P23572 (CDK1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclin-dependent kinase 1
Short name=CDK1
EC=2.7.11.22
EC=2.7.11.23

Alternative name(s):
Cell division control protein 2 homolog
Cell division protein kinase 1
p34 protein kinase

Gene names

Name:	cdc2
Synonyms:	cdk1
ORF Names:	CG5363

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a key role in the control of the eukaryotic cell cycle. It is required in higher cells for entry into S-phase and mitosis. p34 is a component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II. Ref.2
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
Enzyme regulation	Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-161 activates it By similarity.
Subunit structure	Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin.
Subcellular location	Nucleus By similarity.
Developmental stage	Expressed both maternally and zygotically. Ref.2 Ref.8
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from genetic interaction Ref.1. Source: FlyBase G2/M transition of mitotic cell cycle Inferred from mutant phenotype Ref.3. Source: FlyBase asymmetric neuroblast division Inferred from mutant phenotype PubMed 11234018. Source: FlyBase germarium-derived cystoblast division Inferred from mutant phenotype PubMed 16107480. Source: FlyBase male meiosis I Traceable author statement PubMed 9813190. Source: FlyBase meiotic G2/MI transition Traceable author statement PubMed 9813190. Source: FlyBase mitosis Inferred from electronic annotation. Source: UniProtKB-KW regulation of protein localization Inferred from mutant phenotype PubMed 12105185. Source: FlyBase response to DNA damage stimulus Inferred from mutant phenotype PubMed 19543366. Source: FlyBase spermatogonial cell division Inferred from mutant phenotype PubMed 16107480. Source: FlyBase
Cellular_component	microtubule associated complex Inferred from direct assay PubMed 18433294. Source: FlyBase nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from electronic annotation. Source: EC cyclin-dependent protein serine/threonine kinase activity Inferred from sequence or structural similarity Ref.1. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cks85A	Q9VHN1	4	EBI-108689,EBI-122930
CycB3	Q9I7I0	2	EBI-108689,EBI-150964
CycC	P25008	4	EBI-108689,EBI-195485
CycE	P54733	4	EBI-108689,EBI-203549
CycK	Q961D1	4	EBI-108689,EBI-130995
twe	Q03019	4	EBI-108689,EBI-138996

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 297	297	Cyclin-dependent kinase 1		PRO_0000085743
Regions
	Domain	4 – 287	284	Protein kinase
	Nucleotide binding	10 – 18	9	ATP By similarity
Sites
	Active site	128	1	Proton acceptor By similarity
	Binding site	33	1	ATP By similarity
Amino acid modifications
	Modified residue	14	1	Phosphothreonine Ref.9
	Modified residue	15	1	Phosphotyrosine Ref.9
	Modified residue	160	1	Phosphotyrosine Ref.9
	Modified residue	161	1	Phosphothreonine; by CAK Potential
Experimental info
	Mutagenesis	43	1	G → D in cdc2-E1-4; larval-pupal lethal with some adult escapers. Ref.8
	Mutagenesis	145	1	A → V in cdc2-216A; larval-pupal lethal. Ref.3 Ref.8
	Mutagenesis	148	1	G → R in cdc2-D57; embryonic or larval-pupal lethal. Ref.3 Ref.8
	Mutagenesis	176	1	L → Q in cdc2-E10; larval-pupal lethal. Ref.8
	Mutagenesis	196	1	E → K in cdc2-E1-24; larval-pupal lethal with some adult escapers. Ref.3 Ref.8
	Mutagenesis	206	1	G → D in cdc2-E1-23; larval-pupal lethal. Ref.3 Ref.8
	Mutagenesis	242	1	P → S in cdc2-E1-9; larval-pupal lethal. Ref.3 Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P23572 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 952CF136D8AB64C0	FASTA	297	34,439
	10 20 30 40 50 60 MEDFEKIEKI GEGTYGVVYK GRNRLTGQIV AMKKIRLESD DEGVPSTAIR EISLLKELKH 70 80 90 100 110 120 ENIVCLEDVL MEENRIYLIF EFLSMDLKKY MDSLPVDKHM ESELVRSYLY QITSAILFCH 130 140 150 160 170 180 RRRVLHRDLK PQNLLIDKSG LIKVADFGLG RSFGIPVRIY THEIVTLWYR APEVLLGSPR 190 200 210 220 230 240 YSCPVDIWSI GCIFAEMATR KPLFQGDSEI DQLFRMFRIL KTPTEDIWPG VTSLPDYKNT 250 260 270 280 290 FPCWSTNQLT NQLKNLDANG IDLIQKMLIY DPVHRISAKD ILEHPYFNGF QSGLVRN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Drosophila cdc2 homologs: a functional homolog is coexpressed with a cognate variant." Lehner C.F., O'Farrell P.H. EMBO J. 9:3573-3581(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Complementation of fission yeast cdc2ts and cdc25ts mutants identifies two cell cycle genes from Drosophila: a cdc2 homologue and string." Jimenez J., Alphey L., Nurse P., Glover D.M. EMBO J. 9:3565-3571(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
[3]	"Genetic analysis of the Drosophila cdc2 homolog." Stern B., Ried G., Clegg N.J., Grigliatti T.A., Lehner C.F. Development 117:219-232(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], MUTAGENESIS OF ALA-145; GLY-148; GLU-196; GLY-206 AND PRO-242.
[4]	"Widespread adaptive evolution of Drosophila genes with sex-biased expression." Proeschel M., Zhang Z., Parsch J. Genetics 174:893-900(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL229, ZBMEL377, ZBMEL384, ZBMEL398, ZBMEL82, ZBMEL84 and ZBMEL95.
[5]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[6]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[7]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley.
[8]	"A developmental and molecular analysis of cdc2 mutations in Drosophila melanogaster." Clegg N.J., Whitehead I.P., Williams J.A., Spiegelman G.B., Grigliatti T.A. Genome 36:676-685(1993) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF GLY-43; ALA-145; GLY-148; LEU-176; GLU-196; GLY-206 AND PRO-242, DEVELOPMENTAL STAGE.
[9]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; TYR-15; TYR-160 AND THR-161, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X57485 mRNA. Translation: CAA40723.1. X57496 mRNA. Translation: CAA40733.1. S66801 Genomic DNA. Translation: AAP13986.1. S66804 Genomic DNA. Translation: AAP13987.1. S66805 Genomic DNA. Translation: AAP13988.1. S66807 Genomic DNA. Translation: AAP13989.1. S66810 Genomic DNA. Translation: AAP13990.1. AM294319 Genomic DNA. Translation: CAL26249.1. AM294320 Genomic DNA. Translation: CAL26250.1. AM294321 Genomic DNA. Translation: CAL26251.1. AM294322 Genomic DNA. Translation: CAL26252.1. AM294323 Genomic DNA. Translation: CAL26253.1. AM294324 Genomic DNA. Translation: CAL26254.1. AM294325 Genomic DNA. Translation: CAL26255.1. AM294326 Genomic DNA. Translation: CAL26256.1. AM294327 Genomic DNA. Translation: CAL26257.1. AM294328 Genomic DNA. Translation: CAL26258.1. AM294329 Genomic DNA. Translation: CAL26259.1. AE014134 Genomic DNA. Translation: AAF52932.1. AY061450 mRNA. Translation: AAL28998.1.
PIR	S12009.
RefSeq	NP_476797.1. NM_057449.4.
UniGene	Dm.3187.
3D structure databases
ProteinModelPortal	P23572.
SMR	P23572. Positions 1-287.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-649N.
IntAct	P23572. 20 interactions.
MINT	MINT-292976.
Proteomic databases
PaxDb	P23572.
PRIDE	P23572.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0080051; FBpp0079641; FBgn0004106.
GeneID	34411.
KEGG	dme:Dmel_CG5363.
Organism-specific databases
CTD	34411.
FlyBase	FBgn0004106. cdc2.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00690000101791.
InParanoid	P23572.
KO	K02087.
OMA	DILEHPY.
OrthoDB	EOG4QJQ3W.
PhylomeDB	P23572.
Gene expression databases
Bgee	P23572.
GermOnline	CG5363. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	34411.
NextBio	788369.

Entry information

Entry name

CDK1_DROME

Accession

Primary (citable) accession number: P23572
Secondary accession number(s): A0ANT1 , Q86FT5, Q86FT6, Q86FT7, Q86FT8, Q86FT9, Q9TX68, Q9TX69, Q9TX70, Q9TX71, Q9TX72, Q9TX73, Q9TX74, Q9VKX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	May 1, 2013
This is version 145 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project