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

UniProtKB / Swiss-Prot ID :  PGAM1_HUMAN

Gene Name (Synonyms) : 
PGAM1, PGAMA CDABP0006  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity. 

Protein Sequence MAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQKRAIRTLWTV...
Predicted Secondary Structure CCCEEEEEEECCCHHCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHCCCCCCEEEECCCHHHHHHHHHH...
Protein Variant -
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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
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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-acetylalanine.---MAAYKL
---CCCEEE
21.35UniProtKB
Link
5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MAAYKLVLI
CCCEEEEEE
27.65Phosphositeplus
Link
5N6-acetyllysineMAAYKLVLI
CCCEEEEEE
27.65HPRD
Link
5N6-acetyllysineMAAYKLVLI
CCCEEEEEE
27.65Phosphositeplus
Link
14PhosphoserineRHGESAWNL
ECCCHHCCC
43.08HPRD
Link
14PhosphoserineRHGESAWNL
ECCCHHCCC
43.08Phosphositeplus
Link
14PhosphoserineRHGESAWNL
ECCCHHCCC
43.08SysPTM
Link
14Phosphoserine.RHGESAWNL
ECCCHHCCC
43.08UniProtKB
Link
23PhosphoserineENRFSGWYD
CCCCCCCCC
25.77Phosphositeplus
Link
23Phosphoserine (PAK1)ENRFSGWYD
CCCCCCCCC
25.77PhosphoELM
Link
26PhosphotyrosineFSGWYDADL
CCCCCCCCC
12.55HPRD
Link
26PhosphotyrosineFSGWYDADL
CCCCCCCCC
12.55PhosphoELM
Link
26PhosphotyrosineFSGWYDADL
CCCCCCCCC
12.55Phosphositeplus
Link
26Phosphotyrosine.FSGWYDADL
CCCCCCCCC
12.55UniProtKB
Link
31PhosphoserineDADLSPAGH
CCCCCHHHH
17.16HPRD
Link
31PhosphoserineDADLSPAGH
CCCCCHHHH
17.16Phosphositeplus
Link
31Phosphoserine.DADLSPAGH
CCCCCHHHH
17.16UniProtKB
Link
39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HEEAKRGGQ
HHHHHHHHH
55.65Phosphositeplus
Link
50PhosphotyrosineRDAGYEFDI
HHCCCCCCE
18.36Phosphositeplus
Link
92PhosphotyrosineNERHYGGLT
CHHHHHHHC
21.07HPRD
Link
92PhosphotyrosineNERHYGGLT
CHHHHHHHC
21.07Phosphositeplus
Link
92Phosphotyrosine.NERHYGGLT
CHHHHHHHC
21.07UniProtKB
Link
100Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TGLNKAETA
CCCCHHHHH
53.28Phosphositeplus
Link
100N6-acetyllysineTGLNKAETA
CCCCHHHHH
53.28HPRD
Link
100N6-acetyllysineTGLNKAETA
CCCCHHHHH
53.28Phosphositeplus
Link
106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ETAAKHGEA
HHHHHCCCC
50.07Phosphositeplus
Link
106N6-acetyllysineETAAKHGEA
HHHHHCCCC
50.07Phosphositeplus
Link
113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EAQVKIWRR
CCEEEEEEC
25.19Phosphositeplus
Link
113N6-acetyllysineEAQVKIWRR
CCEEEEEEC
25.19HPRD
Link
113N6-acetyllysineEAQVKIWRR
CCEEEEEEC
25.19Phosphositeplus
Link
118PhosphoserineIWRRSYDVP
EEECCCCCC
19.67HPRD
Link
118PhosphoserineIWRRSYDVP
EEECCCCCC
19.67Phosphositeplus
Link
118Phosphoserine (PAK1)IWRRSYDVP
EEECCCCCC
19.67PhosphoELM
Link
118Phosphoserine.IWRRSYDVP
EEECCCCCC
19.67UniProtKB
Link
119PhosphotyrosineWRRSYDVPP
EECCCCCCC
21.10HPRD
Link
119PhosphotyrosineWRRSYDVPP
EECCCCCCC
21.10Phosphositeplus
Link
133PhosphotyrosineDHPFYSNIS
CCCCCCCCC
12.78HPRD
Link
133PhosphotyrosineDHPFYSNIS
CCCCCCCCC
12.78Phosphositeplus
Link
146PhosphothreonineYADLTEDQL
CCCCCHHHC
37.75HPRD
Link
153S-nitrosocysteineQLPSCESLK
HCCCCCCHH
3.78dbSNO
Link
157Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)CESLKDTIA
CCCHHHHHH
63.20Phosphositeplus
Link
176N6-acetyllysineVPQIKEGKR
HHHHHCCCE
55.99HPRD
Link
238PhosphothreonineGDEETVRKA
CCHHHHHHH
24.46Phosphositeplus
Link
251Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AAQGKAKK
HHHCCCCC
44.98Phosphositeplus
Link
251N6-acetyllysine.AAQGKAKK
HHHCCCCC
44.98UniProtKB
Link
253N6-acetyllysine.QGKAKK
HCCCCC
63.60UniProtKB
Link-
254N6-acetyllysine.GKAKK
CCCCC
71.13UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
1433Z_HUMANphysical interactionMINT-3318976MINT15161933
KU70_HUMANphysical interactionEBI-735333
intact16169070
PKP4_HUMANyeast 2-hybridHPRD:01392HPRD16169070
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Regulation of glycolytic enzyme phosphoglycerate mutase-1 by Sirt1protein-mediated deacetylation.";
Hallows W.C., Yu W., Denu J.M.;
J. Biol. Chem. 287:3850-3858(2012).
Cited for: ACETYLATION AT LYS-251; LYS-253 AND LYS-254, AND DEACETYLATION BYSIRT1.
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-26, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; TYR-26; TYR-92 ANDSER-118, AND MASS SPECTROMETRY.
"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-26, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-26, AND MASSSPECTROMETRY.
"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-14 AND SER-31, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures