CHK1_SCHPO
ID CHK1_SCHPO Reviewed; 496 AA.
AC P34208;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Serine/threonine-protein kinase chk1;
DE EC=2.7.11.1;
DE AltName: Full=Checkpoint kinase 1;
GN Name=chk1; Synonyms=rad27; ORFNames=SPCC1259.13;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RX PubMed=8497322; DOI=10.1038/363368a0;
RA Walworth N., Davey S., Beach D.;
RT "Fission yeast chk1 protein kinase links the rad checkpoint pathway to
RT cdc2.";
RL Nature 363:368-371(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=8019001; DOI=10.1091/mbc.5.2.147;
RA Al-Khodairy F., Fotou E., Sheldrick K.S., Griffiths D.J.F., Lehmann A.R.,
RA Carr A.M.;
RT "Identification and characterization of new elements involved in checkpoint
RT and feedback controls in fission yeast.";
RL Mol. Biol. Cell 5:147-160(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9154838; DOI=10.1128/mcb.17.6.3388;
RA Osaka F., Seino H., Seno T., Yamao F.;
RT "A ubiquitin-conjugating enzyme in fission yeast that is essential for the
RT onset of anaphase in mitosis.";
RL Mol. Cell. Biol. 17:3388-3397(1997).
RN [5]
RP INTERACTION WITH CRB2.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9407031; DOI=10.1101/gad.11.24.3387;
RA Saka Y., Esashi F., Matsusaka T., Mochida S., Yanagida M.;
RT "Damage and replication checkpoint control in fission yeast is ensured by
RT interactions of Crb2, a protein with BRCT motif, with Cut5 and Chk1.";
RL Genes Dev. 11:3387-3400(1997).
RN [6]
RP FUNCTION.
RX PubMed=9278510; DOI=10.1126/science.277.5331.1495;
RA Furnari B., Rhind N., Russell P.;
RT "Cdc25 mitotic inducer targeted by chk1 DNA damage checkpoint kinase.";
RL Science 277:1495-1497(1997).
RN [7]
RP INTERACTION WITH CRB2 AND RAD3.
RX PubMed=14739927; DOI=10.1038/sj.emboj.7600018;
RA Mochida S., Esashi F., Aono N., Tamai K., O'Connell M.J., Yanagida M.;
RT "Regulation of checkpoint kinases through dynamic interaction with Crb2.";
RL EMBO J. 23:418-428(2004).
RN [8]
RP INTERACTION WITH RFP1.
RX PubMed=17502373; DOI=10.1074/jbc.m702652200;
RA Kosoy A., Calonge T.M., Outwin E.A., O'Connell M.J.;
RT "Fission yeast Rnf4 homologs are required for DNA repair.";
RL J. Biol. Chem. 282:20388-20394(2007).
RN [9]
RP INTERACTION WITH CRB2.
RX PubMed=22792081; DOI=10.1371/journal.pgen.1002817;
RA Qu M., Yang B., Tao L., Yates J.R., Russell P., Dong M.Q., Du L.L.;
RT "Phosphorylation-dependent interactions between Crb2 and Chk1 are essential
RT for DNA damage checkpoint.";
RL PLoS Genet. 8:E1002817-E1002817(2012).
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
CC (PubMed:8497322). May also negatively regulate cell cycle progression
CC during unperturbed cell cycles. Binds to and phosphorylates CDC25. This
CC leads to negative regulation of CDC25 and prevents mitotic entry
CC (PubMed:9278510). {ECO:0000269|PubMed:8497322,
CC ECO:0000269|PubMed:9278510}.
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 -!- SUBUNIT: Interacts with crb2 (PubMed:9407031, PubMed:14739927,
CC PubMed:22792081). Interacts with rad3 (PubMed:14739927). Interacts with
CC rfp1 (PubMed:17502373). {ECO:0000269|PubMed:14739927,
CC ECO:0000269|PubMed:17502373, ECO:0000269|PubMed:22792081,
CC ECO:0000269|PubMed:9407031}.
CC -!- INTERACTION:
CC P34208; P87074: crb2; NbExp=4; IntAct=EBI-768535, EBI-768448;
CC P34208; O13826: rfp1; NbExp=3; IntAct=EBI-768535, EBI-3647269;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated.
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; L13742; AAA79758.1; -; Genomic_DNA.
DR EMBL; U37421; AAA80539.1; -; mRNA.
DR EMBL; CU329672; CAA22551.1; -; Genomic_DNA.
DR EMBL; D85545; BAA20374.1; -; Genomic_DNA.
DR PIR; S33597; S33597.
DR RefSeq; NP_588070.1; NM_001023062.2.
DR AlphaFoldDB; P34208; -.
DR SMR; P34208; -.
DR BioGRID; 275659; 112.
DR IntAct; P34208; 9.
DR STRING; 4896.SPCC1259.13.1; -.
DR iPTMnet; P34208; -.
DR MaxQB; P34208; -.
DR PaxDb; P34208; -.
DR PRIDE; P34208; -.
DR EnsemblFungi; SPCC1259.13.1; SPCC1259.13.1:pep; SPCC1259.13.
DR PomBase; SPCC1259.13; chk1.
DR VEuPathDB; FungiDB:SPCC1259.13; -.
DR eggNOG; KOG0590; Eukaryota.
DR HOGENOM; CLU_000288_59_8_1; -.
DR InParanoid; P34208; -.
DR OMA; ACIKKAC; -.
DR PhylomeDB; P34208; -.
DR BRENDA; 2.7.11.1; 5613.
DR PRO; PR:P34208; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; IMP:PomBase.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IDA:PomBase.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IGI:PomBase.
DR GO; GO:1990260; P:negative regulation of transcription from RNA polymerase II promoter by transcription factor localization involved in response to DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd14069; STKc_Chk1; 1.
DR InterPro; IPR034670; Chk1_catalytic_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 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 Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..496
FT /note="Serine/threonine-protein kinase chk1"
FT /id="PRO_0000085856"
FT DOMAIN 10..272
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 16..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 496 AA; 56506 MW; 0DEB8E10541F7942 CRC64;
MAQKLDNFPY HIGREIGTGA FASVRLCYDD NAKIYAVKFV NKKHATSCMN AGVWARRMAS
EIQLHKLCNG HKNIIHFYNT AENPQWRWVV LEFAQGGDLF DKIEPDVGID EDVAQFYFAQ
LMEGISFMHS KGVAHRDLKP ENILLDYNGN LKISDFGFAS LFSYKGKSRL LNSPVGSPPY
AAPEITQQYD GSKVDVWSCG IILFALLLGN TPWDEAISNT GDYLLYKKQC ERPSYHPWNL
LSPGAYSIIT GMLRSDPFKR YSVKHVVQHP WLTSSTPFRT KNGNCADPVA LASRLMLKLR
IDLDKPRLAS SRASQNDSGF SMTQPAFKKN DQKELDRVEV YGALSQPVQL NKNIDVTEIL
EKDPSLSQFC ENEGFIKRLA KKAKNFYEIC PPERLTRFYS RASRETIIDH LYDSLRLLAI
SVTMKYVRNQ TILYVNLHDK RKCLLQGVIE LTNLGHNLEL INFIKRNGDP LEWRKFFKNV
VSSIGKPIVL TDVSQN
