YEAST:CDK1

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	CDC28 (synonyms: CDK1, HSL5, SRM5)
Protein Name(s)	Cyclin-dependent kinase 1 CDK1 Cell division control protein 28 Cell division protein kinase 1
External Links
UniProt	P00546
EMBL	X00257 Z36029 X80224 BK006936
PIR	A00657
RefSeq	NP_009718.3
ProteinModelPortal	P00546
SMR	P00546
BioGrid	32859
DIP	DIP-1039N
IntAct	P00546
MINT	P00546
STRING	4932.YBR160W
BindingDB	P00546
ChEMBL	CHEMBL5213
iPTMnet	P00546
MaxQB	P00546
PaxDb	P00546
PRIDE	P00546
EnsemblFungi	YBR160W
GeneID	852457
KEGG	sce:YBR160W
EuPathDB	FungiDB:YBR160W
SGD	S000000364
GeneTree	ENSGT00910000144030
InParanoid	P00546
KO	K04563
OMA	EMMLVYD
OrthoDB	EOG092C2FL8
BioCyc	YEAST:G3O-29110-MONOMER
BRENDA	2.7.11.22
Reactome	R-SCE-110056 R-SCE-176408 R-SCE-2299718 R-SCE-2980767 R-SCE-3214858 R-SCE-4419969 R-SCE-5687128 R-SCE-6804114 R-SCE-68949 R-SCE-68962 R-SCE-69017 R-SCE-69202 R-SCE-69229 R-SCE-69231 R-SCE-69273 R-SCE-69478 R-SCE-69656 R-SCE-75035
PRO	PR:P00546
Proteomes	UP000002311
GO	GO:0005935 GO:0010005 GO:0000307 GO:0005737 GO:0010494 GO:0005829 GO:0005783 GO:0072686 GO:0005634 GO:0005886 GO:0005524 GO:0004693 GO:0042393 GO:0004674 GO:0000993 GO:0006370 GO:0008356 GO:0030154 GO:0044257 GO:0000729 GO:0042023 GO:0006303 GO:0016572 GO:0000706 GO:0044772 GO:1990758 GO:0090307 GO:2001033 GO:0051447 GO:0045930 GO:0045875 GO:0000122 GO:0045892 GO:0018105 GO:0018107 GO:0070816 GO:0045819 GO:0051446 GO:0045931 GO:0010571 GO:0010696 GO:0045944 GO:0045893 GO:1901319 GO:0010898 GO:1990139 GO:0034504 GO:1902889 GO:0010568 GO:1902806 GO:0010569 GO:0010570 GO:0040020 GO:0060303 GO:1905634 GO:0090169 GO:0032210 GO:0009409 GO:0098725 GO:0007130 GO:0016192
InterPro	IPR011009 IPR000719 IPR017441 IPR008271
Pfam	PF00069
SMART	SM00220
SUPFAM	SSF56112
PROSITE	PS00107 PS50011 PS00108

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0006468	protein phosphorylation	PMID:29561844^[1]	ECO:0000314			P		Cdk1 activates Separase (Esp1 in yeast) through phosphorylation to trigger anaphase onse. In figure 1D, Esp1 phosphorylation was detected after around 30 minutes, before the major mitotic cyclin-Cdk complex in yeast (CDK1-Clb2) started to appear in vivo.	complete CACAO 13255
	GO:0006468	protein phosphorylation	PMID:20385771^[2]	ECO:0000315			P		Figs. 1 shows that in S. cerevisiae, Cdk1 (also known as CDC28 in Uniprot) is required for repression of Sum1 by phosphorylation.	complete CACAO 13433
involved_in	GO:1903827	regulation of cellular protein localization	PMID:29263158^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0000084) has_input:(UniProtKB:P49723)	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:16319894^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1902596	negative regulation of DNA replication origin binding	PMID:29388912^[5]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000003642	P	has_regulation_target:(ComplexPortal:CPX-2944)	Seeded From UniProt	complete
involved_in	GO:1903500	negative regulation of mitotic actomyosin contractile ring assembly	PMID:24413167^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:16319894^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0043022	ribosome binding	PMID:16702403^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:25602519^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:Q12495)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:25602519^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q12495)	Seeded From UniProt	complete
involved_in	GO:1905634	regulation of protein localization to chromatin	PMID:25602519^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:Q12495)	Seeded From UniProt	complete
involved_in	GO:0044257	cellular protein catabolic process	PMID:21993622^[9]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P38634	P	has_direct_input:(UniProtKB:P38634)	Seeded From UniProt	complete
part_of	GO:0010494	cytoplasmic stress granule	PMID:26777405^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:27203178^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(SGD:S000002408)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:27203178^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(SGD:S000002408)	Seeded From UniProt	complete
involved_in	GO:1901319	positive regulation of trehalose catabolic process	PMID:27203179^[12]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P32356	P		Seeded From UniProt	complete
involved_in	GO:1901319	positive regulation of trehalose catabolic process	PMID:27203179^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045819	positive regulation of glycogen catabolic process	PMID:27203179^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0018107	peptidyl-threonine phosphorylation	PMID:27068241^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P32599) happens_during:(GO:0000089)	Seeded From UniProt	complete
enables	GO:0004693	cyclin-dependent protein serine/threonine kinase activity	PMID:27068241^[13]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P32599)	Seeded From UniProt	complete
involved_in	GO:0018107	peptidyl-threonine phosphorylation	PMID:27068241^[13]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:P32599) happens_during:(GO:0000089)	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:22056777^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P34161) happens_during:(GO:0000278)	Seeded From UniProt	complete
involved_in	GO:1990758	mitotic sister chromatid biorientation	PMID:22056777^[14]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P27636,UniProtKB:Q08581	P		Seeded From UniProt	complete
involved_in	GO:0006303	double-strand break repair via nonhomologous end joining	PMID:22563681^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P53150)	Seeded From UniProt	complete
involved_in	GO:1902889	protein localization to spindle microtubule	PMID:22521784^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P38991)	Seeded From UniProt	complete
involved_in	GO:0000729	DNA double-strand break processing	PMID:21841787^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P38859)	Seeded From UniProt	complete
involved_in	GO:0090307	mitotic spindle assembly	PMID:21558801^[18]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P30283	P	has_direct_input:(UniProtKB:P50275)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:22563681^[15]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P53150)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:22521784^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_direct_input:(UniProtKB:P38991)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:22521784^[16]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P38991)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:21841787^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_direct_input:(UniProtKB:P38859)	Seeded From UniProt	complete
involved_in	GO:0090169	regulation of spindle assembly	PMID:21558801^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P50275)	Seeded From UniProt	complete
involved_in	GO:0044257	cellular protein catabolic process	PMID:21098119^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P34233)	Seeded From UniProt	complete
involved_in	GO:0032210	regulation of telomere maintenance via telomerase	PMID:19135888^[20]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P32797	P		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:16096060^[21]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P32944)	Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:23314252^[22]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:P43605)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:23314252^[22]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P43605)	Seeded From UniProt	complete
involved_in	GO:2001033	negative regulation of double-strand break repair via nonhomologous end joining	PMID:19699692^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070816	phosphorylation of RNA polymerase II C-terminal domain	PMID:22689984^[24]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051447	negative regulation of meiotic cell cycle	PMID:12081645^[25]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051446	positive regulation of meiotic cell cycle	PMID:16814718^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051446	positive regulation of meiotic cell cycle	PMID:2680756^[27]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051446	positive regulation of meiotic cell cycle	PMID:16814718^[26]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:22689984^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045931	positive regulation of mitotic cell cycle	PMID:2165600^[28]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045931	positive regulation of mitotic cell cycle	PMID:7002718^[29]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045930	negative regulation of mitotic cell cycle	PMID:10074450^[30]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:1652372^[31]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000002553	P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:1652372^[31]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:14993267^[32]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:12081645^[25]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:14993267^[32]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045875	negative regulation of sister chromatid cohesion	PMID:21549314^[33]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042393	histone binding	PMID:20855529^[34]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034504	protein localization to nucleus	PMID:19188495^[35]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:Q05670)	Seeded From UniProt	complete
involved_in	GO:1990139	protein localization to nuclear periphery	PMID:20702586^[36]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P11986)\|has_direct_input:(UniProtKB:P04385)	Seeded From UniProt	complete
involved_in	GO:0006892	post-Golgi vesicle-mediated transport	PMID:22767578^[37]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010898	positive regulation of triglyceride catabolic process	PMID:19150427^[38]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000001797	P		Seeded From UniProt	complete
involved_in	GO:0010898	positive regulation of triglyceride catabolic process	PMID:19150427^[38]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010696	positive regulation of mitotic spindle pole body separation	PMID:16688214^[39]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000000159 SGD:S000000787 SGD:S000005584	P		Seeded From UniProt	complete
involved_in	GO:0010696	positive regulation of mitotic spindle pole body separation	PMID:8887667^[40]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010696	positive regulation of mitotic spindle pole body separation	PMID:16688214^[39]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010571	positive regulation of nuclear cell cycle DNA replication	PMID:12783856^[41]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010571	positive regulation of nuclear cell cycle DNA replication	PMID:4580573^[42]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010571	positive regulation of nuclear cell cycle DNA replication	PMID:14747467^[43]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010571	positive regulation of nuclear cell cycle DNA replication	PMID:14747467^[43]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010570	regulation of filamentous growth	PMID:9891070^[44]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010569	regulation of double-strand break repair via homologous recombination	PMID:15496928^[45]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010568	regulation of budding cell apical bud growth	PMID:17417630^[46]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000003723	P		Seeded From UniProt	complete
involved_in	GO:0010568	regulation of budding cell apical bud growth	PMID:17417630^[46]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007130	synaptonemal complex assembly	PMID:20825495^[47]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006370	7-methylguanosine mRNA capping	PMID:22689984^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060303	regulation of nucleosome density	PMID:20855529^[34]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005935	cellular bud neck	PMID:12554645^[48]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:17560371^[49]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:3312233^[50]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:14685274^[51]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004693	cyclin-dependent protein serine/threonine kinase activity	PMID:2142620^[52]	ECO:0000314	direct assay evidence used in manual assertion		F	happens_during:(GO:0000082) has_input:(UniProtKB:P20438)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:22689984^[24]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(SGD:S000002299)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:24319056^[53]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(SGD:S000004076)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:24319056^[53]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(SGD:S000000520)	Seeded From UniProt	complete
enables	GO:0000993	RNA polymerase II complex binding	PMID:22689984^[24]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000706	meiotic DNA double-strand break processing	PMID:20150422^[54]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000003143	P		Seeded From UniProt	complete
part_of	GO:0000307	cyclin-dependent protein kinase holoenzyme complex	PMID:1849458^[55]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000307	cyclin-dependent protein kinase holoenzyme complex	PMID:2142620^[52]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0030332	cyclin binding	PMID:21873635^[56]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104772 PANTHER:PTN000623979 RGD:70486 UniProtKB:P24941	F		Seeded From UniProt	complete
involved_in	GO:0010389	regulation of G2/M transition of mitotic cell cycle	PMID:21873635^[56]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000623979 PomBase:SPBC11B10.09	P		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:21873635^[56]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104772 PANTHER:PTN000623979 TAIR:locus:2099478 UniProtKB:P24941	P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:21873635^[56]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0004106 FB:FBgn0005640 FB:FBgn0013435 FB:FBgn0013762 FB:FBgn0015618 FB:FBgn0263237 MGI:MGI:101765 MGI:MGI:104772 MGI:MGI:88351 MGI:MGI:88357 PANTHER:PTN000623091 RGD:621124 RGD:70514 SGD:S000001622 SGD:S000001865 SGD:S000005488 SGD:S000005952 SGD:S000005963 SGD:S000006365 TAIR:locus:2119961 UniProtKB:P06493 UniProtKB:P11802 UniProtKB:P21127 UniProtKB:P24941 UniProtKB:P50750 UniProtKB:Q00534 UniProtKB:Q00646 UniProtKB:Q9UQ88 WB:WBGene00000405 WB:WBGene00000407 WB:WBGene00019362 ZFIN:ZDB-GENE-040808-34 dictyBase:DDB_G0267442 dictyBase:DDB_G0272813 dictyBase:DDB_G0288677	