Reviewed, UniProtKB/Swiss-Prot P24867 (PCL1_YEAST)

Names and origin

Protein names

Recommended name:
    PHO85 cyclin-1
Alternative name(s):
    G1/S-specific cyclin PCL1
    Cyclin HCS26

Gene names

Name:	PCL1
Synonyms:	HCS26
Ordered Locus Names:	YNL289W
ORF Names:	N0536

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	279 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. The PCL1-PHO85 cyclin-CDK holoenzyme is involved in phosphorylation of the CDK inhibitor (CKI) SIC1, which is required for its ubiquitination and degradation, releasing repression of b-type cyclins and promoting exit from mitosis. Together with cyclin PCL2, positively controls degradation of sphingoid long chain base kinase LCB4. PCL1-PHO85 phosphorylates LCB4, which is required for its ubiquitination and degradation. PCL1-PHO85 also phosphorylates HMS1, NCP1 and NPA3, which may all have a role in mitotic exit. Ref.5 Ref.7 Ref.8 Ref.9
Subunit structure	Forms a cyclin-CDK complex with PHO85. Interacts with HMS1, NCP1 and NPA3. Ref.7 Ref.3 Ref.4
Subcellular location	Cytoplasm. Nucleus. Note: Localizes to the incipient bud site. Ref.8
Induction	By transcription factor SBF (SWI4-SWI6 cell-cycle box binding factor) in a cell cycle-regulated manner. Peaks in G1 phase. Ref.1
Post-translational modification	Phosphorylated by PHO85 Potential.
Miscellaneous	Present with 606 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the cyclin family. PCL1,2 subfamily. Contains 1 cyclin N-terminal domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm Nucleus
Molecular function	Cyclin
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	G1 phase of mitotic cell cycle Ref.3 Inferred from genetic interaction. Source: SGD cell division Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell division Inferred from electronic annotation. Source: InterPro regulation of cyclin-dependent protein kinase activity Ref.3 Inferred from direct assay. Source: SGD regulation of establishment or maintenance of cell polarity Inferred from genetic interaction. Source: SGD septin ring organization Inferred from genetic interaction. Source: SGD
Cellular component	cyclin-dependent protein kinase holoenzyme complex Ref.3 Inferred from physical interaction. Source: SGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell incipient cellular bud site Ref.8 Inferred from direct assay. Source: SGD nucleus Ref.8 Inferred from direct assay. Source: SGD
Molecular function	cyclin-dependent protein kinase regulator activity Ref.3 Inferred from direct assay. Source: SGD protein kinase binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PHO85	P17157	3	EBI-4495,EBI-13327

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 279	279	PHO85 cyclin-1		PRO_0000080499
Regions
	Domain	19 – 152	134	Cyclin N-terminal

Sequences

	Sequence		Length	Mass (Da)
	P24867-1 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: DC9E05C3C2EBD0F6	FASTA	279	32,095
	10 20 30 40 50 60 MCEYSKALHI LLKSPVTDDI IKFLTDTTLR VVPSSNYPTP PGSPGEKHLT RLPSLMTFIT 70 80 90 100 110 120 RLVRYTNVYT PTLLTAACYL NKLKRILPRD ATGLPSTIHR IFLACLILSA KFHNDSSPLN 130 140 150 160 170 180 KHWARYTDGL FTLEDINLME RQLLQLLNWD LRVNTEDLIL DLQPLLEPIK QDLARSSDQR 190 200 210 220 230 240 KRINMMMSMN RRTCAGTSPI RSNNRFKLYE KQRNVSIASD LSSATLVDSC NDLRRLKDVT 250 260 270 NIANNTVANT NYVRTVEKWN DNVNRQSWDL EQIMSQHGF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Transcriptional activation of CLN1, CLN2, and a putative new G1 cyclin (HCS26) by SWI4, a positive regulator of G1-specific transcription." Ogas J., Andrews B.J., Herskowitz I. Cell 66:1015-1026(1991) [PubMed: 1832336] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Cell cycle control by a complex of the cyclin HCS26 (PCL1) and the kinase PHO85." Espinoza F.H., Ogas J., Herskowitz I., Morgan D.O. Science 266:1388-1391(1994) [PubMed: 7973730] [Abstract] Cited for: CHARACTERIZATION, INTERACTION WITH PHO85.
[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: 9032248] [Abstract] Cited for: INTERACTION WITH PHO85.
[5]	"Phosphorylation of Sic1, a cyclin-dependent kinase (Cdk) inhibitor, by Cdk including Pho85 kinase is required for its prompt degradation." Nishizawa M., Kawasumi M., Fujino M., Toh-e A. Mol. Biol. Cell 9:2393-2405(1998) [PubMed: 9725902] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION OF SIC1.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"The identification of Pcl1-interacting proteins that genetically interact with Cla4 may indicate a link between G1 progression and mitotic exit." Keniry M.E., Kemp H.A., Rivers D.M., Sprague G.F. Jr. Genetics 166:1177-1186(2004) [PubMed: 15082539] [Abstract] Cited for: FUNCTION, INTERACTION WITH HMS1; NCP1 AND NPA3, PHOSPHORYLATION OF HMS1; NCP1 AND NPA3.
[8]	"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: 14688790] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]	"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: 15598647] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION OF LCB4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M73966 Genomic DNA. Translation: AAA34617.1. Z71565 Genomic DNA. Translation: CAA96206.1.
PIR	A40027.
RefSeq	NP_014110.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5803N.
IntAct	P24867. 6 interactions.
STRING	P24867.
Genome annotation databases
Ensembl	YNL289W; YNL289W; YNL289W; Saccharomyces cerevisiae. [Genome view]
GeneID	855427.
KEGG	sce:YNL289W.
NMPDR	fig|4932.3.peg.5172.
Organism-specific databases
CYGD	YNL289w.
SGD	S000005233. PCL1.
Phylogenomic databases
HOGENOM	HBG448666.
OMA	SAKFHND.
OrthoDB	EOG9V70ZR.
Gene expression databases
ArrayExpress	P24867.
Genevestigator	P24867.
GermOnline	YNL289W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006670. Cyclin. IPR011028. Cyclin-like. IPR006671. Cyclin_N. IPR012104. Cyclin_Pcl. IPR013763. Cyclin_related. [Graphical view]
Gene3D	G3DSA:1.10.472.10. Cyclin_related. 1 hit.
Pfam	PF00134. Cyclin_N. 1 hit. [Graphical view]
PIRSF	PIRSF016511. Cyclin_Pcl. 1 hit.
SMART	SM00385. CYCLIN. 1 hit. [Graphical view]
PROSITE	PS00292. CYCLINS. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	979298.

Entry information

Entry name

PCL1_YEAST

Accession

Primary (citable) accession number: P24867

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	December 15, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)