(data stored in ACNUC26462 zone)

HOGENOM: HS22_PE799

ID   HS22_PE799                           STANDARD;      PRT;   543 AA.
AC   HS22_PE799;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Serine/threonine-protein kinase Chk2; EC=2.7.11 1;AltName:
DE   Full=Cds1; (HS22.PE799).
GN   Name=CHEK2; Synonyms=CHK2, RAD53;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS22.PE799.
CC       Homo sapiens chromosome 22 GRCh37  sequence 1..51244566 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:CHK2_HUMAN
CC   -!- FUNCTION: Regulates cell cycle checkpoints and apoptosis in
CC       response to DNA damage, particularly to DNA double-strand breaks.
CC       Inhibits CDC25C phosphatase by phosphorylation on 'Ser-216',
CC       preventing the entry into mitosis. May also play a role in
CC       meiosis. Regulates the TP53 tumor suppressor through
CC       phosphorylation at 'Thr-18' and 'Ser-20'. Phosphorylates NEK6.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Rapidly phosphorylated on Thr-68 by MLTK in
CC       response to DNA damage and to replication block. Kinase activity
CC       is also up-regulated by autophosphorylation.
CC   -!- SUBUNIT: Interacts with PML.
CC   -!- INTERACTION:
CC       Q9NY61:AATF; NbExp=4; IntAct=EBI-1180783, EBI-372428;
CC       Q9Y248:GINS2; NbExp=2; IntAct=EBI-1180783, EBI-747491;
CC       P53350:PLK1; NbExp=6; IntAct=EBI-1180783, EBI-476768;
CC       Q15172:PPP2R5A; NbExp=2; IntAct=EBI-1180783, EBI-641666;
CC       Q15173:PPP2R5B; NbExp=2; IntAct=EBI-1180783, EBI-1369497;
CC       Q13362-1:PPP2R5C; NbExp=3; IntAct=EBI-1180783, EBI-1266170;
CC       Q13362-2:PPP2R5C; NbExp=2; IntAct=EBI-1180783, EBI-1266173;
CC       Q13362-3:PPP2R5C; NbExp=4; IntAct=EBI-1180783, EBI-1266176;
CC       Q16537:PPP2R5E; NbExp=3; IntAct=EBI-1180783, EBI-968374;
CC       P55072:VCP; NbExp=2; IntAct=EBI-1180783, EBI-355164;
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Nucleus. Note=Isoform 10 is
CC       present throughout the cell.
CC   -!- SUBCELLULAR LOCATION: Isoform 4: Nucleus.
CC   -!- SUBCELLULAR LOCATION: Isoform 7: Nucleus.
CC   -!- SUBCELLULAR LOCATION: Isoform 9: Nucleus.
CC   -!- SUBCELLULAR LOCATION: Isoform 12: Nucleus.
CC   -!- SUBCELLULAR LOCATION: Nucleus, PML body. Nucleus, nucleoplasm.
CC       Note=Recruited into PML bodies together with TP53.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=12;
CC       Name=1;
CC         IsoId=O96017-1; Sequence=Displayed;
CC       Name=2; Synonyms=ins2;
CC         IsoId=O96017-2; Sequence=VSP_014564, VSP_014567, VSP_014568;
CC         Note=Lacks enzymatic activity;
CC       Name=3; Synonyms=del2-12;
CC         IsoId=O96017-3; Sequence=VSP_014559;
CC       Name=4; Synonyms=del2-3;
CC         IsoId=O96017-4; Sequence=VSP_014558;
CC         Note=Lacks enzymatic activity;
CC       Name=5; Synonyms=del4;
CC         IsoId=O96017-5; Sequence=VSP_014565, VSP_014566;
CC       Name=6; Synonyms=sub3;
CC         IsoId=O96017-6; Sequence=VSP_014562, VSP_014563;
CC       Name=7; Synonyms=del9-12;
CC         IsoId=O96017-7; Sequence=VSP_014572, VSP_014573;
CC         Note=Lacks enzymatic activity;
CC       Name=8; Synonyms=del7;
CC         IsoId=O96017-8; Sequence=VSP_014569, VSP_014570;
CC       Name=9; Synonyms=insx;
CC         IsoId=O96017-9; Sequence=VSP_014557;
CC         Note=Retains low level of catalytic activity;
CC       Name=10; Synonyms=iso2;
CC         IsoId=O96017-10; Sequence=VSP_014560, VSP_014561;
CC         Note=Lacks enzymatic activity;
CC       Name=11; Synonyms=iso1;
CC         IsoId=O96017-11; Sequence=VSP_014556;
CC       Name=12; Synonyms=del9;
CC         IsoId=O96017-12; Sequence=VSP_014571;
CC         Note=Lacks enzymatic activity;
CC   -!- TISSUE SPECIFICITY: High expression is found in testis, spleen,
CC       colon and peripheral blood leukocytes. Low expression is found in
CC       other tissues.