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[56]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000623979 PomBase:SPBC11B10.09 SGD:S000000364 TAIR:locus:2099478 UniProtKB:P24941	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[56]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015618 FB:FBgn0019949 FB:FBgn0263237 MGI:MGI:101765 MGI:MGI:102956 MGI:MGI:104772 MGI:MGI:1328368 MGI:MGI:88353 MGI:MGI:88357 MGI:MGI:894318 PANTHER:PTN000623091 PomBase:SPAC2F3.15 PomBase:SPBC11B10.09 PomBase:SPBC32H8.10 RGD:1305435 RGD:1359638 RGD:2319 RGD:619874 RGD:621120 RGD:621124 RGD:70486 RGD:70514 SGD:S000000364 SGD:S000001622 SGD:S000002266 SGD:S000005952 TAIR:locus:2008595 TAIR:locus:2027819 TAIR:locus:2033349 TAIR:locus:2080290 TAIR:locus:2084086 TAIR:locus:2099478 TAIR:locus:2119961 TAIR:locus:2158554 TAIR:locus:2194045 UniProtKB:O76039 UniProtKB:O94921 UniProtKB:P06493 UniProtKB:P11802 UniProtKB:P21127 UniProtKB:P24941 UniProtKB:P49336 UniProtKB:P50613 UniProtKB:P61075 UniProtKB:P79432 UniProtKB:Q00534 UniProtKB:Q00535 UniProtKB:Q00646 UniProtKB:Q5B3E4 UniProtKB:Q8IDW1 UniProtKB:Q8IIL5 UniProtKB:Q8IJQ1 UniProtKB:Q8RWN3 UniProtKB:Q8W4P1 UniProtKB:Q92772 UniProtKB:Q96VK3 UniProtKB:Q9NYV4 UniProtKB:Q9UQ88 WB:WBGene00000405 dictyBase:DDB_G0267442 dictyBase:DDB_G0288677	C		Seeded From UniProt	complete
enables	GO:0004693	cyclin-dependent protein serine/threonine kinase activity	PMID:21873635^[56]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0004106 FB:FBgn0005640 FB:FBgn0013762 FB:FBgn0019949 FB:FBgn0263237 MGI:MGI:104772 MGI:MGI:88351 MGI:MGI:88357 PANTHER:PTN000623091 PomBase:SPAC23H4.17c PomBase:SPAC2F3.15 PomBase:SPBC11B10.09 PomBase:SPBC19F8.07 PomBase:SPBC32H8.10 RGD:2319 RGD:621120 RGD:621124 RGD:70486 RGD:70514 SGD:S000000364 SGD:S000001622 SGD:S000005952 SGD:S000005963 SGD:S000006365 TAIR:locus:2011761 UniProtKB:A0A1D8PDA6 UniProtKB:C9K505 UniProtKB:O94921 UniProtKB:P06493 UniProtKB:P11802 UniProtKB:P24941 UniProtKB:P50750 UniProtKB:P61075 UniProtKB:Q00534 UniProtKB:Q00646 UniProtKB:Q8IJQ1 WB:WBGene00000405 ZFIN:ZDB-GENE-010131-2 dictyBase:DDB_G0272813 dictyBase:DDB_G0288677	F		Seeded From UniProt	complete
part_of	GO:0000307	cyclin-dependent protein kinase holoenzyme complex	PMID:21873635^[56]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104772 PANTHER:PTN000623979 PomBase:SPBC11B10.09 SGD:S000000364 UniProtKB:P24941	C		Seeded From UniProt	complete
involved_in	GO:0000082	G1/S transition of mitotic cell cycle	PMID:21873635^[56]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104772 PANTHER:PTN000623979 PomBase:SPBC11B10.09	P		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR017441	F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271	P		Seeded From UniProt	complete
enables	GO:0004693	cyclin-dependent protein serine/threonine kinase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.11.22	F		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0723	F		Seeded From UniProt	complete
involved_in	GO:0007049	cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0131	P		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P		Seeded From UniProt	complete
involved_in	GO:0051301	cell division	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0132	P		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Lianga, N et al. (2018) Cdk1 phosphorylation of Esp1/Separase functions with PP2A and Slk19 to regulate pericentric Cohesin and anaphase onset. PLoS Genet. 14 e1007029 PubMed GONUTS page
↑ Shin, ME et al. (2010) The Cdk1 and Ime2 protein kinases trigger exit from meiotic prophase in Saccharomyces cerevisiae by inhibiting the Sum1 transcriptional repressor. Mol. Cell. Biol. 30 2996-3003 PubMed GONUTS page
↑ Wu, X et al. (2018) Clb6-Cdc28 Promotes Ribonucleotide Reductase Subcellular Redistribution during S Phase. Mol. Cell. Biol. 38 PubMed GONUTS page
↑ ^4.0 ^4.1 Ptacek, J et al. (2005) Global analysis of protein phosphorylation in yeast. Nature 438 679-84 PubMed GONUTS page
↑ Phizicky, DV et al. (2018) Multiple kinases inhibit origin licensing and helicase activation to ensure reductive cell division during meiosis. Elife 7 PubMed GONUTS page
↑ Naylor, SG & Morgan, DO (2014) Cdk1-dependent phosphorylation of Iqg1 governs actomyosin ring assembly prior to cytokinesis. J. Cell. Sci. 127 1128-37 PubMed GONUTS page
↑ Fleischer, TC et al. (2006) Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes. Genes Dev. 20 1294-307 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Jeffery, DC et al. (2015) CDC28 phosphorylates Cac1p and regulates the association of chromatin assembly factor I with chromatin. Cell Cycle 14 74-85 PubMed GONUTS page
↑ Kõivomägi, M et al. (2011) Cascades of multisite phosphorylation control Sic1 destruction at the onset of S phase. Nature 480 128-31 PubMed GONUTS page
↑ Jain, S et al. (2016) ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure. Cell 164 487-98 PubMed GONUTS page
↑ ^11.0 ^11.1 Ewald, JC et al. (2016) The Yeast Cyclin-Dependent Kinase Routes Carbon Fluxes to Fuel Cell Cycle Progression. Mol. Cell 62 532-45 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Zhao, G et al. (2016) Cyclin-Dependent Kinase Co-Ordinates Carbohydrate Metabolism and Cell Cycle in S. cerevisiae. Mol. Cell 62 546-57 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Miao, Y et al. (2016) Fimbrin phosphorylation by metaphase Cdk1 regulates actin cable dynamics in budding yeast. Nat Commun 7 11265 PubMed GONUTS page
↑ ^14.0 ^14.1 Liang, H et al. (2012) Cdk1 promotes kinetochore bi-orientation and regulates Cdc20 expression during recovery from spindle checkpoint arrest. EMBO J. 31 403-16 PubMed GONUTS page
↑ ^15.0 ^15.1 Matsuzaki, K et al. (2012) Cyclin-dependent kinase-dependent phosphorylation of Lif1 and Sae2 controls imprecise nonhomologous end joining accompanied by double-strand break resection. Genes Cells 17 473-93 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Zimniak, T et al. (2012) Spatiotemporal regulation of Ipl1/Aurora activity by direct Cdk1 phosphorylation. Curr. Biol. 22 787-93 PubMed GONUTS page
↑ ^17.0 ^17.1 Chen, X et al. (2011) Cell cycle regulation of DNA double-strand break end resection by Cdk1-dependent Dna2 phosphorylation. Nat. Struct. Mol. Biol. 18 1015-9 PubMed GONUTS page
↑ ^18.0 ^18.1 Juanes, MA et al. (2011) Ase1p phosphorylation by cyclin-dependent kinase promotes correct spindle assembly in S. cerevisiae. Cell Cycle 10 1988-97 PubMed GONUTS page
↑ Liu, Q et al. (2011) SCFCdc4 enables mating type switching in yeast by cyclin-dependent kinase-mediated elimination of the Ash1 transcriptional repressor. Mol. Cell. Biol. 31 584-98 PubMed GONUTS page
↑ Li, S et al. (2009) Cdk1-dependent phosphorylation of Cdc13 coordinates telomere elongation during cell-cycle progression. Cell 136 50-61 PubMed GONUTS page
↑ Harvey, SL et al. (2005) Cdk1-dependent regulation of the mitotic inhibitor Wee1. Cell 122 407-20 PubMed GONUTS page
↑ ^22.0 ^22.1 Lyons, NA et al. (2013) Sequential primed kinases create a damage-responsive phosphodegron on Eco1. Nat. Struct. Mol. Biol. 20 194-201 PubMed GONUTS page
↑ Zhang, Y et al. (2009) Regulation of repair choice: Cdk1 suppresses recruitment of end joining factors at DNA breaks. DNA Repair (Amst.) 8 1235-41 PubMed GONUTS page
↑ ^24.0 ^24.1 ^24.2 ^24.3 ^24.4 Chymkowitch, P et al. (2012) Cdc28 kinase activity regulates the basal transcription machinery at a subset of genes. Proc. Natl. Acad. Sci. U.S.A. 109 10450-5 PubMed GONUTS page
↑ ^25.0 ^25.1 Purnapatre, K et al. (2002) The CLN3/SWI6/CLN2 pathway and SNF1 act sequentially to regulate meiotic initiation in Saccharomyces cerevisiae. Genes Cells 7 675-91 PubMed GONUTS page
↑ ^26.0 ^26.1 Henderson, KA et al. (2006) Cyclin-dependent kinase directly regulates initiation of meiotic recombination. Cell 125 1321-32 PubMed GONUTS page
↑ Shuster, EO & Byers, B (1989) Pachytene arrest and other meiotic effects of the start mutations in Saccharomyces cerevisiae. Genetics 123 29-43 PubMed GONUTS page
↑ Reed, SI & Wittenberg, C (1990) Mitotic role for the Cdc28 protein kinase of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 87 5697-701 PubMed GONUTS page
↑ Reed, SI (1980) The selection of S. cerevisiae mutants defective in the start event of cell division. Genetics 95 561-77 PubMed GONUTS page
↑ Jaspersen, SL et al. (1999) Inhibitory phosphorylation of the APC regulator Hct1 is controlled by the kinase Cdc28 and the phosphatase Cdc14. Curr. Biol. 9 227-36 PubMed GONUTS page
↑ ^31.0 ^31.1 Moll, T et al. (1991) The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SWI5. Cell 66 743-58 PubMed GONUTS page
↑ ^32.0 ^32.1 Geymonat, M et al. (2004) Clb6/Cdc28 and Cdc14 regulate phosphorylation status and cellular localization of Swi6. Mol. Cell. Biol. 24 2277-85 PubMed GONUTS page
↑ Lyons, NA & Morgan, DO (2011) Cdk1-dependent destruction of Eco1 prevents cohesion establishment after S phase. Mol. Cell 42 378-89 PubMed GONUTS page
↑ ^34.0 ^34.1 Chaves, S et al. (2010) Cks1, Cdk1, and the 19S proteasome collaborate to regulate gene induction-dependent nucleosome eviction in yeast. Mol. Cell. Biol. 30 5284-94 PubMed GONUTS page
↑ Ydenberg, CA & Rose, MD (2009) Antagonistic regulation of Fus2p nuclear localization by pheromone signaling and the cell cycle. J. Cell Biol. 184 409-22 PubMed GONUTS page
↑ Brickner, DG & Brickner, JH (2010) Cdk phosphorylation of a nucleoporin controls localization of active genes through the cell cycle. Mol. Biol. Cell 21 3421-32 PubMed GONUTS page
↑ McCusker, D et al. (2012) Cdk1-dependent control of membrane-trafficking dynamics. Mol. Biol. Cell 23 3336-47 PubMed GONUTS page
↑ ^38.0 ^38.1 Kurat, CF et al. (2009) Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 in yeast links lipolysis to cell-cycle progression. Mol. Cell 33 53-63 PubMed GONUTS page
↑ ^39.0 ^39.1 Crasta, K et al. (2006) Cdk1 regulates centrosome separation by restraining proteolysis of microtubule-associated proteins. EMBO J. 25 2551-63 PubMed GONUTS page
↑ Lim, HH et al. (1996) Spindle pole body separation in Saccharomyces cerevisiae requires dephosphorylation of the tyrosine 19 residue of Cdc28. Mol. Cell. Biol. 16 6385-97 PubMed GONUTS page
↑ Benjamin, KR et al. (2003) Control of landmark events in meiosis by the CDK Cdc28 and the meiosis-specific kinase Ime2. Genes Dev. 17 1524-39 PubMed GONUTS page
↑ Hartwell, LH (1973) Three additional genes required for deoxyribonucleic acid synthesis in Saccharomyces cerevisiae. J. Bacteriol. 115 966-74 PubMed GONUTS page
↑ ^43.0 ^43.1 Kesti, T et al. (2004) Cell cycle-dependent phosphorylation of the DNA polymerase epsilon subunit, Dpb2, by the Cdc28 cyclin-dependent protein kinase. J. Biol. Chem. 279 14245-55 PubMed GONUTS page
↑ Edgington, NP et al. (1999) Control of Saccharomyces cerevisiae filamentous growth by cyclin-dependent kinase Cdc28. Mol. Cell. Biol. 19 1369-80 PubMed GONUTS page
↑ Ira, G et al. (2004) DNA end resection, homologous recombination and DNA damage checkpoint activation require CDK1. Nature 431 1011-7 PubMed GONUTS page
↑ ^46.0 ^46.1 McCusker, D et al. (2007) Cdk1 coordinates cell-surface growth with the cell cycle. Nat. Cell Biol. 9 506-15 PubMed GONUTS page
↑ Zhu, Z et al. (2010) Cyclin-dependent kinase promotes formation of the synaptonemal complex in yeast meiosis. Genes Cells 15 1036-50 PubMed GONUTS page
↑ Maekawa, H et al. (2003) Yeast Cdk1 translocates to the plus end of cytoplasmic microtubules to regulate bud cortex interactions. EMBO J. 22 438-49 PubMed GONUTS page
↑ Vergés, E et al. (2007) Cyclin Cln3 is retained at the ER and released by the J chaperone Ydj1 in late G1 to trigger cell cycle entry. Mol. Cell 26 649-62 PubMed GONUTS page
↑ Wittenberg, C et al. (1987) Subcellular localization of a protein kinase required for cell cycle initiation in Saccharomyces cerevisiae: evidence for an association between the CDC28 gene product and the insoluble cytoplasmic matrix. J. Cell Biol. 105 1527-38 PubMed GONUTS page
↑ Wang, H et al. (2004) Recruitment of Cdc28 by Whi3 restricts nuclear accumulation of the G1 cyclin-Cdk complex to late G1. EMBO J. 23 180-90 PubMed GONUTS page
↑ ^52.0 ^52.1 Wittenberg, C et al. (1990) G1-specific cyclins of S. cerevisiae: cell cycle periodicity, regulation by mating pheromone, and association with the p34CDC28 protein kinase. Cell 62 225-37 PubMed GONUTS page
↑ ^53.0 ^53.1 Kao, L et al. (2014) Global analysis of cdc14 dephosphorylation sites reveals essential regulatory role in mitosis and cytokinesis. Mol. Cell Proteomics 13 594-605 PubMed GONUTS page
↑ Manfrini, N et al. (2010) Processing of meiotic DNA double strand breaks requires cyclin-dependent kinase and multiple nucleases. J. Biol. Chem. 285 11628-37 PubMed GONUTS page
↑ Ghiara, JB et al. (1991) A cyclin B homolog in S. cerevisiae: chronic activation of the Cdc28 protein kinase by cyclin prevents exit from mitosis. Cell 65 163-74 PubMed GONUTS page
↑ ^56.0 ^56.1 ^56.2 ^56.3 ^56.4 ^56.5 ^56.6 ^56.7 ^56.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:29561844-1] Lianga, N et al. (2018) Cdk1 phosphorylation of Esp1/Separase functions with PP2A and Slk19 to regulate pericentric Cohesin and anaphase onset. PLoS Genet. 14 e1007029 PubMed GONUTS page

