GPA2_YEAST - dbPTM
GPA2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPA2_YEAST
UniProt AC P10823
Protein Name Guanine nucleotide-binding protein alpha-2 subunit
Gene Name GPA2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 449
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side .
Protein Description Alpha subunit of the heterotrimeric guanine nucleotide-binding protein (G protein) involved in glucose-induced cAMP signaling. Binds to its cognate transmembrane receptor GPR1, which senses extracellular carbon sources, and activates cAMP-PKA signaling and governs diploid pseudohyphal differentiation and haploid invasive growth. The G protein beta-mimic proteins GPB1 and GPB2 inhibit GPA2-GPR1 coupling, probably to reduce signaling in the absence of glucose..
Protein Sequence MGLCASSEKNGSTPDTQTASAGSDNVGKAKVPPKQEPQKTVRTVNTANQQEKQQQRQQQPSPHNVKDRKEQNGSINNAISPTATANTSGSQQINIDSALRDRSSNVAAQPSLSDASSGSNDKELKVLLLGAGESGKSTVLQQLKILHQNGFSEQEIKEYIPLIYQNLLEIGRNLIQARTRFNVNLEPECELTQQDLSRTMSYEMPNNYTGQFPEDIAGVISTLWALPSTQDLVNGPNASKFYLMDSTPYFMENFTRITSPNYRPTQQDILRSRQMTSGIFDTVIDMGSDIKMHIYDVGGQRSERKKWIHCFDNVTLVIFCVSLSEYDQTLMEDKNQNRFQESLVLFDNIVNSRWFARTSVVLFLNKIDLFAEKLSKVPMENYFPDYTGGSDINKAAKYILWRFVQLNRANLSIYPHVTQATDTSNIRLVFAAIKETILENTLKDSGVLQ
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------MGLCASSEK
------CCCCCCCCC		29.48-
2Myristoylation------MGLCASSEK
------CCCCCCCCC		29.4816030250
4S-palmitoylation----MGLCASSEKNG
----CCCCCCCCCCC		2.6016030250
9UbiquitinationGLCASSEKNGSTPDT
CCCCCCCCCCCCCCC		69.4317644757
12PhosphorylationASSEKNGSTPDTQTA
CCCCCCCCCCCCCCC		46.2722369663
13PhosphorylationSSEKNGSTPDTQTAS
CCCCCCCCCCCCCCC		26.9522369663
16PhosphorylationKNGSTPDTQTASAGS
CCCCCCCCCCCCCCC		29.0822369663
18PhosphorylationGSTPDTQTASAGSDN
CCCCCCCCCCCCCCC		25.3622369663
20PhosphorylationTPDTQTASAGSDNVG
CCCCCCCCCCCCCCC		36.2322369663
23PhosphorylationTQTASAGSDNVGKAK
CCCCCCCCCCCCCCC		26.2322369663
28UbiquitinationAGSDNVGKAKVPPKQ
CCCCCCCCCCCCCCC		40.5317644757
46PhosphorylationKTVRTVNTANQQEKQ
CCEEHHHHHHHHHHH		23.7327214570
52UbiquitinationNTANQQEKQQQRQQQ
HHHHHHHHHHHHHHC		49.4123749301
61PhosphorylationQQRQQQPSPHNVKDR
HHHHHCCCCCCCCCH		34.1629136822
74PhosphorylationDRKEQNGSINNAISP
CHHHHCCCCCCCCCC		29.6827214570
82PhosphorylationINNAISPTATANTSG
CCCCCCCCCCCCCCC		29.8330377154
88PhosphorylationPTATANTSGSQQINI
CCCCCCCCCCCCEEC		35.9330377154
90PhosphorylationATANTSGSQQINIDS
CCCCCCCCCCEECCH		20.7628889911
103PhosphorylationDSALRDRSSNVAAQP
CHHHHCCCCCCCCCC		30.4719779198
104PhosphorylationSALRDRSSNVAAQPS
HHHHCCCCCCCCCCC		35.9027017623
111PhosphorylationSNVAAQPSLSDASSG
CCCCCCCCCCCCCCC		28.5522890988
113PhosphorylationVAAQPSLSDASSGSN
CCCCCCCCCCCCCCC		35.1522890988
116PhosphorylationQPSLSDASSGSNDKE
CCCCCCCCCCCCHHH		39.9822890988
117PhosphorylationPSLSDASSGSNDKEL
CCCCCCCCCCCHHHE		48.2222369663
119PhosphorylationLSDASSGSNDKELKV
CCCCCCCCCHHHEEE		43.7522369663
122UbiquitinationASSGSNDKELKVLLL
CCCCCCHHHEEEEEE		70.0223749301
122AcetylationASSGSNDKELKVLLL
CCCCCCHHHEEEEEE		70.0224489116
136UbiquitinationLGAGESGKSTVLQQL
ECCCCCCHHHHHHHH		52.8424961812
242PhosphorylationGPNASKFYLMDSTPY
CCCCHHEEECCCCCC		12.5927017623
247PhosphorylationKFYLMDSTPYFMENF
HEEECCCCCCHHHHC		20.1127017623
249PhosphorylationYLMDSTPYFMENFTR
EECCCCCCHHHHCCC		18.6927017623
342PhosphorylationNQNRFQESLVLFDNI
CCCCHHHHHHHHHCH		17.0030377154
352PhosphorylationLFDNIVNSRWFARTS
HHHCHHCCCHHHHHH		21.7230377154
373AcetylationKIDLFAEKLSKVPME
HHHHHHHHHCCCCHH		55.4124489116
375PhosphorylationDLFAEKLSKVPMENY
HHHHHHHCCCCHHHC		42.5527017623
382PhosphorylationSKVPMENYFPDYTGG
CCCCHHHCCCCCCCC		11.8127017623
390PhosphorylationFPDYTGGSDINKAAK
CCCCCCCCCHHHHHH		36.3427017623
394UbiquitinationTGGSDINKAAKYILW
CCCCCHHHHHHHHHH		50.4823749301
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

Oops, there are no upstream regulatory protein records of GPA2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
2GMyristoylation

12150916
2GPalmitoylation

12150916
4CMyristoylation

16030250
4CPalmitoylation

16030250
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 GPA2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FAR8_YEASTFAR8physical
11805837
IDH1_YEASTIDH1physical
11805837
GPA1_YEASTGPA1physical
11805837
PMA2_YEASTPMA2physical
11805837
SYEC_YEASTGUS1physical
11805837
GPR1_YEASTGPR1physical
10514491
PLC1_YEASTPLC1physical
10514491
FUS3_YEASTFUS3physical
12867033
KSS1_YEASTKSS1physical
12867033
GPB1_YEASTGPB1physical
12150916
GPB2_YEASTGPB2physical
12150916
IME2_YEASTIME2physical
10454558
RGS2_YEASTRGS2physical
10523302
GPG1_YEASTGPG1physical
12150916
GPR1_YEASTGPR1physical
12150916
GPR1_YEASTGPR1physical
9388468
GPR1_YEASTGPR1physical
9524122
GPB2_YEASTGPB2physical
12538771
RAS2_YEASTRAS2genetic
9384580
SCH9_YEASTSCH9genetic
10361302
GPA1_YEASTGPA1genetic
9524122
RAS2_YEASTRAS2genetic
9524122
RAS2_YEASTRAS2genetic
9252333
CYAA_YEASTCYR1genetic
10411752
GPR1_YEASTGPR1genetic
9813141
NOT5_YEASTNOT5genetic
11929548
KAPB_YEASTTPK2genetic
10373537
FOB1_YEASTFOB1genetic
15328540
SIR2_YEASTSIR2genetic
15328540
GPB2_YEASTGPB2physical
16924114
CYAA_YEASTCYR1physical
16924114
IME2_YEASTIME2physical
17584745
GPB2_YEASTGPB2physical
17584745
MEP3_YEASTMEP3physical
18467557
TPO4_YEASTTPO4physical
18467557
TPO2_YEASTTPO2physical
18467557
YG3A_YEASTYGR130Cphysical
18467557
MID2_YEASTMID2physical
18467557
MEP1_YEASTMEP1physical
18467557
YL326_YEASTYLR326Wphysical
18467557
HNM1_YEASTHNM1physical
18467557
WSC2_YEASTWSC2physical
18467557
FLC1_YEASTFLC1physical
18467557
YOR1_YEASTYOR1physical
18467557
YGK8_YEASTYGL108Cphysical
18467557
PDR12_YEASTPDR12physical
18467557
YL413_YEASTINA1physical
18467557
OSH6_YEASTOSH6physical
18467557
MUP1_YEASTMUP1physical
18467557
SLM1_YEASTSLM1physical
18467557
TPO3_YEASTTPO3physical
18467557
DUR3_YEASTDUR3physical
18467557
FTR1_YEASTFTR1physical
18467557
SFK1_YEASTSFK1physical
18467557
YJB6_YEASTYJL016Wphysical
18467557
WSC3_YEASTWSC3physical
18467557
OSH7_YEASTOSH7physical
18467557
SUT2_YEASTSUT2genetic
15030478
RAS1_YEASTRAS1genetic
15030478
RAS2_YEASTRAS2genetic
20826609
GPB1_YEASTGPB1genetic
20826609
GPB2_YEASTGPB2genetic
20826609
TSA1_YEASTTSA1genetic
21884982
SIR2_YEASTSIR2genetic
21902802
GPR1_YEASTGPR1genetic
18622617
MEP3_YEASTMEP3physical
22615397
UBA5_HUMANUBA5physical
27107014
NUCB1_HUMANNUCB1physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GPA2_YEAST

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Related Literatures of Post-Translational Modification
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-90 AND SER-119, 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 SER-117, AND MASSSPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-23, AND MASSSPECTROMETRY.

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