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Protein

PHO85 cyclin-2

Gene

PCL2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

G1/S-specific cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Essential for the control of the cell cycle at the G1/S (start) transition. Together with cyclin PCL1, positively controls degradation of sphingoid long chain base kinase LCB4. The PCL2-PHO85 cyclin-CDK holoenzyme phosphorylates LCB4, which is required for its ubiquitination and degradation. PCL2-PHO85 also phosphorylates RVS167, linking cyclin-CDK activity with organization of the actin cytoskeleton.3 Publications

GO - Molecular functioni

  • cyclin-dependent protein serine/threonine kinase regulator activity Source: SGD

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • regulation of cyclin-dependent protein serine/threonine kinase activity Source: SGD
  • regulation of establishment or maintenance of cell polarity Source: SGD
  • septin ring organization Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

BioCyciYEAST:G3O-29526-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
PHO85 cyclin-2
Alternative name(s):
Cyclin HCS26 homolog
G1/S-specific cyclin PCL2
Gene namesi
Name:PCL2
Synonyms:CLN4
Ordered Locus Names:YDL127W
ORF Names:D2223
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL127W.
SGDiS000002285. PCL2.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

  • Note: Localizes to sites of polarized growth, namely the incipient bud site, the bud tip and the bud neck.

GO - Cellular componenti

  • cellular bud neck Source: SGD
  • cellular bud tip Source: SGD
  • cyclin-dependent protein kinase holoenzyme complex Source: SGD
  • cytoplasm Source: UniProtKB-SubCell
  • incipient cellular bud site Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 308308PHO85 cyclin-2PRO_0000080500Add
BLAST

PTM databases

iPTMnetiP25693.

Expressioni

Inductioni

By transcription factors SBF (SWI4-SWI6 cell-cycle box binding factor) and SWI5 in a cell cycle-regulated manner. Peaks in G1 phase.2 Publications

Interactioni

Subunit structurei

Forms a cyclin-CDK complex with PHO85. Interacts with RVS167.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PHO85P171578EBI-4499,EBI-13327
SSA1P105913EBI-4499,EBI-8591

Protein-protein interaction databases

BioGridi31936. 35 interactions.
DIPiDIP-1495N.
IntActiP25693. 8 interactions.
MINTiMINT-370014.

Structurei

3D structure databases

ProteinModelPortaliP25693.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 146129Cyclin N-terminalAdd
BLAST

Sequence similaritiesi

Belongs to the cyclin family. PCL1,2 subfamily.Curated
Contains 1 cyclin N-terminal domain.Curated

Phylogenomic databases

GeneTreeiENSGT00390000004809.
HOGENOMiHOG000000866.
InParanoidiP25693.
KOiK06657.
OMAiANIQTIP.
OrthoDBiEOG7VHT6Z.

Family and domain databases

InterProiIPR013763. Cyclin-like.
IPR006671. Cyclin_N.
IPR012104. PHO85_cyclin_1/2/9.
[Graphical view]
PfamiPF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFiPIRSF016511. Cyclin_Pcl. 1 hit.
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 1 hit.

Sequencei

Sequence statusi: Complete.

P25693-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNYEALLKF NRKAVSKEMV QYLASTTASI IKIKKTNSMI DIALPAPPLT
60 70 80 90 100
KFINRLIKHS NVQTPTLMAT SVYLAKLRSI IPSNVYGIET TRHRIFLGCL
110 120 130 140 150
ILAAKTLNDS SPLNKHWAEY TDGLLILREV NTIERELLEY FDWDVTISTD
160 170 180 190 200
DLITCLSPFL KPIKEEQLYK SQRDCRTLKN FSAQEKDIVN KTSISHSRSS
210 220 230 240 250
SNMSIPSLAS TSTLSTLESR RSNLSNYSNR IRTLPELHES NNISDKFSPR
260 270 280 290 300
TYNIDSKHDN KENRPIPTIK PFNFSKARPV ILKTGLNKQI IKEDTKVKKS

NWSNYFKS
Length:308
Mass (Da):35,207
Last modified:October 1, 1996 - v2
Checksum:i914BE1E2B92858CA
GO

Sequence cautioni

The sequence CAA98695.1 differs from that shown. Reason: Frameshift at position 263. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56956 Genomic DNA. Translation: CAA40277.1.
Z74175 Genomic DNA. Translation: CAA98695.1. Frameshift.
BK006938 Genomic DNA. Translation: DAA11733.1.
PIRiS67670.
RefSeqiNP_010156.2. NM_001180186.1.

Genome annotation databases

EnsemblFungiiYDL127W; YDL127W; YDL127W.
GeneIDi851430.
KEGGisce:YDL127W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56956 Genomic DNA. Translation: CAA40277.1.
Z74175 Genomic DNA. Translation: CAA98695.1. Frameshift.
BK006938 Genomic DNA. Translation: DAA11733.1.
PIRiS67670.
RefSeqiNP_010156.2. NM_001180186.1.

3D structure databases

ProteinModelPortaliP25693.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31936. 35 interactions.
DIPiDIP-1495N.
IntActiP25693. 8 interactions.
MINTiMINT-370014.

PTM databases

iPTMnetiP25693.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL127W; YDL127W; YDL127W.
GeneIDi851430.
KEGGisce:YDL127W.

Organism-specific databases

EuPathDBiFungiDB:YDL127W.
SGDiS000002285. PCL2.

Phylogenomic databases

GeneTreeiENSGT00390000004809.
HOGENOMiHOG000000866.
InParanoidiP25693.
KOiK06657.
OMAiANIQTIP.
OrthoDBiEOG7VHT6Z.

Enzyme and pathway databases

BioCyciYEAST:G3O-29526-MONOMER.

Miscellaneous databases

PROiP25693.

Family and domain databases

InterProiIPR013763. Cyclin-like.
IPR006671. Cyclin_N.
IPR012104. PHO85_cyclin_1/2/9.
[Graphical view]
PfamiPF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFiPIRSF016511. Cyclin_Pcl. 1 hit.
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation, and gene expression."
    Froehlich K.-U., Fries H.W., Ruediger M., Erdmann R., Botstein D., Mecke D.
    J. Cell Biol. 114:443-453(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Froehlich K.-U.
    Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "The PCL2 (ORFD)-PHO85 cyclin-dependent kinase complex: a cell cycle regulator in yeast."
    Measday V., Moore L., Ogas J., Tyers M., Andrews B.J.
    Science 266:1391-1395(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, INTERACTION WITH PHO85, INDUCTION.
  6. "A family of cyclin-like proteins that interact with the Pho85 cyclin-dependent kinase."
    Measday V., Moore L., Retnakaran R., Lee J., Donoviel M., Neiman A.M., Andrews B.J.
    Mol. Cell. Biol. 17:1212-1223(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHO85.
  7. "Interaction of yeast Rvs167 and Pho85 cyclin-dependent kinase complexes may link the cell cycle to the actin cytoskeleton."
    Lee J., Colwill K., Aneliunas V., Tennyson C.N., Moore L., Ho Y., Andrews B.J.
    Curr. Biol. 8:1310-1321(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RVS167, PHOSPHORYLATION OF RVS167.
  8. "Swi5 controls a novel wave of cyclin synthesis in late mitosis."
    Aerne B.L., Johnson A.L., Toyn J.H., Johnston L.H.
    Mol. Biol. Cell 9:945-956(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF FRAMESHIFT.
  10. "Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation."
    Friesen H., Murphy K., Breitkreutz A., Tyers M., Andrews B.J.
    Mol. Biol. Cell 14:3027-3040(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF RVS167.
  11. "Late-G1 cyclin-CDK activity is essential for control of cell morphogenesis in budding yeast."
    Moffat J., Andrews B.J.
    Nat. Cell Biol. 6:59-66(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "Phosphorylation by Pho85 cyclin-dependent kinase acts as a signal for the down-regulation of the yeast sphingoid long-chain base kinase Lcb4 during the stationary phase."
    Iwaki S., Kihara A., Sano T., Igarashi Y.
    J. Biol. Chem. 280:6520-6527(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION OF LCB4.

Entry informationi

Entry nameiPCL2_YEAST
AccessioniPrimary (citable) accession number: P25693
Secondary accession number(s): D6VRM3, Q07554
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 127 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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 one 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.