[PMID:20385771-2] Shin, ME et al. (2010) The Cdk1 and Ime2 protein kinases trigger exit from meiotic prophase in Saccharomyces cerevisiae by inhibiting the Sum1 transcriptional repressor. Mol. Cell. Biol. 30 2996-3003 PubMed GONUTS page

[PMID:29263158-3] Wu, X et al. (2018) Clb6-Cdc28 Promotes Ribonucleotide Reductase Subcellular Redistribution during S Phase. Mol. Cell. Biol. 38 PubMed GONUTS page

[PMID:16319894-4] 4.0 ^4.1 Ptacek, J et al. (2005) Global analysis of protein phosphorylation in yeast. Nature 438 679-84 PubMed GONUTS page

[PMID:29388912-5] Phizicky, DV et al. (2018) Multiple kinases inhibit origin licensing and helicase activation to ensure reductive cell division during meiosis. Elife 7 PubMed GONUTS page

[PMID:24413167-6] Naylor, SG & Morgan, DO (2014) Cdk1-dependent phosphorylation of Iqg1 governs actomyosin ring assembly prior to cytokinesis. J. Cell. Sci. 127 1128-37 PubMed GONUTS page

[PMID:16702403-7] Fleischer, TC et al. (2006) Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes. Genes Dev. 20 1294-307 PubMed GONUTS page

[PMID:25602519-8] 8.0 ^8.1 ^8.2 Jeffery, DC et al. (2015) CDC28 phosphorylates Cac1p and regulates the association of chromatin assembly factor I with chromatin. Cell Cycle 14 74-85 PubMed GONUTS page

[PMID:21993622-9] Kõivomägi, M et al. (2011) Cascades of multisite phosphorylation control Sic1 destruction at the onset of S phase. Nature 480 128-31 PubMed GONUTS page

[PMID:26777405-10] Jain, S et al. (2016) ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure. Cell 164 487-98 PubMed GONUTS page

[PMID:27203178-11] 11.0 ^11.1 Ewald, JC et al. (2016) The Yeast Cyclin-Dependent Kinase Routes Carbon Fluxes to Fuel Cell Cycle Progression. Mol. Cell 62 532-45 PubMed GONUTS page

[PMID:27203179-12] 12.0 ^12.1 ^12.2 Zhao, G et al. (2016) Cyclin-Dependent Kinase Co-Ordinates Carbohydrate Metabolism and Cell Cycle in S. cerevisiae. Mol. Cell 62 546-57 PubMed GONUTS page

[PMID:27068241-13] 13.0 ^13.1 ^13.2 Miao, Y et al. (2016) Fimbrin phosphorylation by metaphase Cdk1 regulates actin cable dynamics in budding yeast. Nat Commun 7 11265 PubMed GONUTS page

[PMID:22056777-14] 14.0 ^14.1 Liang, H et al. (2012) Cdk1 promotes kinetochore bi-orientation and regulates Cdc20 expression during recovery from spindle checkpoint arrest. EMBO J. 31 403-16 PubMed GONUTS page

