GPA1_YEAST - dbPTM
GPA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPA1_YEAST
UniProt AC P08539
Protein Name Guanine nucleotide-binding protein alpha-1 subunit
Gene Name GPA1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 472
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side. Endosome membrane
Lipid-anchor
Cytoplasmic side. Localizes predominantly to the plasma membrane in its inactive, GDP-bound form, and is directed to endosomes once in its active, GTP-bound form. Concent
Protein Description 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..
Protein Sequence MGCTVSTQTIGDESDPFLQNKRANDVIEQSLQLEKQRDKNEIKLLLLGAGESGKSTVLKQLKLLHQGGFSHQERLQYAQVIWADAIQSMKILIIQARKLGIQLDCDDPINNKDLFACKRILLKAKALDYINASVAGGSDFLNDYVLKYSERYETRRRVQSTGRAKAAFDEDGNISNVKSDTDRDAETVTQNEDADRNNSSRINLQDICKDLNQEGDDQMFVRKTSREIQGQNRRNLIHEDIAKAIKQLWNNDKGIKQCFARSNEFQLEGSAAYYFDNIEKFASPNYVCTDEDILKGRIKTTGITETEFNIGSSKFKVLDAGGQRSERKKWIHCFEGITAVLFVLAMSEYDQMLFEDERVNRMHESIMLFDTLLNSKWFKDTPFILFLNKIDLFEEKVKSMPIRKYFPDYQGRVGDAEAGLKYFEKIFLSLNKTNKPIYVKRTCATDTQTMKFVLSAVTDLIIQQNLKKIGII
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2N-myristoyl glycine------MGCTVSTQT
------CCCEEECCC		18.79-
2Myristoylation------MGCTVSTQT
------CCCEEECCC		18.798702760
3S-palmitoylation-----MGCTVSTQTI
-----CCCEEECCCC		3.07-
3S-palmitoylation-----MGCTVSTQTI
-----CCCEEECCCC		3.0710712512
4Phosphorylation----MGCTVSTQTIG
----CCCEEECCCCC		16.2630377154
6Phosphorylation--MGCTVSTQTIGDE
--CCCEEECCCCCCC		9.1730377154
7Phosphorylation-MGCTVSTQTIGDES
-CCCEEECCCCCCCC		25.9530377154
14PhosphorylationTQTIGDESDPFLQNK
CCCCCCCCCHHHCCH		56.1530377154
21UbiquitinationSDPFLQNKRANDVIE
CCHHHCCHHHHHHHH		39.6717644757
35UbiquitinationEQSLQLEKQRDKNEI
HHHHHHHHHCCHHHE		60.2623749301
35AcetylationEQSLQLEKQRDKNEI
HHHHHHHHHCCHHHE		60.2624489116
39UbiquitinationQLEKQRDKNEIKLLL
HHHHHCCHHHEEEEE		59.6822817900
43UbiquitinationQRDKNEIKLLLLGAG
HCCHHHEEEEEECCC		27.2317644757
52PhosphorylationLLLGAGESGKSTVLK
EEECCCCCCHHHHHH		51.0719823750
54UbiquitinationLGAGESGKSTVLKQL
ECCCCCCHHHHHHHH		52.8417644757
55PhosphorylationGAGESGKSTVLKQLK
CCCCCCHHHHHHHHH		27.5519823750
56PhosphorylationAGESGKSTVLKQLKL
CCCCCHHHHHHHHHH		33.0919823750
62UbiquitinationSTVLKQLKLLHQGGF
HHHHHHHHHHHHCCC		46.6517644757
90UbiquitinationADAIQSMKILIIQAR
HHHHHHHEHHHHHHH		39.3417644757
165UbiquitinationVQSTGRAKAAFDEDG
HHHHCCHHHCCCCCC		38.6023749301
175PhosphorylationFDEDGNISNVKSDTD
CCCCCCCCCCCCCCC		39.3020377248
179PhosphorylationGNISNVKSDTDRDAE
CCCCCCCCCCCCCCC		41.2728889911
187PhosphorylationDTDRDAETVTQNEDA
CCCCCCCHHCCCHHH		30.4923749301
189PhosphorylationDRDAETVTQNEDADR
CCCCCHHCCCHHHCC		32.8517563356
199PhosphorylationEDADRNNSSRINLQD
HHHCCCCCCCCCHHH		25.2521440633
200PhosphorylationDADRNNSSRINLQDI
HHCCCCCCCCCHHHH		39.0217330950
209UbiquitinationINLQDICKDLNQEGD
CCHHHHHHHHCCCCC		66.6323749301
223UbiquitinationDDQMFVRKTSREIQG
CHHHEEHHHHHHHCC		45.6217644757
224PhosphorylationDQMFVRKTSREIQGQ
HHHEEHHHHHHHCCC		23.5824961812
225PhosphorylationQMFVRKTSREIQGQN
HHEEHHHHHHHCCCC		30.8324961812
243AcetylationLIHEDIAKAIKQLWN
CCHHHHHHHHHHHHH		51.4824489116
280UbiquitinationYYFDNIEKFASPNYV
EEECCHHHHCCCCCE		42.2917644757
295UbiquitinationCTDEDILKGRIKTTG
ECCHHHHCCCCCCCC		46.6123749301
301PhosphorylationLKGRIKTTGITETEF
HCCCCCCCCCCEEEE		22.9119779198
312PhosphorylationETEFNIGSSKFKVLD
EEEEECCCCEEEEEC		26.9319779198
313PhosphorylationTEFNIGSSKFKVLDA
EEEECCCCEEEEECC		36.5828889911
314AcetylationEFNIGSSKFKVLDAG
EEECCCCEEEEECCC		51.4024489116
396AcetylationKIDLFEEKVKSMPIR
CHHHHHHHHHCCCHH		48.0024489116
421AcetylationGDAEAGLKYFEKIFL
CCHHHHHHHHHHHHH		47.1524489116
425UbiquitinationAGLKYFEKIFLSLNK
HHHHHHHHHHHHCCC		28.9423749301
429PhosphorylationYFEKIFLSLNKTNKP
HHHHHHHHCCCCCCC		21.1021126336
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
3CMyristoylation

8942643
3CPalmitoylation

8942643
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of GPA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GBG_YEASTSTE18physical
11394869
GBB_YEASTSTE4physical
11394869
FUS3_YEASTFUS3physical
12029138
SST2_YEASTSST2physical
8756677
STE2_YEASTSTE2physical
11287148
GBB_YEASTSTE4physical
10664449
SC160_YEASTSCP160physical
14536090
GBB_YEASTSTE4physical
8702760
GBG_YEASTSTE18physical
8702760
GBB_YEASTSTE4physical
9604890
GBB_YEASTSTE4physical
15197187
STE2_YEASTSTE2physical
15197187
GBB_YEASTSTE4physical
8164677
GBB_YEASTSTE4physical
8942643
CG12_YEASTCLN2genetic
7926787
SYG1_YEASTSYG1genetic
7592711
SCH9_YEASTSCH9genetic
10361302
FNTB_YEASTRAM1genetic
3137119
BUR1_YEASTSGV1genetic
1828190
FUS3_YEASTFUS3genetic
2407613
STE2_YEASTSTE2genetic
3065623
GBB_YEASTSTE4genetic
3065623
STE5_YEASTSTE5genetic
3065623
STE7_YEASTSTE7genetic
3065623
STE11_YEASTSTE11genetic
3065623
STE12_YEASTSTE12genetic
3065623
GBB_YEASTSTE4genetic
9858568
RPN4_YEASTRPN4genetic
9307963
RPN2_YEASTRPN2genetic
9307963
SST2_YEASTSST2physical
16467474
RGS2_YEASTRGS2physical
16467474
MDM1_YEASTMDM1physical
16467474
RAX1_YEASTRAX1physical
16467474
FUS3_YEASTFUS3genetic
2078866
GBB_YEASTSTE4genetic
7796906
VPS15_YEASTVPS15physical
16839886
VPS34_YEASTVPS34physical
16839886
GBB_YEASTSTE4physical
11283351
FUS3_YEASTFUS3genetic
2406028
FUS3_YEASTFUS3physical
18261907
GET3_YEASTGET3physical
18261907
REG1_YEASTREG1physical
18261907
SP110_YEASTSPC110physical
18261907
MDM31_YEASTMDM31physical
18261907
NAA40_YEASTNAT4physical
