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P18852

- GBG_YEAST

UniProt

P18852 - GBG_YEAST

Protein

Guanine nucleotide-binding protein subunit gamma

Gene

STE18

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

    Implicated in the pheromone A- and alpha-factor response pathway. The beta and gamma chains of the putative yeast mating response pathway G protein play a positive role in initiation of the mating response.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. signal transducer activity Source: SGD

    GO - Biological processi

    1. heterotrimeric G-protein complex cycle Source: SGD
    2. pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD

    Keywords - Molecular functioni

    Transducer

    Keywords - Biological processi

    Pheromone response

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31714-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide-binding protein subunit gamma
    Gene namesi
    Name:STE18
    Ordered Locus Names:YJR086W
    ORF Names:J1866
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJR086w.
    SGDiS000003846. STE18.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. heterotrimeric G-protein complex Source: SGD
    3. plasma membrane Source: SGD

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi106 – 1061C → S: Partial loss of function. 1 Publication
    Mutagenesisi107 – 1071C → X: Loss of function. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 107107Guanine nucleotide-binding protein subunit gammaPRO_0000194812Add
    BLAST
    Propeptidei108 – 1103Removed in mature formPRO_0000396775

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi106 – 1061S-palmitoyl cysteine2 Publications
    Modified residuei107 – 1071Cysteine methyl ester1 Publication
    Lipidationi107 – 1071S-farnesyl cysteine2 Publications

    Keywords - PTMi

    Lipoprotein, Methylation, Palmitate, Prenylation

    Proteomic databases

    MaxQBiP18852.
    PaxDbiP18852.

    Expressioni

    Gene expression databases

    GenevestigatoriP18852.

    Interactioni

    Subunit structurei

    G proteins are composed of 3 units, alpha, beta and gamma. The beta-gamma subunit complex (STE4-STE18 complex) interacts with PLP1 and PLP2.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    STE4P188513EBI-7397,EBI-7390

    Protein-protein interaction databases

    BioGridi33841. 12 interactions.
    DIPiDIP-314N.
    IntActiP18852. 2 interactions.
    MINTiMINT-394213.
    STRINGi4932.YJR086W.

    Structurei

    Secondary structure

    1
    110
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi32 – 4615
    Helixi53 – 6614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SCGmodel-G1-110[»]
    ProteinModelPortaliP18852.
    SMRiP18852. Positions 38-72.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi11 – 2212Gln-richAdd
    BLAST
    Compositional biasi96 – 1049Asn/Ser-rich

    Sequence similaritiesi

    Belongs to the G protein gamma family.Curated

    Phylogenomic databases

    eggNOGiNOG39072.
    HOGENOMiHOG000210889.
    KOiK07973.
    OMAiHEETSAC.
    OrthoDBiEOG7D5B1T.

    Family and domain databases

    InterProiIPR015898. G-protein_gamma-like_dom.
    [Graphical view]
    PfamiPF00631. G-gamma. 1 hit.
    [Graphical view]
    SMARTiSM00224. GGL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P18852-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSVQNSPRL QQPQEQQQQQ QQLSLKIKQL KLKRINELNN KLRKELSRER    50
    ITASNACLTI INYTSNTKDY TLPELWGYPV AGSNHFIEGL KNAQKNSQMS 100
    NSNSVCCTLM 110
    Length:110
    Mass (Da):12,625
    Last modified:November 1, 1990 - v1
    Checksum:i6A78E946DA5059FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23983 Genomic DNA. Translation: AAA35110.1.
    L47993 Genomic DNA. Translation: AAB39309.1.
    Z49586 Genomic DNA. Translation: CAA89613.1.
    AY557888 Genomic DNA. Translation: AAS56214.1.
    BK006943 Genomic DNA. Translation: DAA08871.1.
    PIRiB30102.
    RefSeqiNP_012619.1. NM_001181743.1.

    Genome annotation databases

    EnsemblFungiiYJR086W; YJR086W; YJR086W.
    GeneIDi853548.
    KEGGisce:YJR086W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23983 Genomic DNA. Translation: AAA35110.1 .
    L47993 Genomic DNA. Translation: AAB39309.1 .
    Z49586 Genomic DNA. Translation: CAA89613.1 .
    AY557888 Genomic DNA. Translation: AAS56214.1 .
    BK006943 Genomic DNA. Translation: DAA08871.1 .
    PIRi B30102.
    RefSeqi NP_012619.1. NM_001181743.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SCG model - G 1-110 [» ]
    ProteinModelPortali P18852.
    SMRi P18852. Positions 38-72.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33841. 12 interactions.
    DIPi DIP-314N.
    IntActi P18852. 2 interactions.
    MINTi MINT-394213.
    STRINGi 4932.YJR086W.

    Proteomic databases

    MaxQBi P18852.
    PaxDbi P18852.

    Protocols and materials databases

    DNASUi 853548.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJR086W ; YJR086W ; YJR086W .
    GeneIDi 853548.
    KEGGi sce:YJR086W.

    Organism-specific databases

    CYGDi YJR086w.
    SGDi S000003846. STE18.

    Phylogenomic databases

    eggNOGi NOG39072.
    HOGENOMi HOG000210889.
    KOi K07973.
    OMAi HEETSAC.
    OrthoDBi EOG7D5B1T.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31714-MONOMER.

    Miscellaneous databases

    NextBioi 974278.

    Gene expression databases

    Genevestigatori P18852.

    Family and domain databases

    InterProi IPR015898. G-protein_gamma-like_dom.
    [Graphical view ]
    Pfami PF00631. G-gamma. 1 hit.
    [Graphical view ]
    SMARTi SM00224. GGL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The STE4 and STE18 genes of yeast encode potential beta and gamma subunits of the mating factor receptor-coupled G protein."
      Whiteway M., Hougan L., Dignard D., Thomas D.Y., Bell L., Saari G.C., Grant F.J., O'Hara P., Mackay V.L.
      Cell 56:467-477(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading frames and a gene cluster with a counterpart on chromosome XI."
      Huang M.-E., Manus V., Chuat J.-C., Galibert F.
      Yeast 12:869-875(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "Site-directed mutations altering the CAAX box of Ste18, the yeast pheromone-response pathway G gamma subunit."
      Whiteway M.S., Thomas D.Y.
      Genetics 137:967-976(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-107.
    7. "Dual lipid modification of the yeast gamma subunit Ste18p determines membrane localization of Gbetagamma."
      Hirschman J.E., Jenness D.D.
      Mol. Cell. Biol. 19:7705-7711(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOPRENYLATION AT CYS-107, METHYLATION AT CYS-107, PALMITOYLATION AT CYS-106, MUTAGENESIS OF CYS-106.
    8. "Dual lipid modification motifs in G(alpha) and G(gamma) subunits are required for full activity of the pheromone response pathway in Saccharomyces cerevisiae."
      Manahan C.L., Patnana M., Blumer K.J., Linder M.E.
      Mol. Biol. Cell 11:957-968(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOPRENYLATION AT CYS-107, PALMITOYLATION AT CYS-106.
    9. "Functional analysis of Plp1 and Plp2, two homologues of phosducin in yeast."
      Flanary P.L., DiBello P.R., Estrada P., Dohlman H.G.
      J. Biol. Chem. 275:18462-18469(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLP1 AND PLP2.
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Gaitatzes C.G., Neer E.J., Smith T.F.
      Submitted (FEB-1998) to the PDB data bank
      Cited for: 3D-STRUCTURE MODELING.

    Entry informationi

    Entry nameiGBG_YEAST
    AccessioniPrimary (citable) accession number: P18852
    Secondary accession number(s): D6VWQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 125 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 5550 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 X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3