PGK_YEAST - dbPTM
PGK_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGK_YEAST
UniProt AC P00560
Protein Name Phosphoglycerate kinase
Gene Name PGK1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 416
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MSLSSKLSVQDLDLKDKRVFIRVDFNVPLDGKKITSNQRIVAALPTIKYVLEHHPRYVVLASHLGRPNGERNEKYSLAPVAKELQSLLGKDVTFLNDCVGPEVEAAVKASAPGSVILLENLRYHIEEEGSRKVDGQKVKASKEDVQKFRHELSSLADVYINDAFGTAHRAHSSMVGFDLPQRAAGFLLEKELKYFGKALENPTRPFLAILGGAKVADKIQLIDNLLDKVDSIIIGGGMAFTFKKVLENTEIGDSIFDKAGAEIVPKLMEKAKAKGVEVVLPVDFIIADAFSADANTKTVTDKEGIPAGWQGLDNGPESRKLFAATVAKAKTIVWNGPPGVFEFEKFAAGTKALLDEVVKSSAAGNTVIIGGGDTATVAKKYGVTDKISHVSTGGGASLELLEGKELPGVAFLSEKK
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
2Acetylation------MSLSSKLSV
------CCCCCCCCC
36.6422814378
2Phosphorylation------MSLSSKLSV
------CCCCCCCCC
36.6422369663
4Phosphorylation----MSLSSKLSVQD
----CCCCCCCCCCC
20.3722369663
5Phosphorylation---MSLSSKLSVQDL
---CCCCCCCCCCCC
42.8022369663
6Acetylation--MSLSSKLSVQDLD
--CCCCCCCCCCCCC
41.2122865919
6Succinylation--MSLSSKLSVQDLD
--CCCCCCCCCCCCC
41.2123954790
6Ubiquitination--MSLSSKLSVQDLD
--CCCCCCCCCCCCC
41.2124961812
8PhosphorylationMSLSSKLSVQDLDLK
CCCCCCCCCCCCCCC
22.8222369663
152-HydroxyisobutyrylationSVQDLDLKDKRVFIR
CCCCCCCCCCEEEEE
61.95-
15AcetylationSVQDLDLKDKRVFIR
CCCCCCCCCCEEEEE
61.9524489116
15SuccinylationSVQDLDLKDKRVFIR
CCCCCCCCCCEEEEE
61.9523954790
15UbiquitinationSVQDLDLKDKRVFIR
CCCCCCCCCCEEEEE
61.9517644757
17AcetylationQDLDLKDKRVFIRVD
CCCCCCCCEEEEEEE
49.2024489116
17UbiquitinationQDLDLKDKRVFIRVD
CCCCCCCCEEEEEEE
49.2015699485
322-HydroxyisobutyrylationFNVPLDGKKITSNQR
EECCCCCCCCCCCHH
40.44-
32AcetylationFNVPLDGKKITSNQR
EECCCCCCCCCCCHH
40.4424489116
32SuccinylationFNVPLDGKKITSNQR
EECCCCCCCCCCCHH
40.4423954790
32UbiquitinationFNVPLDGKKITSNQR
EECCCCCCCCCCCHH
40.4424961812
332-HydroxyisobutyrylationNVPLDGKKITSNQRI
ECCCCCCCCCCCHHH
57.66-
33UbiquitinationNVPLDGKKITSNQRI
ECCCCCCCCCCCHHH
57.6624961812
35PhosphorylationPLDGKKITSNQRIVA
CCCCCCCCCCHHHHH
30.4221440633
36PhosphorylationLDGKKITSNQRIVAA
CCCCCCCCCHHHHHH
34.1420377248
46PhosphorylationRIVAALPTIKYVLEH
HHHHHHHHHHHHHHH
30.8328152593
482-HydroxyisobutyrylationVAALPTIKYVLEHHP
HHHHHHHHHHHHHCC
31.61-
48AcetylationVAALPTIKYVLEHHP
HHHHHHHHHHHHHCC
31.6124489116
48SuccinylationVAALPTIKYVLEHHP
HHHHHHHHHHHHHCC
31.6123954790
48UbiquitinationVAALPTIKYVLEHHP
HHHHHHHHHHHHHCC
31.6123749301
49PhosphorylationAALPTIKYVLEHHPR
HHHHHHHHHHHHCCC
13.3528889911
62PhosphorylationPRYVVLASHLGRPNG
CCEEEEEHHCCCCCC
18.3228889911
742-HydroxyisobutyrylationPNGERNEKYSLAPVA
CCCCCCCCCCHHHHH
43.62-
74AcetylationPNGERNEKYSLAPVA
CCCCCCCCCCHHHHH
43.6224489116
74UbiquitinationPNGERNEKYSLAPVA
CCCCCCCCCCHHHHH
43.6223749301
75PhosphorylationNGERNEKYSLAPVAK
CCCCCCCCCHHHHHH
11.6122369663
76PhosphorylationGERNEKYSLAPVAKE
CCCCCCCCHHHHHHH
29.1722369663
82AcetylationYSLAPVAKELQSLLG
CCHHHHHHHHHHHHC
60.2224489116
82SuccinylationYSLAPVAKELQSLLG
CCHHHHHHHHHHHHC
60.2223954790
82UbiquitinationYSLAPVAKELQSLLG
CCHHHHHHHHHHHHC
60.2224961812
86PhosphorylationPVAKELQSLLGKDVT
HHHHHHHHHHCCCCE
37.8825521595
90AcetylationELQSLLGKDVTFLND
HHHHHHCCCCEECCC
49.3325381059
90UbiquitinationELQSLLGKDVTFLND
HHHHHHCCCCEECCC
49.3317644757
93PhosphorylationSLLGKDVTFLNDCVG
HHHCCCCEECCCCCC
32.3211283598
98GlutathionylationDVTFLNDCVGPEVEA
CCEECCCCCCHHHHH
3.5722833525
108UbiquitinationPEVEAAVKASAPGSV
HHHHHHHHCCCCCEE
31.7117644757
110PhosphorylationVEAAVKASAPGSVIL
HHHHHHCCCCCEEEE
29.3121082442
114PhosphorylationVKASAPGSVILLENL
HHCCCCCEEEEEECH
12.6222369663
123PhosphorylationILLENLRYHIEEEGS
EEEECHHEEHHHCCC
15.4322369663
130PhosphorylationYHIEEEGSRKVDGQK
EEHHHCCCCCCCCEE
32.0122369663
132UbiquitinationIEEEGSRKVDGQKVK
HHHCCCCCCCCEEEC
46.5022817900
1372-HydroxyisobutyrylationSRKVDGQKVKASKED
CCCCCCEEECCCHHH
51.75-
137AcetylationSRKVDGQKVKASKED
CCCCCCEEECCCHHH
51.7524489116
137UbiquitinationSRKVDGQKVKASKED
CCCCCCEEECCCHHH
51.7522817900
139UbiquitinationKVDGQKVKASKEDVQ
CCCCEEECCCHHHHH
54.7122817900
1422-HydroxyisobutyrylationGQKVKASKEDVQKFR
CEEECCCHHHHHHHH
63.89-
142AcetylationGQKVKASKEDVQKFR
CEEECCCHHHHHHHH
63.8924489116
142SuccinylationGQKVKASKEDVQKFR
CEEECCCHHHHHHHH
63.8923954790
142UbiquitinationGQKVKASKEDVQKFR
CEEECCCHHHHHHHH
63.8922817900
1472-HydroxyisobutyrylationASKEDVQKFRHELSS
CCHHHHHHHHHHHHH
44.19-
147AcetylationASKEDVQKFRHELSS
CCHHHHHHHHHHHHH
44.1924489116
147SuccinylationASKEDVQKFRHELSS
CCHHHHHHHHHHHHH
44.1923954790
147UbiquitinationASKEDVQKFRHELSS
CCHHHHHHHHHHHHH
44.1917644757
153PhosphorylationQKFRHELSSLADVYI
HHHHHHHHHHHHHHH
21.9619779198
154PhosphorylationKFRHELSSLADVYIN
HHHHHHHHHHHHHHH
39.9522369663
159PhosphorylationLSSLADVYINDAFGT
HHHHHHHHHHHHCCC
8.4421440633
172PhosphorylationGTAHRAHSSMVGFDL
CCCHHHHHHCCCCCC
21.1022369663
173PhosphorylationTAHRAHSSMVGFDLP
CCHHHHHHCCCCCCC
13.9722369663
190AcetylationAAGFLLEKELKYFGK
HHHHHHHHHHHHHHH
69.2124489116
190SuccinylationAAGFLLEKELKYFGK
HHHHHHHHHHHHHHH
69.2123954790
190UbiquitinationAAGFLLEKELKYFGK
HHHHHHHHHHHHHHH
69.2123749301
1932-HydroxyisobutyrylationFLLEKELKYFGKALE
HHHHHHHHHHHHHHC
39.36-
193AcetylationFLLEKELKYFGKALE
HHHHHHHHHHHHHHC
39.3624489116
193SuccinylationFLLEKELKYFGKALE
HHHHHHHHHHHHHHC
39.3623954790
193UbiquitinationFLLEKELKYFGKALE
HHHHHHHHHHHHHHC
39.3623749301
197AcetylationKELKYFGKALENPTR
HHHHHHHHHHCCCCC
39.6424489116
197UbiquitinationKELKYFGKALENPTR
HHHHHHHHHHCCCCC
39.6423749301
203PhosphorylationGKALENPTRPFLAIL
HHHHCCCCCCHHHHH
63.6622369663
214AcetylationLAILGGAKVADKIQL
HHHHCCCHHHHHHHH
41.0324489116
214SuccinylationLAILGGAKVADKIQL
HHHHCCCHHHHHHHH
41.0323954790
214UbiquitinationLAILGGAKVADKIQL
HHHHCCCHHHHHHHH
41.0323749301
218AcetylationGGAKVADKIQLIDNL
CCCHHHHHHHHHHHH
23.7124489116
