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Serine/threonine-protein kinase Chk2 (EC 2.7.11.1) (CHK2 checkpoint homolog) (Checkpoint kinase 2)

 CHK2_MOUSE              Reviewed;         546 AA.
Q9Z265;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
20-JUN-2018, entry version 162.
RecName: Full=Serine/threonine-protein kinase Chk2;
EC=2.7.11.1;
AltName: Full=CHK2 checkpoint homolog;
AltName: Full=Checkpoint kinase 2;
Name=Chek2; Synonyms=Chk2, Rad53;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9836640; DOI=10.1126/science.282.5395.1893;
Matsuoka S., Huang M., Elledge S.J.;
"Linkage of ATM to cell cycle regulation by the Chk2 protein kinase.";
Science 282:1893-1897(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NMRI; TISSUE=Mammary gland;
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).
[3]
DISRUPTION PHENOTYPE, FUNCTION IN APOPTOSIS, AND TISSUE SPECIFICITY.
PubMed=12192050; DOI=10.1128/MCB.22.18.6521-6532.2002;
Hirao A., Cheung A., Duncan G., Girard P.M., Elia A.J., Wakeham A.,
Okada H., Sarkissian T., Wong J.A., Sakai T., De Stanchina E.,
Bristow R.G., Suda T., Lowe S.W., Jeggo P.A., Elledge S.J., Mak T.W.;
"Chk2 is a tumor suppressor that regulates apoptosis in both an ataxia
telangiectasia mutated (ATM)-dependent and an ATM-independent
manner.";
Mol. Cell. Biol. 22:6521-6532(2002).
[4]
FUNCTION, AND MUTAGENESIS OF TYR-394.
PubMed=25619829; DOI=10.1038/onc.2014.443;
Wang N., Ding H., Liu C., Li X., Wei L., Yu J., Liu M., Ying M.,
Gao W., Jiang H., Wang Y.;
"A novel recurrent CHEK2 Y390C mutation identified in high-risk
Chinese breast cancer patients impairs its activity and is associated
with increased breast cancer risk.";
Oncogene 34:5198-5205(2015).
-!- FUNCTION: Serine/threonine-protein kinase which is required for
checkpoint-mediated cell cycle arrest, activation of DNA repair
and apoptosis in response to the presence of DNA double-strand
breaks. May also negatively regulate cell cycle progression during
unperturbed cell cycles. Following activation, phosphorylates
numerous effectors preferentially at the consensus sequence [L-X-
R-X-X-S/T]. Regulates cell cycle checkpoint arrest through
phosphorylation of CDC25A, CDC25B and CDC25C, inhibiting their
activity. Inhibition of CDC25 phosphatase activity leads to
increased inhibitory tyrosine phosphorylation of CDK-cyclin
complexes and blocks cell cycle progression. May also
phosphorylate NEK6 which is involved in G2/M cell cycle arrest.
Regulates DNA repair through phosphorylation of BRCA2, enhancing
the association of RAD51 with chromatin which promotes DNA repair
by homologous recombination. Also stimulates the transcription of
genes involved in DNA repair (including BRCA2) through the
phosphorylation and activation of the transcription factor FOXM1.
Regulates apoptosis through the phosphorylation of p53/TP53, MDM4
and PML. Phosphorylation of p53/TP53 at 'Ser-20' by CHEK2 may
alleviate inhibition by MDM2, leading to accumulation of active
p53/TP53. Phosphorylation of MDM4 may also reduce degradation of
p53/TP53. Also controls the transcription of pro-apoptotic genes
through phosphorylation of the transcription factor E2F1. Tumor
suppressor, it may also have a DNA damage-independent function in
mitotic spindle assembly by phosphorylating BRCA1. Its absence may
be a cause of the chromosomal instability observed in some cancer
cells. Promotes the CCAR2-SIRT1 association and is required for
CCAR2-mediated SIRT1 inhibition (By similarity).
