Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Phosphoglycerate kinase 1  

UniProtKB / Swiss-Prot ID :  PGK1_HUMAN

Gene Name (Synonyms) : 
PGK1, PGKA MIG10, OK/SW-cl.110  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). 

Protein Sequence MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGV...
Predicted Secondary Structure CCCCCCCCCEEECCCCCEEEEEEEECCCCCCCEECCCHHHHHHHHHHHHHHHCCCCEEEEEEECCCCCCC...
Protein Variant
LocationDescription
88L -> P (in PGK1D; with congenital non-spherocytic anemia; variant Matsue).
158G -> V (in PGK1D; with chronic hemolyticanemia; variant Shizuoka).
164D -> V (in PGK1D; with chronic hemolyticanemia and mental retardation; variant
191Missing (in PGK1D; with chronic hemolyticanemia; variant Alabama).
206R -> P (in PGK1D; with chronic hemolyticanemia; variant Uppsala).
252E -> A (in PGK1D; with chronic hemolyticanemia; variant Antwerp).
266V -> M (in PGK1D; with chronic non-spherocytic hemolytic anemia; variant
268D -> N (in Munchen; 21% of activity). VAR_006083
285D -> V (in PGK1D; with chronic hemolyticanemia; variant Herlev; 50% of activity).
315D -> N (in PGK1D; with rhabdomyolysis;variant Creteil).
316C -> R (in PGK1D; with chronic hemolyticanemia; variant Michigan).
352T -> N. VAR_006087
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylserine.---MSLSNK
---CCCCCC
40.27UniProtKB
Link
11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LTLDKLDVK
CCCEEECCC
50.10Phosphositeplus
Link
11N6-acetyllysineLTLDKLDVK
CCCEEECCC
50.10HPRD
Link
11N6-acetyllysineLTLDKLDVK
CCCEEECCC
50.10Phosphositeplus
Link
11N6-acetyllysine.LTLDKLDVK
CCCEEECCC
50.10UniProtKB
Link
30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NVPMKNNQI
CCCCCCCEE
46.83Phosphositeplus
Link
30N6-acetyllysineNVPMKNNQI
CCCCCCCEE
46.83HPRD
Link
30N6-acetyllysineNVPMKNNQI
CCCCCCCEE
46.83Phosphositeplus
Link
30N6-acetyllysine.NVPMKNNQI
CCCCCCCEE
46.83UniProtKB
Link
48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VPSIKFCLD
HHHHHHHHH
34.07Phosphositeplus
Link
48N6-acetyllysineVPSIKFCLD
HHHHHHHHH
34.07HPRD
Link
48N6-acetyllysineVPSIKFCLD
HHHHHHHHH
34.07Phosphositeplus
Link
48N6-acetyllysine.VPSIKFCLD
HHHHHHHHH
34.07UniProtKB
Link
50S-nitrosocysteineSIKFCLDNG
HHHHHHHCC
3.86dbSNO
Link
57PhosphoserineNGAKSVVLM
CCCCEEEEE
19.54HPRD
Link
62PhosphoserineVVLMSHLGR
EEEEEECCC
16.05HPRD
Link
75Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PMPDKYSLE
CCCCCCCHH
30.76Phosphositeplus
Link
75N6-acetyllysinePMPDKYSLE
CCCCCCCHH
30.76HPRD
Link
75N6-acetyllysinePMPDKYSLE
CCCCCCCHH
30.76Phosphositeplus
Link
75N6-acetyllysine.PMPDKYSLE
CCCCCCCHH
30.76UniProtKB
Link
76PhosphotyrosineMPDKYSLEP
CCCCCCHHH
26.35Phosphositeplus
Link
77PhosphoserinePDKYSLEPV
CCCCCHHHH
31.81HPRD
Link
86Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AVELKSLLG
HHHHHHHCC
26.08Phosphositeplus
Link
86N6-acetyllysineAVELKSLLG
HHHHHHHCC
26.08HPRD
Link
86N6-acetyllysineAVELKSLLG
HHHHHHHCC
26.08Phosphositeplus
Link
86N6-acetyllysine.AVELKSLLG
HHHHHHHCC
26.08UniProtKB
Link
91N6-acetyllysineSLLGKDVLF
HHCCCCCEE
44.63HPRD
Link
91N6-acetyllysineSLLGKDVLF
HHCCCCCEE
44.63Phosphositeplus
Link
97Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VLFLKDCVG
CEEECCCCC
41.57Phosphositeplus
Link
97N6-acetyllysineVLFLKDCVG
CEEECCCCC
41.57HPRD
Link
97N6-acetyllysineVLFLKDCVG
CEEECCCCC
41.57Phosphositeplus
Link
97N6-acetyllysine.VLFLKDCVG
CEEECCCCC
41.57UniProtKB
Link
99S-nitrosocysteineFLKDCVGPE
EECCCCCHH
3.49dbSNO
Link
108S-nitrosocysteineVEKACANPA
HHHHHHCCC
5.79dbSNO
Link
108S-nitrosocysteineVEKACANPA
HHHHHHCCC
5.79HPRD
Link
131N6-acetyllysineEEEGKGKDA
CCCCCCCCC
67.10HPRD
Link
131N6-acetyllysineEEEGKGKDA
CCCCCCCCC
67.10Phosphositeplus
Link
131N6-acetyllysine; alternate.EEEGKGKDA
CCCCCCCCC
67.10UniProtKB
Link
131N6-malonyllysine; alternate.EEEGKGKDA
CCCCCCCCC
67.10UniProtKB
Link
136PhosphoserineGKDASGNKV
CCCCCCCCC
53.70HPRD
Link-
136PhosphoserineGKDASGNKV
CCCCCCCCC
53.70PhosphoELM
Link-
136PhosphoserineGKDASGNKV
CCCCCCCCC
53.70Phosphositeplus
Link-
136Phosphoserine.GKDASGNKV
CCCCCCCCC
53.70UniProtKB
Link-
141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GNKVKAEPA
CCCCCCCHH
48.95Phosphositeplus
Link-
146Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AEPAKIEAF
CCHHHHHHH
52.36Phosphositeplus
Link
146N6-acetyllysineAEPAKIEAF
CCHHHHHHH
52.36HPRD
Link
146N6-acetyllysineAEPAKIEAF
CCHHHHHHH
52.36Phosphositeplus
Link
146N6-acetyllysine.AEPAKIEAF
CCHHHHHHH
52.36UniProtKB
Link
156N6-acetyllysineASLSKLGDV
HHHHCCCCE
62.88HPRD
Link
161PhosphotyrosineLGDVYVNDA
CCCEEEECC
9.77Phosphositeplus
Link
192Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FLMKKELNY
HHHHHHHHH
54.17Phosphositeplus
Link
196PhosphotyrosineKELNYFAKA
HHHHHHHHH
19.96HPRD
Link
196PhosphotyrosineKELNYFAKA
HHHHHHHHH
19.96PhosphoELM
Link
196PhosphotyrosineKELNYFAKA
HHHHHHHHH
19.96Phosphositeplus
Link
196Phosphotyrosine.KELNYFAKA
HHHHHHHHH
19.96UniProtKB
Link
199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NYFAKALES
HHHHHHHCC
43.54Phosphositeplus
Link
199N6-acetyllysineNYFAKALES
HHHHHHHCC
43.54HPRD
Link
199N6-acetyllysineNYFAKALES
HHHHHHHCC
43.54Phosphositeplus
Link
199N6-acetyllysine.NYFAKALES
HHHHHHHCC
43.54UniProtKB
Link
203PhosphoserineKALESPERP
HHHCCCCCC
32.67HPRD
Link
203PhosphoserineKALESPERP
HHHCCCCCC
32.67PhosphoELM
Link
203PhosphoserineKALESPERP
HHHCCCCCC
32.67Phosphositeplus
Link
203PhosphoserineKALESPERP
HHHCCCCCC
32.67SysPTM
Link
203Phosphoserine.KALESPERP
HHHCCCCCC
32.67UniProtKB
Link
216Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LGGAKVADK
ECCCCHHHH
41.03Phosphositeplus
Link
220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KVADKIQLI
CHHHHHHHH
23.71Phosphositeplus
Link
220N6-acetyllysineKVADKIQLI
CHHHHHHHH
23.71Phosphositeplus
Link
243PhosphothreonineGMAFTFLKV
HHHHHHHHH
20.65Phosphositeplus
Link
243Phosphothreonine.GMAFTFLKV
HHHHHHHHH
20.65UniProtKB
Link
264Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EEGAKIVKD
HHHHHHHHH
59.91Phosphositeplus
Link
267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AKIVKDLMS
HHHHHHHHH
48.93Phosphositeplus
Link
267N6-acetyllysineAKIVKDLMS
HHHHHHHHH
48.93HPRD
Link
267N6-acetyllysineAKIVKDLMS
HHHHHHHHH
48.93Phosphositeplus
Link
267N6-acetyllysine.AKIVKDLMS
HHHHHHHHH
48.93UniProtKB
Link
291Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VTADKFDEN
EEECCCCCC
52.85Phosphositeplus
Link
291N6-acetyllysineVTADKFDEN
EEECCCCCC
52.85HPRD
Link
291N6-acetyllysineVTADKFDEN
EEECCCCCC
52.85Phosphositeplus
Link
291N6-acetyllysine.VTADKFDEN
EEECCCCCC
52.85UniProtKB
Link
323N6-acetyllysineESSKKYAEA
HHHHHHHHH
52.20HPRD
Link
323N6-acetyllysineESSKKYAEA
HHHHHHHHH
52.20Phosphositeplus
Link
323N6-acetyllysine.ESSKKYAEA
HHHHHHHHH
52.20UniProtKB
Link
332Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VTRAKQIVW
HHHCCEEEE
36.95Phosphositeplus
Link
361Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DEVVKATSR
HHHHHCCCC
51.64Phosphositeplus
Link
390PhosphoserineEDKVSHVST
CCCCCEEEC
24.74HPRD
Link
393PhosphoserineVSHVSTGGG
CCEEECCHH
18.86HPRD
Link
406N6-acetyllysineLLEGKVLPG
HHCCCCCCH
31.09HPRD
Link
406N6-acetyllysineLLEGKVLPG
HHCCCCCCH
31.09Phosphositeplus
Link
406N6-acetyllysine.LLEGKVLPG
HHCCCCCCH
31.09UniProtKB
Link
415PhosphoserineVDALSNI
HHHHHCC
33.91HPRD
Link
415PhosphoserineVDALSNI
HHHHHCC
33.91Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
HS105_HUMANphysical interactionMINT-49722MINT14733918
HS105_HUMANphysical interactionMINT-49674MINT14733918
DISC1_HUMANphysical interactionEBI-1106211
intact17043677
G3P_HUMANin vitro
in vivo
HPRD:02412HPRD8075252
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Disease Reference
Kegg disease
OMIM disease
300653Phosphoglycerate kinase 1 deficiency (PGK1D)
Drug Reference
DrugBank
DB00709Lamivudine
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-30; LYS-48; LYS-75;LYS-86; LYS-97; LYS-131; LYS-146; LYS-199; LYS-267; LYS-291; LYS-323AND LYS-406, AND MASS SPECTROMETRY.
N6-malonyllysine
ReferencePubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme.";
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.;
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
Cited for: MALONYLATION AT LYS-131.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-196, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-243, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures