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Protein

Cyclin-dependent kinase 1

Gene

CDC28

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.14 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371ATPPROSITE-ProRule annotation
Active sitei133 – 1331Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 219ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: CGD

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. G1/S transition of mitotic cell cycle Source: CGD
  3. hyphal growth Source: CGD
  4. mitotic nuclear division Source: UniProtKB-KW
  5. protein phosphorylation Source: CGD
  6. regulation of cell cycle Source: CGD
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

BRENDAi2.7.11.22. 1096.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 1 (EC:2.7.11.22)
Short name:
CDK1
Alternative name(s):
Cell division control protein 28
Cell division protein kinase 2
Gene namesi
Name:CDC28
Synonyms:CDK1
ORF Names:CaO19.11337, CaO19.3856
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000000559 Componenti: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0002090. CDC28.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317Cyclin-dependent kinase 1PRO_0000085721Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphothreonineBy similarity
Modified residuei18 – 181Phosphotyrosine; by SWE12 Publications
Modified residuei166 – 1661Phosphothreonine; by CAKBy similarity

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP43063.

Expressioni

Inductioni

Expression is increased during exponential growth and repressed by the antifungal drug plagiochin E (PLE).2 Publications

Interactioni

Subunit structurei

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 HSP90.6 Publications

Protein-protein interaction databases

BioGridi1227932. 3 interactions.
DIPiDIP-497N.
IntActiP43063. 3 interactions.
MINTiMINT-7295535.
STRINGi5476.CAL0002090.

Structurei

3D structure databases

ProteinModelPortaliP43063.
SMRiP43063. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 292286Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
InParanoidiP43063.
KOiK04563.
OrthoDBiEOG7K3TWD.

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.

P43063-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVELSDYQRQ EKVGEGTYGV VYKALDTKHN NRVVALKKIR LESEDEGVPS
60 70 80 90 100
TAIREISLLK EMKDDNIVRL YDIIHSDSHK LYLVFEFLDL DLKKYMESIP
110 120 130 140 150
QGVGLGANMI KRFMNQLIRG IKHCHSHRVL HRDLKPQNLL IDKEGNLKLA
160 170 180 190 200
DFGLARAFGV PLRAYTHEVV TLWYRAPEIL LGGKQYSTGV DMWSVGCIFA
210 220 230 240 250
EMCNRKPLFP GDSEIDEIFR IFRILGTPNE EIWPDVNYLP DFKSSFPQWK
260 270 280 290 300
KKPLSEAVPS LDANGIDLLD QMLVYDPSRR ISAKRALIHP YFNDNDDRDH
310
NNYNEDNIGI DKHQNMQ
Length:317
Mass (Da):36,647
Last modified:November 1, 1995 - v1
Checksum:i2B91EABE5E5C028B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80034 Genomic DNA. Translation: CAA56338.1.
U40405 mRNA. Translation: AAC49450.1.
AACQ01000125 Genomic DNA. Translation: EAK94372.1.
AACQ01000124 Genomic DNA. Translation: EAK94417.1.
PIRiJC4827.
RefSeqiXP_713486.1. XM_708393.1.
XP_713525.1. XM_708432.1.

Genome annotation databases

GeneIDi3644820.
3644838.
KEGGical:CaO19.11337.
cal:CaO19.3856.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80034 Genomic DNA. Translation: CAA56338.1.
U40405 mRNA. Translation: AAC49450.1.
AACQ01000125 Genomic DNA. Translation: EAK94372.1.
AACQ01000124 Genomic DNA. Translation: EAK94417.1.
PIRiJC4827.
RefSeqiXP_713486.1. XM_708393.1.
XP_713525.1. XM_708432.1.

3D structure databases

ProteinModelPortaliP43063.
SMRiP43063. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1227932. 3 interactions.
DIPiDIP-497N.
IntActiP43063. 3 interactions.
MINTiMINT-7295535.
STRINGi5476.CAL0002090.

Proteomic databases

PRIDEiP43063.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3644820.
3644838.
KEGGical:CaO19.11337.
cal:CaO19.3856.

Organism-specific databases

CGDiCAL0002090. CDC28.

Phylogenomic databases

eggNOGiCOG0515.
InParanoidiP43063.
KOiK04563.
OrthoDBiEOG7K3TWD.

Enzyme and pathway databases

BRENDAi2.7.11.22. 1096.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCDK1_CANAL
AccessioniPrimary (citable) accession number: P43063
Secondary accession number(s): Q59V96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 1, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.