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P43063 (CDK1_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 102. 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·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
Alternative name(s):
Cell division control protein 28
Cell division protein kinase 2
Gene names
Name:CDC28
Synonyms:CDK1
ORF Names:CaO19.11337, CaO19.3856
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cyclin-dependent kinase essential for the completion of the start, the controlling event, in the cell cycle. Plays a role in the expression of morphology-related transcription factors, and especially hyphae-specific genes. Binds distinct cyclin subunits as cells progress through the division cycle or flamentous growth. The CDC28-CLB2 complex regulates cytokinesis partly by phosphorylating the actomyosin ring component IQG1. The CDC28-CLN3 complex phosphorylates SLA1 which regulates cortical actin patch dynamics. The CDC28-CCN1 complex phosphorylates CDC11 and SEC2 upon induction of filamentous growth. The CDC28-HGC1 complex also phosphorylates SEC2 and maintains CDC11 phosphorylation throughout hyphal growth. Moreover, the CDC28-HGC1 complex phosphorylates and prevents RGA2 from localizing to hyphal tips, leading to localized CDC42 activation for hyphal extension. Finaly CDC28-HGC1 phosphorylation of EFG1 represses cell separation genes during hyphal growth. Additional substrates for CDC28 are RFA2 in G1-phase; MOB2, which is required for the maintenance of polarisome components and for inhibition of cell separation in hyphae; and GIN4 to regulate its association to SEP7 and subsequent septin ring assembly. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Phosphorylation at Thr-17 or Tyr-18 inactivates the enzyme, while phosphorylation at Thr-166 activates it By similarity.

Subunit structure

Forms several complexes with cyclins CCN1, CLB2, CLN3, and HGC1. The CDC28-CCN1 complex associates with septin CDC11 upon hyphal induction. Interacts with IQG1, RFA2, and HSP90. Ref.5 Ref.9 Ref.11 Ref.17 Ref.18 Ref.19

Induction

Expression is increased during exponential growth and repressed by the antifungal drug plagiochin E (PLE). Ref.10 Ref.13

Post-translational modification

Phosphorylated at Tyr-18 by SWE1 in a cell cycle-dependent manner. Yeast-form and hyphal cells display similar dynamics of phosphorylation and dephosphorylation of Tyr-18. Tyr-18 phosphorylation leads to inhibition of CDC28 kinase activity. Ref.4 Ref.6

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
   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 direct assay Ref.2. Source: CGD

G2/M transition of mitotic cell cycle

Inferred from genetic interaction Ref.2. Source: CGD

cellular amino acid biosynthetic process

Inferred from mutant phenotype PubMed 16215176. Source: CGD

cellular response to N-acetyl-D-glucosamine

Inferred from mutant phenotype PubMed 22406769. Source: CGD

cellular response to drug

Inferred from mutant phenotype PubMed 17604452PubMed 20140194. Source: CGD

cellular response to neutral pH

Inferred from mutant phenotype PubMed 18321992. Source: CGD

filamentous growth

Inferred from mutant phenotype PubMed 18321992PubMed 22365851PubMed 22406769. Source: CGD

filamentous growth of a population of unicellular organisms

Inferred from mutant phenotype PubMed 18321992. Source: CGD

filamentous growth of a population of unicellular organisms in response to biotic stimulus

Inferred from mutant phenotype PubMed 18321992. Source: CGD

filamentous growth of a population of unicellular organisms in response to chemical stimulus

Inferred from mutant phenotype PubMed 22365851PubMed 22406769. Source: CGD

filamentous growth of a population of unicellular organisms in response to neutral pH

Inferred from mutant phenotype PubMed 18321992. Source: CGD

hyphal growth

Inferred from mutant phenotype Ref.7. Source: CGD

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

phosphate-containing compound metabolic process

Inferred from genetic interaction PubMed 10923026. Source: CGD

positive regulation of filamentous growth of a population of unicellular organisms in response to chemical stimulus

Inferred from mutant phenotype PubMed 22406769. Source: CGD

positive regulation of protein kinase activity

Inferred from direct assay PubMed 12084729. Source: GOC

protein phosphorylation

Inferred from direct assay PubMed 12084729Ref.15Ref.16Ref.2. Source: CGD

regulation of cell cycle

Inferred from genetic interaction Ref.1. Source: CGD

regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from genetic interaction PubMed 12084729. Source: CGD

single-species biofilm formation on inanimate substrate

Inferred from mutant phenotype PubMed 18321992. Source: CGD

   Cellular_componentplasma membrane

Inferred from direct assay PubMed 19824013. Source: CGD

protein kinase CK2 complex

Inferred from sequence or structural similarity PubMed 15813744. Source: CGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cyclin-dependent protein kinase activating kinase activity

Inferred from direct assay PubMed 12084729. Source: CGD

cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay Ref.2. Source: CGD

eukaryotic translation initiation factor 2alpha kinase activity

Inferred from mutant phenotype PubMed 16215176. Source: CGD

protein kinase activity

Inferred from sequence alignment PubMed 18321992. Source: CGD

protein serine/threonine kinase activity

Inferred from sequence or structural similarity PubMed 15813744. Source: CGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Cyclin-dependent kinase 1
PRO_0000085721

Regions

Domain7 – 292286Protein kinase
Nucleotide binding13 – 219ATP By similarity

Sites

Active site1331Proton acceptor By similarity
Binding site371ATP By similarity

Amino acid modifications

Modified residue171Phosphothreonine By similarity
Modified residue181Phosphotyrosine; by SWE1 Ref.4 Ref.6
Modified residue1661Phosphothreonine; by CAK By similarity

Sequences

Sequence LengthMass (Da)Tools
P43063 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 2B91EABE5E5C028B

FASTA31736,647
        10         20         30         40         50         60 
MVELSDYQRQ EKVGEGTYGV VYKALDTKHN NRVVALKKIR LESEDEGVPS TAIREISLLK 

        70         80         90        100        110        120 
EMKDDNIVRL YDIIHSDSHK LYLVFEFLDL DLKKYMESIP QGVGLGANMI KRFMNQLIRG 

       130        140        150        160        170        180 
IKHCHSHRVL HRDLKPQNLL IDKEGNLKLA DFGLARAFGV PLRAYTHEVV TLWYRAPEIL 

       190        200        210        220        230        240 
LGGKQYSTGV DMWSVGCIFA EMCNRKPLFP GDSEIDEIFR IFRILGTPNE EIWPDVNYLP 

       250        260        270        280        290        300 
DFKSSFPQWK KKPLSEAVPS LDANGIDLLD QMLVYDPSRR ISAKRALIHP YFNDNDDRDH 

