PHSG_YEAST - dbPTM
PHSG_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHSG_YEAST
UniProt AC P06738
Protein Name Glycogen phosphorylase
Gene Name GPH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 902
Subcellular Localization
Protein Description Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties..
Protein Sequence MPPASTSTTNDMITEEPTSPHQIPRLTRRLTGFLPQEIKSIDTMIPLKSRALWNKHQVKKFNKAEDFQDRFIDHVETTLARSLYNCDDMAAYEAASMSIRDNLVIDWNKTQQKFTTRDPKRVYYLSLEFLMGRALDNALINMKIEDPEDPAASKGKPREMIKGALDDLGFKLEDVLDQEPDAGLGNGGLGRLAACFVDSMATEGIPAWGYGLRYEYGIFAQKIIDGYQVETPDYWLNSGNPWEIERNEVQIPVTFYGYVDRPEGGKTTLSASQWIGGERVLAVAYDFPVPGFKTSNVNNLRLWQARPTTEFDFAKFNNGDYKNSVAQQQRAESITAVLYPNDNFAQGKELRLKQQYFWCAASLHDILRRFKKSKRPWTEFPDQVAIQLNDTHPTLAIVELQRVLVDLEKLDWHEAWDIVTKTFAYTNHTVMQEALEKWPVGLFGHLLPRHLEIIYDINWFFLQDVAKKFPKDVDLLSRISIIEENSPERQIRMAFLAIVGSHKVNGVAELHSELIKTTIFKDFVKFYGPSKFVNVTNGITPRRWLKQANPSLAKLISETLNDPTEEYLLDMAKLTQLGKYVEDKEFLKKWNQVKLNNKIRLVDLIKKENDGVDIINREYLDDTLFDMQVKRIHEYKRQQLNVFGIIYRYLAMKNMLKNGASIEEVAKKYPRKVSIFGGKSAPGYYMAKLIIKLINCVADIVNNDESIEHLLKVVFVADYNVSKAEIIIPASDLSEHISTAGTEASGTSNMKFVMNGGLIIGTVDGANVEITREIGEDNVFLFGNLSENVEELRYNHQYHPQDLPSSLDSVLSYIESGQFSPENPNEFKPLVDSIKYHGDYYLVSDDFESYLATHELVDQEFHNQRSEWLKKSVLSVANVGFFSSDRCIEEYSDTIWNVEPVT
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
5Phosphorylation---MPPASTSTTNDM
---CCCCCCCCCCCC		28.7622369663
6Phosphorylation--MPPASTSTTNDMI
--CCCCCCCCCCCCC		32.0022369663
7Phosphorylation-MPPASTSTTNDMIT
-CCCCCCCCCCCCCC		30.6422369663
8PhosphorylationMPPASTSTTNDMITE
CCCCCCCCCCCCCCC		29.7022369663
9PhosphorylationPPASTSTTNDMITEE
CCCCCCCCCCCCCCC		29.0522369663
14PhosphorylationSTTNDMITEEPTSPH
CCCCCCCCCCCCCHH		27.8824909858
18PhosphorylationDMITEEPTSPHQIPR
CCCCCCCCCHHHHHH		59.1622369663
19PhosphorylationMITEEPTSPHQIPRL
CCCCCCCCHHHHHHH		30.9722369663
27PhosphorylationPHQIPRLTRRLTGFL
HHHHHHHHHHHHCCC		18.287592925
31PhosphorylationPRLTRRLTGFLPQEI
HHHHHHHHCCCCHHH		24.8722369663
39AcetylationGFLPQEIKSIDTMIP
CCCCHHHHCCCCCCC		40.3824489116
43PhosphorylationQEIKSIDTMIPLKSR
HHHHCCCCCCCCCHH		18.4828889911
63AcetylationHQVKKFNKAEDFQDR
HHHHHCCCHHHHHHH		57.1822865919
77PhosphorylationRFIDHVETTLARSLY
HHHHHHHHHHHHHHC		26.4822369663
78PhosphorylationFIDHVETTLARSLYN
HHHHHHHHHHHHHCC		12.6222369663
82PhosphorylationVETTLARSLYNCDDM
HHHHHHHHHCCCCHH		29.6028889911
109AcetylationNLVIDWNKTQQKFTT
CEEECCCCCCCCCCC		43.3824489116
143UbiquitinationDNALINMKIEDPEDP
HHHHHCCEECCCCCH		38.1623749301
143AcetylationDNALINMKIEDPEDP
HHHHHCCEECCCCCH		38.1624489116
267PhosphorylationDRPEGGKTTLSASQW
CCCCCCCEEEEHHHE		35.9222369663
268PhosphorylationRPEGGKTTLSASQWI
CCCCCCEEEEHHHEE		23.3822369663
270PhosphorylationEGGKTTLSASQWIGG
CCCCEEEEHHHEECC		24.6322369663
272PhosphorylationGKTTLSASQWIGGER
CCEEEEHHHEECCEE		23.7522369663
293UbiquitinationDFPVPGFKTSNVNNL
ECCCCCCCCCCCCCE		57.8924961812
294PhosphorylationFPVPGFKTSNVNNLR
CCCCCCCCCCCCCEE		24.2322369663
295PhosphorylationPVPGFKTSNVNNLRL
