GPB1_YEAST - dbPTM
GPB1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPB1_YEAST
UniProt AC Q08886
Protein Name Guanine nucleotide-binding protein subunit beta 1
Gene Name GPB1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 897
Subcellular Localization Cytoplasm .
Protein Description Beta subunit of a guanine nucleotide-binding protein (G proteins). G proteins are involved as modulators or transducers in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Involved in the determination of the cAMP level according to nutritional conditions, most probably as a regulator of cAMP phosphodiesterase. Required for the control of pseudohyphal and haploid invasive growth..
Protein Sequence MPQASTFGSHSLEAHPLHIQPAVHIKLSKEERSHYREQYDSLKYISNYVSVFDQALSDNIDSRIRKENEALLKKYYESRKPFTFTSFRQGSVISSSDSSTGFTERTKTYCFLNDFVSNCVNEVDPYTLKMTVRNRNTALNMENLDDERKSKDDIYDFEDNTDDECNAKCHGAFHYSSERLEILRSRSTISYFKYYKKLLTVDLRDSDVLKRHNLWMPMITRRFRFLLVSSSKPEDVRLTTPIPTFSESDLDIFKNKTCPLFINGTDCVPRSYDTFSGSSVIASIFSEYKLPSLSYHCSVELNDQLFIVGGLMACHRYDEEAPDLKDFYVDGIKNLPPPLIPELINNPSMIPNPHLYCFSLTSSRLTRPDISGYIPPPLVCTQGCKLTERHIFLYGGFEIKSETQVDDKGRYFIRKRAFLNNTGYILDTVTFNFSKIELVAPPYQFAIYNNFSPRFGHMQASISNSNNNVSNENTTTSAKGRRSISPYRQGNGDHKIDDLVGSPGSTDYLEDDAIPPVTNPRSTDSLSSKHCSTATHICSSVNTILIFGGYSQTGDDKYEAMNDMWKINIPVVSRGKRNYYKFADTVTATKIPIIDDPELWPSRRAFSACCVPDYFTKDVEPIETRLLRNLKNDFSIDLEIRPGNKPSQPLFPNIPHSRKEKKSGRDSMHISNSNNSTSEDTSSKSTRNTTSSPPTSPKHTPPLNPSKKCASIGRTIAFHGGSDGYDVCSDMWWFDFDSETWTKIDLYAKTQEESDGLVPINLCMVGHSMTTVGHKVVLIGGLRQGDVDRIYRDETLPEEVISGVPLGSGVINVVDLNTQCLQGCKLIRNDGDTKESVIMDPHVGTPHQVLAVAGTIELVKGTMTLIGGVVAGREDISSLYLRGAVLQFILPSMNLAN
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
66UbiquitinationNIDSRIRKENEALLK
CHHHHHHHHHHHHHH		63.6219722269
78PhosphorylationLLKKYYESRKPFTFT
HHHHHHHHCCCEEEE		29.4924961812
83PhosphorylationYESRKPFTFTSFRQG
HHHCCCEEEEEECCC		34.2324961812
85PhosphorylationSRKPFTFTSFRQGSV
HCCCEEEEEECCCCE		24.7324961812
86PhosphorylationRKPFTFTSFRQGSVI
CCCEEEEEECCCCEE		17.7824961812
91PhosphorylationFTSFRQGSVISSSDS
EEEECCCCEEECCCC		14.1322369663
94PhosphorylationFRQGSVISSSDSSTG
ECCCCEEECCCCCCC		22.9522369663
95PhosphorylationRQGSVISSSDSSTGF
CCCCEEECCCCCCCC		27.3422369663
96PhosphorylationQGSVISSSDSSTGFT
CCCEEECCCCCCCCC		34.4222369663
98PhosphorylationSVISSSDSSTGFTER
CEEECCCCCCCCCCC		31.5722369663
99PhosphorylationVISSSDSSTGFTERT
EEECCCCCCCCCCCC		37.2222369663
100PhosphorylationISSSDSSTGFTERTK
EECCCCCCCCCCCCE		40.0222369663
103PhosphorylationSDSSTGFTERTKTYC
CCCCCCCCCCCEEEE		26.3822369663
150PhosphorylationNLDDERKSKDDIYDF
CCCCCHHCHHHCCCC		47.7621551504
161PhosphorylationIYDFEDNTDDECNAK
CCCCCCCCCCHHHHH		58.0922369663
187PhosphorylationLEILRSRSTISYFKY
HHHHHHCCHHHHHHH		31.1928889911