CC   -!- PTM: Phosphorylated by PLK4.
CC   -!- DISEASE: Defects in CHEK2 are associated with Li-Fraumeni syndrome
CC       2 (LFS2) [MIM:609265]; a highly penetrant familial cancer
CC       phenotype usually associated with inherited mutations in p53/TP53.
CC   -!- DISEASE: Defects in CHEK2 may be a cause of susceptibility to
CC       prostate cancer (PC) [MIM:176807]. It is a malignancy originating
CC       in tissues of the prostate. Most prostate cancers are
CC       adenocarcinomas that develop in the acini of the prostatic ducts.
CC       Other rare histopathologic types of prostate cancer that occur in
CC       approximately 5% of patients include small cell carcinoma,
CC       mucinous carcinoma, prostatic ductal carcinoma, transitional cell
CC       carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid
CC       cystic carcinoma (basaloid), signet-ring cell carcinoma and
CC       neuroendocrine carcinoma.
CC   -!- DISEASE: Defects in CHEK2 are found in some patients with
CC       osteogenic sarcoma (OSRC) [MIM:259500].
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CHK2 subfamily.
CC   -!- SIMILARITY: Contains 1 FHA domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/CHEK2ID312.html";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/CHEK2";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/chek2/";
CC   -!- GENE_FAMILY: HOG000233016 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000183765;ENST00000404276;ENSP00000385747.
DR   EMBL; AB040105; - ;
DR   EMBL; AF086904; - ;
DR   EMBL; AF096279; - ;
DR   EMBL; AF174135; - ;
DR   EMBL; AF217975; - ;
DR   EMBL; AJ131197; - ;
DR   EMBL; AK289360; - ;
DR   EMBL; AK290754; - ;
DR   EMBL; AL117330; - ;
DR   EMBL; AL121825; - ;
DR   EMBL; AY551295; - ;
DR   EMBL; AY551296; - ;
DR   EMBL; AY551297; - ;
DR   EMBL; AY551298; - ;
DR   EMBL; AY551299; - ;
DR   EMBL; AY551300; - ;
DR   EMBL; AY551301; - ;
DR   EMBL; AY551302; - ;
DR   EMBL; AY551303; - ;
DR   EMBL; AY551304; - ;
DR   EMBL; AY551305; - ;
DR   EMBL; AY800241; - ;
DR   EMBL; BC004207; - ;
DR   EMBL; CH471095; - ;
DR   EMBL; CR456418; - ;
DR   UniProtKB/Swiss-Prot; O96017; A8K3Y9; B7ZBF3; B7ZBF4; B7ZBF5; Q6QA03; Q6QA04; Q6QA05; -.
DR   UniProtKB/Swiss-Prot; Q6QA06; Q6QA07; Q6QA08; Q6QA10; Q6QA11; Q6QA12; Q6QA13; Q9HCQ8; -.
DR   UniProtKB/Swiss-Prot; Q9UGF0; Q9UGF1; -.
DR   EMBL; AF086904; AAC83693.1; -; mRNA.
DR   EMBL; AJ131197; CAA10319.1; -; mRNA.
DR   EMBL; AF096279; AAD11784.1; -; mRNA.
DR   EMBL; AY551295; AAS58456.1; -; mRNA.
DR   EMBL; AY551296; AAS58457.1; -; mRNA.
DR   EMBL; AY551297; AAS58458.1; -; mRNA.
DR   EMBL; AY551298; AAS58459.1; -; mRNA.
DR   EMBL; AY551299; AAS58460.1; -; mRNA.
DR   EMBL; AY551300; AAS58461.1; -; mRNA.
DR   EMBL; AY551301; AAS58462.1; -; mRNA.
DR   EMBL; AY551302; AAS58463.1; -; mRNA.
DR   EMBL; AY551303; AAS58464.1; -; mRNA.
DR   EMBL; AY551304; AAS58465.1; -; mRNA.
DR   EMBL; AY551305; AAS58466.1; -; mRNA.
DR   EMBL; CR456418; CAG30304.1; -; mRNA.
DR   EMBL; AF174135; AAD48504.1; -; mRNA.
