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P08539

- GPA1_YEAST

UniProt

P08539 - GPA1_YEAST

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Protein

Guanine nucleotide-binding protein alpha-1 subunit

Gene

GPA1

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

Functioni

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.20 Publications

Enzyme regulationi

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).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi55 – 551MagnesiumBy similarity
Metal bindingi300 – 3001MagnesiumBy similarity
Binding sitei444 – 4441GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 558GTPBy similarity
Nucleotide bindingi294 – 3007GTPBy similarity
Nucleotide bindingi319 – 3235GTPBy similarity
Nucleotide bindingi388 – 3914GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: SGD
  2. GTP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion Source: SGD
  2. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: InterPro
  3. heterotrimeric G-protein complex cycle Source: SGD
  4. inositol lipid-mediated signaling Source: SGD
  5. karyogamy involved in conjugation with cellular fusion Source: SGD
  6. nuclear migration involved in conjugation with cellular fusion Source: SGD
  7. pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD
  8. regulation of MAPK export from nucleus Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Pheromone response

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31070-MONOMER.
ReactomeiREACT_187439. Ca2+ pathway.
REACT_237034. G-protein activation.
REACT_241032. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_242947. G alpha (z) signalling events.
REACT_258039. G alpha (i) signalling events.
REACT_270165. Activation of the phototransduction cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein alpha-1 subunit
Alternative name(s):
GP1-alpha
Gene namesi
Name:GPA1
Synonyms:CDC70, DAC1, SCG1
Ordered Locus Names:YHR005C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VIII

Organism-specific databases

SGDiS000001047. GPA1.

Subcellular locationi

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.

GO - Cellular componenti

  1. endosome Source: SGD
  2. heterotrimeric G-protein complex Source: SGD
  3. plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A: Abolishes both palmitoylation and N-myristoylation. 3 Publications
Mutagenesisi3 – 31C → A: Abolishes palmitoylation but not N-myristoylation. 2 Publications
Mutagenesisi15 – 151D → V: Slightly reduces ligand-dependent pheromone signaling. 1 Publication
Mutagenesisi17 – 171F → L: Leads to a hypersensitive signaling phenotype resulting in greatly enhanced signal at low alpha-factor concentrations. 1 Publication
Mutagenesisi18 – 181L → P or Q: Reduces ligand-dependent pheromone signaling. 1 Publication
Mutagenesisi21 – 222KR → EE: Impairs interaction with FUS3. 1 Publication
Mutagenesisi50 – 501G → D: Confers insensitivity to pheromone. 4 Publications
Mutagenesisi50 – 501G → 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. 4 Publications
Mutagenesisi54 – 541K → E or I: Prevents GDP to GTP exchange; suppressor of L-323. 2 Publications
Mutagenesisi165 – 1651K → R: Substantial decrease in ubiquitination. 1 Publication
Mutagenesisi297 – 2971R → H: Slows hydrolysis of GTP.
Mutagenesisi302 – 3021G → S in GPA1(SST); weakens interaction to SST2 and blocks its negative regulatory effect. 1 Publication
Mutagenesisi321 – 3211G → T: Causes a specific mating defect in alpha cells. 1 Publication
Mutagenesisi322 – 3221G → A, E or R: Confers insensitivity to pheromone. 3 Publications
Mutagenesisi323 – 3231Q → L: Prevents hydrolysis of GTP; eliminates the interaction with STE4 and constitutively activates the pheromone response pathway. 1 Publication
Mutagenesisi327 – 3271R → S: Suppressor of L-323; does not prevent GTP binding to GPA1. 1 Publication
Mutagenesisi345 – 3451A → T: Suppressor of a STE2-L236H mutant. 1 Publication
Mutagenesisi353 – 3531Missing: Suppressor of L-323. 1 Publication
Mutagenesisi355 – 3551E → K: Confers insensitivity to pheromone. 1 Publication
Mutagenesisi364 – 3641E → 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. 3 Publications
Mutagenesisi388 – 3881N → D: Forms a nondissociable complex with the pheromone receptor in response to receptor activation, resulting in reduced pheromone responsiveness. 4 Publications
Mutagenesisi388 – 3881N → K: Causes constitutive activation of the pheromone response pathway. 4 Publications
Mutagenesisi391 – 3911D → A: Causes constitutive activation of the pheromone response pathway. 1 Publication
Mutagenesisi467 – 4671K → P: Impairs pheromone signaling in a and alpha cells. 1 Publication
Mutagenesisi468 – 4681K → P: Impairs pheromone signaling specifically in a cells. 1 Publication
Mutagenesisi470 – 4701G → D: Confers insensitivity to pheromone. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 472471Guanine nucleotide-binding protein alpha-1 subunitPRO_0000203616Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine3 Publications
Lipidationi3 – 31S-palmitoyl cysteine2 Publications
Cross-linki165 – 165Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

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/APT1.5 Publications
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.1 Publication

Keywords - PTMi

Isopeptide bond, Lipoprotein, Myristate, Palmitate, Ubl conjugation

Proteomic databases

MaxQBiP08539.
PaxDbiP08539.
PeptideAtlasiP08539.

Expressioni

Gene expression databases

GenevestigatoriP08539.

Interactioni

Subunit structurei

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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SST2P119723EBI-7376,EBI-18232
STE4P188518EBI-7376,EBI-7390
VPS15P222192EBI-7376,EBI-20347
VPS34P225433EBI-7376,EBI-20405

Protein-protein interaction databases

BioGridi36430. 46 interactions.
DIPiDIP-15N.
IntActiP08539. 16 interactions.
MINTiMINT-509090.
STRINGi4932.YHR005C.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SCGmodel-A1-472[»]
ProteinModelPortaliP08539.
SMRiP08539. Positions 41-136, 240-462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni127 – 235109Insert; not present in other G-proteinsAdd
BLAST

Domaini

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG322962.
GeneTreeiENSGT00770000120503.
HOGENOMiHOG000038730.
InParanoidiP08539.
KOiK04640.
OMAiFDGLNAN.
OrthoDBiEOG7M0P1X.

Family and domain databases

Gene3Di1.10.400.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR002975. Fungi_Gprotein_alpha.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR01241. GPROTEINAFNG.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 2 hits.
SSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

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

P08539-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGCTVSTQTI GDESDPFLQN KRANDVIEQS LQLEKQRDKN EIKLLLLGAG
60 70 80 90 100
ESGKSTVLKQ LKLLHQGGFS HQERLQYAQV IWADAIQSMK ILIIQARKLG
110 120 130 140 150
IQLDCDDPIN NKDLFACKRI LLKAKALDYI NASVAGGSDF LNDYVLKYSE
160 170 180 190 200
RYETRRRVQS TGRAKAAFDE DGNISNVKSD TDRDAETVTQ NEDADRNNSS
210 220 230 240 250
RINLQDICKD LNQEGDDQMF VRKTSREIQG QNRRNLIHED IAKAIKQLWN
260 270 280 290 300
NDKGIKQCFA RSNEFQLEGS AAYYFDNIEK FASPNYVCTD EDILKGRIKT
310 320 330 340 350
TGITETEFNI GSSKFKVLDA GGQRSERKKW IHCFEGITAV LFVLAMSEYD
360 370 380 390 400
QMLFEDERVN RMHESIMLFD TLLNSKWFKD TPFILFLNKI DLFEEKVKSM
410 420 430 440 450
PIRKYFPDYQ GRVGDAEAGL KYFEKIFLSL NKTNKPIYVK RTCATDTQTM
460 470
KFVLSAVTDL IIQQNLKKIG II
Length:472
Mass (Da):54,076
Last modified:January 23, 2007 - v3
Checksum:i2E87C546E133D6E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821W → R in AAA18403. (PubMed:3113738)Curated
Sequence conflicti194 – 1941A → V in AAA18403. (PubMed:3113738)Curated
Sequence conflicti226 – 2261R → K in AAA18403. (PubMed:3113738)Curated
Sequence conflicti246 – 2461K → R in AAA18403. (PubMed:3113738)Curated
Sequence conflicti469 – 4691I → S in AAA18403. (PubMed:3113738)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA25906.
RefSeqiNP_011868.1. NM_001179135.1.

Genome annotation databases

EnsemblFungiiYHR005C; YHR005C; YHR005C.
GeneIDi856394.
KEGGisce:YHR005C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi A25906.
RefSeqi NP_011868.1. NM_001179135.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SCG model - A 1-472 [» ]
ProteinModelPortali P08539.
SMRi P08539. Positions 41-136, 240-462.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36430. 46 interactions.
DIPi DIP-15N.
IntActi P08539. 16 interactions.
MINTi MINT-509090.
STRINGi 4932.YHR005C.

Proteomic databases

MaxQBi P08539.
PaxDbi P08539.
PeptideAtlasi P08539.

Protocols and materials databases

DNASUi 856394.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YHR005C ; YHR005C ; YHR005C .
GeneIDi 856394.
KEGGi sce:YHR005C.

Organism-specific databases

SGDi S000001047. GPA1.

Phylogenomic databases

eggNOGi NOG322962.
GeneTreei ENSGT00770000120503.
HOGENOMi HOG000038730.
InParanoidi P08539.
KOi K04640.
OMAi FDGLNAN.
OrthoDBi EOG7M0P1X.

Enzyme and pathway databases

BioCyci YEAST:G3O-31070-MONOMER.
Reactomei REACT_187439. Ca2+ pathway.
REACT_237034. G-protein activation.
REACT_241032. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_242947. G alpha (z) signalling events.
REACT_258039. G alpha (i) signalling events.
REACT_270165. Activation of the phototransduction cascade.

Miscellaneous databases

NextBioi 981914.

Gene expression databases

Genevestigatori P08539.

Family and domain databases

Gene3Di 1.10.400.10. 2 hits.
3.40.50.300. 2 hits.
InterProi IPR002975. Fungi_Gprotein_alpha.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR10218. PTHR10218. 1 hit.
Pfami PF00503. G-alpha. 1 hit.
[Graphical view ]
PRINTSi PR00318. GPROTEINA.
PR01241. GPROTEINAFNG.
SMARTi SM00275. G_alpha. 1 hit.
[Graphical view ]
SUPFAMi SSF47895. SSF47895. 2 hits.
SSF52540. SSF52540. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. "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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  39. 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.

Entry informationi

Entry nameiGPA1_YEAST
AccessioniPrimary (citable) accession number: P08539
Secondary accession number(s): D3DKU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 167 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 9920 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 VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

External Data

Dasty 3