CCCCCCCCCCCCEEE		39.0922369663
308PhosphorylationRLWQARPTTEFDFAK
EEEECCCCCCCCCCC		33.1422369663
309PhosphorylationLWQARPTTEFDFAKF
EEECCCCCCCCCCCC		37.0222369663
322UbiquitinationKFNNGDYKNSVAQQQ
CCCCCCCCCHHHHHH		47.7023749301
324PhosphorylationNNGDYKNSVAQQQRA
CCCCCCCHHHHHHHH		18.0628889911
333PhosphorylationAQQQRAESITAVLYP
HHHHHHHHCEEEECC		25.0125752575
335PhosphorylationQQRAESITAVLYPND
HHHHHHCEEEECCCC		21.7128889911
348UbiquitinationNDNFAQGKELRLKQQ
CCCCCCCCHHHHHHH		41.3124961812
471AcetylationDVAKKFPKDVDLLSR
HHHHHCCCCHHHHHH		73.7924489116
521AcetylationLIKTTIFKDFVKFYG
HHHHHHHHHHHHHHC		46.5424489116
525AcetylationTIFKDFVKFYGPSKF
HHHHHHHHHHCCHHH		32.6324489116
551PhosphorylationWLKQANPSLAKLISE
HHHHHCHHHHHHHHH		40.5425752575
5792-HydroxyisobutyrylationAKLTQLGKYVEDKEF
HHHHHHHCHHCCHHH		55.50-
579AcetylationAKLTQLGKYVEDKEF
HHHHHHHCHHCCHHH		55.5025381059
580PhosphorylationKLTQLGKYVEDKEFL
HHHHHHCHHCCHHHH		13.7921126336
584AcetylationLGKYVEDKEFLKKWN
HHCHHCCHHHHHHHC		36.5424489116
6062-HydroxyisobutyrylationIRLVDLIKKENDGVD
EEHHHHHHHHCCCCC		62.42-
606AcetylationIRLVDLIKKENDGVD
EEHHHHHHHHCCCCC		62.4224489116
6072-HydroxyisobutyrylationRLVDLIKKENDGVDI
EHHHHHHHHCCCCCC		55.55-
674PhosphorylationKKYPRKVSIFGGKSA
HHCCCEEEEECCCCC		18.4227017623
684PhosphorylationGGKSAPGYYMAKLII
CCCCCCHHHHHHHHH		6.7627017623
685PhosphorylationGKSAPGYYMAKLIIK
CCCCCHHHHHHHHHH		9.1227017623
722PhosphorylationFVADYNVSKAEIIIP
EEEECCCCCCEEEEE		23.6328889911
751OtherASGTSNMKFVMNGGL
CCCCCCCEEEEECCE		38.77-
751N6-(pyridoxal phosphate)lysineASGTSNMKFVMNGGL
CCCCCCCEEEEECCE		38.77-
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 PHSG_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHSG_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 PHSG_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SODC_YEASTSOD1genetic
18804161
SODM_YEASTSOD2genetic
18804161
THRC_YEASTTHR4genetic
27708008
MGR1_YEASTMGR1genetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
QRI7_YEASTQRI7genetic
27708008
CYK3_YEASTCYK3genetic
27708008
MRX8_YEASTYDR336Wgenetic
27708008
PUF6_YEASTPUF6genetic
27708008
HSP12_YEASTHSP12genetic
27708008
YG2G_YEASTYGR079Wgenetic
27708008
HPM1_YEASTHPM1genetic
27708008
CSM2_YEASTCSM2genetic
27708008
YIQ6_YEASTYIL166Cgenetic
27708008
MET28_YEASTMET28genetic
27708008
YJC8_YEASTYJL028Wgenetic
27708008
SDHX_YEASTYJL045Wgenetic
27708008
PRY1_YEASTPRY1genetic
27708008
IME2_YEASTIME2genetic
27708008
PIR5_YEASTYJL160Cgenetic
27708008
YJ24_YEASTKCH1genetic
27708008
MOG1_YEASTMOG1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
IME1_YEASTIME1genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
MDM35_YEASTMDM35genetic
27708008
FABG_YEASTOAR1genetic
27708008
DGR2_YEASTDGR2genetic
27708008
PGM1_YEASTPGM1genetic
27708008
EMC3_YEASTEMC3genetic
27708008
SA190_YEASTSAP190genetic
27708008
RS21A_YEASTRPS21Agenetic
27708008
MTD1_YEASTMTD1genetic
27708008
RL40A_YEASTRPL40Bgenetic
27708008
RL40B_YEASTRPL40Bgenetic
27708008
PCKA_YEASTPCK1genetic
27708008
POM33_YEASTPOM33genetic
27708008
RSSA2_YEASTRPS0Bgenetic
27708008
ENV10_YEASTENV10genetic
27708008
XDJ1_YEASTXDJ1genetic
27708008
SPSY_YEASTSPE4genetic
27708008
SWI6_YEASTSWI6genetic
27708008
YL225_YEASTYLR225Cgenetic
27708008
PEX30_YEASTPEX30genetic
27708008
TO6BL_YEASTREC102genetic
27708008
HMDH2_YEASTHMG2genetic
27708008
GTR1_YEASTGTR1genetic
27708008
GBLP_YEASTASC1genetic
27708008
HSC82_YEASTHSC82genetic
27708008
RAD14_YEASTRAD14genetic
27708008
IDHH_YEASTIDP3genetic
27708008
SIW14_YEASTSIW14genetic
27708008
SNAPN_YEASTSNN1genetic
27708008
RAS2_YEASTRAS2genetic
27708008
RM50_YEASTMRPL50genetic
27708008
FRE7_YEASTFRE7genetic
27708008
AZF1_YEASTAZF1genetic
27708008
LIPA_YEASTLIP5genetic
27708008
CHL1_YEASTCHL1genetic
27708008
CWC27_YEASTCWC27genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
ELP3_YEASTELP3genetic
27708008
DAP1_YEASTDAP1genetic
27708008
YIG1_YEASTYIG1genetic
27708008
USV1_YEASTUSV1genetic
27708008
CCZ1_YEASTCCZ1genetic
29674565
RPN6_YEASTRPN6genetic
29674565
GCN20_YEASTGCN20genetic
29674565
GCN1_YEASTGCN1genetic
29674565
ZPR1_YEASTZPR1genetic
29674565
RS21B_YEASTRPS21Bgenetic
29674565
YJ9I_YEASTYJR141Wgenetic
29674565
XPOT_YEASTLOS1genetic
29674565
SIS2_YEASTSIS2genetic
29674565
PSP2_YEASTPSP2genetic
29674565
AHC1_YEASTAHC1genetic
29674565
DYR_YEASTDFR1genetic
29674565
CEM1_YEASTCEM1genetic
29674565
ESA1_YEASTESA1genetic
29674565
RU2A_YEASTLEA1genetic
29674565
SHE1_YEASTSHE1genetic
29674565
RS6A_YEASTRPS6Bgenetic
29674565
RS6B_YEASTRPS6Bgenetic
29674565
MIX14_YEASTMIX14genetic
29674565
ARO1_YEASTARO1genetic
29674565
RPB7_YEASTRPB7genetic
29674565
BLM10_YEASTBLM10genetic
29674565
VAM7_YEASTVAM7genetic
29674565
BTN1_YEASTYHC3genetic
29674565
ASF1_YEASTASF1genetic
29674565
HSP72_YEASTSSA2genetic
29674565
VPS13_YEASTVPS13genetic
29674565
POM34_YEASTPOM34genetic
29674565
NUP2_YEASTNUP2genetic
29674565
F16P_YEASTFBP1genetic
29674565
COG8_YEASTCOG8genetic
29674565
RNA1_YEASTRNA1genetic
29674565
HST3_YEASTHST3genetic
29674565
SAS5_YEASTSAS5genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHSG_YEAST

loading...

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-18; SER-19; THR-31 ANDSER-333, 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 THR-31, 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-31, AND MASSSPECTROMETRY.
"Amino acid sequence of two functional sites in yeast glycogenphosphorylase.";
Lerch K., Fischer E.H.;
Biochemistry 14:2009-2014(1975).
Cited for: PROTEIN SEQUENCE OF 30-37 AND 737-754, PHOSPHORYLATION AT THR-31, ANDPYRIDOXAL PHOSPHATE AT LYS-751.
"Purification and crystallization of glycogen phosphorylase fromSaccharomyces cerevisiae.";
Rath V.L., Hwang P.K., Fletterick R.J.;
J. Mol. Biol. 225:1027-1034(1992).
Cited for: PROTEIN SEQUENCE OF 2-10, AND PHOSPHORYLATION AT THR-31.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory