Guanine nucleotide-binding protein alpha-2 subunit - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P10823 (GPA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 138. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Guanine nucleotide-binding protein alpha-2 subunit

Alternative name(s):
GP2-alpha

Gene names

Name:	GPA2
Synonyms:	SSP101
Ordered Locus Names:	YER020W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	449 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Guanine nucleotide-binding protein (G protein) involved in glucose-induced cAMP signaling. Its activity is negatively regulated by RGS2. Ref.4
Subunit structure	G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. GPA2 interacts with the beta subunits GBP1 and GPB2 and with the gamma subunit GPG1. Interacts also with RGS2. Ref.4 Ref.5
Subcellular location	Cytoplasm › cell cortex Ref.7.
Miscellaneous	Present with 4570 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the G-alpha family. G(q) subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transducer
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-activating G-protein coupled receptor signaling pathway Inferred from mutant phenotype PubMed 9628870. Source: SGD ascospore formation Inferred from mutant phenotype PubMed 10454558. Source: SGD glucose mediated signaling pathway Inferred from mutant phenotype Ref.1 PubMed 9628870. Source: SGD pseudohyphal growth Inferred from mutant phenotype PubMed 10454558 PubMed 10655215 PubMed 9384580. Source: SGD regulation of cell size Inferred from mutant phenotype PubMed 12089449. Source: SGD replicative cell aging Inferred from mutant phenotype PubMed 15722108. Source: SGD
Cellular_component	cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell heterotrimeric G-protein complex Inferred from Biological aspect of Ancestor. Source: RefGenome mitochondrion Inferred from direct assay PubMed 14576278 PubMed 16823961. Source: SGD
Molecular_function	G-protein beta/gamma-subunit complex binding Inferred from Biological aspect of Ancestor. Source: RefGenome G-protein coupled receptor binding Inferred from Biological aspect of Ancestor. Source: RefGenome GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from direct assay PubMed 16924114. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW signal transducer activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Potential

Chain

2 – 449

448

Guanine nucleotide-binding protein alpha-2 subunit

PRO_0000203617

Regions

Nucleotide binding

130 – 137

GTP By similarity

Nucleotide binding

270 – 276

GTP By similarity

Nucleotide binding

296 – 300

GTP By similarity

Nucleotide binding

365 – 368

GTP By similarity

Sites

Metal binding

137

Magnesium By similarity

Metal binding

276

Magnesium By similarity

Binding site

420

GTP; via amide nitrogen By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.6

Modified residue

Phosphoserine Ref.6

Modified residue

Phosphoserine Ref.10

Modified residue

117

Phosphoserine Ref.9

Modified residue

119

Phosphoserine Ref.10

Lipidation

N-myristoyl glycine

Lipidation

S-palmitoyl cysteine Potential

Experimental info

Mutagenesis

132

G → V: Locks GPA2 in its activated GTP-bound form and abrogates the negative control by RGS2. Ref.4

Sequence conflict

375

S → R in AAA34651. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P10823 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 881B91792AE91748
Show »

FASTA

449

50,448

        10         20         30         40         50         60 
MGLCASSEKN GSTPDTQTAS AGSDNVGKAK VPPKQEPQKT VRTVNTANQQ EKQQQRQQQP 

        70         80         90        100        110        120 
SPHNVKDRKE QNGSINNAIS PTATANTSGS QQINIDSALR DRSSNVAAQP SLSDASSGSN 

       130        140        150        160        170        180 
DKELKVLLLG AGESGKSTVL QQLKILHQNG FSEQEIKEYI PLIYQNLLEI GRNLIQARTR 

       190        200        210        220        230        240 
FNVNLEPECE LTQQDLSRTM SYEMPNNYTG QFPEDIAGVI STLWALPSTQ DLVNGPNASK 

       250        260        270        280        290        300 
FYLMDSTPYF MENFTRITSP NYRPTQQDIL RSRQMTSGIF DTVIDMGSDI KMHIYDVGGQ 

       310        320        330        340        350        360 
RSERKKWIHC FDNVTLVIFC VSLSEYDQTL MEDKNQNRFQ ESLVLFDNIV NSRWFARTSV 

       370        380        390        400        410        420 
VLFLNKIDLF AEKLSKVPME NYFPDYTGGS DINKAAKYIL WRFVQLNRAN LSIYPHVTQA 

       430        440 
TDTSNIRLVF AAIKETILEN TLKDSGVLQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of a second yeast Saccharomyces cerevisiae gene (GPA2) coding for guanine nucleotide-binding regulatory protein: studies on its structure and possible functions." Nakafuku M., Obara T., Kaibuchi K., Miyajima I., Miyajima A., Itoh H., Nakamura S., Arai K., Matsumoto K., Kaziro Y. Proc. Natl. Acad. Sci. U.S.A. 85:1374-1378(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"A novel regulator of G protein signalling in yeast, Rgs2, downregulates glucose-activation of the cAMP pathway through direct inhibition of Gpa2." Versele M., de Winde J.H., Thevelein J.M. EMBO J. 18:5577-5591(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RGS2, MUTAGENESIS OF GLY-132.
[5]	"The Galpha protein Gpa2 controls yeast differentiation by interacting with kelch repeat proteins that mimic Gbeta subunits." Harashima T., Heitman J. Mol. Cell 10:163-173(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GPG1; GPB1 AND GPB2.
[6]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-23, MASS SPECTROMETRY. Strain: 2124.
[7]	"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].
[8]	"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].
[9]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, MASS SPECTROMETRY.
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-119, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03609 Genomic DNA. Translation: AAA34651.1. U18778 Genomic DNA. Translation: AAB64553.1. BK006939 Genomic DNA. Translation: DAA07673.1.
PIR	S50478.
RefSeq	NP_010937.3. NM_001178911.3.
3D structure databases
ProteinModelPortal	P10823.
SMR	P10823. Positions 123-443.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4346N.
IntAct	P10823. 42 interactions.
MINT	MINT-548605.
STRING	4932.YER020W.
Proteomic databases
PaxDb	P10823.
PeptideAtlas	P10823.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YER020W; YER020W; YER020W.
GeneID	856741.
KEGG	sce:YER020W. sce:YER023W.
Organism-specific databases
CYGD	YER020w.
SGD	S000000822. GPA2.
Phylogenomic databases
eggNOG	NOG322962.
GeneTree	ENSGT00690000102066.
HOGENOM	HOG000038730.
KO	K00286. K04640.
OMA	KNILDCI.
OrthoDB	EOG4HTD1X.
Gene expression databases
Genevestigator	P10823.
GermOnline	YER020W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.10.400.10. 1 hit.
InterPro	IPR002975. Fungi_Gprotein_alpha. IPR001019. Gprotein_alpha_su. IPR011025. GproteinA_insert. [Graphical view]
PANTHER	PTHR10218. PTHR10218. 1 hit.
Pfam	PF00503. G-alpha. 1 hit. [Graphical view]
PRINTS	PR00318. GPROTEINA. PR01241. GPROTEINAFNG.
SMART	SM00275. G_alpha. 1 hit. [Graphical view]
SUPFAM	SSF47895. Transducn_insert. 1 hit.
ProtoNet	Search...
Other
NextBio	982873.

Entry information

Entry name

GPA2_YEAST

Accession

Primary (citable) accession number: P10823
Secondary accession number(s): D3DLR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 138 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome V

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents