Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

PHO85 cyclin-10

Gene

PCL10

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Together with cyclin PCL8, negatively controls glycogen accumulation under favorable growth conditions. The PCL10-PHO85 cyclin-CDK holoenzyme has glycogen synthase kinase activity and phosphorylates and negatively regulates glycogen synthase GSY2. Also has minor GLC8 kinase activity.3 Publications

GO - Molecular functioni

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

GO - Biological processi

  • glycogen metabolic process Source: UniProtKB-KW
  • negative regulation of glycogen biosynthetic process Source: SGD
  • regulation of cyclin-dependent protein serine/threonine kinase activity Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Enzyme and pathway databases

BioCyciYEAST:G3O-30629-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
PHO85 cyclin-10
Gene namesi
Name:PCL10
Ordered Locus Names:YGL134W
ORF Names:G2838
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL134W.
SGDiS000003102. PCL10.

Subcellular locationi

GO - Cellular componenti

  • cyclin-dependent protein kinase holoenzyme complex Source: SGD
  • cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433PHO85 cyclin-10PRO_0000202740Add
BLAST

Proteomic databases

MaxQBiP53124.

PTM databases

iPTMnetiP53124.

Interactioni

Subunit structurei

Forms a cyclin-CDK complex with PHO85. Interacts with GSY2, independent of the presence of PHO85.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PHO85P171577EBI-23973,EBI-13327

Protein-protein interaction databases

BioGridi33118. 29 interactions.
DIPiDIP-1494N.
IntActiP53124. 13 interactions.
MINTiMINT-402996.

Structurei

Secondary structure

1
433
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi246 – 2483Combined sources
Helixi262 – 28019Combined sources
Helixi291 – 2988Combined sources
Helixi310 – 32112Combined sources
Helixi325 – 33915Combined sources
Beta strandi340 – 3423Combined sources
Beta strandi348 – 3503Combined sources
Helixi356 – 3583Combined sources
Helixi359 – 37416Combined sources
Helixi381 – 3888Combined sources
Helixi392 – 40615Combined sources
Helixi415 – 42915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4KRCX-ray2.60B227-433[»]
4KRDX-ray1.95B227-433[»]
ProteinModelPortaliP53124.
SMRiP53124. Positions 243-432.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclin family. PHO80 subfamily.Curated

Phylogenomic databases

GeneTreeiENSGT00530000067900.
InParanoidiP53124.
OrthoDBiEOG799310.

Family and domain databases

InterProiIPR013922. Cyclin_PHO80-like.
[Graphical view]
PfamiPF08613. Cyclin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53124-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDMTKNHTTD TEEFDDGDIR PVSLGIVDDY NASFELPLKP KFLQSENFSD
60 70 80 90 100
LTSEWDQSRS NTPGLAEGKT EKAQPCGTTD SSKNRIHVEQ LLESANEMNN
110 120 130 140 150
YLAQNIENIN NFQVGLLNGG KGLYSSMGDD SSACINGTNF SSTSNFELSD
160 170 180 190 200
DELEDTTGCT SSIFDKDLFH QQNGLSIPRR RSPLFKSPTA SFEIGDATDV
210 220 230 240 250
EEQDIDDSIF SECSSITSFD MGGLHISLPH DEEEDQEKTK SESENPLLHG
260 270 280 290 300
IPVDVEVPHI SVDEALANFK ETIELLLKLS GNRKCTGFNT RVEKKEYSNF
310 320 330 340 350
YMKSKPTLSS ADFLKRIQDK CEYQPTVYLV ATFLIDTLFL TRDGNNILQL
360 370 380 390 400
KLNLQEKEVH RMIIAAVRLS TKLLEDFVHS HEYFSKVCGI SKRLLTKLEV
410 420 430
SLLICVCNTK LMVSNRKLAA SKLLLNELRS FCV
Length:433
Mass (Da):48,584
Last modified:October 1, 1996 - v1
Checksum:iDE6608A34BDBDF99
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72656 Genomic DNA. Translation: CAA96845.1.
BK006941 Genomic DNA. Translation: DAA07976.1.
PIRiS64147.
RefSeqiNP_011381.1. NM_001180999.1.

Genome annotation databases

EnsemblFungiiYGL134W; YGL134W; YGL134W.
GeneIDi852743.
KEGGisce:YGL134W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72656 Genomic DNA. Translation: CAA96845.1.
BK006941 Genomic DNA. Translation: DAA07976.1.
PIRiS64147.
RefSeqiNP_011381.1. NM_001180999.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4KRCX-ray2.60B227-433[»]
4KRDX-ray1.95B227-433[»]
ProteinModelPortaliP53124.
SMRiP53124. Positions 243-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33118. 29 interactions.
DIPiDIP-1494N.
IntActiP53124. 13 interactions.
MINTiMINT-402996.

PTM databases

iPTMnetiP53124.

Proteomic databases

MaxQBiP53124.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL134W; YGL134W; YGL134W.
GeneIDi852743.
KEGGisce:YGL134W.

Organism-specific databases

EuPathDBiFungiDB:YGL134W.
SGDiS000003102. PCL10.

Phylogenomic databases

GeneTreeiENSGT00530000067900.
InParanoidiP53124.
OrthoDBiEOG799310.

Enzyme and pathway databases

BioCyciYEAST:G3O-30629-MONOMER.

Miscellaneous databases

NextBioi972162.
PROiP53124.

Family and domain databases

InterProiIPR013922. Cyclin_PHO80-like.
[Graphical view]
PfamiPF08613. Cyclin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a 14.6 kb DNA fragment of Saccharomyces cerevisiae chromosome VII reveals SEC27, SSM1b, a putative S-adenosylmethionine-dependent enzyme and six new open reading frames."
    Escribano V., Eraso P., Portillo F., Mazon M.J.
    Yeast 12:887-892(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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.
  5. "Cyclin partners determine Pho85 protein kinase substrate specificity in vitro and in vivo: control of glycogen biosynthesis by Pcl8 and Pcl10."
    Huang D., Moffat J., Wilson W.A., Moore L., Cheng C., Roach P.J., Andrews B.J.
    Mol. Cell. Biol. 18:3289-3299(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION OF GSY2, INTERACTION WITH GSY2.
  6. "Substrate targeting of the yeast cyclin-dependent kinase Pho85p by the cyclin Pcl10p."
    Wilson W.A., Mahrenholz A.M., Roach P.J.
    Mol. Cell. Biol. 19:7020-7030(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GSY2 AND PHO85.
  7. "Pho85 phosphorylates the Glc7 protein phosphatase regulator Glc8 in vivo."
    Tan Y.S.H., Morcos P.A., Cannon J.F.
    J. Biol. Chem. 278:147-153(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPCL10_YEAST
AccessioniPrimary (citable) accession number: P53124
Secondary accession number(s): D6VU15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 217 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.