Cyclin-dependent kinase inhibitor FAR1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P21268 (FAR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 119. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cyclin-dependent kinase inhibitor FAR1
Short name=CKI FAR1

Alternative name(s):
Factor arrest protein

Gene names

Name:	FAR1
Ordered Locus Names:	YJL157C
ORF Names:	J0565

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	830 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Inhibitor of the cyclin-dependent kinase CDC28. Necessary for cell cycle arrest. Involved in pheromone response. Contributes to mating efficiency. Required for oriented polarization of yeast cells in response to mating pheromones.
Subunit structure	Associates with the CDC28-CLN complex.
Induction	By alpha-factor in a cells.
Domain	There is evidence to suggest that the N-terminal part may be sufficient for cell cycle arrest and the C-terminal may be necessary for some step in mating.
Post-translational modification	Thought to be phosphorylated by MAP kinase FUS3. Thought to enhance the binding of FAR1 to G1-specific cyclin-dependent kinase (CDK) complexes.
Disruption phenotype	Some mutants appear to be defective in mating because they are unable to locate the mating partner. Ref.2
Miscellaneous	Present with 238 molecules/cell in log phase SD medium.
Sequence similarities	Contains 1 RING-type zinc finger.
Sequence caution	The sequence AAA34600.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Protein kinase inhibitor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle arrest in response to pheromone Inferred from mutant phenotype Ref.1. Source: SGD cell division Inferred from electronic annotation. Source: UniProtKB-KW maintenance of protein location in nucleus Inferred from mutant phenotype PubMed 10655592. Source: SGD pheromone-dependent signal transduction involved in conjugation with cellular fusion Inferred from genetic interaction PubMed 10087263. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 22842922 PubMed 9822386. Source: SGD mating projection tip Inferred from direct assay PubMed 14988725. Source: SGD membrane Inferred from direct assay PubMed 14988725. Source: SGD nucleus Inferred from direct assay PubMed 22842922 PubMed 9822386. Source: SGD
Molecular_function	cyclin-dependent protein serine/threonine kinase inhibitor activity Inferred from direct assay Ref.6. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 830

830

Cyclin-dependent kinase inhibitor FAR1

PRO_0000055910

Regions

Zinc finger

202 – 252

RING-type

Amino acid modifications

Modified residue

Phosphoserine; by CDC28 Probable

Modified residue

Phosphoserine Ref.14

Modified residue

110

Phosphoserine Ref.13

Modified residue

114

Phosphoserine Ref.12 Ref.13

Modified residue

306

Phosphothreonine Ref.13

Natural variations

Natural variant

S → P in FAR1-22P; induces cell cycle arrest in the absence of alpha-factor.

Experimental info

Mutagenesis

S → A: Prevents cell cycle-dependent degradation of FAR1. Ref.10

Mutagenesis

306

T → A: Abolishes G1 arrest function. Ref.10

Sequence conflict

D → N Ref.1

Sequence conflict

568

P → R in AAA34600. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P21268 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 834EBB2D7BB9641D
Show »

FASTA

830

94,572

        10         20         30         40         50         60 
MKTPTRVSFE KKIHTPPSGD RDAERSPPKK FLRGLSGKVF RKTPEFKKQQ MPTFGYIEES 

        70         80         90        100        110        120 
QFTPNLGLMM SKRGNIPKPL NLSKPISPPP SLKKTAGSVA SGFSKTGQLS ALQSPVNITS 

       130        140        150        160        170        180 
SNKYNIKATN LTTSLLRESI SDSTTMCDTL SDINLTVMDE DYRIDGDSYY EEDSPTFMIS 

       190        200        210        220        230        240 
LERNIKKCNS QFSPKRYIGE KCLICEESIS STFTGEKVVE STCSHTSHYN CYLMLFETLY 

       250        260        270        280        290        300 
FQGKFPECKI CGEVSKPKDK DIVPEMVSKL LTGAGAHDDG PSSNMQQQWI DLKTARSFTG 

       310        320        330        340        350        360 
EFPQFTPQEQ LIRTADISCD GFRTPRLSNS NQFEAVSYLD SPFLNSPFVN KMATTDPFDL 

       370        380        390        400        410        420 
SDDEKLDCDD EIDESAAEVW FSKTGGEHVM VSVKFQEMRT SDDLGVLQDV NHVDHEELEE 

       430        440        450        460        470        480 
REKEWKKKID QYIETNVDKD SEFGSLILFD KLMYSDDGEQ WVDNNLVILF SKFLVLFDFE 

       490        500        510        520        530        540 
EMKILGKIPR DQFYQVIKFN EDVLLCSLKS TNIPEIYLRF NENCEKWLLP KWKYCLENSS 

       550        560        570        580        590        600 
LETLPLSEIV STVKELSHVN IIGALGAPPD VISAQSHDSR LPWKRLHSDT PLKLIVCLNL 

       610        620        630        640        650        660 
SHADGELYRK RVLKSVHQIL DGLNTDDLLG IVVVGRDGSG VVGPFGTFIG MINKNWDGWT 

       670        680        690        700        710        720 
TFLDNLEVVN PNVFRDEKQQ YKVTLQTCER LASTSAYVDT DDHIATGYAK QILVLNGSDV 

       730        740        750        760        770        780 
VDIEHDQKLK KAFDQLSYHW RYEISQRRMT PLNASIKQFL EELHTKRYLD VTLRLPQATF 

       790        800        810        820        830 
EQVYLGDMAA GEQKTRLIMD EHPHSSLIEI EYFDLVKQQR IHQTLEVPNL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a gene necessary for cell cycle arrest by a negative growth factor of yeast: FAR1 is an inhibitor of a G1 cyclin, CLN2." Chang F., Herskowitz I. Cell 63:999-1011(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"FAR1 and the G1 phase specificity of cell cycle arrest by mating factor in Saccharomyces cerevisiae." McKinney J.D., Cross F.R. Mol. Cell. Biol. 15:2509-2516(1995) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO N-TERMINUS, DISRUPTION PHENOTYPE.
[3]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Stop that cell cycle." Chang F. Curr. Biol. 3:693-695(1993) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[6]	"Direct inhibition of the yeast cyclin-dependent kinase Cdc28-Cln by Far1." Peter M., Herskowitz I. Science 265:1228-1231(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[7]	"FAR1 is required for oriented polarization of yeast cells in response to mating pheromones." Valtz N., Peter M., Herskowitz I. J. Cell Biol. 131:863-873(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Functional analysis of FAR1 in yeast." Valtz N., Peter M. Methods Enzymol. 283:350-365(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[9]	"Phosphorylation- and ubiquitin-dependent degradation of the cyclin-dependent kinase inhibitor Far1p in budding yeast." Henchoz S., Chi Y., Catarin B., Herskowitz I., Deshaies R.J., Peter M. Genes Dev. 11:3046-3060(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[10]	"Pheromone-dependent G1 cell cycle arrest requires Far1 phosphorylation, but may not involve inhibition of Cdc28-Cln2 kinase, in vivo." Gartner A., Jovanovic A., Jeoung D.I., Bourlat S., Cross F.R., Ammerer G. Mol. Cell. Biol. 18:3681-3691(1998) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF SER-87 AND THR-306.
[11]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY. Strain: YAL6B.
[13]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-114 AND THR-306, MASS SPECTROMETRY. Strain: ADR376.
[14]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M60071 Genomic DNA. Translation: AAA34600.1. Different initiation. Z49432 Genomic DNA. Translation: CAA89452.1. BK006943 Genomic DNA. Translation: DAA08646.1.
PIR	S56940.
RefSeq	NP_012378.1. NM_001181590.1.
3D structure databases
ProteinModelPortal	P21268.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2229N.
IntAct	P21268. 22 interactions.
MINT	MINT-364767.
STRING	4932.YJL157C.
Proteomic databases
PaxDb	P21268.
PeptideAtlas	P21268.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJL157C; YJL157C; YJL157C.
GeneID	853283.
KEGG	sce:YJL157C.
Organism-specific databases
CYGD	YJL157c.
SGD	S000003693. FAR1.
Phylogenomic databases
eggNOG	NOG331220.
KO	K06652.
OMA	INELPIC.
OrthoDB	EOG4K6KDD.
Enzyme and pathway databases
BioCyc	YEAST:G3O-31597-MONOMER.
Gene expression databases
Genevestigator	P21268.
GermOnline	YJL157C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	973579.

Entry information

Entry name

FAR1_YEAST

Accession

Primary (citable) accession number: P21268
Secondary accession number(s): D6VW30

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	November 1, 1995
Last modified:	May 29, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents