GYS2_YEAST - dbPTM
GYS2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GYS2_YEAST
UniProt AC P27472
Protein Name Glycogen [starch] synthase isoform 2
Gene Name GSY2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 705
Subcellular Localization
Protein Description Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis of glycogen..
Protein Sequence MSRDLQNHLLFETATEVANRVGGIYSVLKSKAPITVAQYKDHYHLIGPLNKATYQNEVDILDWKKPEAFSDEMRPVQHALQTMESRGVHFVYGRWLIEGAPKVILFDLDSVRGYSNEWKGDLWSLVGIPSPENDFETNDAILLGYTVAWFLGEVAHLDSQHAIVAHFHEWLAGVALPLCRKRRIDVVTIFTTHATLLGRYLCASGSFDFYNCLESVDVDHEAGRFGIYHRYCIERAAAHSADVFTTVSQITAFEAEHLLKRKPDGILPNGLNVIKFQAFHEFQNLHALKKEKINDFVRGHFHGCFDFDLDNTLYFFIAGRYEYKNKGADMFIEALARLNYRLKVSGSKKTVVAFIVMPAKNNSFTVEALKGQAEVRALENTVHEVTTSIGKRIFDHAIRYPHNGLTTELPTDLGELLKSSDKVMLKRRILALRRPEGQLPPIVTHNMVDDANDLILNKIRQVQLFNSPSDRVKMIFHPEFLNANNPILGLDYDEFVRGCHLGVFPSYYEPWGYTPAECTVMGVPSITTNVSGFGAYMEDLIETNQAKDYGIYIVDRRFKAPDESVEQLVDYMEEFVKKTRRQRINQRNRTERLSDLLDWKRMGLEYVKARQLALRRGYPDQFRELVGEELNDSNMDALAGGKKLKVARPLSVPGSPRDLRSNSTVYMTPGDLGTLQEVNNADDYFSLGVNPAADDDDDGPYADDS
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
31UbiquitinationIYSVLKSKAPITVAQ
HHHHHHHCCCEEEEE		57.5023749301
35PhosphorylationLKSKAPITVAQYKDH
HHHCCCEEEEEECCC		14.5522369663
39PhosphorylationAPITVAQYKDHYHLI
CCEEEEEECCCEEEE		14.5122369663
40AcetylationPITVAQYKDHYHLIG
CEEEEEECCCEEEEC		26.4222865919
159PhosphorylationGEVAHLDSQHAIVAH
HHHHCCCCCCHHHHH		30.17-
260UbiquitinationFEAEHLLKRKPDGIL
HHHHHHHHCCCCCCC		65.8123749301
289AcetylationFQNLHALKKEKINDF
HHCHHHHHHHHHCHH		60.7222865919
363PhosphorylationVMPAKNNSFTVEALK
EEECCCCCEEHHHHH		31.5222369663
365PhosphorylationPAKNNSFTVEALKGQ
ECCCCCEEHHHHHCH		19.7722369663
391UbiquitinationEVTTSIGKRIFDHAI
HHHHHHHHHHHHHHH		40.4224961812
418AcetylationTDLGELLKSSDKVML
CCHHHHHCCCCHHHH		61.6124489116
419PhosphorylationDLGELLKSSDKVMLK
CHHHHHCCCCHHHHH		43.6826447709
420PhosphorylationLGELLKSSDKVMLKR
HHHHHCCCCHHHHHH		39.6026447709
467PhosphorylationRQVQLFNSPSDRVKM
HHEECCCCHHHHEEE		20.6022369663
469PhosphorylationVQLFNSPSDRVKMIF
EECCCCHHHHEEEEE		37.5622369663
600UbiquitinationLSDLLDWKRMGLEYV
HHHHHHHHHHCHHHH		31.9723749301
651PhosphorylationLKVARPLSVPGSPRD
CEECEECCCCCCCCC		29.0222369663
655PhosphorylationRPLSVPGSPRDLRSN
EECCCCCCCCCCCCC		15.6422369663
661PhosphorylationGSPRDLRSNSTVYMT
CCCCCCCCCCEEEEC		42.29-
663PhosphorylationPRDLRSNSTVYMTPG
CCCCCCCCEEEECCC		22.09-
668PhosphorylationSNSTVYMTPGDLGTL
CCCEEEECCCCHHCC		13.368754836
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
655SPhosphorylationKinasePHO85P17157
Uniprot
661SPhosphorylationKinasePKA-Uniprot
663SPhosphorylationKinasePKA-Uniprot
668TPhosphorylationKinasePHO85P17157
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GYS2_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 GYS2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GLG2_YEASTGLG2physical
11283351
GAC1_YEASTGAC1physical
11459182
PIG1_YEASTPIG1physical
9046081
PIG2_YEASTPIG2physical
9046081
GLG1_YEASTGLG1physical
16554755
IMB3_YEASTPSE1physical
16554755
MSH2_YEASTMSH2physical
16554755
GYS2_YEASTGSY2physical
11283351
GYS2_YEASTGSY2physical
18467557
PUR92_YEASTADE17physical
18467557
GDE_YEASTGDB1physical
18467557
GLG2_YEASTGLG2physical
10874034
GYS1_YEASTGSY1genetic
18408719
ATP10_YEASTATP10genetic
20093466
EOS1_YEASTEOS1genetic
20093466
YP245_YEASTYPL245Wgenetic
20093466
INP53_YEASTINP53genetic
21623372
AMYG_YEASTSGA1genetic
21623372
6PGD1_YEASTGND1genetic
21623372
TPS2_YEASTTPS2genetic
21623372
PHO89_YEASTPHO89genetic
21623372
GYS2_YEASTGSY2physical
22615397
GYS2_YEASTGSY2physical
21835915
ATP10_YEASTATP10genetic
27708008
YP245_YEASTYPL245Wgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GYS2_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-467; SER-651 ANDSER-655, AND MASS 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 SER-467; SER-651 ANDSER-655, AND MASS SPECTROMETRY.
"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 SER-651 AND SER-655, ANDMASS SPECTROMETRY.
"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-651 AND SER-655, ANDMASS SPECTROMETRY.
"Cyclin partners determine Pho85 protein kinase substrate specificityin vitro and in vivo: control of glycogen biosynthesis by Pcl8 andPcl10.";
Huang D., Moffat J., Wilson W.A., Moore L., Cheng C., Roach P.J.,Andrews B.J.;
Mol. Cell. Biol. 18:3289-3299(1998).
Cited for: PHOSPHORYLATION AT SER-655 AND THR-668.

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