{ECO:0000250|UniProtKB:O96017, ECO:0000269|PubMed:12192050,
ECO:0000269|PubMed:25619829}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Activated through phosphorylation at Thr-68 by
ATM in response to DNA double-strand breaks. Activation is
modulated by several mediators including MDC1 and TP53BP1. Induces
homodimerization with exchange of the T-loop/activation segment
between protomers and transphosphorylation of the protomers. The
autophosphorylated kinase dimer is fully active. Negatively
regulated by PPM1D through dephosphorylation of Thr-68 (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Homodimerization is part of the activation
process but the dimer may dissociate following activation.
Interacts with PML. Interacts with TP53. Interacts with RB1;
phosphorylates RB1. Interacts with BRCA1. Interacts
(phosphorylated at Thr-68) with MDC1; requires ATM-mediated
phosphorylation of CHEK2. Interacts with TP53BP1; modulates CHEK2
phosphorylation at Thr-68 in response to ionizing radiation.
Interacts with CDC25A; phosphorylates CDC25A and mediates its
degradation in response to ionizing radiation. Interacts with
CUL1; mediates CHEK2 ubiquitination and regulation. Interacts with
CDKN2AIP. Interacts (via protein kinase domain) with CCAR2 (via N-
terminus). Interacts with SIRT1 (By similarity).
{ECO:0000250|UniProtKB:O96017}.
-!- SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250}. Nucleus,
nucleoplasm. Note=Recruited into PML bodies together with TP53.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed with higher levels in
the thymus, spleen and colon (at protein level).
{ECO:0000269|PubMed:12192050}.
-!- PTM: Phosphorylated. Phosphorylated at Ser-82 by PLK3 in response
to DNA damage, promoting phosphorylation at Thr-77 by ATM and the
G2/M transition checkpoint. Phosphorylation at Thr-77 induces
homodimerization. Autophosphorylates at Thr-387 and Thr-391 in the
T-loop/activation segment upon dimerization to become fully
active. DNA damage-induced autophosphorylation at Ser-383 induces
CUL1-mediated ubiquitination and regulates the pro-apoptotic
function. Phosphorylation at Ser-460 also regulates
ubiquitination. Phosphorylated by PLK4 (By similarity).
{ECO:0000250}.
-!- PTM: Ubiquitinated. CUL1-mediated ubiquitination regulates the
pro-apoptotic function. Ubiquitination may also regulate protein
stability. Ubiquitinated by RNF8 via 'Lys-48'-linked
ubiquitination (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: No overt morphological phenotype but
apoptosis and cell cycle arrest induced by ionizing radiation are
abolished. {ECO:0000269|PubMed:12192050}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. CHK2 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF086905; AAC83694.1; -; mRNA.
EMBL; BC056617; AAH56617.1; -; mRNA.
CCDS; CCDS19533.1; -.
RefSeq; NP_057890.1; NM_016681.3.
RefSeq; XP_006535132.1; XM_006535069.2.
RefSeq; XP_006535133.1; XM_006535070.2.
UniGene; Mm.279308; -.
ProteinModelPortal; Q9Z265; -.
SMR; Q9Z265; -.
BioGrid; 206143; 5.
IntAct; Q9Z265; 4.
STRING; 10090.ENSMUSP00000066679; -.
iPTMnet; Q9Z265; -.
PhosphoSitePlus; Q9Z265; -.
EPD; Q9Z265; -.
MaxQB; Q9Z265; -.
PaxDb; Q9Z265; -.
PRIDE; Q9Z265; -.
Ensembl; ENSMUST00000066160; ENSMUSP00000066679; ENSMUSG00000029521.
GeneID; 50883; -.
KEGG; mmu:50883; -.
UCSC; uc008yrw.1; mouse.
CTD; 11200; -.
MGI; MGI:1355321; Chek2.
eggNOG; KOG0615; Eukaryota.
eggNOG; ENOG410YA63; LUCA.
GeneTree; ENSGT00800000124190; -.
HOGENOM; HOG000233016; -.
HOVERGEN; HBG108055; -.
InParanoid; Q9Z265; -.
KO; K06641; -.
OMA; SRAVDCW; -.
OrthoDB; EOG091G0DVW; -.
PhylomeDB; Q9Z265; -.
TreeFam; TF101082; -.
BRENDA; 2.7.11.1; 3474.
Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation.
Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
Reactome; R-MMU-69541; Stabilization of p53.
Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-MMU-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
PRO; PR:Q9Z265; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029521; -.
CleanEx; MM_CHEK2; -.
ExpressionAtlas; Q9Z265; baseline and differential.
Genevisible; Q9Z265; MM.
GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0016605; C:PML body; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0016301; F:kinase activity; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0006915; P:apoptotic process; IMP:MGI.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0044257; P:cellular protein catabolic process; ISO:MGI.
GO; GO:1903926; P:cellular response to bisphenol A; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0071480; P:cellular response to gamma radiation; IMP:MGI.
GO; GO:0000077; P:DNA damage checkpoint; ISO:MGI.
GO; GO:0006975; P:DNA damage induced protein phosphorylation; ISS:UniProtKB.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IMP:MGI.
GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISS:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:MGI.
GO; GO:0044773; P:mitotic DNA damage checkpoint; IBA:GO_Central.
GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
GO; GO:0071157; P:negative regulation of cell cycle arrest; ISO:MGI.
GO; GO:2000002; P:negative regulation of DNA damage checkpoint; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
GO; GO:2000210; P:positive regulation of anoikis; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0050821; P:protein stabilization; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0042176; P:regulation of protein catabolic process; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0001302; P:replicative cell aging; ISO:MGI.
GO; GO:0010332; P:response to gamma radiation; IDA:MGI.
GO; GO:1903416; P:response to glycoside; IEA:Ensembl.
GO; GO:0042770; P:signal transduction in response to DNA damage; IDA:MGI.
GO; GO:0072428; P:signal transduction involved in intra-S DNA damage checkpoint; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00060; FHA; 1.
InterPro; IPR000253; FHA_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR008984; SMAD_FHA_dom_sf.
Pfam; PF00498; FHA; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00240; FHA; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF49879; SSF49879; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50006; FHA_DOMAIN; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Apoptosis; ATP-binding; Cell cycle; Cell division; Complete proteome;
DNA damage; DNA repair; Kinase; Magnesium; Metal-binding; Mitosis;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase; Ubl conjugation.
CHAIN 1 546 Serine/threonine-protein kinase Chk2.
/FTId=PRO_0000085859.
DOMAIN 117 179 FHA. {ECO:0000255|PROSITE-
ProRule:PRU00086}.
DOMAIN 224 490 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 231 238 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 306 312 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 355 356 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 372 398 T-loop/activation segment. {ECO:0000250}.
ACT_SITE 351 351 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 253 253 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 372 372 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 68 68 Phosphothreonine; by MAP3K20.
{ECO:0000250}.
MOD_RES 71 71 Phosphoserine; by PLK3.
{ECO:0000250|UniProtKB:O96017}.
MOD_RES 77 77 Phosphothreonine; by ATM and MAP3K20.
{ECO:0000250|UniProtKB:O96017}.
MOD_RES 82 82 Phosphoserine; by PLK3.
{ECO:0000250|UniProtKB:O96017}.
MOD_RES 383 383 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O96017}.
MOD_RES 387 387 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:O96017}.
MOD_RES 391 391 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:O96017}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000250|UniProtKB:O96017}.
MUTAGEN 394 394 Y->C: Does not inhibit cell survival upon
DNA damage. Not phosphorylates p53/TP53.
{ECO:0000269|PubMed:25619829}.
SEQUENCE 546 AA; 61088 MW; A7949EFB5572CDAA 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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