PGM1_YEAST - dbPTM
PGM1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGM1_YEAST
UniProt AC P33401
Protein Name Phosphoglucomutase 1 {ECO:0000303|PubMed:5784209}
Gene Name PGM1 {ECO:0000303|PubMed:5784209}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 570
Subcellular Localization Cytoplasm .
Protein Description Minor phosphoglucomutase isozyme that catalyzes the interconversion of glucose 1-phosphate and glucose 6-phosphate. [PubMed: 5784209 Constitutes about 10-20% of the phosphoglucomutase activity in the cell]
Protein Sequence MSLLIDSVPTVAYKDQKPGTSGLRKKTKVFMDEPHYTENFIQATMQSIPNGSEGTTLVVGGDGRFYNDVIMNKIAAVGAANGVRKLVIGQGGLLSTPAASHIIRTYEEKCTGGGIILTASHNPGGPENDLGIKYNLPNGGPAPESVTNAIWEASKKLTHYKIIKNFPKLNLNKLGKNQKYGPLLVDIIDPAKAYVQFLKEIFDFDLIKSFLAKQRKDKGWKLLFDSLNGITGPYGKAIFVDEFGLPAEEVLQNWHPLPDFGGLHPDPNLTYARTLVDRVDREKIAFGAASDGDGDRNMIYGYGPAFVSPGDSVAIIAEYAPEIPYFAKQGIYGLARSFPTSSAIDRVAAKKGLRCYEVPTGWKFFCALFDAKKLSICGEESFGTGSNHIREKDGLWAIIAWLNILAIYHRRNPEKEASIKTIQDEFWNEYGRTFFTRYDYEHIECEQAEKVVALLSEFVSRPNVCGSHFPADESLTVIDCGDFSYRDLDGSISENQGLFVKFSNGTKFVLRLSGTGSSGATIRLYVEKYTDKKENYGQTADVFLKPVINSIVKFLRFKEILGTDEPTVRT
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
2Phosphorylation------MSLLIDSVP
------CCCCCCCCC		31.7030377154
2Acetylation------MSLLIDSVP
------CCCCCCCCC		31.7022814378
21PhosphorylationKDQKPGTSGLRKKTK
CCCCCCCCCCCCCEE		41.5722369663
73AcetylationYNDVIMNKIAAVGAA
CCHHHHHHHHHHHHC		19.1524489116
73UbiquitinationYNDVIMNKIAAVGAA
CCHHHHHHHHHHHHC		19.1517644757
85UbiquitinationGAANGVRKLVIGQGG
HHCCCCEEEEECCCC		44.7017644757
95PhosphorylationIGQGGLLSTPAASHI
ECCCCCCCCHHHHHH		37.0722369663
96PhosphorylationGQGGLLSTPAASHII
CCCCCCCCHHHHHHH		19.5422369663
100PhosphorylationLLSTPAASHIIRTYE
CCCCHHHHHHHHHHH		19.8222369663
105PhosphorylationAASHIIRTYEEKCTG
HHHHHHHHHHHHHCC		25.5223749301
106PhosphorylationASHIIRTYEEKCTGG
HHHHHHHHHHHHCCC		16.5523749301
111PhosphorylationRTYEEKCTGGGIILT
HHHHHHHCCCEEEEE		50.3522890988
118PhosphorylationTGGGIILTASHNPGG
CCCEEEEEEECCCCC		18.7322369663
120PhosphorylationGGIILTASHNPGGPE
CEEEEEEECCCCCCH		20.6822369663
133UbiquitinationPENDLGIKYNLPNGG
CHHHCCEEEECCCCC		26.7017644757
155UbiquitinationNAIWEASKKLTHYKI
HHHHHHHHHCCCHHH		59.8717644757
155AcetylationNAIWEASKKLTHYKI
HHHHHHHHHCCCHHH		59.8724489116
156UbiquitinationAIWEASKKLTHYKII
HHHHHHHHCCCHHHH		57.0017644757
158PhosphorylationWEASKKLTHYKIIKN
HHHHHHCCCHHHHHC		31.8519823750
160PhosphorylationASKKLTHYKIIKNFP
HHHHCCCHHHHHCCC		9.9219823750
179AcetylationNKLGKNQKYGPLLVD
HHCCCCCCCCCEEEH		62.6624489116
221UbiquitinationQRKDKGWKLLFDSLN
HCCCCCCHHHHHHHC		43.9417644757
226PhosphorylationGWKLLFDSLNGITGP
CCHHHHHHHCCCCCC		19.1924909858
231PhosphorylationFDSLNGITGPYGKAI
HHHHCCCCCCCCCEE		33.2424909858
234PhosphorylationLNGITGPYGKAIFVD
HCCCCCCCCCEEEEE		32.3824909858
236UbiquitinationGITGPYGKAIFVDEF
CCCCCCCCEEEEECC		32.2517644757
372AcetylationFCALFDAKKLSICGE
HHHHHCCCCCEECCC		56.9724489116
420UbiquitinationPEKEASIKTIQDEFW
HHHHHCCHHHHHHHH		36.7617644757
420AcetylationPEKEASIKTIQDEFW
HHHHHCCHHHHHHHH		36.7624489116
460PhosphorylationALLSEFVSRPNVCGS
HHHHHHHCCCCCCCC		47.5528889911
507AcetylationVKFSNGTKFVLRLSG
EEECCCCEEEEEEEC		34.5724489116
513PhosphorylationTKFVLRLSGTGSSGA
CEEEEEEECCCCCCC		28.0730377154
515PhosphorylationFVLRLSGTGSSGATI
EEEEEECCCCCCCEE		30.4330377154
517PhosphorylationLRLSGTGSSGATIRL
EEEECCCCCCCEEEE		25.9922369663
518PhosphorylationRLSGTGSSGATIRLY
EEECCCCCCCEEEEE		33.5222369663
521PhosphorylationGTGSSGATIRLYVEK
CCCCCCCEEEEEEEE		15.3422369663
528UbiquitinationTIRLYVEKYTDKKEN
EEEEEEEECCCCCHH		43.3217644757
529PhosphorylationIRLYVEKYTDKKENY
EEEEEEECCCCCHHH		13.4819823750
530PhosphorylationRLYVEKYTDKKENYG
EEEEEECCCCCHHHC		53.0319823750
532UbiquitinationYVEKYTDKKENYGQT
EEEECCCCCHHHCCC		54.9417644757
533UbiquitinationVEKYTDKKENYGQTA
EEECCCCCHHHCCCH		54.7417644757
536PhosphorylationYTDKKENYGQTADVF
CCCCCHHHCCCHHHH		16.2319823750
539PhosphorylationKKENYGQTADVFLKP
CCHHHCCCHHHHHHH		22.0619823750
545AcetylationQTADVFLKPVINSIV
CCHHHHHHHHHHHHH		26.2724489116
545UbiquitinationQTADVFLKPVINSIV
CCHHHHHHHHHHHHH		26.2717644757
553UbiquitinationPVINSIVKFLRFKEI
HHHHHHHHHHHHHHH		36.6917644757
558AcetylationIVKFLRFKEILGTDE
HHHHHHHHHHHCCCC		37.0924489116
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 PGM1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGM1_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 PGM1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PGM2_YEASTPGM2genetic
8119301
PGM2_YEASTPGM2genetic
16941010
TUS1_YEASTTUS1genetic
23891562
PACC_YEASTRIM101genetic
23891562
PPZ1_YEASTPPZ1genetic
23891562
PFD3_YEASTPAC10genetic
23891562
PFD4_YEASTGIM3genetic
23891562
INP52_YEASTINP52genetic
23891562
RPN6_YEASTRPN6genetic
23891562
RPN5_YEASTRPN5genetic
23891562
RPN3_YEASTRPN3genetic
23891562
PRS6B_YEASTRPT3genetic
23891562
PSB1_YEASTPRE3genetic
23891562
PSB5_YEASTPRE2genetic
23891562
CDC24_YEASTCDC24genetic
27708008
PSB6_YEASTPRE7genetic
27708008
KPC1_YEASTPKC1genetic
27708008
SCC1_YEASTMCD1genetic
27708008
MAK21_YEASTMAK21genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
TCPA_YEASTTCP1genetic
27708008
SNU56_YEASTSNU56genetic
27708008
NSE3_YEASTNSE3genetic
27708008
FCF1_YEASTFCF1genetic
27708008
RSP5_YEASTRSP5genetic
27708008
ACT_YEASTACT1genetic
27708008
PMM_YEASTSEC53genetic
27708008
CDC11_YEASTCDC11genetic
27708008
TAD3_YEASTTAD3genetic
27708008
RPC6_YEASTRPC34genetic
27708008
PSB5_YEASTPRE2genetic
27708008
SLA1_YEASTSLA1genetic
27708008
EDE1_YEASTEDE1genetic
27708008
PIN4_YEASTPIN4genetic
27708008
CSG2_YEASTCSG2genetic
27708008
SLT11_YEASTECM2genetic
27708008
RV161_YEASTRVS161genetic
27708008
IMG2_YEASTIMG2genetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
OST4_YEASTOST4genetic
27708008
SWI5_YEASTSWI5genetic
27708008
RPA14_YEASTRPA14genetic
27708008
PAL1_YEASTPAL1genetic
27708008
EF2_YEASTEFT2genetic
27708008
GNP1_YEASTGNP1genetic
27708008
IES1_YEASTIES1genetic
27708008
SGF73_YEASTSGF73genetic
27708008
QCR9_YEASTQCR9genetic
27708008
YG51_YEASTYGR237Cgenetic
27708008
SLT2_YEASTSLT2genetic
27708008
YHR2_YEASTYHR112Cgenetic
27708008
DAL81_YEASTDAL81genetic
27708008
LPLA_YEASTAIM22genetic
27708008
BCK1_YEASTBCK1genetic
27708008
CYP7_YEASTCPR7genetic
27708008
FRA1_YEASTFRA1genetic
27708008
BRE2_YEASTBRE2genetic
27708008
ROM2_YEASTROM2genetic
27708008
MUB1_YEASTMUB1genetic
27708008
PGM2_YEASTPGM2genetic
27708008
PFKA2_YEASTPFK2genetic
27708008
VPS27_YEASTVPS27genetic
27708008
IRA2_YEASTIRA2genetic
27708008
WHI2_YEASTWHI2genetic
27708008
COQ7_YEASTCAT5genetic
27708008
PALA_YEASTRIM20genetic
27708008
RMI1_YEASTRMI1genetic
27708008
LGE1_YEASTLGE1genetic
27708008
YP066_YEASTRGL1genetic
27708008
AIM44_YEASTAIM44genetic
27708008
MLC2_YEASTMLC2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGM1_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-118 AND SER-120, 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-120, 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 SER-120, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND MASSSPECTROMETRY.

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