Human protein: IPI00014072 * 60915 Da * CHEK2 Isoform 1 of Serine/threonine-protein kinase Chk2 - Liebel-Lab @ KIT
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>CHEK2 Isoform 1 of Serine/threonine-protein kinase Chk2 - Length: 543 AS 
MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEP
EDQEPEEPTPAPWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYI
EDHSGNGTFVNTELVGKGKRRPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFER
KTCKKVAIKIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLK
EATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEEDCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVG
TAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEA
LRHPWLQDEDMKRKFQDLLSEENESTALPQVLAQPSTSRKRPREGEAEGAETTKRPAVCAAVL
Linkouts to other data resources: BioCompare * Entrez * PolyMeta * GeneCard * imaGenes * GenomeBrowser * Google Scholar * Mitocheck
AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page
Diseaselink to OMIM


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page
ACTIVATE: SMART analysis
NameBeginEndE-value
low complexity2362-
low complexity7592-
FHA1121751.70e-03
S_TKc2204862.44e-100

These features and domains are not shown in the diagram, either because their scores are less significant than the required threshold, or because they overlap with some other source of annotation:

NameBeginEndE-valueReason
Pfam:FHA1131925.60e-12overlap
Pfam:Pkinase2204862.30e-91overlap
low complexity458473-overlap


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page

AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page

AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page

AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page
General information
Entry name CHK2_HUMAN
Accession number O96017, Q6QA03, Q6QA04, Q6QA05, Q6QA06, Q6QA07, Q6QA08, Q6QA10, Q6QA11, Q6QA12, Q6QA13, Q9HCQ8, Q9UGF0, Q9UGF1
Integrated 30-MAY-2000, UniProtKB/Swiss-Prot.
Sequence update 01-MAY-1999, sequence version 1
Annotation update 25-NOV-2008, entry version 108
UniSave O96017, Q6QA03, Q6QA04, Q6QA05, Q6QA06, Q6QA07, Q6QA08, Q6QA10, Q6QA11, Q6QA12, Q6QA13, Q9HCQ8, Q9UGF0, Q9UGF1
UniRef100 UniRef100_O96017, UniRef100_O96017-6, UniRef100_O96017-11, UniRef100_O96017-3, UniRef100_O96017-7, UniRef100_O96017-9, UniRef100_O96017-12, UniRef100_O96017-2, UniRef100_O96017-8, UniRef100_O96017-4, UniRef100_O96017-10, UniRef100_O96017-5
UniParc UPI00000316FF, UPI000006EA3C, UPI000034E4A1, UPI000034E4A2, UPI000034E4A3, UPI000034E4A4, UPI000034E4A5, UPI000034E4A6, UPI000034E4A7, UPI000034E4A8, UPI000034E4A9, UPI000034E4AA
Description and origin of the Protein
Description Recommended
Full=Serine/threonine-protein kinase Chk2;
EC=2.7.11.1;
Synonym
Full=Cds1;
Gene name(s) CHEK2
Synonym(s) CHK2 RAD53
Organism source Homo sapiens (Human).
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
NCBI TaxID 9606
References
[1] Matsuoka,S., Huang,M., Elledge,S.J.,
Linkage of ATM to cell cycle regulation by the Chk2 protein kinase.
(1998) Science 282:1893-1897
Position NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF ASP-347.
Medline 99055399
DOI 10.1126/science.282.5395.1893;
PubMed
9836640 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from www.sciencemag.org Subscription requiredClick to get it from www.sciencemag.org FreeClick to get it from www.sciencemag.org Subscription requiredClick to get it from www.sciencemag.org CiteXplore
[2] Blasina,A., van de Weyer,I., Laus,M.C., Luyten,W.H.M.L., Parker,A.E., McGowan,C.H.,
A human homologue of the checkpoint kinase Cds1 directly inhibits Cdc25 phosphatase.
(1999) Curr. Biol. 9:1-10
Position NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
Medline 99108191
DOI 10.1016/S0960-9822(99)80041-4;
PubMed
9889122 Subscription requiredClick to get it from www.current-biology.com Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from ScienceDirect CiteXplore
[3] Brown,A.L., Lee,C.-H., Schwarz,J.K., Mitiku,N., Piwnica-Worms,H., Chung,J.H.,
A human Cds1-related kinase that functions downstream of ATM protein in the cellular response to DNA damage.
(1999) Proc. Natl. Acad. Sci. U.S.A. 96:3745-3750
Position NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
Medline 99199255
DOI 10.1073/pnas.96.7.3745;
PubMed
10097108 Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral Free after 6 monthsClick to get it from www.pnas.org Free after 6 monthsClick to get it from www.pnas.org Free after 6 monthsClick to get it from www.pnas.org Subscription requiredClick to get it from www.pnas.org CiteXplore
[4] Staalesen,V., Falck,J., Geisler,S., Bartkova,J., Borresen-Dale,A.L., Lukas,J., Lillehaug,J.R., Bartek,J., Lonning,P.E.,
Alternative splicing and mutation status of CHEK2 in stage III breast cancer.
(2004) Oncogene 23:8535-8544
Position NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7; 8; 9; 10; 11 AND 12), FUNCTION, AND SUBCELLULAR LOCATION.
Comments TISSUE=Mammary gland;
DOI 10.1038/sj.onc.1207928;
PubMed
15361853 Subscription requiredClick to get it from nature.com Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[5] Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A., Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y., Huckle,E.J., Beare,D.M., Dunham,I.,
A genome annotation-driven approach to cloning the human ORFeome.
(2004) Genome Biol. 5:0-RESEARCH84.11
Position NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
DOI 10.1186/gb-2004-5-10-r84;
PubMed
15461802 Open AccessClick to get it from BioMedCentral Open AccessClick to get it from BioMedCentral Open AccessClick to get it from BioMedCentral Subscription requiredClick to get it from BioMedCentral Open AccessClick to get it from genomebiology.com Open AccessClick to get it from genomebiology.com Open AccessClick to get it from genomebiology.com Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral CiteXplore
[6] Shao,R.-G., Zhang,H., Yu,Q., Pommier,Y.,
Chk2/HuCds1 cell cycle checkpoint protein kinase from human colon carcinoma HT29 cells: regulation by autophosphorylation and DNA- dependent protein kinase and inhibition by cell cycle regulatory drugs.
Submitted JUL-1999 to the EMBL GenBank DDBJ databases
Position NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Comments TISSUE=Colon carcinoma;
[7] Ogawa,A., Okabe-Nakamura,A.,
An alternative spliced Chk2.
Submitted MAR-2000 to the EMBL GenBank DDBJ databases
Position NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12).
Comments TISSUE=T-cell;
[8] Livingston,R.J., Rieder,M.J., Chung,M.-W., Ritchie,T.K., Olson,A.N., Nguyen,C.P., Nguyen,D.A., Poel,C.L., Chambers,S.W., Schackwitz,W.S., Sherwood,J.K., Sherwood,A.M., Leithauser,B.J., Nickerson,D.A.,
NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).
Submitted OCT-2004 to the EMBL GenBank DDBJ databases
Position NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-85; THR-157; MET-436; LYS-446; ILE-447; SER-448; LYS-501 AND VAL-512.
[9] Dunham,I., Hunt,A.R., Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J., Ainscough,R., Almeida,J.P., Babbage,A.K., Bagguley,C., Bailey,J., Barlow,K.F., Bates,K.N., Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., Burton,J., Carder,C., Carter,N.P., Chen,Y., Clark,G., Clegg,S.M., Cobley,V.E., Cole,C.G., Collier,R.E., Connor,R., Conroy,D., Corby,N.R., Coville,G.J., Cox,A.V., Davis,J., Dawson,E., Dhami,P.D., Dockree,C., Dodsworth,S.J., Durbin,R.M., Ellington,A.G., Evans,K.L., Fey,J.M., Fleming,K., French,L., Garner,A.A., Gilbert,J.G.R., Goward,M.E., Grafham,D.V., Griffiths,M.N.D., Hall,C., Hall,R.E., Hall-Tamlyn,G., Heathcott,R.W., Ho,S., Holmes,S., Hunt,S.E., Jones,M.C., Kershaw,J., Kimberley,A.M., King,A., Laird,G.K., Langford,C.F., Leversha,M.A., Lloyd,C., Lloyd,D.M., Martyn,I.D., Mashreghi-Mohammadi,M., Matthews,L.H., Mccann,O.T., Mcclay,J., Mclaren,S., McMurray,A.A., Milne,S.A., Mortimore,B.J., Odell,C.N., Pavitt,R., Pearce,A.V., Pearson,D., Phillimore,B.J.C.T., Phillips,S.H., Plumb,R.W., Ramsay,H., Ramsey,Y., Rogers,L., Ross,M.T., Scott,C.E., Sehra,H.K., Skuce,C.D., Smalley,S., Smith,M.L., Soderlund,C., Spragon,L., Steward,C.A., Sulston,J.E., Swann,R.M., Vaudin,M., Wall,M., Wallis,J.M., Whiteley,M.N., Willey,D.L., Williams,L., Williams,S.A., Williamson,H., Wilmer,T.E., Wilming,L., Wright,C.L., Hubbard,T., Bentley,D.R., Beck,S., Rogers,J., Shimizu,N., Minoshima,S., Kawasaki,K., Sasaki,T., Asakawa,S., Kudoh,J., Shintani,A., Shibuya,K., Yoshizaki,Y., Aoki,N., Mitsuyama,S., Roe,B.A., Chen,F., Chu,L., Crabtree,J., Deschamps,S., Do,A., Do,T., Dorman,A., Fang,F., Fu,Y., Hu,P., Hua,A., Kenton,S., Lai,H., Lao,H.I., Lewis,J., Lewis,S., Lin,S.-P., Loh,P., Malaj,E., Nguyen,T., Pan,H., Phan,S., Qi,S., Qian,Y., Ray,L., Ren,Q., Shaull,S., Sloan,D., Song,L., Wang,Q., Wang,Y., Wang,Z., White,J., Willingham,D., Wu,H., Yao,Z., Zhan,M., Zhang,G., Chissoe,S., Murray,J., Miller,N., Minx,P., Fulton,R., Johnson,D., Bemis,G., Bentley,D., Bradshaw,H., Bourne,S., Cordes,M., Du,Z., Fulton,L., Goela,D., Graves,T., Hawkins,J., Hinds,K., Kemp,K., Latreille,P., Layman,D., Ozersky,P., Rohlfing,T., Scheet,P., Walker,C., Wamsley,A., Wohldmann,P., Pepin,K., Nelson,J., Korf,I., Bedell,J.A., Hillier,L.W., Mardis,E., Waterston,R., Wilson,R., Emanuel,B.S., Shaikh,T., Kurahashi,H., Saitta,S., Budarf,M.L., McDermid,H.E., Johnson,A., Wong,A.C.C., Morrow,B.E., Edelmann,L., Kim,U.J., Shizuya,H., Simon,M.I., Dumanski,J.P., Peyrard,M., Kedra,D., Seroussi,E., Fransson,I., Tapia,I., Bruder,C.E., O'Brien,K.P., Wilkinson,P., Bodenteich,A., Hartman,K., Hu,X., Khan,A.S., Lane,L., Tilahun,Y., Wright,H.,
The DNA sequence of human chromosome 22.
(1999) Nature 402:489-495
Position NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Medline 20057165
DOI 10.1038/990031;
PubMed
10591208 Subscription requiredClick to get it from nature.com Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[10]
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
(2004) Genome Res. 14:2121-2127
Position NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Comments TISSUE=Muscle;
DOI 10.1101/gr.2596504;
PubMed
15489334 Free after 6 monthsClick to get it from www.genome.org Free after 6 monthsClick to get it from www.genome.org FreeClick to get it from www.genome.org Subscription requiredClick to get it from DOI Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral CiteXplore
[11] Tosti,E., Waldbaum,L., Warshaw,G., Gross,E.A., Ruggieri,R.,
The stress kinase MRK contributes to regulation of DNA damage checkpoints through a p38gamma-independent pathway.
(2004) J. Biol. Chem. 279:47652-47660
Position ENZYME REGULATION, PHOSPHORYLATION AT THR-68, AND MUTAGENESIS OF THR-68 AND ASP-368.
DOI 10.1074/jbc.M409961200;
PubMed
15342622 Open AccessClick to get it from intl.jbc.org Open AccessClick to get it from intl.jbc.org Open AccessClick to get it from intl.jbc.org Subscription requiredClick to get it from DOI Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[12] Li,J., Williams,B.L., Haire,L.F., Goldberg,M., Wilker,E., Durocher,D., Yaffe,M.B., Jackson,S.P., Smerdon,S.J.,
Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2.
(2002) Mol. Cell 9:1045-1054
Position X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 64-212.
Medline 22045891
DOI 10.1016/S1097-2765(02)00527-0;
PubMed
12049740 Subscription requiredClick to get it from www.molecule.org Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from ScienceDirect CiteXplore
[13] Bell,D.W., Varley,J.M., Szydlo,T.E., Kang,D.H., Wahrer,D.C.R., Shannon,K.E., Lubratovich,M., Versalis,S.J., Isselbacher,K.J., Fraumeni,J.F. Jr., Birch,J.M., Li,F.P., Garber,J.E., Haber,D.A.,
Heterozygous germ line hCHK2 mutations in Li-Fraumeni syndrome.
(1999) Science 286:2528-2531
Position VARIANT THR-157, AND VARIANT COLON CANCER TRP-145.
Medline 20085462
DOI 10.1126/science.286.5449.2528;
PubMed
10617473 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from www.sciencemag.org Subscription requiredClick to get it from www.sciencemag.org FreeClick to get it from www.sciencemag.org Subscription requiredClick to get it from www.sciencemag.org CiteXplore
[14] Allinen,M., Huusko,P., Maentyniemi,S., Launonen,V., Winqvist,R.,
Mutation analysis of the CHK2 gene in families with hereditary breast cancer.
(2001) Br. J. Cancer 85:209-212
Position VARIANT THR-157.
Medline 21354286
DOI 10.1054/bjoc.2001.1858;
PubMed
11461078 Subscription requiredClick to get it from nature.com Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[15] Lee,S.B., Kim,S.H., Bell,D.W., Wahrer,D.C.R., Schiripo,T.A., Jorczak,M.M., Sgroi,D.C., Garber,J.E., Li,F.P., Nichols,K.E., Varley,J.M., Godwin,A.K., Shannon,K.M., Harlow,E., Haber,D.A.,
Destabilization of CHK2 by a missense mutation associated with Li- Fraumeni Syndrome.
(2001) Cancer Res. 61:8062-8067
Position VARIANT LFS2 TRP-145.
Medline 21575821
PubMed
11719428 Subscription requiredClick to get it from cancerres.aacrjournals.org Subscription requiredClick to get it from cancerres.aacrjournals.org FreeClick to get it from cancerres.aacrjournals.org Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[16] Ingvarsson,S., Sigbjornsdottir,B.I., Huiping,C., Hafsteinsdottir,S.H., Ragnarsson,G., Barkardottir,R.B., Arason,A., Egilsson,V., Bergthorsson,J.T.,
Mutation analysis of the CHK2 gene in breast carcinoma and other cancers.
(2002) Breast Cancer Res. 4:0-R4
Position VARIANT MULTIPLE CANCERS LYS-59.
DOI 10.1186/bcr435;
PubMed
12052256 Open AccessClick to get it from BioMedCentral Open AccessClick to get it from BioMedCentral Open AccessClick to get it from BioMedCentral Subscription requiredClick to get it from BioMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral CiteXplore
[17] Sodha,N., Bullock,S., Taylor,R., Mitchell,G., Guertl-Lackner,B., Williams,R.D., Bevan,S., Bishop,K., McGuire,S., Houlston,R.S., Eeles,R.A.,
CHEK2 variants in susceptibility to breast cancer and evidence of retention of the wild type allele in tumours.
(2002) Br. J. Cancer 87:1445-1448
Position VARIANTS GLY-117; GLN-137 AND HIS-180.
Medline 22340809
DOI 10.1038/sj.bjc.6600637;
PubMed
12454775 Subscription requiredClick to get it from nature.com Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[18] Miller,C.W., Ikezoe,T., Krug,U., Hofmann,W.K., Tavor,S., Vegesna,V., Tsukasaki,K., Takeuchi,S., Koeffler,H.P.,
Mutations of the CHK2 gene are found in some osteosarcomas, but are rare in breast, lung, and ovarian tumors.
(2002) Genes Chromosomes Cancer 33:17-21
Position VARIANTS OSTEOSARCOMA SER-17 AND LEU-85.
Medline 21610705
DOI 10.1002/gcc.1207;
PubMed
11746983 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from WileyInterScience CiteXplore
[19] Dong,X., Wang,L., Taniguchi,K., Wang,X., Cunningham,J.M., McDonnell,S.K., Qian,C., Marks,A.F., Slager,S.L., Peterson,B.J., Smith,D.I., Cheville,J.C., Blute,M.L., Jacobsen,S.J., Schaid,D.J., Tindall,D.J., Thibodeau,S.N., Liu,W.,
Mutations in CHEK2 associated with prostate cancer risk.
(2003) Am. J. Hum. Genet. 72:270-280
Position VARIANTS PROSTATE CANCER LYS-64; PRO-145; ARG-167; CYS-180; HIS-180; CYS-181; HIS-181; LYS-239; PHE-251; HIS-318; PRO-323; CYS-327 AND LYS-476, AND VARIANT THR-157.
Medline 22428307
DOI 10.1086/346094;
PubMed
12533788 Subscription requiredClick to get it from www.journals.uchicago.edu Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral CiteXplore
[20] Schutte,M., Seal,S., Barfoot,R., Meijers-Heijboer,H., Wasielewski,M., Evans,D.G., Eccles,D., Meijers,C., Lohman,F., Klijn,J., van den Ouweland,A., Brady,A., Cole,T., Collins,A., Cox,H., Donaldson,A., Eeles,R., Evans,G., Gregory,H., Gray,J., Houlston,R., Lalloo,F., Lucassen,A., Mackay,J., Mitchell,G., Morrison,P., Murday,V., Narod,S., Patterson,J., Peretz,T., Phelan,C.M., Rogers,M., Schofield,A., Tonin,P., Weber,B., Weber,W., Futreal,P.A., Nathanson,K.L., Weber,B.L., Easton,D.F., Stratton,M.R., Rahman,N.,
Variants in CHEK2 other than 1100delC do not make a major contribution to breast cancer susceptibility.
(2003) Am. J. Hum. Genet. 72:1023-1028
Position VARIANTS GLY-117; TRP-145 AND THR-157.
Medline 22534962
DOI 10.1086/373965;
PubMed
12610780 Subscription requiredClick to get it from www.journals.uchicago.edu Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral CiteXplore
[21] Seppaelae,E.H., Ikonen,T., Mononen,N., Autio,V., Roekman,A., Matikainen,M.P., Tammela,T.L.J., Schleutker,J.,
CHEK2 variants associate with hereditary prostate cancer.
(2003) Br. J. Cancer 89:1966-1970
Position VARIANT THR-157.
Medline 22973597
DOI 10.1038/sj.bjc.6601425;
PubMed
14612911 Subscription requiredClick to get it from nature.com Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[22] Cybulski,C., Gorski,B., Huzarski,T., Masojc,B., Mierzejewski,M., Debniak,T., Teodorczyk,U., Byrski,T., Gronwald,J., Matyjasik,J., Zlowocka,E., Lenner,M., Grabowska,E., Nej,K., Castaneda,J., Medrek,K., Szymanska,A., Szymanska,J., Kurzawski,G., Suchy,J., Oszurek,O., Witek,A., Narod,S.A., Lubinski,J.,
CHEK2 is a multiorgan cancer susceptibility gene.
(2004) Am. J. Hum. Genet. 75:1131-1135
Position VARIANT THR-157.
DOI 10.1086/426403;
PubMed
15492928 Subscription requiredClick to get it from www.journals.uchicago.edu Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral CiteXplore
[23] Friedrichsen,D.M., Malone,K.E., Doody,D.R., Daling,J.R., Ostrander,E.A.,
Frequency of CHEK2 mutations in a population based, case-control study of breast cancer in young women.
(2004) Breast Cancer Res. 6:0-R635
Position VARIANTS TRP-145 AND THR-157.
DOI 10.1186/bcr933;
PubMed
15535844 Open AccessClick to get it from BioMedCentral Open AccessClick to get it from BioMedCentral Open AccessClick to get it from BioMedCentral Subscription requiredClick to get it from BioMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral CiteXplore
[24] Cybulski,C., Huzarski,T., Gorski,B., Masojc,B., Mierzejewski,M., Debniak,T., Gliniewicz,B., Matyjasik,J., Zlowocka,E., Kurzawski,G., Sikorski,A., Posmyk,M., Szwiec,M., Czajka,R., Narod,S.A., Lubinski,J.,
A novel founder CHEK2 mutation is associated with increased prostate cancer risk.
(2004) Cancer Res. 64:2677-2679
Position VARIANT THR-157.
DOI 10.1158/0008-5472.CAN-04-0341;
PubMed
15087378 Free after 12 monthsClick to get it from cancerres.aacrjournals.org Free after 12 monthsClick to get it from cancerres.aacrjournals.org FreeClick to get it from cancerres.aacrjournals.org Subscription requiredClick to get it from aacrjournals.org Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[25] Dufault,M.R., Betz,B., Wappenschmidt,B., Hofmann,W., Bandick,K., Golla,A., Pietschmann,A., Nestle-Kraemling,C., Rhiem,K., Huettner,C., von Lindern,C., Dall,P., Kiechle,M., Untch,M., Jonat,W., Meindl,A., Scherneck,S., Niederacher,D., Schmutzler,R.K., Arnold,N.,
Limited relevance of the CHEK2 gene in hereditary breast cancer.
(2004) Int. J. Cancer 110:320-325
Position VARIANT THR-157.
DOI 10.1002/ijc.20073;
PubMed
15095295 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from www.chestjournal.org CiteXplore
[26] Kilpivaara,O., Vahteristo,P., Falck,J., Syrjaekoski,K., Eerola,H., Easton,D., Bartkova,J., Lukas,J., Heikkilae,P., Aittomaeki,K., Holli,K., Blomqvist,C., Kallioniemi,O.-P., Bartek,J., Nevanlinna,H.,
CHEK2 variant I157T may be associated with increased breast cancer risk.
(2004) Int. J. Cancer 111:543-547
Position VARIANT THR-157.
DOI 10.1002/ijc.20299;
PubMed
15239132 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from pubs.acs.com CiteXplore
[27] Shaag,A., Walsh,T., Renbaum,P., Kirchhoff,T., Nafa,K., Shiovitz,S., Mandell,J.B., Welcsh,P., Lee,M.K., Ellis,N., Offit,K., Levy-Lahad,E., King,M.-C.,
Functional and genomic approaches reveal an ancient CHEK2 allele associated with breast cancer in the Ashkenazi Jewish population.
(2005) Hum. Mol. Genet. 14:555-563
Position VARIANTS LEU-85 AND PHE-428.
DOI 10.1093/hmg/ddi052;
PubMed
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[28] Bogdanova,N., Enbetaen-Dubrowinskaja,N., Feshchenko,S., Lazjuk,G.I., Rogov,Y.I., Dammann,O., Bremer,M., Karstens,J.H., Sohn,C., Doerk,T.,
Association of two mutations in the CHEK2 gene with breast cancer.
(2005) Int. J. Cancer 116:263-266
Position VARIANT THR-157.
DOI 10.1002/ijc.21022;
PubMed
15810020 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from pubs.acs.com CiteXplore
[29] van Puijenbroek,M., van Asperen,C.J., van Mil,A., Devilee,P., van Wezel,T., Morreau,H.,
Homozygosity for a CHEK2*1100delC mutation identified in familial colorectal cancer does not lead to a severe clinical phenotype.
(2005) J. Pathol. 206:198-204
Position VARIANTS GLY-117; GLN-137; TRP-145; THR-157 AND HIS-180.
DOI 10.1002/path.1764;
PubMed
15818573 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from pubs.acs.com CiteXplore
Comments
FUNCTION Regulates cell cycle checkpoints and apoptosis in response to DNA damage, particularly to DNA double-strand breaks. Inhibits CDC25C phosphatase by phosphorylation on 'Ser-216', preventing the entry into mitosis. May also play a role in meiosis. Regulates the TP53 tumor suppressor through phosphorylation at 'Thr-18' and 'Ser-20'.
CATALYTIC ACTIVITY ATP + a protein = ADP + a phosphoprotein.
COFACTOR Magnesium.
ENZYME REGULATION Rapidly phosphorylated on Thr-68 by MLTK in response to DNA damage and to replication block. Kinase activity is also up-regulated by autophosphorylation.
INTERACTION
Q9NY61:AATF NbExp=3 IntAct=EBI-1180783, EBI-372428
Q9Y248:GINS2 NbExp=1 IntAct=EBI-1180783, EBI-747491
P53350:PLK1 NbExp=3 IntAct=EBI-1180783, EBI-476768
Q15172:PPP2R5A NbExp=1 IntAct=EBI-1180783, EBI-641666
Q15173:PPP2R5B NbExp=1 IntAct=EBI-1180783, EBI-1369497
Q13362-1:PPP2R5C NbExp=3 IntAct=EBI-1180783, EBI-1266170
Q13362-2:PPP2R5C NbExp=1 IntAct=EBI-1180783, EBI-1266173
Q13362-3:PPP2R5C NbExp=3 IntAct=EBI-1180783, EBI-1266176
Q16537:PPP2R5E NbExp=3 IntAct=EBI-1180783, EBI-968374
P02340:Tp53 (xeno) NbExp=1 IntAct=EBI-1180783, EBI-474016
P55072:VCP NbExp=2 IntAct=EBI-1180783, EBI-355164
SUBCELLULAR LOCATION Isoform 2: Nucleus. Note=Isoform 10 is present throughout the cell.
SUBCELLULAR LOCATION Isoform 4: Nucleus.
SUBCELLULAR LOCATION Isoform 7: Nucleus.
SUBCELLULAR LOCATION Isoform 9: Nucleus.
SUBCELLULAR LOCATION Isoform 12: Nucleus.
ALTERNATIVE PRODUCTS Event=Alternative splicing; Named isoforms=12;
Name=1;
IsoId=O96017-1; Sequence=Displayed;
Name=2; Synonyms=ins2;
IsoId=O96017-2; Sequence=VSP_014564, VSP_014567, VSP_014568;
Note=Catalytically inactive;
Name=3; Synonyms=del2-12;
IsoId=O96017-3; Sequence=VSP_014559;
Name=4; Synonyms=del2-3;
IsoId=O96017-4; Sequence=VSP_014558;
Note=Catalytically active;
Name=5; Synonyms=del4;
IsoId=O96017-5; Sequence=VSP_014565, VSP_014566;
Name=6; Synonyms=sub3;
IsoId=O96017-6; Sequence=VSP_014562, VSP_014563;
Name=7; Synonyms=del9-12;
IsoId=O96017-7; Sequence=VSP_014572, VSP_014573;
Note=Catalytically inactive;
Name=8; Synonyms=del7;
IsoId=O96017-8; Sequence=VSP_014569, VSP_014570;
Name=9; Synonyms=insx;
IsoId=O96017-9; Sequence=VSP_014557;
Note=Retains low level of catalytic activity;
Name=10; Synonyms=iso2;
IsoId=O96017-10; Sequence=VSP_014560, VSP_014561;
Note=Catalytically inactive;
Name=11; Synonyms=iso1;
IsoId=O96017-11; Sequence=VSP_014556;
Name=12; Synonyms=del9;
IsoId=O96017-12; Sequence=VSP_014571;
Note=Catalytically inactive;
TISSUE SPECIFICITY High expression is found in testis, spleen, colon and peripheral blood leukocytes. Low expression is found in other tissues.
DISEASE Defects in CHEK2 are associated with Li-Fraumeni syndrome 2 (LFS2) [MIM:609265]; a highly penetrant familial cancer phenotype usually associated with inherited mutations in p53/TP53.