DR   EMBL; AB040105; BAB17231.1; -; mRNA.
DR   EMBL; AK290754; BAF83443.1; -; mRNA.
DR   EMBL; AY800241; AAV41895.1; -; Genomic_DNA.
DR   EMBL; AL121825; CAH73823.1; -; Genomic_DNA.
DR   EMBL; AL117330; CAH73823.1; JOINED; Genomic_DNA.
DR   EMBL; AL117330; CAH73875.1; -; Genomic_DNA.
DR   EMBL; AL121825; CAH73875.1; JOINED; Genomic_DNA.
DR   EMBL; AL121825; CAX11957.1; -; Genomic_DNA.
DR   EMBL; AL117330; CAX11957.1; JOINED; Genomic_DNA.
DR   EMBL; AL121825; CAX11958.1; -; Genomic_DNA.
DR   EMBL; AL117330; CAX11958.1; JOINED; Genomic_DNA.
DR   EMBL; AL121825; CAX11959.1; -; Genomic_DNA.
DR   EMBL; AL117330; CAX11959.1; JOINED; Genomic_DNA.
DR   EMBL; AL117330; CAX14026.1; -; Genomic_DNA.
DR   EMBL; AL121825; CAX14026.1; JOINED; Genomic_DNA.
DR   EMBL; AL117330; CAX14027.1; -; Genomic_DNA.
DR   EMBL; AL121825; CAX14027.1; JOINED; Genomic_DNA.
DR   EMBL; AL117330; CAX14028.1; -; Genomic_DNA.
DR   EMBL; AL121825; CAX14028.1; JOINED; Genomic_DNA.
DR   EMBL; CH471095; EAW59755.1; -; Genomic_DNA.
DR   EMBL; BC004207; AAH04207.1; -; mRNA.
DR   IPI; IPI00014072; -.
DR   IPI; IPI00030746; -.
DR   IPI; IPI00423146; -.
DR   IPI; IPI00423149; -.
DR   IPI; IPI00423156; -.
DR   IPI; IPI00423157; -.
DR   IPI; IPI00607619; -.
DR   IPI; IPI00607680; -.
DR   IPI; IPI00607709; -.
DR   IPI; IPI00607739; -.
DR   IPI; IPI00607753; -.
DR   IPI; IPI00607851; -.
DR   RefSeq; NP_001005735.1; NM_001005735.1.
DR   RefSeq; NP_009125.1; NM_007194.3.
DR   RefSeq; NP_665861.1; NM_145862.2.
DR   UniGene; Hs.291363; -.
DR   UniGene; Hs.505297; -.
DR   PDB; 1GXC; X-ray; 2.70 A; A/D/G/J=64-212.
DR   PDB; 2CN5; X-ray; 2.25 A; A=210-531.
DR   PDB; 2CN8; X-ray; 2.70 A; A=210-531.
DR   PDB; 2W0J; X-ray; 2.05 A; A=210-531.
DR   PDB; 2W7X; X-ray; 2.07 A; A=210-531.
DR   PDB; 2WTC; X-ray; 3.00 A; A=210-531.
DR   PDB; 2WTD; X-ray; 2.75 A; A=210-531.
DR   PDB; 2WTI; X-ray; 2.50 A; A=210-531.
DR   PDB; 2WTJ; X-ray; 2.10 A; A=210-531.
DR   PDB; 2XBJ; X-ray; 2.30 A; A=210-531.
DR   PDB; 2XM8; X-ray; 3.40 A; A=210-531.
DR   PDB; 2XM9; X-ray; 2.50 A; A=210-531.
DR   PDB; 3I6U; X-ray; 3.00 A; A/B=84-502.
DR   PDB; 3I6W; X-ray; 3.25 A; A/B/C/D/E/F/G/H=70-512.
DR   PDBsum; 1GXC; -.
DR   PDBsum; 2CN5; -.
DR   PDBsum; 2CN8; -.
DR   PDBsum; 2W0J; -.
DR   PDBsum; 2W7X; -.
DR   PDBsum; 2WTC; -.
DR   PDBsum; 2WTD; -.
DR   PDBsum; 2WTI; -.
DR   PDBsum; 2WTJ; -.
DR   PDBsum; 2XBJ; -.
DR   PDBsum; 2XM8; -.
DR   PDBsum; 2XM9; -.
DR   PDBsum; 3I6U; -.
DR   PDBsum; 3I6W; -.
DR   ProteinModelPortal; O96017; -.
DR   SMR; O96017; 89-504.
DR   DIP; DIP-24270N; -.
DR   IntAct; O96017; 16.
DR   MINT; MINT-124588; -.
DR   STRING; O96017; -.
DR   PhosphoSite; O96017; -.
DR   PRIDE; O96017; -.
DR   Ensembl; ENST00000328354; ENSP00000329178; ENSG00000183765.
DR   Ensembl; ENST00000404276; ENSP00000385747; ENSG00000183765.
DR   Ensembl; ENST00000405598; ENSP00000386087; ENSG00000183765.
DR   GeneID; 11200; -.
DR   KEGG; hsa:11200; -.
DR   UCSC; uc003adu.1; human.
DR   UCSC; uc003adv.1; human.
DR   UCSC; uc003ady.1; human.
DR   CTD; 11200; -.
DR   GeneCards; GC22M012048; -.
DR   HGNC; HGNC:16627; CHEK2.
DR   HPA; CAB002030; -.
DR   HPA; HPA001878; -.
DR   MIM; 176807; phenotype.
DR   MIM; 259500; phenotype.
DR   MIM; 604373; gene+phenotype.
DR   MIM; 609265; phenotype.
DR   neXtProt; NX_O96017; -.
DR   Orphanet; 1331; Familial prostate cancer.
DR   Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
DR   Orphanet; 524; Li-Fraumeni syndrome.
DR   Orphanet; 668; Osteosarcoma.
DR   PharmGKB; PA404; -.
DR   eggNOG; prNOG16187; -.
DR   OMA; PKARFTT; -.
DR   OrthoDB; EOG4M0F1R; -.
DR   PhylomeDB; O96017; -.
DR   BRENDA; 2.7.11.1; 2681.
DR   Pathway_Interaction_DB; foxm1pathway; FOXM1 transcription factor network.
DR   Reactome; REACT_1538; Cell Cycle Checkpoints.
DR   NextBio; 42629; -.
DR   ArrayExpress; O96017; -.
DR   Bgee; O96017; -.
DR   Genevestigator; O96017; -.
DR   GermOnline; ENSG00000183765; Homo sapiens.
DR   GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000077; P:DNA damage checkpoint; TAS:UniProtKB.
DR   GO; GO:0008630; P:DNA damage response, signal transduction resulting in induction of apoptosis; IDA:UniProtKB.
DR   GO; GO:0090399; P:replicative senescence; NAS:BHF-UCL.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_kinase_dom.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   HOGENOMDNA; HS22.PE799; -.
KW   ENSG000001837651755old_1320000031; ENSP000003857477901old_1320000031;
KW   A8JZZ5_HUMAN; B7ZBF2_HUMAN; Q9HBS5_HUMAN; AB040105; AF086904; AF096279;
KW   AF217975; AJ131197; AK289360; AK290754; AL117330; AL121825; AY551295;
KW   AY551297; AY551298; AY551299; AY551300; AY551301; AY551302; AY551303;
KW   AY551305; AY800241; BC004207; CH471095; CR456418;
KW   3D-structure; Alternative splicing; ATP-binding; Cell cycle;
KW   Complete proteome; Disease mutation; Kinase; Li-Fraumeni syndrome;
KW   Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Polymorphism; Proto-oncogene; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
SQ   SEQUENCE   543 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS QSSHSSSGTL
     SSLETVSTQE LYSIPEDQEP EDQEPEEPTP APWARLWALQ DGFANLECVN DNYWFGRDKS
     CEYCFDEPLL KRTDKYRTYS KKHFRIFREV GPKNSYIAYI EDHSGNGTFV NTELVGKGKR
     RPLNNNSEIA LSLSRNKVFV FFDLTVDDQS VYPKALRDEY IMSKTLGSGA CGEVKLAFER
     KTCKKVAIKI ISKRKFAIGS AREADPALNV ETEIEILKKL NHPCIIKIKN FFDAEDYYIV
     LELMEGGELF DKVVGNKRLK EATCKLYFYQ MLLAVQYLHE NGIIHRDLKP ENVLLSSQEE
     DCLIKITDFG HSKILGETSL MRTLCGTPTY LAPEVLVSVG TAGYNRAVDC WSLGVILFIC
     LSGYPPFSEH RTQVSLKDQI TSGKYNFIPE VWAEVSEKAL DLVKKLLVVD PKARFTTEEA
     LRHPWLQDED MKRKFQDLLS EENESTALPQ VLAQPSTSRK RPREGEAEGA ETTKRPAVCA
     AVL
//

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