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P23572 (CDK1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processCell cycle
Cell division
Mitosis
   Cellular componentNucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/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

cellular process

Inferred from mutant phenotype PubMed 14764878. Source: FlyBase

cellular response to DNA damage stimulus

Inferred from mutant phenotype PubMed 19543366. Source: FlyBase

germarium-derived cystoblast division

Inferred from mutant phenotype PubMed 16107480. Source: FlyBase

male meiosis

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

mitotic G2 DNA damage checkpoint

Inferred from mutant phenotype PubMed 24214341. Source: FlyBase

mitotic G2/M transition checkpoint

Inferred from mutant phenotype PubMed 24214341. Source: FlyBase

mitotic cell cycle

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

neurogenesis

Inferred from mutant phenotype PubMed 21549331. Source: FlyBase

protein phosphorylation

Inferred from direct assay PubMed 8675008. Source: FlyBase

regulation of protein localization

Inferred from mutant phenotype PubMed 12105185. Source: FlyBase

spermatogenesis

Traceable author statement PubMed 9813190. Source: FlyBase

spermatogonial cell division

Inferred from mutant phenotype PubMed 16107480. Source: FlyBase

   Cellular_componentmicrotubule associated complex

Inferred from direct assay PubMed 18433294. Source: FlyBase

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cyclin-dependent protein serine/threonine kinase activity

Inferred from genetic interaction Ref.1. Source: FlyBase

protein binding

Inferred from physical interaction PubMed 9851980. Source: UniProtKB

protein kinase activity

Inferred from direct assay PubMed 24214341. Source: FlyBase

protein serine/threonine kinase activity

Non-traceable author statement PubMed 10908587. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Cyclin-dependent kinase 1
PRO_0000085743

Regions

Domain4 – 287284Protein kinase
Nucleotide binding10 – 189ATP By similarity

Sites

Active site1281Proton acceptor By similarity
Binding site331ATP By similarity

Amino acid modifications

Modified residue141Phosphothreonine Ref.9
Modified residue151Phosphotyrosine Ref.9
Modified residue1601Phosphotyrosine Ref.9
Modified residue1611Phosphothreonine; by CAK Potential

Experimental info

Mutagenesis431G → D in cdc2-E1-4; larval-pupal lethal with some adult escapers. Ref.8
Mutagenesis1451A → V in cdc2-216A; larval-pupal lethal. Ref.3 Ref.8
Mutagenesis1481G → R in cdc2-D57; embryonic or larval-pupal lethal. Ref.3 Ref.8
Mutagenesis1761L → Q in cdc2-E10; larval-pupal lethal. Ref.8
Mutagenesis1961E → K in cdc2-E1-24; larval-pupal lethal with some adult escapers. Ref.3 Ref.8
Mutagenesis2061G → D in cdc2-E1-23; larval-pupal lethal. Ref.3 Ref.8
Mutagenesis2421P → S in cdc2-E1-9; larval-pupal lethal. Ref.3 Ref.8

Sequences

Sequence LengthMass (Da)Tools
P23572 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 952CF136D8AB64C0

FASTA29734,439
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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.
PIRS12009.
RefSeqNP_476797.1. NM_057449.4.
UniGeneDm.3187.

3D structure databases

ProteinModelPortalP23572.
SMRP23572. Positions 1-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60495. 38 interactions.
DIPDIP-649N.
IntActP23572. 25 interactions.
MINTMINT-292976.

Proteomic databases

PaxDbP23572.
PRIDEP23572.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080051; FBpp0079641; FBgn0004106.
GeneID34411.
KEGGdme:Dmel_CG5363.

Organism-specific databases

CTD34411.
FlyBaseFBgn0004106. cdc2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00720000108415.
InParanoidP23572.
KOK02087.
OMADILEHPY.
OrthoDBEOG7966H8.
PhylomeDBP23572.

Enzyme and pathway databases

SignaLinkP23572.

Gene expression databases

BgeeP23572.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi34411.
NextBio788369.
PROP23572.

Entry information

Entry nameCDK1_DROME
AccessionPrimary (citable) accession number: P23572
Secondary accession number(s): A0ANT1 expand/collapse secondary AC list , 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: July 9, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase