CDK1_SCHPO
ID CDK1_SCHPO Reviewed; 297 AA.
AC P04551;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Cyclin-dependent kinase 1 {ECO:0000250|UniProtKB:P00546};
DE Short=CDK1 {ECO:0000250|UniProtKB:P00546};
DE EC=2.7.11.22 {ECO:0000269|PubMed:11486016};
DE AltName: Full=Cell division control protein 2;
DE AltName: Full=Cell division protein kinase 1;
DE AltName: Full=p34 protein kinase;
GN Name=cdc2 {ECO:0000303|PubMed:6526270};
GN Synonyms=cdk1, swo2, tws1 {ECO:0000303|PubMed:6581157};
GN ORFNames=pi002, SPBC11B10.09;
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], AND MUTAGENESIS OF CYS-67.
RX PubMed=6526270; DOI=10.1016/0378-1119(84)90203-8;
RA Hindley J., Phear G.A.;
RT "Sequence of the cell division gene CDC2 from Schizosaccharomyces pombe;
RT patterns of splicing and homology to protein kinases.";
RL Gene 31:129-134(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
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 FUNCTION.
RX PubMed=6581157; DOI=10.1128/jb.157.1.334-336.1984;
RA Nakaseko Y., Niwa O., Yanagida M.;
RT "A meiotic mutant of the fission yeast Schizosaccharomyces pombe that
RT produces mature asci containing two diploid spores.";
RL J. Bacteriol. 157:334-336(1984).
RN [5]
RP ASSOCIATION WITH SUC1.
RX PubMed=3322810; DOI=10.1002/j.1460-2075.1987.tb02676.x;
RA Brizuela L., Draetta G., Beach D.;
RT "p13suc1 acts in the fission yeast cell division cycle as a component of
RT the p34cdc2 protein kinase.";
RL EMBO J. 6:3507-3515(1987).
RN [6]
RP FUNCTION.
RX DOI=10.1007/BF00435510;
RA Grallert B., Sipiczki M.;
RT "Initiation of the second meiotic division in Schizosaccharomyces pombe
RT shares common functions with that of mitosis.";
RL Curr. Genet. 15:231-233(1989).
RN [7]
RP PHOSPHORYLATION AT TYR-15.
RX PubMed=2682257; DOI=10.1038/342039a0;
RA Gould K.L., Nurse P.;
RT "Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase
RT regulates entry into mitosis.";
RL Nature 342:39-45(1989).
RN [8]
RP FUNCTION.
RX PubMed=2274045; DOI=10.1007/bf00633860;
RA Grallert B., Sipiczki M.;
RT "Dissociation of meiotic and mitotic roles of the fission yeast cdc2
RT gene.";
RL Mol. Gen. Genet. 222:473-475(1990).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF PHE-210; GLY-212; LEU-269 AND TYR-292.
RX PubMed=1896017; DOI=10.1007/bf00264219;
RA MacNeill S.A., Creanor J., Nurse P.;
RT "Isolation, characterisation and molecular cloning of new mutant alleles of
RT the fission yeast p34cdc2+ protein kinase gene: identification of
RT temperature-sensitive G2-arresting alleles.";
RL Mol. Gen. Genet. 229:109-118(1991).
RN [10]
RP INTERACTION WITH CIG2.
RX PubMed=8455610; DOI=10.1128/mcb.13.4.2286-2297.1993;
RA Bueno A., Russell P.;
RT "Two fission yeast B-type cyclins, cig2 and Cdc13, have different functions
RT in mitosis.";
RL Mol. Cell. Biol. 13:2286-2297(1993).
RN [11]
RP MUTAGENESIS OF TYR-15.
RX PubMed=8437586; DOI=10.1007/bf00277142;
RA McNeill S.A., Nurse P.;
RT "Mutational analysis of the fission yeast p34cdc2 protein kinase gene.";
RL Mol. Gen. Genet. 236:415-426(1993).
RN [12]
RP FUNCTION.
RX PubMed=8087848; DOI=10.1016/s0092-8674(94)90542-8;
RA Hayles J., Fisher D., Woollard A., Nurse P.;
RT "Temporal order of S phase and mitosis in fission yeast is determined by
RT the state of the p34cdc2-mitotic B cyclin complex.";
RL Cell 78:813-822(1994).
RN [13]
RP FUNCTION.
RX PubMed=7498766; DOI=10.1093/genetics/140.4.1235;
RA Iino Y., Hiramine Y., Yamamoto M.;
RT "The role of cdc2 and other genes in meiosis in Schizosaccharomyces
RT pombe.";
RL Genetics 140:1235-1245(1995).
