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Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 28) (Cell division protein kinase 1)

 CDK1_YEAST              Reviewed;         298 AA.
P00546; D6VQF5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
22-NOV-2017, entry version 196.
RecName: Full=Cyclin-dependent kinase 1;
Short=CDK1;
EC=2.7.11.22;
AltName: Full=Cell division control protein 28;
AltName: Full=Cell division protein kinase 1;
Name=CDC28; Synonyms=CDK1, HSL5, SRM5; OrderedLocusNames=YBR160W;
ORFNames=YBR1211;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6361575; DOI=10.1038/307183a0;
Lorincz A.T., Reed S.I.;
"Primary structure homology between the product of yeast cell division
control gene CDC28 and vertebrate oncogenes.";
Nature 307:183-185(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7597849; DOI=10.1002/yea.320110508;
Baur S., Becker J., Li Z., Niegemann E., Wehner E., Wolter R.,
Brendel M.;
"Sequence analysis of a 5.6 kb fragment of chromosome II from
Saccharomyces cerevisiae reveals two new open reading frames next to
CDC28.";
Yeast 11:455-458(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
PHOSPHORYLATION SUBSTRATES.
PubMed=14574415; DOI=10.1038/nature02062;
Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D.,
Shah K., Shokat K.M., Morgan D.O.;
"Targets of the cyclin-dependent kinase Cdk1.";
Nature 425:859-864(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19 AND THR-169, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: This protein is essential for the completion of the
start, the controlling event, in the cell cycle. More than 200
substrates have been identified.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Phosphorylation at Thr-18 or Tyr-19 inactivates
the enzyme, while phosphorylation at Thr-169 activates it.
{ECO:0000250}.
-!- SUBUNIT: Forms a stable but non-covalent complex with the CKS1
protein and with a cyclin.
-!- INTERACTION:
P03070:- (xeno); NbExp=3; IntAct=EBI-4253, EBI-617698;
P43568:CAK1; NbExp=3; IntAct=EBI-4253, EBI-3953;
P09119:CDC6; NbExp=2; IntAct=EBI-4253, EBI-4447;
P20486:CKS1; NbExp=9; IntAct=EBI-4253, EBI-4746;
P30283:CLB5; NbExp=5; IntAct=EBI-4253, EBI-4538;
P32943:CLB6; NbExp=3; IntAct=EBI-4253, EBI-2049771;
P20437:CLN1; NbExp=7; IntAct=EBI-4253, EBI-4479;
P20438:CLN2; NbExp=10; IntAct=EBI-4253, EBI-4483;
P13365:CLN3; NbExp=6; IntAct=EBI-4253, EBI-4490;
-!- MISCELLANEOUS: Present with 6670 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X00257; CAA25065.1; -; Genomic_DNA.
EMBL; Z36029; CAA85119.1; -; Genomic_DNA.
EMBL; X80224; CAA56509.1; -; Genomic_DNA.
EMBL; BK006936; DAA07275.1; -; Genomic_DNA.
PIR; A00657; TVBY8.
RefSeq; NP_009718.3; NM_001178508.3.
ProteinModelPortal; P00546; -.
SMR; P00546; -.
BioGrid; 32859; 1273.
DIP; DIP-1039N; -.
IntAct; P00546; 87.
MINT; MINT-569037; -.
STRING; 4932.YBR160W; -.
BindingDB; P00546; -.
ChEMBL; CHEMBL5213; -.
iPTMnet; P00546; -.
MaxQB; P00546; -.
PRIDE; P00546; -.
EnsemblFungi; YBR160W; YBR160W; YBR160W.
GeneID; 852457; -.
KEGG; sce:YBR160W; -.
EuPathDB; FungiDB:YBR160W; -.
SGD; S000000364; CDC28.
GeneTree; ENSGT00900000140881; -.
InParanoid; P00546; -.
KO; K04563; -.
OMA; EMMLVYD; -.
OrthoDB; EOG092C2FL8; -.
BioCyc; YEAST:G3O-29110-MONOMER; -.
BRENDA; 2.7.11.22; 984.
Reactome; R-SCE-110056; MAPK3 (ERK1) activation.
Reactome; R-SCE-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-SCE-2299718; Condensation of Prophase Chromosomes.
Reactome; R-SCE-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7.
Reactome; R-SCE-3214858; RMTs methylate histone arginines.
Reactome; R-SCE-4419969; Depolymerisation of the Nuclear Lamina.
Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
Reactome; R-SCE-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-SCE-68949; Orc1 removal from chromatin.
Reactome; R-SCE-68962; Activation of the pre-replicative complex.
Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-SCE-69202; Cyclin E associated events during G1/S transition.
Reactome; R-SCE-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-SCE-69231; Cyclin D associated events in G1.