246PhosphorylationTTPIPTFSESDLDIF
CCCCCCCCHHHHHHH		38.3722369663
248PhosphorylationPIPTFSESDLDIFKN
CCCCCCHHHHHHHCC		42.1322369663
356PhosphorylationMIPNPHLYCFSLTSS
HCCCCEEEEEEECCC		6.6023749301
359PhosphorylationNPHLYCFSLTSSRLT
CCEEEEEEECCCCCC		27.4623749301
361PhosphorylationHLYCFSLTSSRLTRP
EEEEEEECCCCCCCC		24.3723749301
485PhosphorylationAKGRRSISPYRQGNG
CCCCCCCCCCCCCCC		19.6821551504
502PhosphorylationKIDDLVGSPGSTDYL
CCHHCCCCCCCCCCC		20.7121440633
505PhosphorylationDLVGSPGSTDYLEDD
HCCCCCCCCCCCCCC		22.8420377248
506PhosphorylationLVGSPGSTDYLEDDA
CCCCCCCCCCCCCCC		34.2821551504
508PhosphorylationGSPGSTDYLEDDAIP
CCCCCCCCCCCCCCC		16.4520377248
518PhosphorylationDDAIPPVTNPRSTDS
CCCCCCCCCCCCCCC		45.3321440633
522PhosphorylationPPVTNPRSTDSLSSK
CCCCCCCCCCCCCCC		37.5121551504
523PhosphorylationPVTNPRSTDSLSSKH
CCCCCCCCCCCCCCC		30.7725752575
525PhosphorylationTNPRSTDSLSSKHCS
CCCCCCCCCCCCCCH		30.1825752575
528PhosphorylationRSTDSLSSKHCSTAT
CCCCCCCCCCCHHHH		31.5421551504
663PhosphorylationHSRKEKKSGRDSMHI
CCCCCCCCCCCCCCC		50.5628889911
667PhosphorylationEKKSGRDSMHISNSN
CCCCCCCCCCCCCCC		15.7625704821
671PhosphorylationGRDSMHISNSNNSTS
CCCCCCCCCCCCCCC		21.3721551504
676PhosphorylationHISNSNNSTSEDTSS
CCCCCCCCCCCCCCC		37.2523749301
685PhosphorylationSEDTSSKSTRNTTSS
CCCCCCCCCCCCCCC		34.2528889911
686PhosphorylationEDTSSKSTRNTTSSP
CCCCCCCCCCCCCCC		31.5128889911
689PhosphorylationSSKSTRNTTSSPPTS
CCCCCCCCCCCCCCC		25.4321440633
690PhosphorylationSKSTRNTTSSPPTSP
CCCCCCCCCCCCCCC		30.6523749301
691PhosphorylationKSTRNTTSSPPTSPK
CCCCCCCCCCCCCCC		38.5228889911
692PhosphorylationSTRNTTSSPPTSPKH
CCCCCCCCCCCCCCC		32.5725521595
695PhosphorylationNTTSSPPTSPKHTPP
CCCCCCCCCCCCCCC		62.1319684113
696PhosphorylationTTSSPPTSPKHTPPL
CCCCCCCCCCCCCCC		37.4125521595
700PhosphorylationPPTSPKHTPPLNPSK
CCCCCCCCCCCCCCC		32.5021440633
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 GPB1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPB1_YEAST !!
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 GPB1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GPA2_YEASTGPA2physical
12150916
GPG1_YEASTGPG1physical
12150916
GPB2_YEASTGPB2genetic
12150916
IRA1_YEASTIRA1physical
16793550
IRA2_YEASTIRA2physical
16793550
KAPR_YEASTBCY1genetic
20826609
RV161_YEASTRVS161genetic
20526336
IRA2_YEASTIRA2physical
20160012
UB2D1_HUMANUBE2D1physical
20160012
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GPB1_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 THR-161 AND SER-187, ANDMASS SPECTROMETRY.
"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-161, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND MASSSPECTROMETRY.

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