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P23572

- CDK1_DROME

UniProt

P23572 - CDK1_DROME

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Protein

Cyclin-dependent kinase 1

Gene

cdc2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

Enzyme regulationi

Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-161 activates it.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331ATPPROSITE-ProRule annotation
Active sitei128 – 1281Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 189ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: FlyBase
  3. protein kinase activity Source: FlyBase
  4. protein serine/threonine kinase activity Source: FlyBase
  5. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. asymmetric neuroblast division Source: FlyBase
  2. cellular process Source: FlyBase
  3. cellular response to DNA damage stimulus Source: FlyBase
  4. G1/S transition of mitotic cell cycle Source: FlyBase
  5. G2/M transition of mitotic cell cycle Source: FlyBase
  6. germarium-derived cystoblast division Source: FlyBase
  7. male meiosis Source: FlyBase
  8. male meiosis I Source: FlyBase
  9. meiotic G2/MI transition Source: FlyBase
  10. mitotic cell cycle Source: FlyBase
  11. mitotic G2/M transition checkpoint Source: FlyBase
  12. mitotic G2 DNA damage checkpoint Source: FlyBase
  13. mitotic nuclear division Source: UniProtKB-KW
  14. neurogenesis Source: FlyBase
  15. protein phosphorylation Source: FlyBase
  16. regulation of protein localization Source: FlyBase
  17. spermatogenesis Source: FlyBase
  18. spermatogonial cell division Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_180285. G1/S-Specific Transcription.
REACT_184285. Condensation of Prometaphase Chromosomes.
REACT_184304. Nuclear Pore Complex (NPC) Disassembly.
REACT_184356. MASTL Facilitates Mitotic Progression.
REACT_209388. E2F mediated regulation of DNA replication.
REACT_219169. Depolymerisation of the Nuclear Lamina.
REACT_220914. ERK1 activation.
REACT_222733. E2F-enabled inhibition of pre-replication complex formation.
REACT_224351. Regulation of APC/C activators between G1/S and early anaphase.
REACT_225636. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_33104. APC/C:Cdc20 mediated degradation of Cyclin B.
SignaLinkiP23572.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 1 (EC:2.7.11.22, EC:2.7.11.23)
Short name:
CDK1
Alternative name(s):
Cell division control protein 2 homolog
Cell division protein kinase 1
p34 protein kinase
Gene namesi
Name:cdc2
Synonyms:cdk1
ORF Names:CG5363
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0004106. cdc2.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. microtubule associated complex Source: FlyBase
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi43 – 431G → D in cdc2-E1-4; larval-pupal lethal with some adult escapers. 1 Publication
Mutagenesisi145 – 1451A → V in cdc2-216A; larval-pupal lethal. 2 Publications
Mutagenesisi148 – 1481G → R in cdc2-D57; embryonic or larval-pupal lethal. 2 Publications
Mutagenesisi176 – 1761L → Q in cdc2-E10; larval-pupal lethal. 1 Publication
Mutagenesisi196 – 1961E → K in cdc2-E1-24; larval-pupal lethal with some adult escapers. 2 Publications
Mutagenesisi206 – 2061G → D in cdc2-E1-23; larval-pupal lethal. 2 Publications
Mutagenesisi242 – 2421P → S in cdc2-E1-9; larval-pupal lethal. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297Cyclin-dependent kinase 1PRO_0000085743Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Phosphothreonine1 Publication
Modified residuei15 – 151Phosphotyrosine1 Publication
Modified residuei160 – 1601Phosphotyrosine1 Publication
Modified residuei161 – 1611Phosphothreonine; by CAKSequence Analysis

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP23572.
PRIDEiP23572.

Expressioni

Developmental stagei

Expressed both maternally and zygotically.2 Publications

Gene expression databases

BgeeiP23572.
ExpressionAtlasiP23572. differential.

Interactioni

Subunit structurei

Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin.

