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P08539 (GPA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. 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 alpha-1 subunit
Alternative name(s):
GP1-alpha
Gene names
Name:GPA1
Synonyms:CDC70, DAC1, SCG1
Ordered Locus Names:YHR005C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alpha subunit of the heterotrimeric guanine nucleotide-binding protein (G protein) that mediates mating pheromone signal transduction. Binding of alpha-factor or a-factor to its cognate transmembrane receptor STE2 and STE3, respectively, allows the receptor to serve as a guanine nucleotide exchange factor (GEF) on GPA1. The exchange of GDP for GTP on the G protein alpha subunit alters its interaction with the G protein beta subunit STE4, leading to dissociation of the G protein beta-gamma dimer STE4-STE18. The dissociated subunits activate downstream effectors to activate the mating response pathway and induce changes necessary to produce mating-competent cells. STE4-STE18 activate the downstream pheromone signaling MAP kinase cascade leading to expression of mating-specific genes, inducing cell cycle arrest in G1, promoting polarized cell growth to form mating projections (shmoos), and establishing the changes in plasma membrane, cell wall and nuclear envelope to permit cell-cell fusion (plasmogamy) and fusion of the two haploid nuclei (karyogamy). GPA1 transmits a signal that requires direct binding to the effector enzyme PI3K located at the endosome, promoting increased PI3 production. The intrinsic GTPase activity of GPA1 determines the duration of signaling, and is dramatically accelerated by the RGS protein SST2. In unstimulated cells, GDP-bound GPA1 sequesters the G protein beta-gamma subunit STE4-STE18, preventing it from activating the downstream effectors. Also down-regulates the signal by inhibiting the pheromone-induced accumulation of FUS3 in the nucleus. Ref.2 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.18 Ref.23 Ref.24 Ref.28 Ref.35 Ref.36 Ref.37 Ref.40 Ref.44 Ref.45

Enzyme regulation

Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by the G protein coupled receptors (GPCRs) STE2 and STE3, which serve as guanine nucleotide-exchange factors (GEFs), and inactivated by SST2, probably acting as a GTPase-activating protein (GAP). Ref.46

Subunit structure

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. In its GDP-bound form, binds to the G protein beta-gamma dimer STE4-STE18. Directly interacts with the beta subunit STE4. Probably forms preactivation complexes with unligated receptors STE2 and STE3. Interacts with FUS3. Pheromone-induced activation of GPA1 increases its association with FUS3. Interacts with SCP160. SCP160 binds specifically to the GTP-bound form of GPA1. Interacts with the phoshpatidylinositol 3-kinase (PI3K) subunits VPS15 and VPS34 at the endosome. The GTP-bound form of GPA1 binds directly and selectively to the catalytic subunit VPS34, while the GDP-bound form binds to VPS15, which appears to function as an alternative G protein beta subunit for GPA1. Interacts with regulators of G protein signaling (RGS) proteins MDM1, RAX1, RGS2 and SST2, but SST2 alone binds preferentially to the transition state conformation of GPA1, indicating that it acts as a GAP for this G protein. Ref.17 Ref.22 Ref.24 Ref.35 Ref.36 Ref.45 Ref.46

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Endosome membrane; Lipid-anchor; Cytoplasmic side. Note: Localizes predominantly to the plasma membrane in its inactive, GDP-bound form, and is directed to endosomes once in its active, GTP-bound form. Concentrates at the tip of the mating projections. Ref.13 Ref.21 Ref.35 Ref.38 Ref.45

Domain

Contains an 'insertion' sequence of 109 residues which is not present in other G-protein alpha chains.

Post-translational modification

N-myristoylation by NMT1 is pheromone-stimulated and required for palmitoylation of Cys-3. This lipid modification anchors the protein to membranes. Depalmitoylated by YLR118C/APT1. Ref.20 Ref.29 Ref.34

Monoubiquitination targets the protein for degradation to the vacuole, and polyubiquitination tags the protein for degradation by the proteasome. This may be an additional signaling regulation mechanism.

Miscellaneous

Present with 9920 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the G-alpha family. G(q) subfamily.

Ontologies

Keywords
   Biological processPheromone response
   Cellular componentCell membrane
Endosome
Membrane
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransducer
   PTMIsopeptide bond
Lipoprotein
Myristate
Palmitate
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion

Inferred from mutant phenotype Ref.37Ref.11. Source: SGD

adenylate cyclase-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

heterotrimeric G-protein complex cycle

Inferred from mutant phenotype Ref.10. Source: SGD

inositol lipid-mediated signaling

Inferred from mutant phenotype Ref.45. Source: SGD

karyogamy involved in conjugation with cellular fusion

Inferred from mutant phenotype PubMed 19386762. Source: SGD

nuclear migration involved in conjugation with cellular fusion

Inferred from mutant phenotype PubMed 19386762. Source: SGD

pheromone-dependent signal transduction involved in conjugation with cellular fusion

Inferred from mutant phenotype PubMed 3113739. Source: SGD

regulation of MAPK export from nucleus

Inferred from mutant phenotype Ref.37. Source: SGD

   Cellular_componentendosome

Inferred from direct assay Ref.45. Source: SGD

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

heterotrimeric G-protein complex

Inferred from direct assay Ref.32. Source: SGD

plasma membrane

Inferred from direct assay Ref.22. Source: SGD

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from direct assay Ref.32. Source: SGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 10664449PubMed 10749875PubMed 11283351PubMed 16429126Ref.46Ref.45PubMed 8164677Ref.17Ref.22. Source: IntAct

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 472471Guanine nucleotide-binding protein alpha-1 subunit
PRO_0000203616

Regions

Nucleotide binding48 – 558GTP By similarity
Nucleotide binding294 – 3007GTP By similarity
Nucleotide binding319 – 3235GTP By similarity
Nucleotide binding388 – 3914GTP By similarity
Region127 – 235109Insert; not present in other G-proteins

Sites

Metal binding551Magnesium By similarity
Metal binding3001Magnesium By similarity
Binding site4441GTP; via amide nitrogen By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine Ref.16 Ref.19 Ref.21
Lipidation31S-palmitoyl cysteine Ref.20 Ref.29 Ref.34
Cross-link165Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.33

Experimental info

Mutagenesis21G → A: Abolishes both palmitoylation and N-myristoylation. Ref.20 Ref.21 Ref.29 Ref.35
Mutagenesis31C → A: Abolishes palmitoylation but not N-myristoylation. Ref.20 Ref.29 Ref.35
Mutagenesis151D → V: Slightly reduces ligand-dependent pheromone signaling. Ref.35 Ref.43
Mutagenesis171F → L: Leads to a hypersensitive signaling phenotype resulting in greatly enhanced signal at low alpha-factor concentrations. Ref.35 Ref.43
Mutagenesis181L → P or Q: Reduces ligand-dependent pheromone signaling. Ref.35 Ref.43
Mutagenesis21 – 222KR → EE: Impairs interaction with FUS3. Ref.35
Mutagenesis501G → D: Confers insensitivity to pheromone. Ref.9 Ref.12 Ref.15 Ref.31 Ref.35
Mutagenesis501G → V: Has increased GTP occupancy and moderately reduces hydrolysis of GTP, resulting in a constitutively active form that down-regulates the pheromone response and causes hyperadaptation to pheromone. Ref.9 Ref.12 Ref.15 Ref.31 Ref.35
Mutagenesis541K → E or I: Prevents GDP to GTP exchange; suppressor of L-323. Ref.26 Ref.35 Ref.43
Mutagenesis1651K → R: Substantial decrease in ubiquitination. Ref.33 Ref.35
Mutagenesis2971R → H: Slows hydrolysis of GTP. Ref.35
Mutagenesis3021G → S in GPA1(SST); weakens interaction to SST2 and blocks its negative regulatory effect. Ref.25 Ref.35
Mutagenesis3211G → T: Causes a specific mating defect in alpha cells. Ref.27 Ref.35
Mutagenesis3221G → A, E or R: Confers insensitivity to pheromone. Ref.12 Ref.15 Ref.23 Ref.35
Mutagenesis3231Q → L: Prevents hydrolysis of GTP; eliminates the interaction with STE4 and constitutively activates the pheromone response pathway. Ref.27 Ref.35
Mutagenesis3271R → S: Suppressor of L-323; does not prevent GTP binding to GPA1. Ref.26 Ref.35
Mutagenesis3451A → T: Suppressor of a STE2-L236H mutant. Ref.30 Ref.35
Mutagenesis3531Missing: Suppressor of L-323. Ref.26 Ref.35
Mutagenesis3551E → K: Confers insensitivity to pheromone. Ref.12 Ref.35
Mutagenesis3641E → K: Enhances the rate of GDP for GTP exchange and slows hydrolysis of GTP, resulting in a constitutively active form that down-regulates the pheromone response independently of the pheromone receptor. Ref.12 Ref.23 Ref.32 Ref.35
Mutagenesis3881N → D: Forms a nondissociable complex with the pheromone receptor in response to receptor activation, resulting in reduced pheromone responsiveness. Ref.15 Ref.23 Ref.32 Ref.35 Ref.41
Mutagenesis3881N → K: Causes constitutive activation of the pheromone response pathway. Ref.15 Ref.23 Ref.32 Ref.35 Ref.41
Mutagenesis3911D → A: Causes constitutive activation of the pheromone response pathway. Ref.15 Ref.35
Mutagenesis4671K → P: Impairs pheromone signaling in a and alpha cells. Ref.14 Ref.35
Mutagenesis4681K → P: Impairs pheromone signaling specifically in a cells. Ref.14 Ref.35
Mutagenesis4701G → D: Confers insensitivity to pheromone. Ref.12 Ref.35
Sequence conflict821W → R in AAA18403. Ref.2
Sequence conflict1941A → V in AAA18403. Ref.2
Sequence conflict2261R → K in AAA18403. Ref.2
Sequence conflict2461K → R in AAA18403. Ref.2
Sequence conflict4691I → S in AAA18403. Ref.2

Secondary structure

......................................................................... 472
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08539 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2E87C546E133D6E5

FASTA47254,076
        10         20         30         40         50         60 
MGCTVSTQTI GDESDPFLQN KRANDVIEQS LQLEKQRDKN EIKLLLLGAG ESGKSTVLKQ 

        70         80         90        100        110        120 
LKLLHQGGFS HQERLQYAQV IWADAIQSMK ILIIQARKLG IQLDCDDPIN NKDLFACKRI 

       130        140        150        160        170        180 
LLKAKALDYI NASVAGGSDF LNDYVLKYSE RYETRRRVQS TGRAKAAFDE DGNISNVKSD 

       190        200        210        220        230        240 
TDRDAETVTQ NEDADRNNSS RINLQDICKD LNQEGDDQMF VRKTSREIQG QNRRNLIHED 

       250        260        270        280        290        300 
IAKAIKQLWN NDKGIKQCFA RSNEFQLEGS AAYYFDNIEK FASPNYVCTD EDILKGRIKT 

       310        320        330        340        350        360 
TGITETEFNI GSSKFKVLDA GGQRSERKKW IHCFEGITAV LFVLAMSEYD QMLFEDERVN 

       370        380        390        400        410        420 
RMHESIMLFD TLLNSKWFKD TPFILFLNKI DLFEEKVKSM PIRKYFPDYQ GRVGDAEAGL 