       310 
NNYNEDNIGI DKHQNMQ 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and analysis of CDC28 and cyclin homologues from the human fungal pathogen Candida albicans."
Sherlock G., Bahman A.M., Mahal A., Shieh J.C., Ferreira M., Rosamond J.
Mol. Gen. Genet. 245:716-723(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SGY126.
[2]"Candida albicans CDK1 and CYB1: cDNA homologues of the cdc2/CDC28 and cdc13/CLB1/CLB2 cell cycle control genes."
Damagnez V., Cottarel G.
Gene 172:137-141(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.
[4]"Hyphal elongation is regulated independently of cell cycle in Candida albicans."
Hazan I., Sepulveda-Becerra M., Liu H.
Mol. Biol. Cell 13:134-145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-18, FUNCTION.
[5]"Hgc1, a novel hypha-specific G1 cyclin-related protein regulates Candida albicans hyphal morphogenesis."
Zheng X., Wang Y., Wang Y.
EMBO J. 23:1845-1856(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HGC1.
[6]"Candida albicans protein kinase CaHsl1p regulates cell elongation and virulence."
Umeyama T., Kaneko A., Nagai Y., Hanaoka N., Tanabe K., Takano Y., Niimi M., Uehara Y.
Mol. Microbiol. 55:381-395(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-18 BY SWE1, FUNCTION.
[7]"Repression of CDC28 reduces the expression of the morphology-related transcription factors, Efg1p, Nrg1p, Rbf1p, Rim101p, Fkh2p and Tec1p and induces cell elongation in Candida albicans."
Umeyama T., Kaneko A., Niimi M., Uehara Y.
Yeast 23:537-552(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Phosphorylation of Rga2, a Cdc42 GAP, by CDK/Hgc1 is crucial for Candida albicans hyphal growth."
Zheng X.D., Lee R.T., Wang Y.M., Lin Q.S., Wang Y.
EMBO J. 26:3760-3769(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF RGA2.
[9]"Cyclin-dependent kinases control septin phosphorylation in Candida albicans hyphal development."
Sinha I., Wang Y.M., Philp R., Li C.R., Yap W.H., Wang Y.
Dev. Cell 13:421-432(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HGC1; CCN1 AND CDC11, FUNCTION IN PHOSPHORYLATION OF CDC11.
[10]"Defining Candida albicans stationary phase by cellular and DNA replication, gene expression and regulation."
Uppuluri P., Chaffin W.L.
Mol. Microbiol. 64:1572-1586(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[11]"The IQGAP Iqg1 is a regulatory target of CDK for cytokinesis in Candida albicans."
Li C.R., Wang Y.M., Wang Y.
EMBO J. 27:2998-3010(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLB2 AND IQG1, FUNCTION IN PHOSPHORYLATION OF IQG1.
[12]"Hyphal chain formation in Candida albicans: Cdc28-Hgc1 phosphorylation of Efg1 represses cell separation genes."
Wang A., Raniga P.P., Lane S., Lu Y., Liu H.
Mol. Cell. Biol. 29:4406-4416(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF EFG1.
[13]"Plagiochin E, an antifungal active macrocyclic bis(bibenzyl), induced apoptosis in Candida albicans through a metacaspase-dependent apoptotic pathway."
Wu X.Z., Chang W.Q., Cheng A.X., Sun L.M., Lou H.X.
Biochim. Biophys. Acta 1800:439-447(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[14]"Hyphal growth in Candida albicans requires the phosphorylation of Sec2 by the Cdc28-Ccn1/Hgc1 kinase."
Bishop A., Lane R., Beniston R., Chapa-y-Lazo B., Smythe C., Sudbery P.
EMBO J. 29:2930-2942(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF SEC2.
[15]"CDK-dependent phosphorylation of Mob2 is essential for hyphal development in Candida albicans."
Gutierrez-Escribano P., Gonzalez-Novo A., Suarez M.B., Li C.R., Wang Y., de Aldana C.R., Correa-Bordes J.
Mol. Biol. Cell 22:2458-2469(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF MOB2.
[16]"CDK regulates septin organization through cell-cycle-dependent phosphorylation of the Nim1-related kinase Gin4."
Li C.R., Yong J.Y., Wang Y.M., Wang Y.
J. Cell Sci. 125:2533-2543(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF GIN4.
[17]"Cdc28 provides a molecular link between Hsp90, morphogenesis, and cell cycle progression in Candida albicans."
Senn H., Shapiro R.S., Cowen L.E.
Mol. Biol. Cell 23:268-283(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HSP90.
[18]"Cdc28-Cln3 phosphorylation of Sla1 regulates actin patch dynamics in different modes of fungal growth."
Zeng G., Wang Y.M., Wang Y.
Mol. Biol. Cell 23:3485-3497(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLN3, FUNCTION IN PHOSPHORYLATION OF SLA1.
[19]"Rfa2 is specifically dephosphorylated by Pph3 in Candida albicans."
Wang H., Gao J., Wong A.H., Hu K., Li W., Wang Y., Sang J.
Biochem. J. 449:673-681(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RFA2, FUNCTION IN PHOSPHORYLATION OF RFA2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80034 Genomic DNA. Translation: CAA56338.1.
U40405 mRNA. Translation: AAC49450.1.
AACQ01000125 Genomic DNA. Translation: EAK94372.1.
AACQ01000124 Genomic DNA. Translation: EAK94417.1.
PIRJC4827.
RefSeqXP_713486.1. XM_708393.1.
XP_713525.1. XM_708432.1.

3D structure databases

ProteinModelPortalP43063.
SMRP43063. Positions 1-294.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1227932. 3 interactions.
DIPDIP-497N.
IntActP43063. 3 interactions.
MINTMINT-7295535.
STRING5476.CAL0002090.

Proteomic databases

PRIDEP43063.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3644820.
3644838.
KEGGcal:CaO19.11337.
cal:CaO19.3856.

Organism-specific databases

CGDCAL0002090. CDC28.

Phylogenomic databases

eggNOGCOG0515.
KOK04563.
OrthoDBEOG7K3TWD.

Enzyme and pathway databases

BRENDA2.7.11.22. 1096.

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...

Entry information

Entry nameCDK1_CANAL
AccessionPrimary (citable) accession number: P43063
Secondary accession number(s): Q59V96
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 14, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Candida albicans

Candida albicans: entries and gene names