CHK1_YEAST
ID CHK1_YEAST Reviewed; 527 AA.
AC P38147; D6VQS0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Serine/threonine-protein kinase CHK1;
DE EC=2.7.11.1;
DE AltName: Full=Checkpoint kinase 1;
GN Name=CHK1; OrderedLocusNames=YBR274W; ORFNames=YBR1742;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10550056; DOI=10.1126/science.286.5442.1166;
RA Sanchez Y., Bachant J., Wang H., Hu F., Liu D., Tetzlaff M., Elledge S.J.;
RT "Control of the DNA damage checkpoint by chk1 and rad53 protein kinases
RT through distinct mechanisms.";
RL Science 286:1166-1171(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Serine/threonine-protein kinase which is required for
CC checkpoint-mediated cell cycle arrest and activation of DNA repair in
CC response to the presence of DNA damage or unreplicated DNA. May also
CC negatively regulate cell cycle progression during unperturbed cell
CC cycles. Controls phosphorylation and abundance of PDS1 to prevent
CC anaphase entry. Also helps prevent mitotic exit.
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 -!- 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;
CC -!- INTERACTION:
CC P38147; Q00684: CDC14; NbExp=2; IntAct=EBI-4593, EBI-4192;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 2530 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. NIM1 subfamily. {ECO:0000305}.
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DR EMBL; AF117345; AAD17231.1; -; Genomic_DNA.
DR EMBL; Z36143; CAA85237.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07390.1; -; Genomic_DNA.
DR PIR; S46155; S46155.
DR RefSeq; NP_009833.1; NM_001178622.1.
DR AlphaFoldDB; P38147; -.
DR SMR; P38147; -.
DR BioGRID; 32969; 425.
DR DIP; DIP-1253N; -.
DR IntAct; P38147; 37.
DR MINT; P38147; -.
DR STRING; 4932.YBR274W; -.
DR iPTMnet; P38147; -.
DR MaxQB; P38147; -.
DR PaxDb; P38147; -.
DR PRIDE; P38147; -.
DR EnsemblFungi; YBR274W_mRNA; YBR274W; YBR274W.
DR GeneID; 852577; -.
DR KEGG; sce:YBR274W; -.
DR SGD; S000000478; CHK1.
DR VEuPathDB; FungiDB:YBR274W; -.
DR eggNOG; KOG0590; Eukaryota.
DR GeneTree; ENSGT00940000167959; -.
DR HOGENOM; CLU_000288_59_8_1; -.
DR InParanoid; P38147; -.
DR OMA; ACIKKAC; -.
DR BioCyc; YEAST:G3O-29195-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P38147; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38147; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IPI:SGD.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0005524; F:ATP 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; IDA:SGD.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0048478; P:replication fork protection; IGI:SGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; DNA damage; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..527
FT /note="Serine/threonine-protein kinase CHK1"
FT /id="PRO_0000085857"
FT DOMAIN 15..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 527 AA; 60017 MW; 0BD66B74FE079DCA CRC64;
MSLSQVSPLP HIKDVVLGDT VGQGAFACVK NAHLQMDPSI ILAVKFIHVP TCKKMGLSDK
DITKEVVLQS KCSKHPNVLR LIDCNVSKEY MWIILEMADG GDLFDKIEPD VGVDSDVAQF
YFQQLVSAIN YLHVECGVAH RDIKPENILL DKNGNLKLAD FGLASQFRRK DGTLRVSMDQ
RGSPPYMAPE VLYSEEGYYA DRTDIWSIGI LLFVLLTGQT PWELPSLENE DFVFFIENDG
NLNWGPWSKI EFTHLNLLRK ILQPDPNKRV TLKALKLHPW VLRRASFSGD DGLCNDPELL
AKKLFSHLKV SLSNENYLKF TQDTNSNNRY ISTQPIGNEL AELEHDSMHF QTVSNTQRAF
TSYDSNTNYN SGTGMTQEAK WTQFISYDIA ALQFHSDEND CNELVKRHLQ FNPNKLTKFY
TLQPMDVLLP ILEKALNLSQ IRVKPDLFAN FERLCELLGY DNVFPLIINI KTKSNGGYQL
CGSISIIKIE EELKSVGFER KTGDPLEWRR LFKKISTICR DIILIPN