Binary interactionsi

WithEntry#Exp.IntActNotes
Cks85AQ9VHN14EBI-108689,EBI-122930
CycB3Q9I7I02EBI-108689,EBI-150964
CycCP250084EBI-108689,EBI-195485
CycEP547336EBI-108689,EBI-203549
CycKQ961D14EBI-108689,EBI-130995
tweQ030194EBI-108689,EBI-138996

Protein-protein interaction databases

BioGridi60495. 38 interactions.
DIPiDIP-649N.
IntActiP23572. 25 interactions.
MINTiMINT-292976.

Structurei

3D structure databases

ProteinModelPortaliP23572.
SMRiP23572. Positions 1-287.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 287284Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119154.
InParanoidiP23572.
KOiK02087.
OMAiDILEHPY.
OrthoDBiEOG7966H8.
PhylomeDBiP23572.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23572-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEDFEKIEKI GEGTYGVVYK GRNRLTGQIV AMKKIRLESD DEGVPSTAIR
60 70 80 90 100
EISLLKELKH ENIVCLEDVL MEENRIYLIF EFLSMDLKKY MDSLPVDKHM
110 120 130 140 150
ESELVRSYLY QITSAILFCH RRRVLHRDLK PQNLLIDKSG LIKVADFGLG
160 170 180 190 200
RSFGIPVRIY THEIVTLWYR APEVLLGSPR YSCPVDIWSI GCIFAEMATR
210 220 230 240 250
KPLFQGDSEI DQLFRMFRIL KTPTEDIWPG VTSLPDYKNT FPCWSTNQLT
260 270 280 290
NQLKNLDANG IDLIQKMLIY DPVHRISAKD ILEHPYFNGF QSGLVRN
Length:297
Mass (Da):34,439
Last modified:November 1, 1991 - v1
Checksum:i952CF136D8AB64C0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS12009.
RefSeqiNP_476797.1. NM_057449.4.
UniGeneiDm.3187.

Genome annotation databases

EnsemblMetazoaiFBtr0080051; FBpp0079641; FBgn0004106.
GeneIDi34411.
KEGGidme:Dmel_CG5363.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S12009.
RefSeqi NP_476797.1. NM_057449.4.
UniGenei Dm.3187.

3D structure databases

ProteinModelPortali P23572.
SMRi P23572. Positions 1-287.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 60495. 38 interactions.
DIPi DIP-649N.
IntActi P23572. 25 interactions.
MINTi MINT-292976.

Proteomic databases

PaxDbi P23572.
PRIDEi P23572.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0080051 ; FBpp0079641 ; FBgn0004106 .
GeneIDi 34411.
KEGGi dme:Dmel_CG5363.

Organism-specific databases

CTDi 34411.
FlyBasei FBgn0004106. cdc2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119154.
InParanoidi P23572.
KOi K02087.
OMAi DILEHPY.
OrthoDBi EOG7966H8.
PhylomeDBi P23572.

Enzyme and pathway databases

Reactomei REACT_180285. G1/S-Specific Transcription.
REACT_184285. Condensation of Prometaphase Chromosomes.
REACT_184304. Nuclear Pore Complex (NPC) Disassembly.
REACT_184356. MASTL Facilitates Mitotic Progression.
REACT_209388. E2F mediated regulation of DNA replication.
REACT_219169. Depolymerisation of the Nuclear Lamina.
REACT_220914. ERK1 activation.
REACT_222733. E2F-enabled inhibition of pre-replication complex formation.
REACT_224351. Regulation of APC/C activators between G1/S and early anaphase.
REACT_225636. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_33104. APC/C:Cdc20 mediated degradation of Cyclin B.
SignaLinki P23572.

Miscellaneous databases

GenomeRNAii 34411.
NextBioi 788369.
PROi P23572.

Gene expression databases

Bgeei P23572.
ExpressionAtlasi P23572. differential.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  7. 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.

Entry informationi

Entry nameiCDK1_DROME
AccessioniPrimary (citable) accession number: P23572
Secondary accession number(s): A0ANT1
, Q86FT5, Q86FT6, Q86FT7, Q86FT8, Q86FT9, Q9TX68, Q9TX69, Q9TX70, Q9TX71, Q9TX72, Q9TX73, Q9TX74, Q9VKX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: October 29, 2014
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3