljuaesen R.G., Wilkinson C.J.,
Nigg E.A., Bartek J., Lukas J.;
"Centrosome-associated Chk1 prevents premature activation of cyclin-B-Cdk1
kinase.";
Nat. Cell Biol. 6:884-891(2004).
[35]
INTERACTION WITH CLSPN, AND PHOSPHORYLATION AT SER-296; SER-317 AND
SER-345.
PubMed=15707391; DOI=10.1042/bj20041966;
Clarke C.A.L., Clarke P.R.;
"DNA-dependent phosphorylation of Chk1 and claspin in a human cell-free
system.";
Biochem. J. 388:705-712(2005).
[36]
SUBCELLULAR LOCATION.
PubMed=15710331; DOI=10.1016/j.ccr.2005.01.009;
Puc J., Keniry M., Li H.S., Pandita T.K., Choudhury A.D., Memeo L.,
Mansukhani M., Murty V.V.V.S., Gaciong Z., Meek S.E.M., Piwnica-Worms H.,
Hibshoosh H., Parsons R.;
"Lack of PTEN sequesters CHK1 and initiates genetic instability.";
Cancer Cell 7:193-204(2005).
[37]
INTERACTION WITH PPM1D, PHOSPHORYLATION AT SER-317 AND SER-345, AND
DEPHOSPHORYLATION BY PPM1D.
PubMed=15870257; DOI=10.1101/gad.1291305;
Lu X., Nannenga B., Donehower L.A.;
"PPM1D dephosphorylates Chk1 and p53 and abrogates cell cycle
checkpoints.";
Genes Dev. 19:1162-1174(2005).
[38]
FUNCTION IN PHOSPHORYLATION OF TP53, AND FUNCTION IN TP53-DEPENDENT
TRANSCRIPTION.
PubMed=15659650; DOI=10.1091/mbc.e04-08-0689;
Ou Y.-H., Chung P.-H., Sun T.-P., Shieh S.-Y.;
"p53 C-terminal phosphorylation by CHK1 and CHK2 participates in the
regulation of DNA-damage-induced C-terminal acetylation.";
Mol. Biol. Cell 16:1684-1695(2005).
[39]
INTERACTION WITH TIMELESS.
PubMed=15798197; DOI=10.1128/mcb.25.8.3109-3116.2005;
Uensal-Kacmaz K., Mullen T.E., Kaufmann W.K., Sancar A.;
"Coupling of human circadian and cell cycles by the timeless protein.";
Mol. Cell. Biol. 25:3109-3116(2005).
[40]
FUNCTION IN HOMOLOGOUS RECOMBINATION REPAIR, FUNCTION IN PHOSPHORYLATION OF
RAD51, INTERACTION WITH RAD51, AND MUTAGENESIS OF SER-317 AND SER-345.
PubMed=15665856; DOI=10.1038/ncb1212;
Soerensen C.S., Hansen L.T., Dziegielewski J., Syljuaesen R.G., Lundin C.,
Bartek J., Helleday T.;
"The cell-cycle checkpoint kinase Chk1 is required for mammalian homologous
recombination repair.";
Nat. Cell Biol. 7:195-201(2005).
[41]
FUNCTION IN MITOTIC EXIT, AND PHOSPHORYLATION AT SER-345.
PubMed=15650047; DOI=10.1073/pnas.0409130102;
Huang X., Tran T., Zhang L., Hatcher R., Zhang P.;
"DNA damage-induced mitotic catastrophe is mediated by the Chk1-dependent
mitotic exit DNA damage checkpoint.";
Proc. Natl. Acad. Sci. U.S.A. 102:1065-1070(2005).
[42]
FUNCTION IN TP53 ACTIVATION, AND FUNCTION IN PHOSPHORYLATION OF MDM4.
PubMed=16511572; DOI=10.1038/sj.emboj.7601010;
Jin Y., Dai M.S., Lu S.Z., Xu Y., Luo Z., Zhao Y., Lu H.;
"14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1,
resulting in p53 activation.";
EMBO J. 25:1207-1218(2006).
[43]
FUNCTION IN PHOSPHORYLATION OF CLSPN, AND INTERACTION WITH CLSPN.
PubMed=16963448; DOI=10.1074/jbc.m604373200;
Chini C.C., Chen J.;
"Repeated phosphopeptide motifs in human Claspin are phosphorylated by Chk1
and mediate Claspin function.";
J. Biol. Chem. 281:33276-33282(2006).
[44]
FUNCTION IN PHOSPHORYLATION OF RB1.
PubMed=17380128; DOI=10.1038/sj.emboj.7601652;
Inoue Y., Kitagawa M., Taya Y.;
"Phosphorylation of pRB at Ser612 by Chk1/2 leads to a complex between pRB
and E2F-1 after DNA damage.";
EMBO J. 26:2083-2093(2007).
[45]
FUNCTION IN DNA CROSS-LINKS REPAIR, AND FUNCTION IN PHOSPHORYLATION OF
FANCE.
PubMed=17296736; DOI=10.1128/mcb.02357-06;
Wang X., Kennedy R.D., Ray K., Stuckert P., Ellenberger T., D'Andrea A.D.;
"Chk1-mediated phosphorylation of FANCE is required for the Fanconi
anemia/BRCA pathway.";
Mol. Cell. Biol. 27:3098-3108(2007).
[46]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[47]
FUNCTION IN APOPTOSIS.
PubMed=18510930; DOI=10.1016/j.cell.2008.03.037;
Sidi S., Sanda T., Kennedy R.D., Hagen A.T., Jette C.A., Hoffmans R.,
Pascual J., Imamura S., Kishi S., Amatruda J.F., Kanki J.P., Green D.R.,
D'Andrea A.A., Look A.T.;
"Chk1 suppresses a caspase-2 apoptotic response to DNA damage that bypasses
p53, Bcl-2, and caspase-3.";
Cell 133:864-877(2008).
[48]
FUNCTION IN PHOSPHORYLATION OF NEK6.
PubMed=18728393; DOI=10.4161/cc.7.17.6551;
Lee M.Y., Kim H.J., Kim M.A., Jee H.J., Kim A.J., Bae Y.S., Park J.I.,
Chung J.H., Yun J.;
"Nek6 is involved in G2/M phase cell cycle arrest through DNA damage-
induced phosphorylation.";
Cell Cycle 7:2705-2709(2008).
[49]
FUNCTION IN REPLICATION FORK MAINTENANCE, AND FUNCTION IN PCNA
UBIQUITINATION.
PubMed=18451105; DOI=10.1101/gad.1632808;
Yang X.H., Shiotani B., Classon M., Zou L.;
"Chk1 and Claspin potentiate PCNA ubiquitination.";
Genes Dev. 22:1147-1152(2008).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[51]
FUNCTION IN RAD51-MEDIATED DNA REPAIR, AND FUNCTION IN PHOSPHORYLATION OF
BRCA2 AND RAD51.
PubMed=18317453; DOI=10.1038/onc.2008.17;
Bahassi E.M., Ovesen J.L., Riesenberg A.L., Bernstein W.Z., Hasty P.E.,
Stambrook P.J.;
"The checkpoint kinases Chk1 and Chk2 regulate the functional associations
between hBRCA2 and Rad51 in response to DNA damage.";
Oncogene 27:3977-3985(2008).
[52]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286; SER-296 AND SER-301, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[53]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[54]
INTERACTION WITH CDK5RAP3.
PubMed=19223857; DOI=10.1038/cr.2009.14;
Jiang H., Wu J., He C., Yang W., Li H.;
"Tumor suppressor protein C53 antagonizes checkpoint kinases to promote
cyclin-dependent kinase 1 activation.";
Cell Res. 19:458-468(2009).
[55]
PHOSPHORYLATION AT SER-345, UBIQUITINATION AT LYS-436, INTERACTION WITH
FBXO6, AND MUTAGENESIS OF SER-345; ARG-372; ARG-376; ARG-379 AND LYS-436.
PubMed=19716789; DOI=10.1016/j.molcel.2009.06.030;
Zhang Y.-W., Brognard J., Coughlin C., You Z., Dolled-Filhart M.,
Aslanian A., Manning G., Abraham R.T., Hunter T.;
"The F box protein Fbx6 regulates Chk1 stability and cellular sensitivity
to replication stress.";
Mol. Cell 35:442-453(2009).
[56]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[57]
FUNCTION IN NEK11 PHOSPHORYLATION.
PubMed=19734889; DOI=10.1038/ncb1969;
Melixetian M., Klein D.K., Soerensen C.S., Helin K.;
"NEK11 regulates CDC25A degradation and the IR-induced G2/M checkpoint.";
Nat. Cell Biol. 11:1247-1253(2009).
[58]
INTERACTION WITH FEM1B.
PubMed=19330022; DOI=10.1038/onc.2009.58;
Sun T.P., Shieh S.Y.;
"Human FEM1B is required for Rad9 recruitment and CHK1 activation in
response to replication stress.";
Oncogene 28:1971-1981(2009).
[59]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[60]
FUNCTION IN CDC25A DEGRADATION.
PubMed=20090422; DOI=10.4161/cc.9.3.10513;
Soerensen C.S., Melixetian M., Klein D.K., Helin K.;
"NEK11: linking CHK1 and CDC25A in DNA damage checkpoint signaling.";
Cell Cycle 9:450-455(2010).
[61]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286; SER-296 AND SER-301, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[62]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[63]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[64]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-296; SER-301;
SER-331; SER-467 AND SER-468, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[65]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-289.
PubMed=10761933; DOI=10.1016/s0092-8674(00)80704-7;
Chen P., Luo C., Deng Y., Ryan K., Register J., Margosiak S.,
Tempczyk-Russell A., Nguyen B., Myers P., Lundgren K., Kan C.-C.,
O'Connor P.M.;
"The 1.7 A crystal structure of human cell cycle checkpoint kinase Chk1:
implications for Chk1 regulation.";
Cell 100:681-692(2000).
[66]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-289.
PubMed=12244092; DOI=10.1074/jbc.m201233200;
Zhao B., Bower M.J., McDevitt P.J., Zhao H., Davis S.T., Johanson K.O.,
Green S.M., Concha N.O., Zhou B.-B.S.;
"Structural basis for Chk1 inhibition by UCN-01.";
J. Biol. Chem. 277:46609-46615(2002).
[67]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-289.
PubMed=15974586; DOI=10.1021/jm049022c;
Foloppe N., Fisher L.M., Howes R., Kierstan P., Potter A.,
Robertson A.G.S., Surgenor A.E.;
"Structure-based design of novel Chk1 inhibitors: insights into hydrogen
bonding and protein-ligand affinity.";
J. Med. Chem. 48:4332-4345(2005).
[68]
VARIANTS [LARGE SCALE ANALYSIS] VAL-223 AND MET-312.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Serine/threonine-protein kinase which is required for
checkpoint-mediated cell cycle arrest and activation of DNA repair in
response to the presence of DNA damage or unreplicated DNA. May also
negatively regulate cell cycle progression during unperturbed cell
cycles. This regulation is achieved by a number of mechanisms that
together help to preserve the integrity of the genome. Recognizes the
substrate consensus sequence [R-X-X-S/T]. Binds to and phosphorylates
CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at 'Ser-178' and
'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding
sites for 14-3-3 proteins which inhibit CDC25A and CDC25C.
Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279'
and 'Ser-293' promotes proteolysis of CDC25A. Phosphorylation of CDC25A
at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-
79', 'Ser-82' and 'Ser-88' by NEK11, which is required for
polyubiquitination and degradation of CDCD25A. Inhibition of CDC25
leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin
complexes and blocks cell cycle progression. Also phosphorylates NEK6.
Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the
release of RAD51 from BRCA2 and enhances the association of RAD51 with
chromatin, thereby promoting DNA repair by homologous recombination.
Phosphorylates multiple sites within the C-terminus of TP53, which
promotes activation of TP53 by acetylation and promotes cell cycle
arrest and suppression of cellular proliferation. Also promotes repair
of DNA cross-links through phosphorylation of FANCE. Binds to and
phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent
phosphorylation of the chromatin assembly factor ASF1A. This may
enhance chromatin assembly both in the presence or absence of DNA
damage. May also play a role in replication fork maintenance through
regulation of PCNA. May regulate the transcription of genes that
regulate cell-cycle progression through the phosphorylation of
histones. Phosphorylates histone H3.1 (to form H3T11ph), which leads to
epigenetic inhibition of a subset of genes. May also phosphorylate RB1
to promote its interaction with the E2F family of transcription factors
and subsequent cell cycle arrest.
-!- FUNCTION: [Isoform 2]: Endogenous repressor of isoform 1, interacts
with, and antagonizes CHK1 to promote the S to G2/M phase transition.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- ACTIVITY REGULATION: Activated through phosphorylation predominantly by
ATR but also by ATM in response to DNA damage or inhibition of DNA
replication. Activation is modulated by several mediators including
CLSPN, BRCA1 and FEM1B.
-!- SUBUNIT: Interacts (phosphorylated by ATR) with RAD51. Interacts with
and phosphorylates CLSPN, an adapter protein that regulates the ATR-
dependent phosphorylation of CHEK1. Interacts with BRCA1. Interacts
with and phosphorylates CDC25A, CDC25B and CDC25C. Interacts with
FBXO6, which regulates CHEK1. Interacts with PPM1D, which regulates
CHEK1 through dephosphorylation. Interacts with TIMELESS; DNA damage-
dependent. Interacts with FEM1B; activates CHEK1 in response to stress.
Interacts with TLK1. Interacts with XPO1 and YWHAZ. Isoform 1
associates with isoform 2, the interaction is disrupted upon
phosphorylation by ATR. Interacts with CDK5RAP3; antagonizes CHEK1
(PubMed:19223857). {ECO:0000269|PubMed:11836499,
ECO:0000269|PubMed:12676962, ECO:0000269|PubMed:12766152,
ECO:0000269|PubMed:15665856, ECO:0000269|PubMed:15707391,
ECO:0000269|PubMed:15798197, ECO:0000269|PubMed:15870257,
ECO:0000269|PubMed:16963448, ECO:0000269|PubMed:19223857,
ECO:0000269|PubMed:19330022, ECO:0000269|PubMed:19716789,
ECO:0000269|PubMed:9278511}.
-!- INTERACTION:
O14757; P38398: BRCA1; NbExp=3; IntAct=EBI-974488, EBI-349905;
O14757; P30307: CDC25C; NbExp=2; IntAct=EBI-974488, EBI-974439;
O14757; Q9HAW4: CLSPN; NbExp=5; IntAct=EBI-974488, EBI-1369377;
O14757; Q9UJM3: ERRFI1; NbExp=2; IntAct=EBI-974488, EBI-2941912;
O14757; P08238: HSP90AB1; NbExp=3; IntAct=EBI-974488, EBI-352572;
O14757; O00255: MEN1; NbExp=2; IntAct=EBI-974488, EBI-592789;
O14757; Q06609: RAD51; NbExp=3; IntAct=EBI-974488, EBI-297202;
O14757; P06400: RB1; NbExp=3; IntAct=EBI-974488, EBI-491274;
O14757; Q9HCE7-2: SMURF1; NbExp=4; IntAct=EBI-974488, EBI-9845742;
O14757; Q9UNS1: TIMELESS; NbExp=2; IntAct=EBI-974488, EBI-2212315;
O14757; P61981: YWHAG; NbExp=7; IntAct=EBI-974488, EBI-359832;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome. Note=Nuclear export is
mediated at least in part by XPO1/CRM1. Also localizes to the
centrosome specifically during interphase, where it may protect
centrosomal CDC2 kinase from inappropriate activation by cytoplasmic
CDC25B.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O14757-1; Sequence=Displayed;
Name=2; Synonyms=Chk1-short, Chk1-S;
IsoId=O14757-2; Sequence=VSP_044008, VSP_044009;
Name=3;
IsoId=O14757-3; Sequence=VSP_045075;
-!- TISSUE SPECIFICITY: Expressed ubiquitously with the most abundant
expression in thymus, testis, small intestine and colon.
{ECO:0000269|PubMed:9278511, ECO:0000269|PubMed:9382850}.
-!- DOMAIN: The autoinhibitory region (AIR) inhibits the activity of the
kinase domain. {ECO:0000269|PubMed:14681223}.
-!- PTM: Phosphorylated by ATR in a RAD17-dependent manner in response to
ultraviolet irradiation and inhibition of DNA replication.
Phosphorylated by ATM in response to ionizing irradiation. ATM and ATR
can both phosphorylate Ser-317 and Ser-345 and this results in enhanced
kinase activity. Phosphorylation at Ser-345 induces a change in the
conformation of the protein, activates the kinase activity and is a
prerequisite for interaction with FBXO6 and subsequent ubiquitination
at Lys-436. Phosphorylation at Ser-345 also increases binding to 14-3-3
proteins and promotes nuclear retention. Conversely, dephosphorylation
at Ser-345 by PPM1D may contribute to exit from checkpoint mediated
cell cycle arrest. Phosphorylation at Ser-280 by AKT1/PKB, may promote
mono and/or diubiquitination. Also phosphorylated at undefined residues
during mitotic arrest, resulting in decreased activity.
{ECO:0000269|PubMed:10859164, ECO:0000269|PubMed:11390642,
ECO:0000269|PubMed:12446774, ECO:0000269|PubMed:12588868,
ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:12676583,
ECO:0000269|PubMed:12676925, ECO:0000269|PubMed:12676962,
ECO:0000269|PubMed:14657349, ECO:0000269|PubMed:14681223,
ECO:0000269|PubMed:14988723, ECO:0000269|PubMed:15650047,
ECO:0000269|PubMed:15707391, ECO:0000269|PubMed:15870257,
ECO:0000269|PubMed:19716789}.
-!- PTM: Ubiquitinated. Mono or diubiquitination promotes nuclear exclusion
(By similarity). The activated form (phosphorylated on Ser-345) is
polyubiquitinated at Lys-436 by some SCF-type E3 ubiquitin ligase
complex containing FBXO6 promoting its degradation. Ubiquitination and
degradation are required to terminate the checkpoint and ensure that
activated CHEK1 does not accumulate as cells progress through S phase,
when replication forks encounter transient impediments during normal
DNA replication. {ECO:0000250, ECO:0000269|PubMed:10859164,
ECO:0000269|PubMed:11390642, ECO:0000269|PubMed:12446774,
ECO:0000269|PubMed:12676583, ECO:0000269|PubMed:12676925,
ECO:0000269|PubMed:12676962, ECO:0000269|PubMed:14681223,
ECO:0000269|PubMed:14988723, ECO:0000269|PubMed:15650047,
ECO:0000269|PubMed:15707391, ECO:0000269|PubMed:15870257,
ECO:0000269|PubMed:19716789}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
protein kinase family. NIM1 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/chek1/";
---------------------------------------------------------------------------
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EMBL; AF016582; AAC51736.1; -; mRNA.
EMBL; AF032874; AAB88852.1; -; mRNA.
EMBL; AB032387; BAA84577.1; -; Genomic_DNA.
EMBL; JF289264; AEB71796.1; -; mRNA.
EMBL; AK292549; BAF85238.1; -; mRNA.
EMBL; AK293143; BAG56691.1; -; mRNA.
EMBL; AK299783; BAG61665.1; -; mRNA.
EMBL; AF527555; AAM78553.1; -; Genomic_DNA.
EMBL; AB451222; BAG70036.1; -; mRNA.
EMBL; AB451345; BAG70159.1; -; mRNA.
EMBL; AP001132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW67644.1; -; Genomic_DNA.
EMBL; BC004202; AAH04202.1; -; mRNA.
EMBL; BC017575; AAH17575.1; -; mRNA.
CCDS; CCDS58191.1; -. [O14757-3]
CCDS; CCDS81645.1; -. [O14757-2]
CCDS; CCDS8459.1; -. [O14757-1]
RefSeq; NP_001107593.1; NM_001114121.2. [O14757-1]
RefSeq; NP_001107594.1; NM_001114122.2. [O14757-1]
RefSeq; NP_001231775.1; NM_001244846.1. [O14757-3]
RefSeq; NP_001265.2; NM_001274.5. [O14757-1]
RefSeq; NP_001317357.1; NM_001330428.1. [O14757-2]
RefSeq; XP_016872635.1; XM_017017146.1. [O14757-1]
PDB; 1IA8; X-ray; 1.70 A; A=1-289.
PDB; 1NVQ; X-ray; 2.00 A; A=1-289.
PDB; 1NVR; X-ray; 1.80 A; A=1-289.
PDB; 1NVS; X-ray; 1.80 A; A=1-289.
PDB; 1ZLT; X-ray; 1.74 A; A=1-289.
PDB; 1ZYS; X-ray; 1.70 A; A=1-273.
PDB; 2AYP; X-ray; 2.90 A; A=1-269.
PDB; 2BR1; X-ray; 2.00 A; A=1-289.
PDB; 2BRB; X-ray; 2.10 A; A=1-289.
PDB; 2BRG; X-ray; 2.10 A; A=1-289.
PDB; 2BRH; X-ray; 2.10 A; A=1-289.
PDB; 2BRM; X-ray; 2.20 A; A=1-289.
PDB; 2BRN; X-ray; 2.80 A; A=1-289.
PDB; 2BRO; X-ray; 2.20 A; A=1-289.
PDB; 2C3J; X-ray; 2.10 A; A=1-289.
PDB; 2C3K; X-ray; 2.60 A; A=1-289.
PDB; 2C3L; X-ray; 2.35 A; A=1-289.
PDB; 2CGU; X-ray; 2.50 A; A=1-289.
PDB; 2CGV; X-ray; 2.60 A; A=1-289.
PDB; 2CGW; X-ray; 2.20 A; A=1-289.
PDB; 2CGX; X-ray; 2.20 A; A=1-289.
PDB; 2E9N; X-ray; 2.50 A; A=2-270.
PDB; 2E9O; X-ray; 2.10 A; A=2-270.
PDB; 2E9P; X-ray; 2.60 A; A=2-270.
PDB; 2E9U; X-ray; 2.00 A; A=2-270.
PDB; 2E9V; X-ray; 2.00 A; A/B=2-269.
PDB; 2GDO; X-ray; 3.00 A; A=1-289.
PDB; 2GHG; X-ray; 3.50 A; A=2-270.
PDB; 2HOG; X-ray; 1.90 A; A=2-307.
PDB; 2HXL; X-ray; 1.80 A; A=2-307.
PDB; 2HXQ; X-ray; 2.00 A; A=2-307.
PDB; 2HY0; X-ray; 1.70 A; A=2-307.
PDB; 2QHM; X-ray; 2.00 A; A=1-307.
PDB; 2QHN; X-ray; 1.70 A; A=1-307.
PDB; 2R0U; X-ray; 1.90 A; A=1-307.
PDB; 2WMQ; X-ray; 2.48 A; A=1-289.
PDB; 2WMR; X-ray; 2.43 A; A=1-289.
PDB; 2WMS; X-ray; 2.70 A; A=1-289.
PDB; 2WMT; X-ray; 2.55 A; A=1-289.
PDB; 2WMU; X-ray; 2.60 A; A=1-289.
PDB; 2WMV; X-ray; 2.01 A; A=1-289.
PDB; 2WMW; X-ray; 2.43 A; A=1-289.
PDB; 2WMX; X-ray; 2.45 A; A=1-289.
PDB; 2X8D; X-ray; 1.90 A; A=1-289.
PDB; 2X8E; X-ray; 2.50 A; A=1-276.
PDB; 2X8I; X-ray; 1.92 A; A=1-289.
PDB; 2XEY; X-ray; 2.70 A; A=1-289.
PDB; 2XEZ; X-ray; 2.25 A; A=1-289.
PDB; 2XF0; X-ray; 2.40 A; A=1-289.
PDB; 2YDI; X-ray; 1.60 A; A=1-289.
PDB; 2YDJ; X-ray; 1.85 A; A/B=1-276.
PDB; 2YDK; X-ray; 1.90 A; A=1-276.
PDB; 2YER; X-ray; 1.83 A; A=1-276.
PDB; 2YEX; X-ray; 1.30 A; A=1-276.
PDB; 2YM3; X-ray; 2.01 A; A=1-289.
PDB; 2YM4; X-ray; 2.35 A; A=1-289.
PDB; 2YM5; X-ray; 2.03 A; A=1-289.
PDB; 2YM6; X-ray; 2.01 A; A=1-289.
PDB; 2YM7; X-ray; 1.81 A; A=1-289.
PDB; 2YM8; X-ray; 2.07 A; A=1-289.
PDB; 2YWP; X-ray; 2.90 A; A=2-270.
PDB; 3F9N; X-ray; 1.90 A; A=2-307.
PDB; 3JVR; X-ray; 1.76 A; A=2-272.
PDB; 3JVS; X-ray; 1.90 A; A=2-272.
PDB; 3NLB; X-ray; 1.90 A; A=1-289.
PDB; 3OT3; X-ray; 1.44 A; A=2-274.
PDB; 3OT8; X-ray; 1.65 A; A=2-274.
PDB; 3PA3; X-ray; 1.40 A; A=2-274.
PDB; 3PA4; X-ray; 1.59 A; A=2-274.
PDB; 3PA5; X-ray; 1.70 A; A=2-274.
PDB; 3TKH; X-ray; 1.79 A; A=1-307.
PDB; 3TKI; X-ray; 1.60 A; A=1-307.
PDB; 3U9N; X-ray; 1.85 A; A=2-274.
PDB; 4FSM; X-ray; 2.30 A; A=2-280.
PDB; 4FSN; X-ray; 2.10 A; A=4-280.
PDB; 4FSQ; X-ray; 2.40 A; A=2-280.
PDB; 4FSR; X-ray; 2.50 A; A=2-280.
PDB; 4FST; X-ray; 1.90 A; A=2-270.
PDB; 4FSU; X-ray; 2.10 A; A=2-280.
PDB; 4FSW; X-ray; 2.30 A; A=2-280.
PDB; 4FSY; X-ray; 2.30 A; A=2-280.
PDB; 4FSZ; X-ray; 2.30 A; A=2-280.
PDB; 4FT0; X-ray; 2.30 A; A=2-280.
PDB; 4FT3; X-ray; 2.50 A; A=2-280.
PDB; 4FT5; X-ray; 2.40 A; A=2-280.
PDB; 4FT7; X-ray; 2.20 A; A=2-280.
PDB; 4FT9; X-ray; 2.20 A; A=2-280.
PDB; 4FTA; X-ray; 2.40 A; A=2-280.
PDB; 4FTC; X-ray; 2.00 A; A=2-280.
PDB; 4FTI; X-ray; 2.20 A; A=2-280.
PDB; 4FTJ; X-ray; 2.20 A; A=2-280.
PDB; 4FTK; X-ray; 2.30 A; A=2-280.
PDB; 4FTL; X-ray; 2.50 A; A=2-280.
PDB; 4FTM; X-ray; 1.90 A; A=2-280.
PDB; 4FTN; X-ray; 2.02 A; A=2-280.
PDB; 4FTO; X-ray; 2.10 A; A=2-280.
PDB; 4FTQ; X-ray; 2.00 A; A=2-280.
PDB; 4FTR; X-ray; 2.25 A; A=2-280.
PDB; 4FTT; X-ray; 2.30 A; A=2-280.
PDB; 4FTU; X-ray; 2.10 A; A=2-280.
PDB; 4GH2; X-ray; 2.03 A; A=2-280.
PDB; 4HYH; X-ray; 1.70 A; A=1-289.
PDB; 4HYI; X-ray; 1.40 A; A=1-289.
PDB; 4JIK; X-ray; 1.90 A; A=2-274.
PDB; 4QYE; X-ray; 2.05 A; A=1-289.
PDB; 4QYF; X-ray; 2.15 A; A=1-289.
PDB; 4QYG; X-ray; 1.75 A; A/B=1-289.
PDB; 4QYH; X-ray; 1.90 A; A/B=1-289.
PDB; 4RVK; X-ray; 1.85 A; A=1-289.
PDB; 4RVL; X-ray; 1.85 A; A=1-289.
PDB; 4RVM; X-ray; 1.86 A; A=1-289.
PDB; 5DLS; X-ray; 2.15 A; A=1-289.
PDB; 5F4N; X-ray; 1.91 A; A=1-273.
PDB; 5OOP; X-ray; 1.70 A; A=1-289.
PDB; 5OOR; X-ray; 1.90 A; A=1-289.
PDB; 5OOT; X-ray; 2.10 A; A=1-289.
PDB; 5OP2; X-ray; 1.90 A; A=1-289.
PDB; 5OP4; X-ray; 2.00 A; A=1-289.
PDB; 5OP5; X-ray; 1.90 A; A=1-289.
PDB; 5OP7; X-ray; 1.80 A; A=1-289.
PDB; 5OPB; X-ray; 1.55 A; A=1-289.
PDB; 5OPR; X-ray; 1.95 A; A=1-289.
PDB; 5OPS; X-ray; 2.00 A; A=1-289.
PDB; 5OPU; X-ray; 1.55 A; A=1-289.
PDB; 5OPV; X-ray; 1.90 A; A=1-289.
PDB; 5OQ5; X-ray; 1.40 A; A=1-289.
PDB; 5OQ6; X-ray; 1.95 A; A=1-289.
PDB; 5OQ7; X-ray; 2.10 A; A/B=1-289.
PDB; 5OQ8; X-ray; 2.00 A; A=1-289.
PDB; 5WI2; X-ray; 2.50 A; A/B=377-476.
PDB; 6FC8; X-ray; 1.61 A; A=1-276.
PDB; 6FCF; X-ray; 1.85 A; A=1-276.
PDB; 6FCK; X-ray; 1.90 A; A=1-276.
PDBsum; 1IA8; -.
PDBsum; 1NVQ; -.
PDBsum; 1NVR; -.
PDBsum; 1NVS; -.
PDBsum; 1ZLT; -.
PDBsum; 1ZYS; -.
PDBsum; 2AYP; -.
PDBsum; 2BR1; -.
PDBsum; 2BRB; -.
PDBsum; 2BRG; -.
PDBsum; 2BRH; -.
PDBsum; 2BRM; -.
PDBsum; 2BRN; -.
PDBsum; 2BRO; -.
PDBsum; 2C3J; -.
PDBsum; 2C3K; -.
PDBsum; 2C3L; -.
PDBsum; 2CGU; -.
PDBsum; 2CGV; -.
PDBsum; 2CGW; -.
PDBsum; 2CGX; -.
PDBsum; 2E9N; -.
PDBsum; 2E9O; -.
PDBsum; 2E9P; -.
PDBsum; 2E9U; -.
PDBsum; 2E9V; -.
PDBsum; 2GDO; -.
PDBsum; 2GHG; -.
PDBsum; 2HOG; -.
PDBsum; 2HXL; -.
PDBsum; 2HXQ; -.
PDBsum; 2HY0; -.
PDBsum; 2QHM; -.
PDBsum; 2QHN; -.
PDBsum; 2R0U; -.
PDBsum; 2WMQ; -.
PDBsum; 2WMR; -.
PDBsum; 2WMS; -.
PDBsum; 2WMT; -.
PDBsum; 2WMU; -.
PDBsum; 2WMV; -.
PDBsum; 2WMW; -.
PDBsum; 2WMX; -.
PDBsum; 2X8D; -.
PDBsum; 2X8E; -.
PDBsum; 2X8I; -.
PDBsum; 2XEY; -.
PDBsum; 2XEZ; -.
PDBsum; 2XF0; -.
PDBsum; 2YDI; -.
PDBsum; 2YDJ; -.
PDBsum; 2YDK; -.
PDBsum; 2YER; -.
PDBsum; 2YEX; -.
PDBsum; 2YM3; -.
PDBsum; 2YM4; -.
PDBsum; 2YM5; -.
PDBsum; 2YM6; -.
PDBsum; 2YM7; -.
PDBsum; 2YM8; -.
PDBsum; 2YWP; -.
PDBsum; 3F9N; -.
PDBsum; 3JVR; -.
PDBsum; 3JVS; -.
PDBsum; 3NLB; -.
PDBsum; 3OT3; -.
PDBsum; 3OT8; -.
PDBsum; 3PA3; -.
PDBsum; 3PA4; -.
PDBsum; 3PA5; -.
PDBsum; 3TKH; -.
PDBsum; 3TKI; -.
PDBsum; 3U9N; -.
PDBsum; 4FSM; -.
PDBsum; 4FSN; -.
PDBsum; 4FSQ; -.
PDBsum; 4FSR; -.
PDBsum; 4FST; -.
PDBsum; 4FSU; -.
PDBsum; 4FSW; -.
PDBsum; 4FSY; -.
PDBsum; 4FSZ; -.
PDBsum; 4FT0; -.
PDBsum; 4FT3; -.
PDBsum; 4FT5; -.
PDBsum; 4FT7; -.
PDBsum; 4FT9; -.
PDBsum; 4FTA; -.
PDBsum; 4FTC; -.
PDBsum; 4FTI; -.
PDBsum; 4FTJ; -.
PDBsum; 4FTK; -.
PDBsum; 4FTL; -.
PDBsum; 4FTM; -.
PDBsum; 4FTN; -.
PDBsum; 4FTO; -.
PDBsum; 4FTQ; -.
PDBsum; 4FTR; -.
PDBsum; 4FTT; -.
PDBsum; 4FTU; -.
PDBsum; 4GH2; -.
PDBsum; 4HYH; -.
PDBsum; 4HYI; -.
PDBsum; 4JIK; -.
PDBsum; 4QYE; -.
PDBsum; 4QYF; -.
PDBsum; 4QYG; -.
PDBsum; 4QYH; -.
PDBsum; 4RVK; -.
PDBsum; 4RVL; -.
PDBsum; 4RVM; -.
PDBsum; 5DLS; -.
PDBsum; 5F4N; -.
PDBsum; 5OOP; -.
PDBsum; 5OOR; -.
PDBsum; 5OOT; -.
PDBsum; 5OP2; -.
PDBsum; 5OP4; -.
PDBsum; 5OP5; -.
PDBsum; 5OP7; -.
PDBsum; 5OPB; -.
PDBsum; 5OPR; -.
PDBsum; 5OPS; -.
PDBsum; 5OPU; -.
PDBsum; 5OPV; -.
PDBsum; 5OQ5; -.
PDBsum; 5OQ6; -.
PDBsum; 5OQ7; -.
PDBsum; 5OQ8; -.
PDBsum; 5WI2; -.
PDBsum; 6FC8; -.
PDBsum; 6FCF; -.
PDBsum; 6FCK; -.
SMR; O14757; -.
BioGRID; 107536; 176.
CORUM; O14757; -.
DIP; DIP-24182N; -.
ELM; O14757; -.
IntAct; O14757; 55.
MINT; O14757; -.
STRING; 9606.ENSP00000388648; -.
BindingDB; O14757; -.
ChEMBL; CHEMBL4630; -.
DrugBank; DB07647; (2R)-1-[(5,6-DIPHENYL-7H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)AMINO]PROPAN-2-OL.
DrugBank; DB07648; (2R)-3-{[(4Z)-5,6-DIPHENYL-6,7-DIHYDRO-4H-PYRROLO[2,3-D]PYRIMIDIN-4-YLIDENE]AMINO}PROPANE-1,2-DIOL.
DrugBank; DB07037; (2S)-1-AMINO-3-[(5-NITROQUINOLIN-8-YL)AMINO]PROPAN-2-OL.
DrugBank; DB07243; (3-ENDO)-8-METHYL-8-AZABICYCLO[3.2.1]OCT-3-YL 1H-PYRROLO[2,3-B]PYRIDINE-3-CARBOXYLATE.
DrugBank; DB07078; (3Z)-6-(4-HYDROXY-3-METHOXYPHENYL)-3-(1H-PYRROL-2-YLMETHYLENE)-1,3-DIHYDRO-2H-INDOL-2-ONE.
DrugBank; DB07654; (5,6-DIPHENYL-FURO[2,3-D]PYRIMIDIN-4-YLAMINO)-ACETIC.
DrugBank; DB07213; (5-{3-[5-(PIPERIDIN-1-YLMETHYL)-1H-INDOL-2-YL]-1H-INDAZOL-6-YL}-2H-1,2,3-TRIAZOL-4-YL)METHANOL.
DrugBank; DB07314; 1-(5-CHLORO-2,4-DIMETHOXYPHENYL)-3-(5-CYANOPYRAZIN-2-YL)UREA.
DrugBank; DB07228; 1-(5-CHLORO-2-METHOXYPHENYL)-3-{6-[2-(DIMETHYLAMINO)-1-METHYLETHOXY]PYRAZIN-2-YL}UREA.
DrugBank; DB08781; 1-[(2S)-4-(5-BROMO-1H-PYRAZOLO[3,4-B]PYRIDIN-4-YL)MORPHOLIN-2-YL]METHANAMINE.
DrugBank; DB08774; 1-[(2S)-4-(5-phenyl-1H-pyrazolo[3,4-b]pyridin-4-yl)morpholin-2-yl]methanamine.
DrugBank; DB07311; 18-CHLORO-11,12,13,14-TETRAHYDRO-1H,10H-8,4-(AZENO)-9,15,1,3,6-BENZODIOXATRIAZACYCLOHEPTADECIN-2-ONE.
DrugBank; DB07034; 2,2'-{[9-(HYDROXYIMINO)-9H-FLUORENE-2,7-DIYL]BIS(OXY)}DIACETIC ACID.
DrugBank; DB07038; 2-(cyclohexylamino)benzoic acid.