218UbiquitinationGGAKVADKIQLIDNL
CCCHHHHHHHHHHHH
23.7124961812
241PhosphorylationIGGGMAFTFKKVLEN
ECCCHHEEHHHHHHC
25.6328889911
243UbiquitinationGGMAFTFKKVLENTE
CCHHEEHHHHHHCCC
38.6317644757
2442-HydroxyisobutyrylationGMAFTFKKVLENTEI
CHHEEHHHHHHCCCC
48.11-
244UbiquitinationGMAFTFKKVLENTEI
CHHEEHHHHHHCCCC
48.1117644757
249PhosphorylationFKKVLENTEIGDSIF
HHHHHHCCCCCCHHH
21.4329136822
254PhosphorylationENTEIGDSIFDKAGA
HCCCCCCHHHHHHCC
21.6829136822
258AcetylationIGDSIFDKAGAEIVP
CCCHHHHHHCCCHHH
37.6624489116
258SuccinylationIGDSIFDKAGAEIVP
CCCHHHHHHCCCHHH
37.6623954790
258UbiquitinationIGDSIFDKAGAEIVP
CCCHHHHHHCCCHHH
37.6623749301
2662-HydroxyisobutyrylationAGAEIVPKLMEKAKA
HCCCHHHHHHHHHHH
49.96-
266AcetylationAGAEIVPKLMEKAKA
HCCCHHHHHHHHHHH
49.9624489116
266SuccinylationAGAEIVPKLMEKAKA
HCCCHHHHHHHHHHH
49.9623954790
266UbiquitinationAGAEIVPKLMEKAKA
HCCCHHHHHHHHHHH
49.9623749301
2702-HydroxyisobutyrylationIVPKLMEKAKAKGVE
HHHHHHHHHHHCCCE
41.02-
274UbiquitinationLMEKAKAKGVEVVLP
HHHHHHHCCCEEEEE
63.8822106047
297UbiquitinationFSADANTKTVTDKEG
CCCCCCCCCCCCCCC
40.5822817900
298PhosphorylationSADANTKTVTDKEGI
CCCCCCCCCCCCCCC
26.9728889911
300PhosphorylationDANTKTVTDKEGIPA
CCCCCCCCCCCCCCC
46.7328132839
3022-HydroxyisobutyrylationNTKTVTDKEGIPAGW
CCCCCCCCCCCCCCC
48.77-
302AcetylationNTKTVTDKEGIPAGW
CCCCCCCCCCCCCCC
48.7724489116
302SuccinylationNTKTVTDKEGIPAGW
CCCCCCCCCCCCCCC
48.7723954790
302UbiquitinationNTKTVTDKEGIPAGW
CCCCCCCCCCCCCCC
48.7723749301
318PhosphorylationGLDNGPESRKLFAAT
CCCCCHHHHHHHHHH
37.5411283598
320AcetylationDNGPESRKLFAATVA
CCCHHHHHHHHHHHH
58.1822865919
320UbiquitinationDNGPESRKLFAATVA
CCCHHHHHHHHHHHH
58.1823749301
325PhosphorylationSRKLFAATVAKAKTI
HHHHHHHHHHCCEEE
19.9820377248
3282-HydroxyisobutyrylationLFAATVAKAKTIVWN
HHHHHHHCCEEEEEC
46.19-
328SuccinylationLFAATVAKAKTIVWN
HHHHHHHCCEEEEEC
46.1923954790
328UbiquitinationLFAATVAKAKTIVWN
HHHHHHHCCEEEEEC
46.1917644757
3302-HydroxyisobutyrylationAATVAKAKTIVWNGP
HHHHHCCEEEEECCC
37.77-
330AcetylationAATVAKAKTIVWNGP
HHHHHCCEEEEECCC
37.7724489116
330UbiquitinationAATVAKAKTIVWNGP
HHHHHCCEEEEECCC
37.7717644757
331PhosphorylationATVAKAKTIVWNGPP
HHHHCCEEEEECCCC
26.1422369663
3452-HydroxyisobutyrylationPGVFEFEKFAAGTKA
CCCEEHHHHHCHHHH
45.70-
345AcetylationPGVFEFEKFAAGTKA
CCCEEHHHHHCHHHH
45.7024489116
345UbiquitinationPGVFEFEKFAAGTKA
CCCEEHHHHHCHHHH
45.7023749301
350PhosphorylationFEKFAAGTKALLDEV
HHHHHCHHHHHHHHH
14.3921440633
3512-HydroxyisobutyrylationEKFAAGTKALLDEVV
HHHHCHHHHHHHHHH
35.80-
351AcetylationEKFAAGTKALLDEVV
HHHHCHHHHHHHHHH
35.8024489116
351UbiquitinationEKFAAGTKALLDEVV
HHHHCHHHHHHHHHH
35.8023749301
359AcetylationALLDEVVKSSAAGNT
HHHHHHHHHCCCCCE
43.8224489116
359SuccinylationALLDEVVKSSAAGNT
HHHHHHHHHCCCCCE
43.8223954790
360PhosphorylationLLDEVVKSSAAGNTV
HHHHHHHHCCCCCEE
17.3822369663
361PhosphorylationLDEVVKSSAAGNTVI
HHHHHHHCCCCCEEE
19.2022369663
366PhosphorylationKSSAAGNTVIIGGGD
HHCCCCCEEEECCCC
16.5022369663
374PhosphorylationVIIGGGDTATVAKKY
EEECCCCHHHHHHHH
27.7422369663
376PhosphorylationIGGGDTATVAKKYGV
ECCCCHHHHHHHHCC
24.0822369663
379AcetylationGDTATVAKKYGVTDK
CCHHHHHHHHCCCCC
42.0424489116
379SuccinylationGDTATVAKKYGVTDK
CCHHHHHHHHCCCCC
42.0423954790
379UbiquitinationGDTATVAKKYGVTDK
CCHHHHHHHHCCCCC
42.0422817900
3802-HydroxyisobutyrylationDTATVAKKYGVTDKI
CHHHHHHHHCCCCCC
37.18-
380AcetylationDTATVAKKYGVTDKI
CHHHHHHHHCCCCCC
37.1824489116
380UbiquitinationDTATVAKKYGVTDKI
CHHHHHHHHCCCCCC
37.1823749301
386AcetylationKKYGVTDKISHVSTG
HHHCCCCCCEEEECC
36.4224489116
388PhosphorylationYGVTDKISHVSTGGG
HCCCCCCEEEECCCC
24.4722369663
391PhosphorylationTDKISHVSTGGGASL
CCCCEEEECCCCCCE
18.8622369663
392PhosphorylationDKISHVSTGGGASLE
CCCEEEECCCCCCEE
38.4622369663
397PhosphorylationVSTGGGASLELLEGK
EECCCCCCEEHHCCC
26.1722369663
404AcetylationSLELLEGKELPGVAF
CEEHHCCCCCCCEEE
46.8624489116
413PhosphorylationLPGVAFLSEKK----
CCCEEEEECCC----
40.7022369663
415AcetylationGVAFLSEKK------
CEEEEECCC------
61.4824489116
415SuccinylationGVAFLSEKK------
CEEEEECCC------
61.4823954790
4162-HydroxyisobutyrylationVAFLSEKK-------
EEEEECCC-------
62.61-

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 PGK_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGK_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 PGK_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COPA_YEASTCOP1physical
11805826
COPB2_YEASTSEC27physical
11805826
LSM1_YEASTLSM1physical
17513695
LSM2_YEASTLSM2physical
17513695
LSM3_YEASTLSM3physical
17513695
LSM4_YEASTLSM4physical
17513695
LSM5_YEASTLSM5physical
17513695
LSM6_YEASTLSM6physical
17513695
LSM7_YEASTLSM7physical
17513695
PAT1_YEASTPAT1physical
17513695
KCC4_YEASTKCC4genetic
19269370
PGK_YEASTPGK1physical
16353200
CSG2_YEASTCSG2genetic
20093466
EFM4_YEASTEFM4genetic
20093466
MET28_YEASTMET28genetic
20093466
SDHX_YEASTYJL045Wgenetic
20093466
YJ24_YEASTKCH1genetic
20093466
ADE_YEASTAAH1genetic
20093466
BUD21_YEASTBUD21genetic
20093466
NAM7_YEASTNAM7physical
23928302
NMD2_YEASTNMD2physical
23928302
UPF3_YEASTUPF3physical
23928302
HSP71_YEASTSSA1physical
23928302

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGK_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-4,AND MASS SPECTROMETRY.
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-5; SER-8; SER-76;THR-93; SER-114; THR-203; THR-241; THR-331; THR-376; SER-391 ANDTHR-392, 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-391 AND SER-413, 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-36; SER-110; SER-114;SER-130 AND SER-397, 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-154; THR-331 ANDTHR-392, AND MASS SPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-4,AND MASS SPECTROMETRY.

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