18261907
CTU2_YEASTNCS2physical
18261907
KAR3_YEASTKAR3physical
19386762
KAR3_YEASTKAR3genetic
19386762
GBB_YEASTSTE4physical
19820940
GBB_YEASTSTE4physical
19445518
MET30_YEASTMET30physical
15687504
GBG_YEASTSTE18physical
19079053
SST2_YEASTSST2genetic
11779797
STE2_YEASTSTE2genetic
8307334
STE3_YEASTSTE3genetic
8307334
ELM1_YEASTELM1physical
21521692
GPA1_YEASTGPA1physical
22940862
SAK1_YEASTSAK1physical
24003255
REG1_YEASTREG1physical
24003255
GPR1_YEASTGPR1genetic
25044394
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GPA1_YEAST

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Regulation of membrane and subunit interactions by N-myristoylationof a G protein alpha subunit in yeast.";
Song J., Hirschman J., Gunn K., Dohlman H.G.;
J. Biol. Chem. 271:20273-20283(1996).
Cited for: MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2, AND SUBCELLULARLOCATION.
"Pheromone action regulates G-protein alpha-subunit myristoylation inthe yeast Saccharomyces cerevisiae.";
Dohlman H.G., Goldsmith P., Spiegel A.M., Thorner J.;
Proc. Natl. Acad. Sci. U.S.A. 90:9688-9692(1993).
Cited for: MYRISTOYLATION AT GLY-2.
"N-myristoylation is required for function of the pheromone-responsiveG alpha protein of yeast: conditional activation of the pheromoneresponse 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).
Cited for: MYRISTOYLATION AT GLY-2.
Palmitoylation
ReferencePubMed
"Characterization of Saccharomyces cerevisiae acyl-proteinthioesterase 1, the enzyme responsible for G protein alpha subunitdeacylation in vivo.";
Duncan J.A., Gilman A.G.;
J. Biol. Chem. 277:31740-31752(2002).
Cited for: DEPALMITOYLATION.
"Dual lipid modification motifs in G(alpha) and G(gamma) subunits arerequired for full activity of the pheromone response pathway inSaccharomyces cerevisiae.";
Manahan C.L., Patnana M., Blumer K.J., Linder M.E.;
Mol. Biol. Cell 11:957-968(2000).
Cited for: PALMITOYLATION AT CYS-3, AND MUTAGENESIS OF GLY-2 AND CYS-3.
"Partial constitutive activation of pheromone responses by apalmitoylation-site mutant of a G protein alpha subunit in yeast.";
Song J., Dohlman H.G.;
Biochemistry 35:14806-14817(1996).
Cited for: PALMITOYLATION AT CYS-3, AND MUTAGENESIS OF GLY-2 AND CYS-3.
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189 AND SER-200, ANDMASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Direct identification of a G protein ubiquitination site by massspectrometry.";
Marotti L.A. Jr., Newitt R., Wang Y., Aebersold R., Dohlman H.G.;
Biochemistry 41:5067-5074(2002).
Cited for: UBIQUITINATION AT LYS-165, MUTAGENESIS OF LYS-165, AND MASSSPECTROMETRY.

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