DISEASE Defects in CHEK2 are found in some patients with prostate cancer (CaP) [MIM:176807].
DISEASE Defects in CHEK2 are found in some patients with osteosarcoma (OSRC) [MIM:259500].
SIMILARITY Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CHK2 subfamily.
SIMILARITY Contains 1 FHA domain.
SIMILARITY Contains 1 protein kinase domain.
WEB RESOURCE Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CHEK2ID312.html";
WEB RESOURCE Name=GeneReviews; URL="http://www.genetests.org/query?gene=CHEK2";
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms Distributed under the Creative Commons Attribution-NoDerivs License
Database cross-references
EMBL
AF086904; AAC83693.1; -; mRNA.
AJ131197; CAA10319.1; -; mRNA.
AF096279; AAD11784.1; -; mRNA.
AY551295; AAS58456.1; -; mRNA.
AY551296; AAS58457.1; -; mRNA.
AY551297; AAS58458.1; -; mRNA.
AY551298; AAS58459.1; -; mRNA.
AY551299; AAS58460.1; -; mRNA.
AY551300; AAS58461.1; -; mRNA.
AY551301; AAS58462.1; -; mRNA.
AY551302; AAS58463.1; -; mRNA.
AY551303; AAS58464.1; -; mRNA.
AY551304; AAS58465.1; -; mRNA.
AY551305; AAS58466.1; -; mRNA.
CR456418; CAG30304.1; -; mRNA.
AF174135; AAD48504.1; -; mRNA.
AB040105; BAB17231.1; -; mRNA.
AY800241; AAV41895.1; -; Genomic_DNA.
AL121825; CAH73823.1; -; Genomic_DNA.
AL117330; CAH73823.1; JOINED; Genomic_DNA.
AL117330; CAH73875.1; -; Genomic_DNA.
AL121825; CAH73875.1; JOINED; Genomic_DNA.
BC004207; AAH04207.1; -; mRNA.
RefSeq
NP_001005735.1; -.
NP_009125.1; -.
NP_665861.1; -.
UniGene
Hs.291363; -.
Hs.505297; -.
Hs.632780; -.
PDB
1GXC; X-ray; 2.70 A; A/D/G/J=64-212.
2CN5; X-ray; 2.25 A; A=210-531.
2CN8; X-ray; 2.70 A; A=210-531.
PDBsum
1GXC; -.
2CN5; -.
2CN8; -.
DIP
DIP:24270N; -.
IntAct
O96017; -.
PhosphoSite
O96017; -.
Ensembl
ENSG00000183765; Homo sapiens.
GeneID
11200; -.
KEGG
hsa:11200; -.
H-InvDB
HIX0016341; -.
HIX0038241; -.
HGNC
HGNC:16627; CHEK2.
HPA
CAB002030; -.
HPA001878; -.
MIM
176807; phenotype.
259500; phenotype.
604373; gene+phenotype.
609265; phenotype.
Orphanet
145; Breast cancer, familial.
524; Li-Fraumeni syndrome.
668; Osteosarcoma.
1331; Prostate cancer, familial.
PharmGKB
PA404; -.
HOVERGEN
O96017; -.
Reactome
REACT_1538; Cell Cycle Checkpoints.
NextBio
42629; -.
ArrayExpress
O96017; -.
GermOnline
ENSG00000183765; Homo sapiens.
GO
GO:0016605; C:PML body; IDA:UniProtKB.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
GO:0005515; F:protein binding; IPI:UniProtKB.
GO:0004674; F:protein serine/threonine kinase activity; TAS:UniProtKB.
GO:0000077; P:DNA damage checkpoint; TAS:UniProtKB.
GO:0008630; P:DNA damage response, signal transduction re...; IDA:UniProtKB.
GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
InterPro
IPR000253; FHA.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Gene3D
G3DSA:2.60.200.20; FHA; 1.
Pfam
PF00498; FHA; 1.
PF00069; Pkinase; 1.
ProDom
PD000001; Prot_kinase; 1.
SMART
SM00240; FHA; 1.
SM00220; S_TKc; 1.
PROSITE
PS50006; FHA_DOMAIN; 1.
PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
Protein Existence
1: Evidence at protein level;
Keywords
3D-structure; Alternative splicing; ATP-binding; Cell cycle; Disease mutation; Kinase; Li-Fraumeni syndrome; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Serine/threonine-protein kinase; Transferase;
CHAIN: 1 543, Serine/threonine-protein kinase Chk2. /FTId=PRO_0000085858. DOMAIN: 113 175, FHA. DOMAIN: 220 486, Protein kinase. NP_BIND: 226 234, ATP (By similarity). ACT_SITE: 347 347, Proton acceptor. BINDING: 249 249, ATP (By similarity). MOD_RES: 68 68, Phosphothreonine; by MLTK. VAR_SEQ: 75 392, Missing (in isoform 11). /FTId=VSP_014556. VAR_SEQ: 107 487, Missing (in isoform 3). /FTId=VSP_014559. VAR_SEQ: 107 197, Missing (in isoform 4). /FTId=VSP_014558. VAR_SEQ: 107 107, E -> ETESGHVTQSDLELLLSSDPPASASQSAGIRGVRHH PRPVCSLK (in isoform 9). /FTId=VSP_014557. VAR_SEQ: 131 147, KRTDKYRTYSKKHFRIF -> EFRSYSFYLP (in isoform 10). /FTId=VSP_014560. VAR_SEQ: 148 543, Missing (in isoform 10). /FTId=VSP_014561. VAR_SEQ: 150 165, VGPKNSYIAYIEDHSG -> ENLSCPYRIWFNFCLF (in isoform 6). /FTId=VSP_014562. VAR_SEQ: 166 543, Missing (in isoform 6). /FTId=VSP_014563. VAR_SEQ: 198 224, VFVFFDLTVDDQSVYPKALRDEYIMSK -> EKILKIYSLS RFSKIRRGAVAHVFNPS (in isoform 2). /FTId=VSP_014564. VAR_SEQ: 199 203, FVFFD -> VPVER (in isoform 5). /FTId=VSP_014565. VAR_SEQ: 204 543, Missing (in isoform 5). /FTId=VSP_014566. VAR_SEQ: 228 234, SGACGEV -> GRGWQIT (in isoform 2). /FTId=VSP_014567. VAR_SEQ: 235 543, Missing (in isoform 2). /FTId=VSP_014568. VAR_SEQ: 283 289, PCIIKIK -> DGRGRAV (in isoform 8). /FTId=VSP_014569. VAR_SEQ: 290 543, Missing (in isoform 8). /FTId=VSP_014570. VAR_SEQ: 337 365, Missing (in isoform 12). /FTId=VSP_014571. VAR_SEQ: 337 339, YLH -> MKT (in isoform 7). /FTId=VSP_014572. VAR_SEQ: 340 543, Missing (in isoform 7). /FTId=VSP_014573. VARIANT: 17 17, A -> S (in osteosarcoma; somatic mutation; might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer). /FTId=VAR_019101. VARIANT: 59 59, T -> K (in multiple cancers). /FTId=VAR_026630. VARIANT: 64 64, E -> K (in prostate cancer; somatic mutation). /FTId=VAR_019107. VARIANT: 85 85, P -> L (in osteosarcoma; is a neutral allele among Ashkenazi Jewish women; dbSNP:rs17883862). /FTId=VAR_019102. VARIANT: 117 117, R -> G (might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer). /FTId=VAR_022461. VARIANT: 137 137, R -> Q (might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer). /FTId=VAR_022462. VARIANT: 145 145, R -> P (in prostate cancer; somatic mutation). /FTId=VAR_019108. VARIANT: 145 145, R -> W (in colon cancer and LFS2; does not cause protein abrogation in familial colorectal cancer). /FTId=VAR_008554. VARIANT: 157 157, I -> T (might influence susceptibility to diffferent types of cancer; does not cause protein abrogation in familial colorectal cancer; dbSNP:rs17879961). /FTId=VAR_008555. VARIANT: 167 167, G -> R (in prostate cancer; somatic mutation). /FTId=VAR_019109. VARIANT: 180 180, R -> C (in prostate cancer; somatic mutation). /FTId=VAR_019103. VARIANT: 180 180, R -> H (in prostate cancer; somatic mutation). /FTId=VAR_019110. VARIANT: 181 181, R -> C (in prostate cancer; somatic mutation). /FTId=VAR_019104. VARIANT: 181 181, R -> H (in prostate cancer; somatic mutation). /FTId=VAR_019105. VARIANT: 239 239, E -> K (in prostate cancer; germline mutation). /FTId=VAR_019106. VARIANT: 251 251, I -> F (in prostate cancer; germline mutation). /FTId=VAR_019111. VARIANT: 318 318, R -> H (in prostate cancer; somatic mutation). /FTId=VAR_019112. VARIANT: 323 323, T -> P (in prostate cancer; somatic mutation). /FTId=VAR_019113. VARIANT: 327 327, Y -> C (in prostate cancer; somatic mutation). /FTId=VAR_019114. VARIANT: 347 347, D -> N (in dbSNP:rs28909980). /FTId=VAR_029154. VARIANT: 406 406, R -> H (in dbSNP:rs299671). /FTId=VAR_024572. VARIANT: 428 428, S -> F (increases breast cancer risk approximately 2-fold among Ashkenazi Jewish women). /FTId=VAR_022463. VARIANT: 436 436, L -> M (in dbSNP:rs17882922). /FTId=VAR_021117. VARIANT: 446 446, N -> K (in dbSNP:rs17880867). /FTId=VAR_021118. VARIANT: 447 447, F -> I (in dbSNP:rs17881473). /FTId=VAR_021119. VARIANT: 448 448, I -> S (in dbSNP:rs17886163). /FTId=VAR_021120. VARIANT: 476 476, T -> K (in prostate cancer; somatic mutation). /FTId=VAR_019115. VARIANT: 500 500, S -> C (in dbSNP:rs28909981). /FTId=VAR_029155. VARIANT: 501 501, E -> K (in dbSNP:rs17883172). /FTId=VAR_021121. VARIANT: 512 512, L -> V (in dbSNP:rs17882942). /FTId=VAR_021122. MUTAGEN: 68 68, T->A: Loss of activation and phosphorylation. MUTAGEN: 347 347, D->A: Loss of kinase activity. MUTAGEN: 368 368, D->N: Loss of autophosphorylation activity. STRAND: 94 98, STRAND: 106 108, STRAND: 110 118, STRAND: 122 124, STRAND: 144 150, STRAND: 154 162, STRAND: 168 170, STRAND: 180 182, STRAND: 187 193, STRAND: 197 203, STRAND: 220 228, STRAND: 230 239, STRAND: 244 252, STRAND: 288 302, STRAND: 353 361, STRAND: 364 366, STRAND: 429 431, HELIX: 128 132, HELIX: 135 138, HELIX: 214 219, HELIX: 270 279, HELIX: 309 312, HELIX: 321 340, HELIX: 350 352, HELIX: 378 384, HELIX: 388 390, HELIX: 393 397, HELIX: 407 422, HELIX: 436 442, HELIX: 449 452, HELIX: 457 466, HELIX: 477 481, HELIX: 484 486, HELIX: 489 502, TURN: 240 243, TURN: 398 403, TURN: 471 473, CHAIN: 1 543, Serine/threonine-protein kinase Chk2. /FTId=PRO_0000085858. DOMAIN: 113 175, FHA. DOMAIN: 220 486, Protein kinase. NP_BIND: 226 234, ATP (By similarity). ACT_SITE: 347 347, Proton acceptor. BINDING: 249 249, ATP (By similarity). MOD_RES: 68 68, Phosphothreonine; by MLTK. VAR_SEQ: 75 392, Missing (in isoform 11). /FTId=VSP_014556. VAR_SEQ: 107 487, Missing (in isoform 3). /FTId=VSP_014559. VAR_SEQ: 107 197, Missing (in isoform 4). /FTId=VSP_014558. VAR_SEQ: 107 107, E -> ETESGHVTQSDLELLLSSDPPASASQSAGIRGVRHH PRPVCSLK (in isoform 9). /FTId=VSP_014557. VAR_SEQ: 131 147, KRTDKYRTYSKKHFRIF -> EFRSYSFYLP (in isoform 10). /FTId=VSP_014560. VAR_SEQ: 148 543, Missing (in isoform 10). /FTId=VSP_014561. VAR_SEQ: 150 165, VGPKNSYIAYIEDHSG -> ENLSCPYRIWFNFCLF (in isoform 6). /FTId=VSP_014562. VAR_SEQ: 166 543, Missing (in isoform 6). /FTId=VSP_014563. VAR_SEQ: 198 224, VFVFFDLTVDDQSVYPKALRDEYIMSK -> EKILKIYSLS RFSKIRRGAVAHVFNPS (in isoform 2). /FTId=VSP_014564. VAR_SEQ: 199 203, FVFFD -> VPVER (in isoform 5). /FTId=VSP_014565. VAR_SEQ: 204 543, Missing (in isoform 5). /FTId=VSP_014566. VAR_SEQ: 228 234, SGACGEV -> GRGWQIT (in isoform 2). /FTId=VSP_014567. VAR_SEQ: 235 543, Missing (in isoform 2). /FTId=VSP_014568. VAR_SEQ: 283 289, PCIIKIK -> DGRGRAV (in isoform 8). /FTId=VSP_014569. VAR_SEQ: 290 543, Missing (in isoform 8). /FTId=VSP_014570. VAR_SEQ: 337 365, Missing (in isoform 12). /FTId=VSP_014571. VAR_SEQ: 337 339, YLH -> MKT (in isoform 7). /FTId=VSP_014572. VAR_SEQ: 340 543, Missing (in isoform 7). /FTId=VSP_014573. VARIANT: 17 17, A -> S (in osteosarcoma; somatic mutation; might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer). /FTId=VAR_019101. VARIANT: 59 59, T -> K (in multiple cancers). /FTId=VAR_026630. VARIANT: 64 64, E -> K (in prostate cancer; somatic mutation). /FTId=VAR_019107. VARIANT: 85 85, P -> L (in osteosarcoma; is a neutral allele among Ashkenazi Jewish women; dbSNP:rs17883862). /FTId=VAR_019102. VARIANT: 117 117, R -> G (might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer). /FTId=VAR_022461. VARIANT: 137 137, R -> Q (might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer). /FTId=VAR_022462. VARIANT: 145 145, R -> P (in prostate cancer; somatic mutation). /FTId=VAR_019108. VARIANT: 145 145, R -> W (in colon cancer and LFS2; does not cause protein abrogation in familial colorectal cancer). /FTId=VAR_008554. VARIANT: 157 157, I -> T (might influence susceptibility to diffferent types of cancer; does not cause protein abrogation in familial colorectal cancer; dbSNP:rs17879961). /FTId=VAR_008555. VARIANT: 167 167, G -> R (in prostate cancer; somatic mutation). /FTId=VAR_019109. VARIANT: 180 180, R -> C (in prostate cancer; somatic mutation). /FTId=VAR_019103. VARIANT: 180 180, R -> H (in prostate cancer; somatic mutation). /FTId=VAR_019110. VARIANT: 181 181, R -> C (in prostate cancer; somatic mutation). /FTId=VAR_019104. VARIANT: 181 181, R -> H (in prostate cancer; somatic mutation). /FTId=VAR_019105. VARIANT: 239 239, E -> K (in prostate cancer; germline mutation). /FTId=VAR_019106. VARIANT: 251 251, I -> F (in prostate cancer; germline mutation). /FTId=VAR_019111. VARIANT: 318 318, R -> H (in prostate cancer; somatic mutation). /FTId=VAR_019112. VARIANT: 323 323, T -> P (in prostate cancer; somatic mutation). /FTId=VAR_019113. VARIANT: 327 327, Y -> C (in prostate cancer; somatic mutation). /FTId=VAR_019114. VARIANT: 347 347, D -> N (in dbSNP:rs28909980). /FTId=VAR_029154. VARIANT: 406 406, R -> H (in dbSNP:rs299671). /FTId=VAR_024572. VARIANT: 428 428, S -> F (increases breast cancer risk approximately 2-fold among Ashkenazi Jewish women). /FTId=VAR_022463. VARIANT: 436 436, L -> M (in dbSNP:rs17882922). /FTId=VAR_021117. VARIANT: 446 446, N -> K (in dbSNP:rs17880867). /FTId=VAR_021118. VARIANT: 447 447, F -> I (in dbSNP:rs17881473). /FTId=VAR_021119. VARIANT: 448 448, I -> S (in dbSNP:rs17886163). /FTId=VAR_021120. VARIANT: 476 476, T -> K (in prostate cancer; somatic mutation). /FTId=VAR_019115. VARIANT: 500 500, S -> C (in dbSNP:rs28909981). /FTId=VAR_029155. VARIANT: 501 501, E -> K (in dbSNP:rs17883172). /FTId=VAR_021121. VARIANT: 512 512, L -> V (in dbSNP:rs17882942). /FTId=VAR_021122. MUTAGEN: 68 68, T->A: Loss of activation and phosphorylation. MUTAGEN: 347 347, D->A: Loss of kinase activity. MUTAGEN: 368 368, D->N: Loss of autophosphorylation activity. STRAND: 94 98, STRAND: 106 108, STRAND: 110 118, STRAND: 122 124, HELIX: 128 132, HELIX: 135 138, STRAND: 144 150, STRAND: 154 162, STRAND: 168 170, STRAND: 180 182, STRAND: 187 193, STRAND: 197 203, HELIX: 214 219, STRAND: 220 228, STRAND: 230 239, TURN: 240 243, STRAND: 244 252, HELIX: 270 279, STRAND: 288 302, HELIX: 309 312, HELIX: 321 340, HELIX: 350 352, STRAND: 353 361, STRAND: 364 366, HELIX: 378 384, HELIX: 388 390, HELIX: 393 397, TURN: 398 403, HELIX: 407 422, STRAND: 429 431, HELIX: 436 442, HELIX: 449 452, HELIX: 457 466, TURN: 471 473, HELIX: 477 481, HELIX: 484 486, HELIX: 489 502,
Key Begin End Length Description RESID
  CHAIN 1 543 543 Serine/threonine-protein kinase Chk2. /FTId=PRO_0000085858.
  DOMAIN 113 175 63 FHA.
  DOMAIN 220 486 267 Protein kinase.
  NP_BIND 226 234 9 ATP (By similarity).
  ACT_SITE 347 347 1 Proton acceptor.
  BINDING 249 249 1 ATP (By similarity).
  MOD_RES 68 68 1 Phosphothreonine; by MLTK.
  VAR_SEQ 75 392 318 Missing (in isoform 11). /FTId=VSP_014556.
  VAR_SEQ 107 487 381 Missing (in isoform 3). /FTId=VSP_014559.
  VAR_SEQ 107 197 91 Missing (in isoform 4). /FTId=VSP_014558.
  VAR_SEQ 107 107 1 E -> ETESGHVTQSDLELLLSSDPPASASQSAGIRGVRHH PRPVCSLK (in isoform 9). /FTId=VSP_014557.
  VAR_SEQ 131 147 17 KRTDKYRTYSKKHFRIF -> EFRSYSFYLP (in isoform 10). /FTId=VSP_014560.
  VAR_SEQ 148 543 396 Missing (in isoform 10). /FTId=VSP_014561.
  VAR_SEQ 150 165 16 VGPKNSYIAYIEDHSG -> ENLSCPYRIWFNFCLF (in isoform 6). /FTId=VSP_014562.
  VAR_SEQ 166 543 378 Missing (in isoform 6). /FTId=VSP_014563.
  VAR_SEQ 198 224 27 VFVFFDLTVDDQSVYPKALRDEYIMSK -> EKILKIYSLS RFSKIRRGAVAHVFNPS (in isoform 2). /FTId=VSP_014564.
  VAR_SEQ 199 203 5 FVFFD -> VPVER (in isoform 5). /FTId=VSP_014565.
  VAR_SEQ 204 543 340 Missing (in isoform 5). /FTId=VSP_014566.
  VAR_SEQ 228 234 7 SGACGEV -> GRGWQIT (in isoform 2). /FTId=VSP_014567.
  VAR_SEQ 235 543 309 Missing (in isoform 2). /FTId=VSP_014568.
  VAR_SEQ 283 289 7 PCIIKIK -> DGRGRAV (in isoform 8). /FTId=VSP_014569.
  VAR_SEQ 290 543 254 Missing (in isoform 8). /FTId=VSP_014570.
  VAR_SEQ 337 365 29 Missing (in isoform 12). /FTId=VSP_014571.
  VAR_SEQ 337 339 3 YLH -> MKT (in isoform 7). /FTId=VSP_014572.
  VAR_SEQ 340 543 204 Missing (in isoform 7). /FTId=VSP_014573.
  VARIANT 17 17 1 A -> S (in osteosarcoma; somatic mutation; might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer). /FTId=VAR_019101.
  VARIANT 59 59 1 T -> K (in multiple cancers). /FTId=VAR_026630.
  VARIANT 64 64 1 E -> K (in prostate cancer; somatic mutation). /FTId=VAR_019107.