Reactome; R-SCE-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-SCE-69478; G2/M DNA replication checkpoint.
Reactome; R-SCE-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-SCE-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
PRO; PR:P00546; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0005935; C:cellular bud neck; IDA:SGD.
GO; GO:0010005; C:cortical microtubule, transverse to long axis; IEA:EnsemblPlants.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:SGD.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IEA:EnsemblPlants.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:SGD.
GO; GO:0042393; F:histone binding; IDA:SGD.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
GO; GO:0000993; F:RNA polymerase II core binding; IDA:SGD.
GO; GO:0006370; P:7-methylguanosine mRNA capping; IMP:SGD.
GO; GO:0008356; P:asymmetric cell division; IEA:EnsemblPlants.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0042023; P:DNA endoreduplication; IEA:EnsemblPlants.
GO; GO:0016572; P:histone phosphorylation; IBA:GO_Central.
GO; GO:0000706; P:meiotic DNA double-strand break processing; IGI:SGD.
GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
GO; GO:1990758; P:mitotic sister chromatid biorientation; IGI:SGD.
GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IMP:SGD.
GO; GO:0051447; P:negative regulation of meiotic cell cycle; IMP:SGD.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:SGD.
GO; GO:0045875; P:negative regulation of sister chromatid cohesion; IMP:SGD.
GO; GO:0007070; P:negative regulation of transcription from RNA polymerase II promoter during mitotic cell cycle; IMP:SGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:SGD.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:SGD.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:SGD.
GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:EnsemblPlants.
GO; GO:0045819; P:positive regulation of glycogen catabolic process; IMP:SGD.
GO; GO:0051446; P:positive regulation of meiotic cell cycle; IDA:SGD.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:SGD.
GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IDA:SGD.
GO; GO:0010696; P:positive regulation of spindle pole body separation; IMP:SGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:SGD.
GO; GO:1901319; P:positive regulation of trehalose catabolic process; IMP:SGD.
GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IMP:SGD.
GO; GO:1990139; P:protein localization to nuclear periphery; IMP:SGD.
GO; GO:0034504; P:protein localization to nucleus; IMP:SGD.
GO; GO:1902002; P:protein phosphorylation involved in cellular protein catabolic process; IMP:SGD.
GO; GO:1990802; P:protein phosphorylation involved in DNA double-strand break processing; IMP:SGD.
GO; GO:1990804; P:protein phosphorylation involved in double-strand break repair via nonhomologous end joining; IMP:SGD.
GO; GO:1990801; P:protein phosphorylation involved in mitotic spindle assembly; IGI:SGD.
GO; GO:1990803; P:protein phosphorylation involved in protein localization to spindle microtubule; IMP:SGD.
GO; GO:0010568; P:regulation of budding cell apical bud growth; IMP:SGD.
GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IEA:EnsemblPlants.
GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:SGD.
GO; GO:0010570; P:regulation of filamentous growth; IMP:SGD.
GO; GO:0040020; P:regulation of meiotic nuclear division; IEA:EnsemblPlants.
GO; GO:0060303; P:regulation of nucleosome density; IMP:SGD.
GO; GO:1905634; P:regulation of protein localization to chromatin; IDA:SGD.
GO; GO:0090169; P:regulation of spindle assembly; IMP:SGD.
GO; GO:0032210; P:regulation of telomere maintenance via telomerase; IGI:SGD.
GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
GO; GO:0098725; P:symmetric cell division; IEA:EnsemblPlants.
GO; GO:0007130; P:synaptonemal complex assembly; IMP:SGD.
GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Cell cycle; Cell division;
Complete proteome; Kinase; Mitosis; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 298 Cyclin-dependent kinase 1.
/FTId=PRO_0000085722.
DOMAIN 8 295 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 14 22 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 136 136 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 40 40 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 19 19 Phosphotyrosine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 169 169 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
SEQUENCE 298 AA; 34061 MW; 57A7A2B97A90DC6C CRC64;
MSGELANYKR LEKVGEGTYG VVYKALDLRP GQGQRVVALK KIRLESEDEG VPSTAIREIS
LLKELKDDNI VRLYDIVHSD AHKLYLVFEF LDLDLKRYME GIPKDQPLGA DIVKKFMMQL
CKGIAYCHSH RILHRDLKPQ NLLINKDGNL KLGDFGLARA FGVPLRAYTH EIVTLWYRAP
EVLLGGKQYS TGVDTWSIGC IFAEMCNRKP IFSGDSEIDQ IFKIFRVLGT PNEAIWPDIV
YLPDFKPSFP QWRRKDLSQV VPSLDPRGID LLDKLLAYDP INRISARRAA IHPYFQES


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