[PMID:22563681-15] 15.0 ^15.1 Matsuzaki, K et al. (2012) Cyclin-dependent kinase-dependent phosphorylation of Lif1 and Sae2 controls imprecise nonhomologous end joining accompanied by double-strand break resection. Genes Cells 17 473-93 PubMed GONUTS page

[PMID:22521784-16] 16.0 ^16.1 ^16.2 Zimniak, T et al. (2012) Spatiotemporal regulation of Ipl1/Aurora activity by direct Cdk1 phosphorylation. Curr. Biol. 22 787-93 PubMed GONUTS page

[PMID:21841787-17] 17.0 ^17.1 Chen, X et al. (2011) Cell cycle regulation of DNA double-strand break end resection by Cdk1-dependent Dna2 phosphorylation. Nat. Struct. Mol. Biol. 18 1015-9 PubMed GONUTS page

[PMID:21558801-18] 18.0 ^18.1 Juanes, MA et al. (2011) Ase1p phosphorylation by cyclin-dependent kinase promotes correct spindle assembly in S. cerevisiae. Cell Cycle 10 1988-97 PubMed GONUTS page

[PMID:21098119-19] Liu, Q et al. (2011) SCFCdc4 enables mating type switching in yeast by cyclin-dependent kinase-mediated elimination of the Ash1 transcriptional repressor. Mol. Cell. Biol. 31 584-98 PubMed GONUTS page

[PMID:19135888-20] Li, S et al. (2009) Cdk1-dependent phosphorylation of Cdc13 coordinates telomere elongation during cell-cycle progression. Cell 136 50-61 PubMed GONUTS page

[PMID:16096060-21] Harvey, SL et al. (2005) Cdk1-dependent regulation of the mitotic inhibitor Wee1. Cell 122 407-20 PubMed GONUTS page

[PMID:23314252-22] 22.0 ^22.1 Lyons, NA et al. (2013) Sequential primed kinases create a damage-responsive phosphodegron on Eco1. Nat. Struct. Mol. Biol. 20 194-201 PubMed GONUTS page

[PMID:19699692-23] Zhang, Y et al. (2009) Regulation of repair choice: Cdk1 suppresses recruitment of end joining factors at DNA breaks. DNA Repair (Amst.) 8 1235-41 PubMed GONUTS page

[PMID:22689984-24] 24.0 ^24.1 ^24.2 ^24.3 ^24.4 Chymkowitch, P et al. (2012) Cdc28 kinase activity regulates the basal transcription machinery at a subset of genes. Proc. Natl. Acad. Sci. U.S.A. 109 10450-5 PubMed GONUTS page

[PMID:12081645-25] 25.0 ^25.1 Purnapatre, K et al. (2002) The CLN3/SWI6/CLN2 pathway and SNF1 act sequentially to regulate meiotic initiation in Saccharomyces cerevisiae. Genes Cells 7 675-91 PubMed GONUTS page

[PMID:16814718-26] 26.0 ^26.1 Henderson, KA et al. (2006) Cyclin-dependent kinase directly regulates initiation of meiotic recombination. Cell 125 1321-32 PubMed GONUTS page

[PMID:2680756-27] Shuster, EO & Byers, B (1989) Pachytene arrest and other meiotic effects of the start mutations in Saccharomyces cerevisiae. Genetics 123 29-43 PubMed GONUTS page

[PMID:2165600-28] Reed, SI & Wittenberg, C (1990) Mitotic role for the Cdc28 protein kinase of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 87 5697-701 PubMed GONUTS page

[PMID:7002718-29] Reed, SI (1980) The selection of S. cerevisiae mutants defective in the start event of cell division. Genetics 95 561-77 PubMed GONUTS page

[PMID:10074450-30] Jaspersen, SL et al. (1999) Inhibitory phosphorylation of the APC regulator Hct1 is controlled by the kinase Cdc28 and the phosphatase Cdc14. Curr. Biol. 9 227-36 PubMed GONUTS page

[PMID:1652372-31] 31.0 ^31.1 Moll, T et al. (1991) The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SWI5. Cell 66 743-58 PubMed GONUTS page

[PMID:14993267-32] 32.0 ^32.1 Geymonat, M et al. (2004) Clb6/Cdc28 and Cdc14 regulate phosphorylation status and cellular localization of Swi6. Mol. Cell. Biol. 24 2277-85 PubMed GONUTS page

[PMID:21549314-33] Lyons, NA & Morgan, DO (2011) Cdk1-dependent destruction of Eco1 prevents cohesion establishment after S phase. Mol. Cell 42 378-89 PubMed GONUTS page

[PMID:20855529-34] 34.0 ^34.1 Chaves, S et al. (2010) Cks1, Cdk1, and the 19S proteasome collaborate to regulate gene induction-dependent nucleosome eviction in yeast. Mol. Cell. Biol. 30 5284-94 PubMed GONUTS page

[PMID:19188495-35] Ydenberg, CA & Rose, MD (2009) Antagonistic regulation of Fus2p nuclear localization by pheromone signaling and the cell cycle. J. Cell Biol. 184 409-22 PubMed GONUTS page

[PMID:20702586-36] Brickner, DG & Brickner, JH (2010) Cdk phosphorylation of a nucleoporin controls localization of active genes through the cell cycle. Mol. Biol. Cell 21 3421-32 PubMed GONUTS page

[PMID:22767578-37] McCusker, D et al. (2012) Cdk1-dependent control of membrane-trafficking dynamics. Mol. Biol. Cell 23 3336-47 PubMed GONUTS page

[PMID:19150427-38] 38.0 ^38.1 Kurat, CF et al. (2009) Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 in yeast links lipolysis to cell-cycle progression. Mol. Cell 33 53-63 PubMed GONUTS page

[PMID:16688214-39] 39.0 ^39.1 Crasta, K et al. (2006) Cdk1 regulates centrosome separation by restraining proteolysis of microtubule-associated proteins. EMBO J. 25 2551-63 PubMed GONUTS page

[PMID:8887667-40] Lim, HH et al. (1996) Spindle pole body separation in Saccharomyces cerevisiae requires dephosphorylation of the tyrosine 19 residue of Cdc28. Mol. Cell. Biol. 16 6385-97 PubMed GONUTS page

[PMID:12783856-41] Benjamin, KR et al. (2003) Control of landmark events in meiosis by the CDK Cdc28 and the meiosis-specific kinase Ime2. Genes Dev. 17 1524-39 PubMed GONUTS page

[PMID:4580573-42] Hartwell, LH (1973) Three additional genes required for deoxyribonucleic acid synthesis in Saccharomyces cerevisiae. J. Bacteriol. 115 966-74 PubMed GONUTS page

[PMID:14747467-43] 43.0 ^43.1 Kesti, T et al. (2004) Cell cycle-dependent phosphorylation of the DNA polymerase epsilon subunit, Dpb2, by the Cdc28 cyclin-dependent protein kinase. J. Biol. Chem. 279 14245-55 PubMed GONUTS page

[PMID:9891070-44] Edgington, NP et al. (1999) Control of Saccharomyces cerevisiae filamentous growth by cyclin-dependent kinase Cdc28. Mol. Cell. Biol. 19 1369-80 PubMed GONUTS page

[PMID:15496928-45] Ira, G et al. (2004) DNA end resection, homologous recombination and DNA damage checkpoint activation require CDK1. Nature 431 1011-7 PubMed GONUTS page

[PMID:17417630-46] 46.0 ^46.1 McCusker, D et al. (2007) Cdk1 coordinates cell-surface growth with the cell cycle. Nat. Cell Biol. 9 506-15 PubMed GONUTS page

[PMID:20825495-47] Zhu, Z et al. (2010) Cyclin-dependent kinase promotes formation of the synaptonemal complex in yeast meiosis. Genes Cells 15 1036-50 PubMed GONUTS page

[PMID:12554645-48] Maekawa, H et al. (2003) Yeast Cdk1 translocates to the plus end of cytoplasmic microtubules to regulate bud cortex interactions. EMBO J. 22 438-49 PubMed GONUTS page

[PMID:17560371-49] Vergés, E et al. (2007) Cyclin Cln3 is retained at the ER and released by the J chaperone Ydj1 in late G1 to trigger cell cycle entry. Mol. Cell 26 649-62 PubMed GONUTS page

[PMID:3312233-50] Wittenberg, C et al. (1987) Subcellular localization of a protein kinase required for cell cycle initiation in Saccharomyces cerevisiae: evidence for an association between the CDC28 gene product and the insoluble cytoplasmic matrix. J. Cell Biol. 105 1527-38 PubMed GONUTS page

[PMID:14685274-51] Wang, H et al. (2004) Recruitment of Cdc28 by Whi3 restricts nuclear accumulation of the G1 cyclin-Cdk complex to late G1. EMBO J. 23 180-90 PubMed GONUTS page

[PMID:2142620-52] 52.0 ^52.1 Wittenberg, C et al. (1990) G1-specific cyclins of S. cerevisiae: cell cycle periodicity, regulation by mating pheromone, and association with the p34CDC28 protein kinase. Cell 62 225-37 PubMed GONUTS page

[PMID:24319056-53] 53.0 ^53.1 Kao, L et al. (2014) Global analysis of cdc14 dephosphorylation sites reveals essential regulatory role in mitosis and cytokinesis. Mol. Cell Proteomics 13 594-605 PubMed GONUTS page

[PMID:20150422-54] Manfrini, N et al. (2010) Processing of meiotic DNA double strand breaks requires cyclin-dependent kinase and multiple nucleases. J. Biol. Chem. 285 11628-37 PubMed GONUTS page

[PMID:1849458-55] Ghiara, JB et al. (1991) A cyclin B homolog in S. cerevisiae: chronic activation of the Cdc28 protein kinase by cyclin prevents exit from mitosis. Cell 65 163-74 PubMed GONUTS page

[PMID:21873635-56] 56.0 ^56.1 ^56.2 ^56.3 ^56.4 ^56.5 ^56.6 ^56.7 ^56.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]

[18]

[19]

[20]

[21]

[22]

[23]

[24]

[25]

[26]

[27]

[28]

[29]

[30]

[31]

[32]

[33]

[34]

[35]

[36]

[37]

[38]

[39]

[40]

[41]

[42]

[43]

[44]

[45]

[46]

[47]

[48]

[49]

[50]

[51]

[52]

[53]

[54]

[55]

[56]

YEAST:CDK1

Contents

Annotations

Notes

References

7

a

c

d

e

f

g

h

k

m

n

o

p

r

s

t

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools