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P21268

- FAR1_YEAST

UniProt

P21268 - FAR1_YEAST

Protein

Cyclin-dependent kinase inhibitor FAR1

Gene

FAR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri202 – 25251RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cyclin-dependent protein serine/threonine kinase inhibitor activity Source: SGD
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell cycle arrest in response to pheromone Source: SGD
    2. cell division Source: UniProtKB-KW
    3. maintenance of protein location in nucleus Source: SGD
    4. negative regulation of protein serine/threonine kinase activity Source: GOC
    5. pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD

    Keywords - Molecular functioni

    Protein kinase inhibitor

    Keywords - Biological processi

    Cell cycle, Cell division

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31597-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-dependent kinase inhibitor FAR1
    Short name:
    CKI FAR1
    Alternative name(s):
    Factor arrest protein
    Gene namesi
    Name:FAR1
    Ordered Locus Names:YJL157C
    ORF Names:J0565
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJL157c.
    SGDiS000003693. FAR1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. mating projection tip Source: SGD
    3. membrane Source: SGD
    4. nucleus Source: SGD

    Pathology & Biotechi

    Disruption phenotypei

    Some mutants appear to be defective in mating because they are unable to locate the mating partner.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi87 – 871S → A: Prevents cell cycle-dependent degradation of FAR1. 1 Publication
    Mutagenesisi306 – 3061T → A: Abolishes G1 arrest function. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 830830Cyclin-dependent kinase inhibitor FAR1PRO_0000055910Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei87 – 871Phosphoserine; by CDC28Curated
    Modified residuei110 – 1101Phosphoserine1 Publication
    Modified residuei114 – 1141Phosphoserine1 Publication
    Modified residuei306 – 3061Phosphothreonine1 Publication

    Post-translational modificationi

    Thought to be phosphorylated by MAP kinase FUS3. Thought to enhance the binding of FAR1 to G1-specific cyclin-dependent kinase (CDK) complexes.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP21268.
    PaxDbiP21268.
    PeptideAtlasiP21268.

    Expressioni

    Inductioni

    By alpha-factor in a cells.

    Gene expression databases

    GenevestigatoriP21268.

    Interactioni

    Subunit structurei

    Associates with the CDC28-CLN complex.

    Protein-protein interaction databases

    BioGridi33603. 74 interactions.
    DIPiDIP-2229N.
    IntActiP21268. 20 interactions.
    MINTiMINT-364767.
    STRINGi4932.YJL157C.

    Structurei

    3D structure databases

    ProteinModelPortaliP21268.
    SMRiP21268. Positions 198-256.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    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.

    Sequence similaritiesi

    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri202 – 25251RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG331220.
    KOiK06652.
    OMAiAIFEETH.
    OrthoDBiEOG7712HK.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P21268-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTPTRVSFE KKIHTPPSGD RDAERSPPKK FLRGLSGKVF RKTPEFKKQQ    50
    MPTFGYIEES QFTPNLGLMM SKRGNIPKPL NLSKPISPPP SLKKTAGSVA 100
    SGFSKTGQLS ALQSPVNITS SNKYNIKATN LTTSLLRESI SDSTTMCDTL 150
    SDINLTVMDE DYRIDGDSYY EEDSPTFMIS LERNIKKCNS QFSPKRYIGE 200
    KCLICEESIS STFTGEKVVE STCSHTSHYN CYLMLFETLY FQGKFPECKI 250
    CGEVSKPKDK DIVPEMVSKL LTGAGAHDDG PSSNMQQQWI DLKTARSFTG 300
    EFPQFTPQEQ LIRTADISCD GFRTPRLSNS NQFEAVSYLD SPFLNSPFVN 350
    KMATTDPFDL SDDEKLDCDD EIDESAAEVW FSKTGGEHVM VSVKFQEMRT 400
    SDDLGVLQDV NHVDHEELEE REKEWKKKID QYIETNVDKD SEFGSLILFD 450
    KLMYSDDGEQ WVDNNLVILF SKFLVLFDFE EMKILGKIPR DQFYQVIKFN 500
    EDVLLCSLKS TNIPEIYLRF NENCEKWLLP KWKYCLENSS LETLPLSEIV 550
    STVKELSHVN IIGALGAPPD VISAQSHDSR LPWKRLHSDT PLKLIVCLNL 600
    SHADGELYRK RVLKSVHQIL DGLNTDDLLG IVVVGRDGSG VVGPFGTFIG 650
    MINKNWDGWT TFLDNLEVVN PNVFRDEKQQ YKVTLQTCER LASTSAYVDT 700
    DDHIATGYAK QILVLNGSDV VDIEHDQKLK KAFDQLSYHW RYEISQRRMT 750
    PLNASIKQFL EELHTKRYLD VTLRLPQATF EQVYLGDMAA GEQKTRLIMD 800
    EHPHSSLIEI EYFDLVKQQR IHQTLEVPNL 830
    Length:830
    Mass (Da):94,572
    Last modified:November 1, 1995 - v2
    Checksum:i834EBB2D7BB9641D
    GO

    Sequence cautioni

    The sequence AAA34600.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201D → N(PubMed:2147873)Curated
    Sequence conflicti568 – 5681P → R in AAA34600. (PubMed:2147873)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti87 – 871S → P in FAR1-22P; induces cell cycle arrest in the absence of alpha-factor.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60071 Genomic DNA. Translation: AAA34600.1. Different initiation.
    Z49432 Genomic DNA. Translation: CAA89452.1.
    BK006943 Genomic DNA. Translation: DAA08646.1.
    PIRiS56940.
    RefSeqiNP_012378.1. NM_001181590.1.

    Genome annotation databases

    EnsemblFungiiYJL157C; YJL157C; YJL157C.
    GeneIDi853283.
    KEGGisce:YJL157C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60071 Genomic DNA. Translation: AAA34600.1 . Different initiation.
    Z49432 Genomic DNA. Translation: CAA89452.1 .
    BK006943 Genomic DNA. Translation: DAA08646.1 .
    PIRi S56940.
    RefSeqi NP_012378.1. NM_001181590.1.

    3D structure databases

    ProteinModelPortali P21268.
    SMRi P21268. Positions 198-256.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33603. 74 interactions.
    DIPi DIP-2229N.
    IntActi P21268. 20 interactions.
    MINTi MINT-364767.
    STRINGi 4932.YJL157C.

    Proteomic databases

    MaxQBi P21268.
    PaxDbi P21268.
    PeptideAtlasi P21268.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJL157C ; YJL157C ; YJL157C .
    GeneIDi 853283.
    KEGGi sce:YJL157C.

    Organism-specific databases

    CYGDi YJL157c.
    SGDi S000003693. FAR1.

    Phylogenomic databases

    eggNOGi NOG331220.
    KOi K06652.
    OMAi AIFEETH.
    OrthoDBi EOG7712HK.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31597-MONOMER.

    Miscellaneous databases

    NextBioi 973579.

    Gene expression databases

    Genevestigatori P21268.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
      EMBO J. 15:2031-2049(1996) [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. 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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    12. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.

    Entry informationi

    Entry nameiFAR1_YEAST
    AccessioniPrimary (citable) accession number: P21268
    Secondary accession number(s): D6VW30
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 238 molecules/cell in log phase SD medium.1 Publication

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

    External Data

    Dasty 3