CHK2_CAEEL
ID CHK2_CAEEL Reviewed; 476 AA.
AC Q9U1Y5; Q9GR99; Q9GRB8;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Serine/threonine-protein kinase chk-2;
DE EC=2.7.11.1;
DE AltName: Full=Ce-cds-1;
DE AltName: Full=Ce-chk-2;
GN Name=chk-2; Synonyms=cds-1; ORFNames=Y60A3A.12;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:CAB60407.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11158318; DOI=10.1128/mcb.21.4.1329-1335.2001;
RA Oishi I., Iwai K., Kagohashi Y., Fujimoto H., Kariya K., Kataoka T.,
RA Sawa H., Okano H., Otani H., Yamamura H., Minami Y.;
RT "Critical role of Caenorhabditis elegans homologs of cds1 (Chk2)-related
RT kinases in meiotic recombination.";
RL Mol. Cell. Biol. 21:1329-1335(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-476, FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Gonad;
RX PubMed=11086161; DOI=10.1016/s0014-5793(00)02178-5;
RA Higashitani A., Aoki H., Mori A., Sasagawa Y., Takanami T., Takahashi H.;
RT "Caenorhabditis elegans Chk2-like gene is essential for meiosis but
RT dispensable for DNA repair.";
RL FEBS Lett. 485:35-39(2000).
CC -!- FUNCTION: Serine/threonine-protein kinase which is required for
CC checkpoint-mediated cell cycle arrest, activation of DNA repair and
CC apoptosis in response to the presence of DNA double-strand breaks. May
CC also negatively regulate cell cycle progression during unperturbed cell
CC cycles. Phosphorylates and inhibits cdc25 phosphatase, preventing entry
CC into mitosis. Required for nuclear reorganization and homologous
CC chromosome pairing during meiotic prophase.
CC {ECO:0000269|PubMed:11086161, ECO:0000269|PubMed:11158318}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P05132};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P05132};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11086161,
CC ECO:0000269|PubMed:11158318}.
CC -!- TISSUE SPECIFICITY: Highly expressed in germline tissue.
CC {ECO:0000269|PubMed:11086161}.
CC -!- DEVELOPMENTAL STAGE: Low expression in embryos and L2 larvae, high
CC expression in hermaphrodite adults. {ECO:0000269|PubMed:11086161}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CHK2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15803.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB041996; BAB20578.1; -; mRNA.
DR EMBL; AL117207; CAB60407.2; -; Genomic_DNA.
DR EMBL; AB049441; BAB15803.1; ALT_INIT; mRNA.
DR RefSeq; NP_001024271.1; NM_001029100.3.
DR AlphaFoldDB; Q9U1Y5; -.
DR SMR; Q9U1Y5; -.
DR BioGRID; 45265; 5.
DR STRING; 6239.Y60A3A.12; -.
DR PaxDb; Q9U1Y5; -.
DR EnsemblMetazoa; Y60A3A.12.1; Y60A3A.12.1; WBGene00000499.
DR GeneID; 180304; -.
DR KEGG; cel:CELE_Y60A3A.12; -.
DR UCSC; Y60A3A.12; c. elegans.
DR CTD; 180304; -.
DR WormBase; Y60A3A.12; CE27297; WBGene00000499; chk-2.
DR eggNOG; KOG0615; Eukaryota.
DR GeneTree; ENSGT00800000124190; -.
DR HOGENOM; CLU_000288_63_47_1; -.
DR InParanoid; Q9U1Y5; -.
DR OMA; MLCAVQY; -.
DR OrthoDB; 1510589at2759; -.
DR PhylomeDB; Q9U1Y5; -.
DR Reactome; R-CEL-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-CEL-69473; G2/M DNA damage checkpoint.
DR PRO; PR:Q9U1Y5; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000499; Expressed in adult organism and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; IMP:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; DNA damage; DNA repair; Kinase;
KW Magnesium; Metal-binding; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..476
FT /note="Serine/threonine-protein kinase chk-2"
FT /id="PRO_0000085860"
FT DOMAIN 66..127
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086,
FT ECO:0000305"
FT DOMAIN 170..436
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 252..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 305..306
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 10..13
FT /note="SSAE -> ARRK (in Ref. 3; BAB15803)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53338 MW; 9762018F599F9A7B CRC64;
MVRGTKRRRS SAEKPIVVVP VTRDDTMPVD EDLVVGESQC AASKPFAKLV GVRRGISSID
LADDHFVCGR GSDDAPTNFN FSQVAKDVGL YRFISKIQFS IDRDTETRRI YLHDHSRNGT
LVNQEMIGKG LSRELMNGDL ISIGIPALII FVYESADADH HPEELTKKYH VTSHSLGKGG
FGKVLLGYKK SDRSVVAIKQ LNTQFSTRCS RAIAKTRDIR NEVEVMKKLS HPNIVAIYDW
ITVAKYSYMV IEYVGGGEFF SKVVDSKYNR MGLGESLGKY FAFQLIDAIL YLHSVGICHR
DIKPENILCS DKAERCILKL TDFGMAKNSV NRMKTRCGTP SYNAPEIVAN EGVEYTPKVD
IWSLGCVLFI TFSGYPPFSE EYTDMTMDEQ VLTGRLIFHA QWRRITVETQ NMIKWMLTVE
PSNRPSAVEL MSTQWMKCAD CRTAKQDILK SIKPISAAAP AALQTTQAGP VKKAKM