  VARIANT 85 85 1 P -> L (in osteosarcoma; is a neutral allele among Ashkenazi Jewish women; dbSNP:rs17883862). /FTId=VAR_019102.
  VARIANT 117 117 1 R -> G (might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer). /FTId=VAR_022461.
  VARIANT 137 137 1 R -> Q (might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer). /FTId=VAR_022462.
  VARIANT 145 145 1 R -> P (in prostate cancer; somatic mutation). /FTId=VAR_019108.
  VARIANT 145 145 1 R -> W (in colon cancer and LFS2; does not cause protein abrogation in familial colorectal cancer). /FTId=VAR_008554.
  VARIANT 157 157 1 I -> T (might influence susceptibility to diffferent types of cancer; does not cause protein abrogation in familial colorectal cancer; dbSNP:rs17879961). /FTId=VAR_008555.
  VARIANT 167 167 1 G -> R (in prostate cancer; somatic mutation). /FTId=VAR_019109.
  VARIANT 180 180 1 R -> C (in prostate cancer; somatic mutation). /FTId=VAR_019103.
  VARIANT 180 180 1 R -> H (in prostate cancer; somatic mutation). /FTId=VAR_019110.
  VARIANT 181 181 1 R -> C (in prostate cancer; somatic mutation). /FTId=VAR_019104.
  VARIANT 181 181 1 R -> H (in prostate cancer; somatic mutation). /FTId=VAR_019105.
  VARIANT 239 239 1 E -> K (in prostate cancer; germline mutation). /FTId=VAR_019106.
  VARIANT 251 251 1 I -> F (in prostate cancer; germline mutation). /FTId=VAR_019111.
  VARIANT 318 318 1 R -> H (in prostate cancer; somatic mutation). /FTId=VAR_019112.
  VARIANT 323 323 1 T -> P (in prostate cancer; somatic mutation). /FTId=VAR_019113.
  VARIANT 327 327 1 Y -> C (in prostate cancer; somatic mutation). /FTId=VAR_019114.
  VARIANT 347 347 1 D -> N (in dbSNP:rs28909980). /FTId=VAR_029154.
  VARIANT 406 406 1 R -> H (in dbSNP:rs299671). /FTId=VAR_024572.
  VARIANT 428 428 1 S -> F (increases breast cancer risk approximately 2-fold among Ashkenazi Jewish women). /FTId=VAR_022463.
  VARIANT 436 436 1 L -> M (in dbSNP:rs17882922). /FTId=VAR_021117.
  VARIANT 446 446 1 N -> K (in dbSNP:rs17880867). /FTId=VAR_021118.
  VARIANT 447 447 1 F -> I (in dbSNP:rs17881473). /FTId=VAR_021119.
  VARIANT 448 448 1 I -> S (in dbSNP:rs17886163). /FTId=VAR_021120.
  VARIANT 476 476 1 T -> K (in prostate cancer; somatic mutation). /FTId=VAR_019115.
  VARIANT 500 500 1 S -> C (in dbSNP:rs28909981). /FTId=VAR_029155.
  VARIANT 501 501 1 E -> K (in dbSNP:rs17883172). /FTId=VAR_021121.
  VARIANT 512 512 1 L -> V (in dbSNP:rs17882942). /FTId=VAR_021122.
  MUTAGEN 68 68 1 T->A: Loss of activation and phosphorylation.
  MUTAGEN 347 347 1 D->A: Loss of kinase activity.
  MUTAGEN 368 368 1 D->N: Loss of autophosphorylation activity.
  STRAND 94 98 5
  STRAND 106 108 3
  STRAND 110 118 9
  STRAND 122 124 3
  HELIX 128 132 5
  HELIX 135 138 4
  STRAND 144 150 7
  STRAND 154 162 9
  STRAND 168 170 3
  STRAND 180 182 3
  STRAND 187 193 7
  STRAND 197 203 7
  HELIX 214 219 6
  STRAND 220 228 9
  STRAND 230 239 10
  TURN 240 243 4
  STRAND 244 252 9
  HELIX 270 279 10
  STRAND 288 302 15
  HELIX 309 312 4
  HELIX 321 340 20
  HELIX 350 352 3
  STRAND 353 361 9
  STRAND 364 366 3
  HELIX 378 384 7
  HELIX 388 390 3
  HELIX 393 397 5
  TURN 398 403 6
  HELIX 407 422 16
  STRAND 429 431 3
  HELIX 436 442 7
  HELIX 449 452 4
  HELIX 457 466 10
  TURN 471 473 3
  HELIX 477 481 5
  HELIX 484 486 3
  HELIX 489 502 14


IPI crosslinks:
SP O96017-1 IPI00014072 A8JZZ5;A8K3Y9; HAVANA:ENSP00000385747;HAVANA:ENSP00000386087;ENSP00000329178; REVIEWED:NP_009125; AAC83693;AAD11784;AAD48504;AAH04207;AAV41895;CAA10319;CAH73823;CAH73875; 16627,CHEK2; 11200,CHEK2; UPI00000316FF Hs.291363;Hs.505297; CCDS13843.1; GI:6005850; OTTHUMP00000028871;OTTHUMP00000198969;OTTHUMP00000199044;OTTHUMP00000199045;
IPI gene crosslinks:
22 27413731 27467822 -1 22q12.1 ENSG00000183765 16627,CHEK2 11200,CHEK2 IPI00014072;IPI00030746;IPI00423149;IPI00423157;IPI00423146;IPI00607619;IPI00607709;IPI00423156;IPI00871524;IPI00872374;IPI00607851;IPI00607753;IPI00607739;IPI00607680;IPI00877689;IPI00878496;IPI00877980;IPI00878892;IPI00878345;IPI00879227;IPI00878704;IPI00879419; O96017-1;O96017-10;O96017-11;O96017-12;O96017-2;O96017-3;O96017-4;O96017-5;O96017-6;O96017-7;O96017-8;O96017-9; A8JZZ5;A8K3Y9;Q683Z8;Q9HBS5; ENSP00000329012;ENSP00000329178;ENSP00000371996;ENSP00000372003;ENSP00000372006;ENSP00000372007;ENSP00000372021;ENSP00000372023;ENSP00000381099;ENSP00000381103;HAVANA:ENSP00000384835;HAVANA:ENSP00000384919;HAVANA:ENSP00000385747;HAVANA:ENSP00000386087; REVIEWED:NP_001005735;REVIEWED:NP_009125;REVIEWED:NP_665861; HIT000275825; Hs.291363;Hs.505297; CCDS13843.1;CCDS13844.1;CCDS33629.1; GI:22209009;GI:54112407;GI:6005850; OTTHUMG00000151023;OTTHUMG00000030771; OTTHUMP00000028871;OTTHUMP00000198968;OTTHUMP00000198969;OTTHUMP00000198970;OTTHUMP00000198971;OTTHUMP00000199044;OTTHUMP00000199045;OTTHUMP00000199046;OTTHUMP00000199047;OTTHUMP00000199048;OTTHUMP00000199049;OTTHUMP00000199050;OTTHUMP00000199051;OTTHUMP00000199052;OTTHUMP00000199053;OTTHUMP00000199064;OTTHUMP00000199065;OTTHUMP00000199115;OTTHUMP00000199116;