(data stored in ACNUC26462 zone)

HOGENOM: MOUSE5_PE1891

ID   MOUSE5_PE1891                        STANDARD;      PRT;   546 AA.
AC   MOUSE5_PE1891; Q9Z265;
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;
DE   (MOUSE5.PE1891).
GN   Name=Chek2; Synonyms=Chk2, Rad53;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE5.PE1891.
CC       Mus musculus chromosome 5 NCBIM37  sequence 1..152537259 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:CHK2_MOUSE
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, preventing the
CC       entry into mitosis. May also play a role in meiosis. Regulates the
CC       TP53 tumor suppressor through phosphorylation at 'Thr-20' and
CC       'Ser-23'. Phosphorylates NEK6 (By similarity).
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 (By similarity).
CC   -!- SUBUNIT: Interacts with PML (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, PML body (By similarity). Nucleus,
CC       nucleoplasm. Note=Recruited into PML bodies together with TP53 (By
CC       similarity).
CC   -!- PTM: Phosphorylated by PLK4 (By similarity).
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   -!- GENE_FAMILY: HOG000233016 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000029521;ENSMUST00000066160;ENSMUSP00000066679.
DR   EMBL; AF086905; - ;
DR   EMBL; AK044913; - ;
DR   EMBL; BC056617; - ;
DR   UniProtKB/Swiss-Prot; Q9Z265; -.
DR   EMBL; AF086905; AAC83694.1; -; mRNA.
DR   EMBL; BC056617; AAH56617.1; -; mRNA.
DR   IPI; IPI00130553; -.
DR   RefSeq; NP_057890.1; NM_016681.3.
DR   UniGene; Mm.279308; -.
DR   ProteinModelPortal; Q9Z265; -.
DR   SMR; Q9Z265; 94-506.
DR   IntAct; Q9Z265; 4.
DR   STRING; Q9Z265; -.
DR   PhosphoSite; Q9Z265; -.
DR   PRIDE; Q9Z265; -.
DR   Ensembl; ENSMUST00000066160; ENSMUSP00000066679; ENSMUSG00000029521.
DR   GeneID; 50883; -.
DR   KEGG; mmu:50883; -.
DR   CTD; 11200; -.
DR   MGI; MGI:1355321; Chek2.
DR   GeneTree; ENSGT00570000079241; -.
DR   InParanoid; Q9Z265; -.
DR   OMA; PKARFTT; -.
DR   OrthoDB; EOG4M0F1R; -.
DR   PhylomeDB; Q9Z265; -.
DR   BRENDA; 2.7.11.1; 3474.
DR   NextBio; 307865; -.
DR   ArrayExpress; Q9Z265; -.
DR   Bgee; Q9Z265; -.
DR   CleanEx; MM_CHEK2; -.
DR   Genevestigator; Q9Z265; -.
DR   GermOnline; ENSMUSG00000029521; Mus musculus.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IMP:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0010332; P:response to gamma radiation; IDA:MGI.
DR   GO; GO:0042770; P:signal transduction in response to DNA damage; IDA:MGI.
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; MOUSE5.PE1891; -.
KW   ENSMUSG000000295215old_1320000031; ENSMUSP000000666791old_1320000031;
KW   Q543W6_MOUSE; AF086905; AK044913; BC056617;
KW   ATP-binding; Cell cycle; Complete proteome; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
SQ   SEQUENCE   546 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKSHHQSHSS TSSKAHDSAS CSQSQGGFSQ PQGTPSQLHE LSQYQGSSSS STGTVPSSSQ
     SSHSSSGTLS SLETVSTQEL CSIPEDQEPE EPGPAPWARL WALQDGFSNL DCVNDNYWFG
     RDKSCEYCFD GPLLRRTDKY RTYSKKHFRI FREMGPKNCY IVYIEDHSGN GTFVNTELIG
     KGKRCPLSNN SEIALSLCRN KVFVFFDLTV DDQSVYPKEL RDEYIMSKTL GSGACGEVKM
     AFERKTCQKV AIKIISKRRF ALGSSREADT APSVETEIEI LKKLNHPCII KIKDVFDAED
     YYIVLELMEG GELFDRVVGN KRLKEATCKL YFYQMLVAVQ YLHENGIIHR DLKPENVLLS
     SQEEDCLIKI TDFGQSKILG ETSLMRTLCG TPTYLAPEVL VSNGTAGYSR AVDCWSLGVI
     LFICLSGYPP FSEHKTQVSL KDQITSGKYN FIPEVWTDVS EEALDLVKKL LVVDPKARLT
     TEEALNHPWL QDEYMKKKFQ DLLVQEKNSV TLPVAPAQTS SQKRPLELEV EGMPSTKRLS
     VCGAVL
//

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