GYS1_YEAST - dbPTM
GYS1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GYS1_YEAST
UniProt AC P23337
Protein Name Glycogen [starch] synthase isoform 1
Gene Name GSY1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 708
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 MARDLQNHLLFEVATEVTNRVGGIYSVLKSKAPVTVAQYGDNYTLLGPLNKATYESEVEKLDWEDESIFPEELLPIQKTLMSMREKGVNFVYGNWLIEGAPRVILFELDSVRHFLNEWKADLWSLVGIPSPEHDHETNDAILLGYVVVWFLGEVSKLDSSHAIIGHFHEWLAGVALPLCRKKRIDVVTIFTTHATLLGRYLCAAGDVDFYNNLQYFDVDQEAGKRGIYHRYCIERAAAHTADVFTTVSQITALEAEHLLKRKPDGILPNGLNVVKFQAVHEFQNLHALKKDKINDFVRGHFHGCFDFDLDNTVYFFIAGRYEYKNKGADMFIESLARLNYRLKVSGSKKTVVAFLIMPAKTNSFTVEALKSQAIVKSLENTVNEVTASIGKRIFEHTMRYPHNGLESELPTNLDELLKSSEKVLLKKRVLALRRPYGELPPVVTHNMCDDANDPILNQIRHVRLFNDSSDRVKVIFHPEFLNANNPILGLDYDEFVRGCHLGVFPSYYEPWGYTPAECTVMGVPSITTNVSGFGAYMEDLIETDQAKDYGIYIVDRRFKSPDESVEQLADYMEEFVNKTRRQRINQRNRTERLSDLLDWKRMGLEYVKARQLGLRRAYPEQFKQLVGETISDANMNTLAGGKKFKIARPLSVPGSPKVRSNSTVYMTPGDLGTLQDANNADDYFNLSTNGAIDNDDDDNDTSAYYEDN
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
29AcetylationGGIYSVLKSKAPVTV
CCHHHHHHCCCCEEE		47.9924489116
56PhosphorylationLNKATYESEVEKLDW
CCCCCCHHHHHHCCC		36.2127717283
159PhosphorylationGEVSKLDSSHAIIGH
HCHHCCCCCCCHHHH		34.16-
363PhosphorylationIMPAKTNSFTVEALK
EEECCCCCEEHHHHH		27.76-
371PhosphorylationFTVEALKSQAIVKSL
EEHHHHHHHHHHHHH		26.2028889911
386PhosphorylationENTVNEVTASIGKRI
HHHHHHHHHHHHHHH		14.4424961812
388PhosphorylationTVNEVTASIGKRIFE
HHHHHHHHHHHHHHH		23.6224961812
391UbiquitinationEVTASIGKRIFEHTM
HHHHHHHHHHHHHHC		40.4224961812
418AcetylationTNLDELLKSSEKVLL
CCHHHHHHHCHHHHH		65.6424489116
419PhosphorylationNLDELLKSSEKVLLK
CHHHHHHHCHHHHHH		43.6419779198
468PhosphorylationHVRLFNDSSDRVKVI
EEEEECCCCCCEEEE		34.9322369663
469PhosphorylationVRLFNDSSDRVKVIF
EEEECCCCCCEEEEE		32.0922369663
560PhosphorylationIVDRRFKSPDESVEQ
EEECCCCCCCHHHHH		34.57-
600UbiquitinationLSDLLDWKRMGLEYV
HHHHHHHHHHCHHHH		31.9723749301
629PhosphorylationFKQLVGETISDANMN
HHHHHCCCCCHHCCC		21.6122369663
631PhosphorylationQLVGETISDANMNTL
HHHCCCCCHHCCCCC		37.7822369663
637PhosphorylationISDANMNTLAGGKKF
CCHHCCCCCCCCCCE		13.7622369663
651PhosphorylationFKIARPLSVPGSPKV
EEECEECCCCCCCCC		29.0222369663
655PhosphorylationRPLSVPGSPKVRSNS
EECCCCCCCCCCCCC		18.5822369663
660PhosphorylationPGSPKVRSNSTVYMT
CCCCCCCCCCEEEEC		37.81-
662PhosphorylationSPKVRSNSTVYMTPG
CCCCCCCCEEEECCC		22.09-
667PhosphorylationSNSTVYMTPGDLGTL
CCCEEEECCCCCCCC		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
660SPhosphorylationKinasePKA-Uniprot
662SPhosphorylationKinasePKA-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GYS1_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 GYS1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GLG1_YEASTGLG1physical
16554755
GYS2_YEASTGSY2physical
16554755
GYS1_YEASTGSY1physical
11283351
GLG2_YEASTGLG2physical
11283351
GYS2_YEASTGSY2physical
11283351
HSP7Q_YEASTSSQ1physical
19536198
SSB1_YEASTSSB1physical
19536198
GYS2_YEASTGSY2genetic
16941010
GYS2_YEASTGSY2physical
20826334
ERG2_YEASTERG2genetic
21623372
FOLE_YEASTMET7genetic
21623372
ADH3_YEASTADH3genetic
21623372
UBP8_YEASTUBP8genetic
27708008
NEW1_YEASTNEW1genetic
27708008
PEX22_YEASTPEX22genetic
27708008
HAP3_YEASTHAP3genetic
27708008
NPL4_YEASTNPL4genetic
27708008
MBA1_YEASTMBA1genetic
27708008
UGX2_YEASTUGX2genetic
27708008
ATIF_YEASTINH1genetic
27708008
ARO1_YEASTARO1genetic
27708008
UME6_YEASTUME6genetic
27708008
GNTK_YEASTYDR248Cgenetic
27708008
OMS1_YEASTOMS1genetic
27708008
LSM6_YEASTLSM6genetic
27708008
GMC1_YEASTGMC1genetic
27708008
PT122_YEASTPET122genetic
27708008
RAD4_YEASTRAD4genetic
27708008
MRM2_YEASTMRM2genetic
27708008
CLG1_YEASTCLG1genetic
27708008
YG5B_YEASTYGR250Cgenetic
27708008
SODM_YEASTSOD2genetic
27708008
COX23_YEASTCOX23genetic
27708008
SDS3_YEASTSDS3genetic
27708008
YJ24_YEASTKCH1genetic
27708008
FABG_YEASTOAR1genetic
27708008
HAP4_YEASTHAP4genetic
27708008
AEP2_YEASTAEP2genetic
27708008
GAS1_YEASTGAS1genetic
27708008
COX5A_YEASTCOX5Agenetic
27708008
APJ1_YEASTAPJ1genetic
27708008
NIS1_YEASTNIS1genetic
27708008
TRM10_YEASTTRM10genetic
27708008
HMI1_YEASTHMI1genetic
27708008
RTC1_YEASTRTC1genetic
27708008
OST3_YEASTOST3genetic
27708008
RFM1_YEASTRFM1genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
YP153_YEASTYPR153Wgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GYS1_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-651 AND SER-655, 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 SER-651 AND SER-655, ANDMASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, ANDMASS 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.

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