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Protein Page:
PGAM1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PGAM1 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. Homodimer. In mammalian tissues there are two types of phosphoglycerate mutase isozymes: type-M in muscles and type-B in other tissues. Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily. Note: This description may include information from UniProtKB.
Protein type: EC 3.1.3.13; Phosphatase (non-protein); Isomerase; EC 5.4.2.1; Carbohydrate Metabolism - glycolysis and gluconeogenesis; EC 5.4.2.4
Cellular Component: membrane; cytoplasm; cytosol
Molecular Function: protein binding; phosphoglycerate mutase activity; bisphosphoglycerate mutase activity; bisphosphoglycerate phosphatase activity; protein kinase binding
Biological Process: respiratory burst; glycolysis; dephosphorylation; regulation of glycolysis; carbohydrate metabolic process; glucose metabolic process; regulation of pentose-phosphate shunt; gluconeogenesis
Reference #:  P18669 (UniProtKB)
Alt. Names/Synonyms: BPG-dependent PGAM 1; PGAM-B; PGAM1; PGAMA; Phosphoglycerate mutase 1; phosphoglycerate mutase 1 (brain); phosphoglycerate mutase A, nonmuscle form; Phosphoglycerate mutase isozyme B
Gene Symbols: PGAM1
Molecular weight: 28,804 Da
Basal Isoelectric point: 6.67  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PGAM1

Protein Structure Not Found.


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Sites Implicated In
enzymatic activity, inhibited: S23‑p, S118‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 10 K5-ac ___MAAYkLVLIRhG
0 6 K5-ub ___MAAYkLVLIRhG
3 0 H11-p YkLVLIRhGEsAWNL
0 35 S14-p VLIRhGEsAWNLENR
1 18 S23-p WNLENRFsGWyDADL
1 1008 Y26-p ENRFsGWyDADLsPA
0 9 S31-p GWyDADLsPAGHEEA
0 27 K39-ac PAGHEEAkRGGQALR
0 3 K39-ub PAGHEEAkRGGQALR
0 5 Y50-p QALRDAGyEFDICFT
1 2239 Y92-p WRLNERHyGGLtGLN
0 58 T96-p ERHyGGLtGLNkAET
0 24 K100-ac GGLtGLNkAETAAkH
0 15 K100-ub GGLtGLNkAETAAkH
0 2 K106-ac NkAETAAkHGEAQVk
0 83 K106-ub NkAETAAkHGEAQVk
0 10 K113-ac kHGEAQVkIWRRsyD
0 14 K113-ub kHGEAQVkIWRRsyD
1 25 S118-p QVkIWRRsyDVPPPP
0 34 Y119-p VkIWRRsyDVPPPPM
0 18 Y133-p MEPDHPFySNISkDR
0 2 K138-ub PFySNISkDRRYADL
0 15 K157-ub LPSCESLkDTIARAL
0 4 K157-ac LPSCESLkDTIARAL
0 1 K176 EEIVPQIKEGKRVLI
0 4 S189-p LIAAHGNsLRGIVkH
0 1 K195 NsLRGIVKHLEGLSE
0 4 K195-ub NsLRGIVkHLEGLSE
0 1 T238-p QFLGDEEtVRKAMEA
0 3 K241 GDEEtVRKAMEAVAA
0 4 K251-ub EAVAAQGkAKK____
  mouse

 
K5-ac ___MAAYkLVLIRHG
K5-ub ___MAAYkLVLIRHG
H11 YkLVLIRHGEsAWNL
S14-p VLIRHGEsAWNLENR
S23-p WNLENRFsGWyDADL
Y26-p ENRFsGWyDADLsPA
S31-p GWyDADLsPAGHEEA
K39-ac PAGHEEAkRGGQALR
K39 PAGHEEAKRGGQALR
Y50 QALRDAGYEFDICFT
Y92-p WRLNERHyGGLTGLN
T96 ERHyGGLTGLNkAET
K100-ac GGLTGLNkAETAAkH
K100-ub GGLTGLNkAETAAkH
K106 NkAETAAKHGEAQVk
K106-ub NkAETAAkHGEAQVk
K113 kHGEAQVKIWRRsyD
K113-ub kHGEAQVkIWRRsyD
S118-p QVkIWRRsyDVPPPP
Y119-p VkIWRRsyDVPPPPM
Y133-p MEPDHPFySNISkDR
K138-ub PFySNISkDRRYADL
K157-ub LPSCESLkDTIARAL
K157-ac LPSCESLkDTIARAL
K176-ub EEIVPQIkEGKRVLI
S189 LIAAHGNSLRGIVkH
K195-ac NSLRGIVkHLEGLSE
K195 NSLRGIVKHLEGLSE
T238 QFLGDEETVRkAMEA
K241-ub GDEETVRkAMEAVAA
K251-ub EAVAAQGkVKK____
  rat

 
K5 ___MAAYKLVLIRHG
K5 ___MAAYKLVLIRHG
H11 YKLVLIRHGEsAWNL
S14-p VLIRHGEsAWNLENR
S23-p WNLENRFsGWyDADL
Y26-p ENRFsGWyDADLSPA
S31 GWyDADLSPAGHEEA
K39 PAGHEEAKRGGQALR
K39 PAGHEEAKRGGQALR
Y50-p QALRDAGyEFDICFT
Y92-p WRLNERHyGGLTGLN
T96 ERHyGGLTGLNKAET
K100 GGLTGLNKAETAAkH
K100 GGLTGLNKAETAAkH
K106 NKAETAAKHGEAQVk
K106-ub NKAETAAkHGEAQVk
K113 kHGEAQVKIWRRSyD
K113-ub kHGEAQVkIWRRSyD
S118 QVkIWRRSyDVPPPP
Y119-p VkIWRRSyDVPPPPM
Y133 MEPDHPFYSNISKDR
K138 PFYSNISKDRRYADL
K157 LPSCESLKDTIARAL
K157 LPSCESLKDTIARAL
K176 EEIVPQIKEGKRVLI
S189 LIAAHGNSLRGIVKH
K195 NSLRGIVKHLEGLSE
K195 NSLRGIVKHLEGLSE
T238 QFLGDEETVRKAMEA
K241 GDEETVRKAMEAVAA
K251 EAVAAQGKVKK____
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