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P18852 (GBG_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein subunit gamma
Gene names
Name:STE18
Ordered Locus Names:YJR086W
ORF Names:J1866
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length110 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

G proteins are composed of 3 units, alpha, beta and gamma. The beta-gamma subunit complex (STE4-STE18 complex) interacts with PLP1 and PLP2. Ref.9

Subcellular location

Membrane; Lipid-anchor.

Miscellaneous

Present with 5550 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the G protein gamma family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

STE4P188513EBI-7397,EBI-7390

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 107107Guanine nucleotide-binding protein subunit gamma
PRO_0000194812
Propeptide108 – 1103Removed in mature form
PRO_0000396775

Regions

Compositional bias11 – 2212Gln-rich
Compositional bias96 – 1049Asn/Ser-rich

Amino acid modifications

Modified residue1071Cysteine methyl ester Ref.7
Lipidation1061S-palmitoyl cysteine Ref.7 Ref.8
Lipidation1071S-farnesyl cysteine Ref.7 Ref.8

Experimental info

Mutagenesis1061C → S: Partial loss of function. Ref.7
Mutagenesis1071C → X: Loss of function. Ref.6

Secondary structure

..... 110
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18852 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 6A78E946DA5059FA

FASTA11012,625
        10         20         30         40         50         60 
MTSVQNSPRL QQPQEQQQQQ QQLSLKIKQL KLKRINELNN KLRKELSRER ITASNACLTI 

        70         80         90        100        110 
INYTSNTKDY TLPELWGYPV AGSNHFIEGL KNAQKNSQMS NSNSVCCTLM 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"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].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB30102.
RefSeqNP_012619.1. NM_001181743.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SCGmodel-G1-110[»]
ProteinModelPortalP18852.
SMRP18852. Positions 38-72.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33841. 12 interactions.
DIPDIP-314N.
IntActP18852. 2 interactions.
MINTMINT-394213.
STRING4932.YJR086W.

Proteomic databases

MaxQBP18852.
PaxDbP18852.

Protocols and materials databases

DNASU853548.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJR086W; YJR086W; YJR086W.
GeneID853548.
KEGGsce:YJR086W.

Organism-specific databases

CYGDYJR086w.
SGDS000003846. STE18.

Phylogenomic databases

eggNOGNOG39072.
HOGENOMHOG000210889.
KOK07973.
OMAHEETSAC.
OrthoDBEOG7D5B1T.

Enzyme and pathway databases

BioCycYEAST:G3O-31714-MONOMER.

Gene expression databases

GenevestigatorP18852.

Family and domain databases

InterProIPR015898. G-protein_gamma-like_dom.
[Graphical view]
PfamPF00631. G-gamma. 1 hit.
[Graphical view]
SMARTSM00224. GGL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio974278.

Entry information

Entry nameGBG_YEAST
AccessionPrimary (citable) accession number: P18852
Secondary accession number(s): D6VWQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 11, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references