RN [14]
RP REVIEW.
RX PubMed=8855663; DOI=10.1016/s0168-9525(96)80016-3;
RA Stern B., Nurse P.;
RT "A quantitative model for the cdc2 control of S phase and mitosis in
RT fission yeast.";
RL Trends Genet. 12:345-350(1996).
RN [15]
RP FUNCTION.
RX PubMed=9042863; DOI=10.1101/gad.11.4.504;
RA Rhind N., Furnari B., Russell P.;
RT "Cdc2 tyrosine phosphorylation is required for the DNA damage checkpoint in
RT fission yeast.";
RL Genes Dev. 11:504-511(1997).
RN [16]
RP INTERACTION WITH CIG2.
RX PubMed=11163211; DOI=10.1016/s1097-2765(00)00135-0;
RA Yamano H., Kitamura K., Kominami K., Lehmann A., Hunt T., Toda T.;
RT "The spike of S phase cyclin Cig2 expression at the G1-S border in fission
RT yeast requires both APC and SCF ubiquitin ligases.";
RL Mol. Cell 6:1377-1387(2000).
RN [17]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11486016; DOI=10.1128/mcb.21.17.5767-5777.2001;
RA Vas A., Mok W., Leatherwood J.;
RT "Control of DNA rereplication via Cdc2 phosphorylation sites in the origin
RT recognition complex.";
RL Mol. Cell. Biol. 21:5767-5777(2001).
RN [18]
RP FUNCTION.
RX PubMed=16049013; DOI=10.1074/jbc.m504746200;
RA Shimada M., Namikawa-Yamada C., Nakanishi M., Murakami H.;
RT "Regulation of Cdc2p and Cdc13p is required for cell cycle arrest induced
RT by defective RNA splicing in fission yeast.";
RL J. Biol. Chem. 280:32640-32648(2005).
RN [19]
RP FUNCTION.
RX PubMed=16920624; DOI=10.1016/j.cub.2006.06.065;
RA Aoki K., Nakaseko Y., Kinoshita K., Goshima G., Yanagida M.;
RT "CDC2 phosphorylation of the fission yeast dis1 ensures accurate chromosome
RT segregation.";
RL Curr. Biol. 16:1627-1635(2006).
RN [20]
RP INTERACTION WITH CDC13 AND CDC37.
RX PubMed=16390871; DOI=10.1242/jcs.02729;
RA Turnbull E.L., Martin I.V., Fantes P.A.;
RT "Activity of Cdc2 and its interaction with the cyclin Cdc13 depend on the
RT molecular chaperone Cdc37 in Schizosaccharomyces pombe.";
RL J. Cell Sci. 119:292-302(2006).
RN [21]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [22]
RP FUNCTION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND THR-167, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [23]
RP FUNCTION.
RX PubMed=27984725; DOI=10.1016/j.cell.2016.11.034;
RA Swaffer M.P., Jones A.W., Flynn H.R., Snijders A.P., Nurse P.;
RT "CDK Substrate Phosphorylation and Ordering the Cell Cycle.";
RL Cell 167:1750-1761(2016).
CC -!- FUNCTION: Cyclin-dependent kinase that acts as a master regulator of
CC the mitotic and meiotic cell cycles (PubMed:8087848, PubMed:9042863,
CC PubMed:1896017, PubMed:2274045, PubMed:6581157, PubMed:7498766, Ref.6).
CC Required to drive the G1-S and G2-M transitions, and initiation of
CC premeiotic DNA replication and meiosis II (PubMed:8087848,
CC PubMed:9042863, PubMed:1896017, PubMed:2274045, PubMed:6581157,
CC PubMed:7498766, Ref.6). More than 200 substrates have been identified
CC (PubMed:27984725). Substrate specificity is in part regulated by the
CC bound cyclin protein (PubMed:27984725). When complexed with cyclin
CC cig2, it drives the G1-S phase transition (PubMed:8087848). When
CC complexed with cyclin cdc13, it drives the G2-M transition and
CC initiation of meiosis II (PubMed:8087848, PubMed:7498766). Its activity
CC rises throughout the cell cycle and substrate specificity is further
CC influenced by activity thresholds with more sensitive substrates
CC phosphorylated earlier in the cell cycle than less sensitive substrates
CC (PubMed:27984725). Phosphorylates dis1 during metaphase to ensure
CC proper microtubule dynamics and accurate chromosome segregation
CC (PubMed:16920624). Phosphorylates the repetitive C-terminus of the
CC large subunit of RNA polymerase II rpb1 (Probable). Inactivated by
CC checkpoint signaling following detection of cellular damage, leading to
CC cell cycle arrest to allow damage repair (PubMed:9042863,
CC PubMed:16049013). Inactivated during G2 DNA damage checkpoint signaling
CC (PubMed:9042863). Inactivated in response to defective RNA splicing
CC (PubMed:16049013). {ECO:0000269|PubMed:16049013,
CC ECO:0000269|PubMed:16920624, ECO:0000269|PubMed:1896017,
CC ECO:0000269|PubMed:2274045, ECO:0000269|PubMed:27984725,
CC ECO:0000269|PubMed:6581157, ECO:0000269|PubMed:7498766,
CC ECO:0000269|PubMed:8087848, ECO:0000269|PubMed:9042863,
CC ECO:0000269|Ref.6, ECO:0000305|PubMed:18257517}.
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=2.7.11.22;
CC Evidence={ECO:0000250|UniProtKB:P24941};
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=2.7.11.22; Evidence={ECO:0000269|PubMed:11486016};
CC -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC the enzyme, while phosphorylation at Thr-167 activates it.
CC {ECO:0000250|UniProtKB:P06493}.
CC -!- SUBUNIT: Forms a stable but non-covalent complex with regulatory
CC subunit suc1 and with a cyclin (PubMed:3322810). Interacts with cyclin
CC cdc13 (PubMed:16390871). Interacts with cyclin cig2 (PubMed:8455610,
CC PubMed:11163211). Interacts with cdc37 (PubMed:8455610,
CC PubMed:11163211, PubMed:16390871). {ECO:0000269|PubMed:11163211,
CC ECO:0000269|PubMed:16390871, ECO:0000269|PubMed:3322810,
CC ECO:0000269|PubMed:8455610}.
CC -!- INTERACTION:
CC P04551; Q09142: orc2; NbExp=2; IntAct=EBI-1187862, EBI-2028187;
CC P04551; O74627: pch1; NbExp=2; IntAct=EBI-1187862, EBI-443575;
CC P04551; P40380: rum1; NbExp=2; IntAct=EBI-1187862, EBI-1187892;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; M12912; AAA35293.1; -; Genomic_DNA.
DR EMBL; AB004534; BAA21379.1; -; Genomic_DNA.
DR EMBL; CU329671; CAC37513.1; -; Genomic_DNA.
DR PIR; A23359; TVZP2.
DR RefSeq; NP_595629.1; NM_001021523.2.
DR AlphaFoldDB; P04551; -.
DR SMR; P04551; -.
DR BioGRID; 276415; 103.
DR DIP; DIP-1076N; -.
DR IntAct; P04551; 6.
DR STRING; 4896.SPBC11B10.09.1; -.
DR iPTMnet; P04551; -.
DR MaxQB; P04551; -.
DR PaxDb; P04551; -.
DR PRIDE; P04551; -.
DR EnsemblFungi; SPBC11B10.09.1; SPBC11B10.09.1:pep; SPBC11B10.09.
DR PomBase; SPBC11B10.09; cdc2.
DR VEuPathDB; FungiDB:SPBC11B10.09; -.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; P04551; -.
DR OMA; NNDVWPE; -.
DR PhylomeDB; P04551; -.
DR BRENDA; 2.7.11.22; 5613.
DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SPO-3214858; RMTs methylate histone arginines.
DR Reactome; R-SPO-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-SPO-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR Reactome; R-SPO-68962; Activation of the pre-replicative complex.
DR Reactome; R-SPO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SPO-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-SPO-69231; Cyclin D associated events in G1.
DR Reactome; R-SPO-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-SPO-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SPO-9754119; Drug-mediated inhibition of CDK4/CDK6 activity.
DR SABIO-RK; P04551; -.
DR PRO; PR:P04551; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; EXP:PomBase.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; EXP:PomBase.
DR GO; GO:0000776; C:kinetochore; EXP:PomBase.
DR GO; GO:0072687; C:meiotic spindle; IDA:PomBase.
DR GO; GO:0035974; C:meiotic spindle pole body; EXP:PomBase.
DR GO; GO:0072686; C:mitotic spindle; EXP:PomBase.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; EXP:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR GO; GO:0097472; F:cyclin-dependent protein kinase activity; IDA:PomBase.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0004672; F:protein kinase activity; IDA: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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0061245; P:establishment or maintenance of bipolar cell polarity; IDA:PomBase.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0031568; P:mitotic G1 cell size control checkpoint signaling; IGI:PomBase.
DR GO; GO:1905785; P:negative regulation of anaphase-promoting complex-dependent catabolic process; IMP:PomBase.
DR GO; GO:1902424; P:negative regulation of attachment of mitotic spindle microtubules to kinetochore; IMP:PomBase.
DR GO; GO:0110045; P:negative regulation of cell cycle switching, mitotic to meiotic cell cycle; IMP:PomBase.
DR GO; GO:0031138; P:negative regulation of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IMP:PomBase.
DR GO; GO:0001100; P:negative regulation of exit from mitosis; EXP:PomBase.
DR GO; GO:1903500; P:negative regulation of mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:1902413; P:negative regulation of mitotic cytokinesis; EXP:PomBase.
DR GO; GO:1903467; P:negative regulation of mitotic DNA replication initiation; IMP:PomBase.
DR GO; GO:1902845; P:negative regulation of mitotic spindle elongation; IMP:PomBase.
DR GO; GO:1904537; P:negative regulation of mitotic telomere tethering at nuclear periphery; IPI:PomBase.
DR GO; GO:1905757; P:negative regulation of primary cell septum biogenesis; IMP:PomBase.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IMP:PomBase.
DR GO; GO:0031536; P:positive regulation of exit from mitosis; IMP:PomBase.
DR GO; GO:1904514; P:positive regulation of initiation of premeiotic DNA replication; IMP:PomBase.
DR GO; GO:0051446; P:positive regulation of meiotic cell cycle; IMP:PomBase.
DR GO; GO:1905263; P:positive regulation of meiotic DNA double-strand break formation involved in reciprocal meiotic recombination; IMP:PomBase.
DR GO; GO:1903465; P:positive regulation of mitotic cell cycle DNA replication; EXP:PomBase.
DR GO; GO:1903380; P:positive regulation of mitotic chromosome condensation; IMP:PomBase.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:PomBase.
DR GO; GO:0140429; P:positive regulation of mitotic sister chromatid biorientation; IMP:PomBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:PomBase.
DR GO; GO:0031031; P:positive regulation of septation initiation signaling; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0110044; P:regulation of cell cycle switching, mitotic to meiotic cell cycle; IDA:PomBase.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0062123; P:regulation of linear element maturation; IMP:PomBase.
DR GO; GO:0072429; P:response to intra-S DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:0072441; P:response to meiotic DNA replication checkpoint signaling; EXP:PomBase.
DR GO; GO:1990820; P:response to mitotic DNA integrity checkpoint signaling; IGI:PomBase.
DR GO; GO:0072435; P:response to mitotic G2 DNA damage checkpoint signaling; IMP:PomBase.
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; Cell division; Cytoplasm; Kinase; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..297
FT /note="Cyclin-dependent kinase 1"
FT /id="PRO_0000085720"
FT DOMAIN 4..293
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517,
FT ECO:0000269|PubMed:2682257"
FT MOD_RES 167
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 15
FT /note="Y->F: Premature entry into mitosis."
FT /evidence="ECO:0000269|PubMed:8437586"
FT MUTAGEN 67
FT /note="C->F: In cdc2-4W."
FT /evidence="ECO:0000269|PubMed:6526270"
FT MUTAGEN 67
FT /note="C->Y: In cdc2-3W."
FT /evidence="ECO:0000269|PubMed:6526270"
FT MUTAGEN 210
FT /note="F->L: Arrests in G1 or G2 at high temperature."
FT /evidence="ECO:0000269|PubMed:1896017"
FT MUTAGEN 212
FT /note="G->S: Arrests in G2 at high temperature."
FT /evidence="ECO:0000269|PubMed:1896017"
FT MUTAGEN 269
FT /note="L->S: Arrests in G2 at high temperature."
FT /evidence="ECO:0000269|PubMed:1896017"
FT MUTAGEN 292
FT /note="Y->H: Arrests in G1 or G2 at high temperature."
FT /evidence="ECO:0000269|PubMed:1896017"
SQ SEQUENCE 297 AA; 34359 MW; D04EF14BA1492875 CRC64;
MENYQKVEKI GEGTYGVVYK ARHKLSGRIV AMKKIRLEDE SEGVPSTAIR EISLLKEVND
ENNRSNCVRL LDILHAESKL YLVFEFLDMD LKKYMDRISE TGATSLDPRL VQKFTYQLVN
GVNFCHSRRI IHRDLKPQNL LIDKEGNLKL ADFGLARSFG VPLRNYTHEI VTLWYRAPEV
LLGSRHYSTG VDIWSVGCIF AEMIRRSPLF PGDSEIDEIF KIFQVLGTPN EEVWPGVTLL
QDYKSTFPRW KRMDLHKVVP NGEEDAIELL SAMLVYDPAH RISAKRALQQ NYLRDFH