       430        440        450        460        470 
KYFEKIFLSL NKTNKPIYVK RTCATDTQTM KFVLSAVTDL IIQQNLKKIG II 

« Hide

References

« Hide 'large scale' references
[1]"Occurrence in Saccharomyces cerevisiae of a gene homologous to the cDNA coding for the alpha subunit of mammalian G proteins."
Nakafuku M., Itoh H., Nakamura S., Kaziro Y.
Proc. Natl. Acad. Sci. U.S.A. 84:2140-2144(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The yeast SCG1 gene: a G alpha-like protein implicated in the a- and alpha-factor response pathway."
Dietzel C., Kurjan J.
Cell 50:1001-1010(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [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]"Mutations in a gene encoding the alpha subunit of a Saccharomyces cerevisiae G protein indicate a role in mating pheromone signaling."
Jahng K.-Y., Ferguson J., Reed S.I.
Mol. Cell. Biol. 8:2484-2493(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Constitutive mutants in the yeast pheromone response: ordered function of the gene products."
Blinder D., Bouvier S., Jenness D.D.
Cell 56:479-486(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The yeast G-protein homolog is involved in the mating pheromone signal transduction system."
Fujimura H.A.
Mol. Cell. Biol. 9:152-158(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"GPA1Val-50 mutation in the mating-factor signaling pathway in Saccharomyces cerevisiae."
Miyajima I., Arai K., Matsumoto K.
Mol. Cell. Biol. 9:2289-2297(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-50.
[10]"Regulation of the yeast pheromone response pathway by G protein subunits."
Nomoto S., Nakayama N., Arai K., Matsumoto K.
EMBO J. 9:691-696(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Stoichiometry of G protein subunits affects the Saccharomyces cerevisiae mating pheromone signal transduction pathway."
Cole G.M., Stone D.E., Reed S.I.
Mol. Cell. Biol. 10:510-517(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"G protein mutations that alter the pheromone response in Saccharomyces cerevisiae."
Stone D.E., Reed S.I.
Mol. Cell. Biol. 10:4439-4446(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-50; GLY-322; GLU-355; GLU-364 AND GLY-470.
[13]"Beta and gamma subunits of a yeast guanine nucleotide-binding protein are not essential for membrane association of the alpha subunit but are required for receptor coupling."
Blumer K.J., Thorner J.
Proc. Natl. Acad. Sci. U.S.A. 87:4363-4367(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]"The carboxyl terminus of Scg1, the G alpha subunit involved in yeast mating, is implicated in interactions with the pheromone receptors."
Hirsch J.P., Dietzel C., Kurjan J.
Genes Dev. 5:467-474(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-467 AND LYS-468.
[15]"Mutations in the guanine nucleotide-binding domains of a yeast G alpha protein confer a constitutive or uninducible state to the pheromone response pathway."
Kurjan J., Hirsch J.P., Dietzel C.
Genes Dev. 5:475-483(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-50; GLY-322; ASN-388 AND ASP-391.
[16]"N-myristoylation is required for function of the pheromone-responsive G alpha protein of yeast: conditional activation of the pheromone response by a temperature-sensitive N-myristoyl transferase."
Stone D.E., Cole G.M., de Barros Lopes M., Goebl M., Reed S.I.
Genes Dev. 5:1969-1981(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2.
[17]"Interactions among the subunits of the G protein involved in Saccharomyces cerevisiae mating."
Clark K.L., Dignard D., Thomas D.Y., Whiteway M.
Mol. Cell. Biol. 13:1-8(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STE4.
[18]"Suppression of a dominant G-protein beta-subunit mutation in yeast by G alpha protein expression."
Zhang M., Tipper D.J.
Mol. Microbiol. 9:813-821(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"Pheromone action regulates G-protein alpha-subunit myristoylation in the yeast Saccharomyces cerevisiae."
Dohlman H.G., Goldsmith P., Spiegel A.M., Thorner J.
Proc. Natl. Acad. Sci. U.S.A. 90:9688-9692(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2.
[20]"Partial constitutive activation of pheromone responses by a palmitoylation-site mutant of a G protein alpha subunit in yeast."
Song J., Dohlman H.G.
Biochemistry 35:14806-14817(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-3, MUTAGENESIS OF GLY-2 AND CYS-3.
[21]"Regulation of membrane and subunit interactions by N-myristoylation of a G protein alpha subunit in yeast."
Song J., Hirschman J., Gunn K., Dohlman H.G.
J. Biol. Chem. 271:20273-20283(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2, SUBCELLULAR LOCATION.
[22]"Sst2, a negative regulator of pheromone signaling in the yeast Saccharomyces cerevisiae: Expression, localization, and genetic interaction and physical association with Gpa1 (the G-protein alpha subunit)."
Dohlman H.G., Song J., Ma D., Courchesne W.E., Thorner J.
Mol. Cell. Biol. 16:5194-5209(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SST2.
[23]"The mating-specific G(alpha) protein of Saccharomyces cerevisiae downregulates the mating signal by a mechanism that is dependent on pheromone and independent of G(beta)(gamma) sequestration."
Stratton H.F., Zhou J., Reed S.I., Stone D.E.
Mol. Cell. Biol. 16:6325-6337(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-322; GLU-364 AND ASN-388.
[24]"Sst2 is a GTPase-activating protein for Gpa1: purification and characterization of a cognate RGS-Galpha protein pair in yeast."
Apanovitch D.M., Slep K.C., Sigler P.B., Dohlman H.G.
Biochemistry 37:4815-4822(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SST2.
[25]"Selective uncoupling of RGS action by a single point mutation in the G protein alpha-subunit."
DiBello P.R., Garrison T.R., Apanovitch D.M., Hoffman G., Shuey D.J., Mason K., Cockett M.I., Dohlman H.G.
J. Biol. Chem. 273:5780-5784(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-302.
[26]"Second site suppressor mutations of a GTPase-deficient G-protein alpha-subunit."
Apanovitch D.M., Iiri T., Karasawa T., Bourne H.R., Dohlman H.G.
J. Biol. Chem. 273:28597-28602(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-54; ARG-327 AND LEU-353.
[27]"Switch-domain mutations in the Saccharomyces cerevisiae G protein alpha-subunit Gpa1p identify a receptor subtype-biased mating defect."
DeSimone S.M., Kurjan J.
Mol. Gen. Genet. 257:662-671(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-321 AND GLN-323.
[28]"The yeast pheromone-responsive G alpha protein stimulates recovery from chronic pheromone treatment by two mechanisms that are activated at distinct levels of stimulus."
Zhou J., Arora M., Stone D.E.
Cell Biochem. Biophys. 30:193-212(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[29]"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: PALMITOYLATION AT CYS-3, MUTAGENESIS OF GLY-2 AND CYS-3.
[30]"The C terminus of the Saccharomyces cerevisiae alpha-factor receptor contributes to the formation of preactivation complexes with its cognate G protein."
Dosil M., Schandel K.A., Gupta E., Jenness D.D., Konopka J.B.
Mol. Cell. Biol. 20:5321-5329(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ALA-345, FORMATION OF PREACTIVATION COMPLEXES.
[31]"The GTP hydrolysis defect of the Saccharomyces cerevisiae mutant G-protein Gpa1(G50V)."
Kallal L., Fishel R.
Yeast 16:387-400(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-50.
[32]"Biochemical analysis of yeast G(alpha) mutants that enhance adaptation to pheromone."
Cismowski M.J., Metodiev M.V., Draper E., Stone D.E.
Biochem. Biophys. Res. Commun. 284:247-254(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-364 AND ASN-388.
[33]"Direct identification of a G protein ubiquitination site by mass spectrometry."
Marotti L.A. Jr., Newitt R., Wang Y., Aebersold R., Dohlman H.G.
Biochemistry 41:5067-5074(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-165, MUTAGENESIS OF LYS-165, IDENTIFICATION BY MASS SPECTROMETRY.
[34]"Characterization of Saccharomyces cerevisiae acyl-protein thioesterase 1, the enzyme responsible for G protein alpha subunit deacylation in vivo."
Duncan J.A., Gilman A.G.
J. Biol. Chem. 277:31740-31752(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DEPALMITOYLATION.
[35]"Regulation of MAPK function by direct interaction with the mating-specific G(alpha) in yeast."
Metodiev M.V., Matheos D., Rose M.D., Stone D.E.
Science 296:1483-1486(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FUS3, MUTAGENESIS OF 21-LSY-ARG-22, SUBCELLULAR LOCATION.
[36]"The yeast G protein alpha subunit Gpa1 transmits a signal through an RNA binding effector protein Scp160."
Guo M., Aston C., Burchett S.A., Dyke C., Fields S., Rajarao S.J.R., Uetz P., Wang Y., Young K., Dohlman H.G.
Mol. Cell 12:517-524(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SCP160.
[37]"Effect of the pheromone-responsive G(alpha) and phosphatase proteins of Saccharomyces cerevisiae on the subcellular localization of the Fus3 mitogen-activated protein kinase."
Blackwell E., Halatek I.M., Kim H.-J.N., Ellicott A.T., Obukhov A.A., Stone D.E.
Mol. Cell. Biol. 23:1135-1150(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[38]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[39]"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].
[40]"A quantitative characterization of the yeast heterotrimeric G protein cycle."
Yi T.-M., Kitano H., Simon M.I.
Proc. Natl. Acad. Sci. U.S.A. 100:10764-10769(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[41]"Dominant-negative inhibition of pheromone receptor signaling by a single point mutation in the G protein alpha subunit."
Wu Y.-L., Hooks S.B., Harden T.K., Dohlman H.G.
J. Biol. Chem. 279:35287-35297(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-388.
[42]Erratum
Wu Y.-L., Hooks S.B., Harden T.K., Dohlman H.G.
J. Biol. Chem. 280:29988-29988(2005)
[43]"Effects of mutations in the N terminal region of the yeast G protein alpha-subunit Gpa1p on signaling by pheromone receptors."
Roginskaya M., Connelly S.M., Kim K.S., Patel D., Dumont M.E.
Mol. Genet. Genomics 271:237-248(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-15; PHE-17; LEU-18 AND LYS-54.
[44]"Differential regulation of G protein alpha subunit trafficking by mono-and polyubiquitination."
Wang Y., Marotti L.A. Jr., Lee M.J., Dohlman H.G.
J. Biol. Chem. 280:284-291(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF UBIQUITINATION.
[45]"Activation of the phosphatidylinositol 3-kinase Vps34 by a G protein alpha subunit at the endosome."
Slessareva J.E., Routt S.M., Temple B., Bankaitis V.A., Dohlman H.G.
Cell 126:191-203(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VPS15 AND VPS34, SUBCELLULAR LOCATION.
[46]"Genome-scale analysis reveals Sst2 as the principal regulator of mating pheromone signaling in the yeast Saccharomyces cerevisiae."
Chasse S.A., Flanary P., Parnell S.C., Hao N., Cha J.Y., Siderovski D.P., Dohlman H.G.
Eukaryot. Cell 5:330-346(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MDM1; RAX1; RGS2 AND SST2, ENZYME REGULATION.
[47]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[48]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[49]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
M15867 Genomic DNA. Translation: AAA34650.1.
M17414 Unassigned DNA. Translation: AAA18403.1.
U10555 Genomic DNA. Translation: AAB68432.1.
AY692963 Genomic DNA. Translation: AAT92982.1.
BK006934 Genomic DNA. Translation: DAA06692.1.
PIRA25906.
RefSeqNP_011868.1. NM_001179135.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SCGmodel-A1-472[»]
ProteinModelPortalP08539.
SMRP08539. Positions 41-136, 240-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36430. 45 interactions.
DIPDIP-15N.
IntActP08539. 16 interactions.
MINTMINT-509090.
STRING4932.YHR005C.

Proteomic databases

MaxQBP08539.
PaxDbP08539.
PeptideAtlasP08539.

Protocols and materials databases

DNASU856394.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR005C; YHR005C; YHR005C.
GeneID856394.
KEGGsce:YHR005C.

Organism-specific databases

SGDS000001047. GPA1.

Phylogenomic databases

eggNOGNOG322962.
GeneTreeENSGT00690000102066.
HOGENOMHOG000038730.
KOK04640.
OMAFDGLNAN.
OrthoDBEOG7M0P1X.

Enzyme and pathway databases

BioCycYEAST:G3O-31070-MONOMER.

Gene expression databases

GenevestigatorP08539.

Family and domain databases

Gene3D1.10.400.10. 2 hits.
3.40.50.300. 2 hits.
InterProIPR002975. Fungi_Gprotein_alpha.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10218. PTHR10218. 1 hit.
PfamPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSPR00318. GPROTEINA.
PR01241. GPROTEINAFNG.
SMARTSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMSSF47895. SSF47895. 2 hits.
SSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

NextBio981914.

Entry information

Entry nameGPA1_YEAST
AccessionPrimary (citable) accession number: P08539
Secondary accession number(s): D3DKU8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 164 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: 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