DrugBank; DB08779; 2-(methylsulfanyl)-5-(thiophen-2-ylmethyl)-1H-imidazol-4-ol.
DrugBank; DB08393; 2-[(5,6-DIPHENYLFURO[2,3-D]PYRIMIDIN-4-YL)AMINO]ETHANOL.
DrugBank; DB08392; 2-[5,6-BIS-(4-METHOXY-PHENYL)-FURO[2,3-D]PYRIMIDIN-4-YLAMINO]-ETHANOL.
DrugBank; DB07959; 3-(1H-BENZIMIDAZOL-2-YL)-1H-INDAZOLE.
DrugBank; DB07075; 3-(5-{[4-(AMINOMETHYL)PIPERIDIN-1-YL]METHYL}-1H-INDOL-2-YL)-1H-INDAZOLE-6-CARBONITRILE.
DrugBank; DB07025; 3-(5-{[4-(AMINOMETHYL)PIPERIDIN-1-YL]METHYL}-1H-INDOL-2-YL)QUINOLIN-2(1H)-ONE.
DrugBank; DB07655; 3-AMINO-3-BENZYL-[4.3.0]BICYCLO-1,6-DIAZANONAN-2-ONE.
DrugBank; DB07320; 4-(6-{[(4-METHYLCYCLOHEXYL)AMINO]METHYL}-1,4-DIHYDROINDENO[1,2-C]PYRAZOL-3-YL)BENZOIC ACID.
DrugBank; DB07336; 4-[3-(1H-BENZIMIDAZOL-2-YL)-1H-INDAZOL-6-YL]-2-METHOXYPHENOL.
DrugBank; DB08777; 5,6,7,8-TETRAHYDRO[1]BENZOTHIENO[2,3-D]PYRIMIDIN-4(3H)-ONE.
DrugBank; DB07158; 5-ETHYL-3-METHYL-1,5-DIHYDRO-4H-PYRAZOLO[4,3-C]QUINOLIN-4-ONE.
DrugBank; DB08780; 6-MORPHOLIN-4-YL-9H-PURINE.
DrugBank; DB08778; [4-amino-2-(tert-butylamino)-1,3-thiazol-5-yl](phenyl)methanone.
DrugBank; DB06852; CHIR-124.
DrugBank; DB06486; Enzastaurin.
DrugBank; DB12010; Fostamatinib.
DrugBank; DB08776; N-(4-OXO-5,6,7,8-TETRAHYDRO-4H-[1,3]THIAZOLO[5,4-C]AZEPIN-2-YL)ACETAMIDE.
DrugBank; DB07653; N-(5,6-DIPHENYLFURO[2,3-D]PYRIMIDIN-4-YL)GLYCINE.
DrugBank; DB06876; N-{5-[4-(4-METHYLPIPERAZIN-1-YL)PHENYL]-1H-PYRROLO[2,3-B]PYRIDIN-3-YL}NICOTINAMIDE.
DrugBank; DB08683; REL-(9R,12S)-9,10,11,12-TETRAHYDRO-9,12-EPOXY-1H-DIINDOLO[1,2,3-FG:3',2',1'-KL]PYRROLO[3,4-I][1,6]BENZODIAZOCINE-1,3(2H)-DIONE.
DrugBank; DB05149; XL844.
DrugCentral; O14757; -.
GuidetoPHARMACOLOGY; 1987; -.
iPTMnet; O14757; -.
MetOSite; O14757; -.
PhosphoSitePlus; O14757; -.
BioMuta; CHEK1; -.
CPTAC; CPTAC-3223; -.
CPTAC; CPTAC-3282; -.
CPTAC; CPTAC-922; -.
EPD; O14757; -.
jPOST; O14757; -.
MassIVE; O14757; -.
MaxQB; O14757; -.
PaxDb; O14757; -.
PeptideAtlas; O14757; -.
PRIDE; O14757; -.
ProteomicsDB; 27577; -.
ProteomicsDB; 48208; -. [O14757-1]
ProteomicsDB; 48209; -. [O14757-2]
Antibodypedia; 3671; 1758 antibodies.
DNASU; 1111; -.
Ensembl; ENST00000278916; ENSP00000278916; ENSG00000149554. [O14757-3]
Ensembl; ENST00000428830; ENSP00000412504; ENSG00000149554. [O14757-1]
Ensembl; ENST00000438015; ENSP00000388648; ENSG00000149554. [O14757-1]
Ensembl; ENST00000524737; ENSP00000432890; ENSG00000149554. [O14757-1]
Ensembl; ENST00000532449; ENSP00000481616; ENSG00000149554. [O14757-1]
Ensembl; ENST00000534070; ENSP00000435371; ENSG00000149554. [O14757-1]
Ensembl; ENST00000544373; ENSP00000442317; ENSG00000149554. [O14757-2]
GeneID; 1111; -.
KEGG; hsa:1111; -.
UCSC; uc001qcf.5; human. [O14757-1]
CTD; 1111; -.
DisGeNET; 1111; -.
EuPathDB; HostDB:ENSG00000149554.12; -.
GeneCards; CHEK1; -.
HGNC; HGNC:1925; CHEK1.
HPA; ENSG00000149554; Tissue enhanced (ductus deferens, seminal vesicle).
MalaCards; CHEK1; -.
MIM; 603078; gene.
neXtProt; NX_O14757; -.
OpenTargets; ENSG00000149554; -.
PharmGKB; PA110; -.
eggNOG; KOG0590; Eukaryota.
GeneTree; ENSGT00940000159682; -.
InParanoid; O14757; -.
KO; K02216; -.
OMA; KPYHAQP; -.
PhylomeDB; O14757; -.
TreeFam; TF351441; -.
BRENDA; 2.7.11.1; 2681.
PathwayCommons; O14757; -.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
SignaLink; O14757; -.
SIGNOR; O14757; -.
BioGRID-ORCS; 1111; 787 hits in 904 CRISPR screens.
ChiTaRS; CHEK1; human.
EvolutionaryTrace; O14757; -.
GeneWiki; CHEK1; -.
GenomeRNAi; 1111; -.
Pharos; O14757; Tchem.
PRO; PR:O14757; -.
Proteomes; UP000005640; Chromosome 11.
RNAct; O14757; protein.
Bgee; ENSG00000149554; Expressed in secondary oocyte and 169 other tissues.
ExpressionAtlas; O14757; baseline and differential.
Genevisible; O14757; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0000785; C:chromatin; ISS:UniProtKB.
GO; GO:0000794; C:condensed nuclear chromosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0035402; F:histone kinase activity (H3-T11 specific); IDA:UniProtKB.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0004672; F:protein kinase activity; IMP:CACAO.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0048096; P:chromatin-mediated maintenance of transcription; ISS:UniProtKB.
GO; GO:0000077; P:DNA damage checkpoint; IDA:UniProtKB.
GO; GO:0006975; P:DNA damage induced protein phosphorylation; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
GO; GO:0006260; P:DNA replication; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
GO; GO:0045839; P:negative regulation of mitotic nuclear division; IDA:UniProtKB.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:UniProtKB.
GO; GO:0045787; P:positive regulation of cell cycle; IDA:CAFA.
GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
GO; GO:2000615; P:regulation of histone H3-K9 acetylation; ISS:UniProtKB.
GO; GO:0046602; P:regulation of mitotic centrosome separation; IDA:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0010767; P:regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage; ISS:UniProtKB.
GO; GO:0090399; P:replicative senescence; NAS:BHF-UCL.
GO; GO:0072425; P:signal transduction involved in G2 DNA damage checkpoint; IMP:UniProtKB.
CDD; cd14069; STKc_Chk1; 1.
InterPro; IPR034670; Chk1_catalytic_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cytoplasm;
Cytoskeleton; DNA damage; DNA repair; Isopeptide bond; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Ubl conjugation.
CHAIN 1..476
/note="Serine/threonine-protein kinase Chk1"
/id="PRO_0000085848"
DOMAIN 9..265
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 15..23
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
REGION 1..265
/note="Interaction with CLSPN"
/evidence="ECO:0000250"
REGION 391..476
/note="Autoinhibitory region"
ACT_SITE 130
/note="Proton acceptor"
BINDING 38
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 280
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 286
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231"
MOD_RES 296
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:15707391"
MOD_RES 301
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
MOD_RES 317
/note="Phosphoserine; by ATM and ATR"
/evidence="ECO:0000269|PubMed:11390642,
ECO:0000269|PubMed:12446774, ECO:0000269|PubMed:12588868,
ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:12676583,
ECO:0000269|PubMed:12676962, ECO:0000269|PubMed:14657349,
ECO:0000269|PubMed:15707391, ECO:0000269|PubMed:15870257"
MOD_RES 331
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 345
/note="Phosphoserine; by ATM and ATR"
/evidence="ECO:0000269|PubMed:10859164,
ECO:0000269|PubMed:11390642, ECO:0000269|PubMed:12446774,
ECO:0000269|PubMed:12676583, ECO:0000269|PubMed:12676925,
ECO:0000269|PubMed:12676962, ECO:0000269|PubMed:14681223,
ECO:0000269|PubMed:14988723, ECO:0000269|PubMed:15650047,
ECO:0000269|PubMed:15707391, ECO:0000269|PubMed:15870257,
ECO:0000269|PubMed:19716789"
MOD_RES 467
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 468
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
CROSSLNK 436
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:19716789"
VAR_SEQ 1..94
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:22184239"
/id="VSP_044008"
VAR_SEQ 95..97
/note="RIE -> MEK (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:22184239"
/id="VSP_044009"
VAR_SEQ 412..445
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_045075"
VARIANT 156
/note="R -> Q (in dbSNP:rs3731410)"
/evidence="ECO:0000269|Ref.6"
/id="VAR_021123"
VARIANT 223
/note="E -> V (in dbSNP:rs35817404)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040407"
VARIANT 312
/note="V -> M (in dbSNP:rs34097480)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040408"
VARIANT 471
/note="I -> V (in dbSNP:rs506504)"
/evidence="ECO:0000269|PubMed:10717241,
ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:19054851, ECO:0000269|PubMed:9278511,
ECO:0000269|PubMed:9382850, ECO:0000269|Ref.6,
ECO:0000269|Ref.9"
/id="VAR_024571"
MUTAGEN 38
/note="K->R: Abolishes kinase activity."
/evidence="ECO:0000269|PubMed:12446774,
ECO:0000269|PubMed:14681223"
MUTAGEN 130
/note="D->A: Abolishes kinase activity."
/evidence="ECO:0000269|PubMed:10673501,
ECO:0000269|PubMed:11390642, ECO:0000269|PubMed:11535615,
ECO:0000269|PubMed:11821419, ECO:0000269|PubMed:12588868,
ECO:0000269|PubMed:14681206, ECO:0000269|PubMed:15311285,
ECO:0000269|PubMed:9278511"
MUTAGEN 317
/note="S->A: Abrogates interaction with RAD51; when
associated with A-345. Reduces phosphorylation and impairs
activation by hydroxyurea and ionizing radiation. Abrogates
nuclear retention upon checkpoint activation. Impairs
interaction with FBXO6."
/evidence="ECO:0000269|PubMed:11390642,
ECO:0000269|PubMed:12588868, ECO:0000269|PubMed:12676583,
ECO:0000269|PubMed:12676962, ECO:0000269|PubMed:15665856"
MUTAGEN 317
/note="S->E: Enhances interaction with RAD51; when
associated with E-345."
/evidence="ECO:0000269|PubMed:11390642,
ECO:0000269|PubMed:12588868, ECO:0000269|PubMed:12676583,
ECO:0000269|PubMed:12676962, ECO:0000269|PubMed:15665856"
MUTAGEN 344
/note="F->A: Impairs nuclear export."
/evidence="ECO:0000269|PubMed:12676962"
MUTAGEN 345
/note="S->A: Abrogates interaction with RAD51; when
associated with A-317. Reduces phosphorylation and impairs
activation by hydroxyurea and ionizing radiation. Impairs
interaction with YWHAZ which is required for nuclear
retention after checkpoint activation."
/evidence="ECO:0000269|PubMed:11390642,
ECO:0000269|PubMed:12588868, ECO:0000269|PubMed:12676583,
ECO:0000269|PubMed:12676962, ECO:0000269|PubMed:15665856,
ECO:0000269|PubMed:19716789"
MUTAGEN 345
/note="S->E: Enhances interaction with RAD51; when
associated with E-317."
/evidence="ECO:0000269|PubMed:11390642,
ECO:0000269|PubMed:12588868, ECO:0000269|PubMed:12676583,
ECO:0000269|PubMed:12676962, ECO:0000269|PubMed:15665856,
ECO:0000269|PubMed:19716789"
MUTAGEN 353
/note="M->A: Impairs nuclear export."
/evidence="ECO:0000269|PubMed:12676962"
MUTAGEN 357
/note="S->A: No effect on phosphorylation induced by
hydroxyurea."
/evidence="ECO:0000269|PubMed:11390642"
MUTAGEN 366
/note="S->A: No effect on phosphorylation induced by
hydroxyurea."
/evidence="ECO:0000269|PubMed:11390642"
MUTAGEN 372
/note="R->E: In 3RE mutant. Disrupts the folding and/or
conformation, allowing increased accessibility to FBXO6
component of SCF-type E3 ubiquitin ligase complex; when
associated with E-376 and E-379."
/evidence="ECO:0000269|PubMed:19716789"
MUTAGEN 376
/note="R->E: In 3RE mutant. Disrupts the folding and/or
conformation, allowing increased accessibility to FBXO6
component of SCF-type E3 ubiquitin ligase complex; when
associated with E-372 and E-379."
/evidence="ECO:0000269|PubMed:19716789"
MUTAGEN 379
/note="R->E: In 3RE mutant. Disrupts the folding and/or
conformation, allowing increased accessibility to FBXO6
component of SCF-type E3 ubiquitin ligase complex; when
associated with E-372 and E-376."
/evidence="ECO:0000269|PubMed:19716789"
MUTAGEN 436
/note="K->R: Enhances stability of the protein, probably by
preventing ubiquitination at this site."
/evidence="ECO:0000269|PubMed:19716789"
MUTAGEN 468
/note="S->A: No effect on phosphorylation induced by
hydroxyurea."
/evidence="ECO:0000269|PubMed:11390642"
CONFLICT 163
/note="L -> S (in Ref. 5; BAG56691)"
/evidence="ECO:0000305"
CONFLICT 220
/note="D -> G (in Ref. 4; BAG61665)"
/evidence="ECO:0000305"
CONFLICT 381
/note="F -> L (in Ref. 4; BAG61665)"
/evidence="ECO:0000305"
HELIX 3..8
/evidence="ECO:0000244|PDB:2YEX"
STRAND 9..17
/evidence="ECO:0000244|PDB:2YEX"
STRAND 19..28
/evidence="ECO:0000244|PDB:2YEX"
TURN 29..31
/evidence="ECO:0000244|PDB:2YEX"
STRAND 34..41
/evidence="ECO:0000244|PDB:2YEX"
HELIX 42..44
/evidence="ECO:0000244|PDB:2YEX"
HELIX 48..60
/evidence="ECO:0000244|PDB:2YEX"
STRAND 70..76
/evidence="ECO:0000244|PDB:2YEX"
STRAND 79..85
/evidence="ECO:0000244|PDB:2YEX"
STRAND 88..91
/evidence="ECO:0000244|PDB:2GDO"
HELIX 92..95
/evidence="ECO:0000244|PDB:2YEX"
TURN 98..100
/evidence="ECO:0000244|PDB:2YEX"
HELIX 104..123
/evidence="ECO:0000244|PDB:2YEX"
STRAND 125..127
/evidence="ECO:0000244|PDB:2GHG"
HELIX 133..135
/evidence="ECO:0000244|PDB:2YEX"
STRAND 136..138
/evidence="ECO:0000244|PDB:2YEX"
STRAND 144..146
/evidence="ECO:0000244|PDB:2YEX"
HELIX 149..151
/evidence="ECO:0000244|PDB:2C3J"
STRAND 153..157
/evidence="ECO:0000244|PDB:3JVR"
HELIX 171..173
/evidence="ECO:0000244|PDB:2YEX"
HELIX 176..179
/evidence="ECO:0000244|PDB:2YEX"
STRAND 182..184
/evidence="ECO:0000244|PDB:2YEX"
HELIX 186..203
/evidence="ECO:0000244|PDB:2YEX"
STRAND 209..211
/evidence="ECO:0000244|PDB:4HYI"
STRAND 213..215
/evidence="ECO:0000244|PDB:2XEY"
HELIX 216..222
/evidence="ECO:0000244|PDB:2YEX"
STRAND 227..229
/evidence="ECO:0000244|PDB:2E9U"
HELIX 231..233
/evidence="ECO:0000244|PDB:2YEX"
HELIX 236..245
/evidence="ECO:0000244|PDB:2YEX"
TURN 250..252
/evidence="ECO:0000244|PDB:2YEX"
HELIX 256..259
/evidence="ECO:0000244|PDB:2YEX"
TURN 263..266
/evidence="ECO:0000244|PDB:2YEX"
STRAND 379..384
/evidence="ECO:0000244|PDB:5WI2"
HELIX 386..399
/evidence="ECO:0000244|PDB:5WI2"
STRAND 403..417
/evidence="ECO:0000244|PDB:5WI2"
STRAND 423..432
/evidence="ECO:0000244|PDB:5WI2"
STRAND 434..446
/evidence="ECO:0000244|PDB:5WI2"
HELIX 448..461
/evidence="ECO:0000244|PDB:5WI2"
HELIX 463..465
/evidence="ECO:0000244|PDB:5WI2"
SEQUENCE 476 AA; 54434 MW; 0ABD0FAB67E60F67 CRC64;
MAVPFVEDWD LVQTLGEGAY GEVQLAVNRV TEEAVAVKIV DMKRAVDCPE NIKKEICINK
MLNHENVVKF YGHRREGNIQ YLFLEYCSGG ELFDRIEPDI GMPEPDAQRF FHQLMAGVVY
LHGIGITHRD IKPENLLLDE RDNLKISDFG LATVFRYNNR ERLLNKMCGT LPYVAPELLK
RREFHAEPVD VWSCGIVLTA MLAGELPWDQ PSDSCQEYSD WKEKKTYLNP WKKIDSAPLA
LLHKILVENP SARITIPDIK KDRWYNKPLK KGAKRPRVTS GGVSESPSGF SKHIQSNLDF
SPVNSASSEE NVKYSSSQPE PRTGLSLWDT SPSYIDKLVQ GISFSQPTCP DHMLLNSQLL
GTPGSSQNPW QRLVKRMTRF FTKLDADKSY QCLKETCEKL GYQWKKSCMN QVTISTTDRR
NNKLIFKVNL LEMDDKILVD FRLSKGDGLE FKRHFLKIKG KLIDIVSSQK IWLPAT


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Related Genes :
[CHEK1 CHK1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Cell cycle checkpoint kinase) (Checkpoint kinase-1)
[Chek1 Chk1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1)
[Chek1 Chk1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1)
[chek1 chk1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1) (xChk1)
[CHEK1 CHK1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1)
[chk1 rad27 SPCC1259.13] Serine/threonine-protein kinase chk1 (EC 2.7.11.1) (Checkpoint kinase 1)
[CHK1 YBR274W YBR1742] Serine/threonine-protein kinase CHK1 (EC 2.7.11.1) (Checkpoint kinase 1)
[grp CG17161] Serine/threonine-protein kinase grp (EC 2.7.11.1) (Chk1 homolog) (Protein grapes)
[chk-1 Y39H10A.7] Serine/threonine-protein kinase chk-1 (EC 2.7.11.1)
[CHEK2 CDS1 CHK2 RAD53] Serine/threonine-protein kinase Chk2 (EC 2.7.11.1) (CHK2 checkpoint homolog) (Cds1 homolog) (Hucds1) (hCds1) (Checkpoint kinase 2)
[MEC1 ESR1 SAD3 YBR136W YBR1012] Serine/threonine-protein kinase MEC1 (EC 2.7.11.1) (ATR homolog) (DNA-damage checkpoint kinase MEC1) (Mitosis entry checkpoint protein 1)
[TEL1 YBL088C YBL0706] Serine/threonine-protein kinase TEL1 (EC 2.7.11.1) (ATM homolog) (DNA-damage checkpoint kinase TEL1) (Telomere length regulation protein 1)
[tel1 SPCC23B6.03c] Serine/threonine-protein kinase tel1 (EC 2.7.11.1) (ATM homolog) (DNA-damage checkpoint kinase tel1) (Telomere length regulation protein 1)
[BUB1B BUBR1 MAD3L SSK1] Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (hBUBR1) (Mitotic checkpoint kinase MAD3L) (Protein SSK1)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDK1 CDC2 CDC28A CDKN1 P34CDC2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[mei-41 CG4252] Serine/threonine-protein kinase ATR (EC 2.7.11.1) (Ataxia telangiectasia and Rad3-related protein homolog) (ATR homolog) (dATR) (Meiotic protein 41)
[Cdk1 cdc2 CG5363] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CHK1 UMAG_11087] Serine/threonine-protein kinase CHK1 (EC 2.7.11.1) (Checkpoint kinase 1)
[BUB1 BUB1L] Mitotic checkpoint serine/threonine-protein kinase BUB1 (hBUB1) (EC 2.7.11.1) (BUB1A)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDK1 CDC2 CDKN1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[zyg-1 F59E12.2] Probable serine/threonine-protein kinase zyg-1 (EC 2.7.11.1) (Zygote defective protein 1)
[Bub1] Mitotic checkpoint serine/threonine-protein kinase BUB1 (mBUB1) (EC 2.7.11.1) (BUB1A)
[BUB1 YGR188C G7542] Checkpoint serine/threonine-protein kinase BUB1 (EC 2.7.11.1)
[bub1 SPCC1322.12c] Checkpoint serine/threonine-protein kinase bub1 (EC 2.7.11.1)
[crb2 rhp9 SPBC342.05] DNA repair protein crb2 (Checkpoint mediator protein crb2) (Cut5-repeat binding protein 2) (RAD9 protein homolog)
[TLK2] Serine/threonine-protein kinase tousled-like 2 (EC 2.7.11.1) (HsHPK) (PKU-alpha) (Tousled-like kinase 2)
[Rad9a Rad9] Cell cycle checkpoint control protein RAD9A (mRAD9) (EC 3.1.11.2) (DNA repair exonuclease rad9 homolog A) (Rad9-like protein)
[ATR FRP1] Serine/threonine-protein kinase ATR (EC 2.7.11.1) (Ataxia telangiectasia and Rad3-related protein) (FRAP-related protein 1)

Bibliography :