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Protein Page:
PGAM2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
PGAM2 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. Defects in PGAM2 are the cause of glycogen storage disease type 10 (GSD10). A metabolic disorder characterized by myoglobinuria, increased serum creatine kinase levels, decreased phosphoglycerate mutase activity, myalgia, muscle pain, muscle cramps and excercise intolerance. 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; Carbohydrate Metabolism - glycolysis and gluconeogenesis; EC 5.4.2.1; Isomerase; EC 5.4.2.4; Phosphatase (non-protein)
Cellular Component: cytosol; nucleus
Molecular Function: phosphoglycerate mutase activity; bisphosphoglycerate mutase activity; bisphosphoglycerate phosphatase activity; cofactor binding; 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
Biological Process: response to mercury ion; glycolysis; striated muscle contraction; carbohydrate metabolic process; glucose metabolic process; spermatogenesis; gluconeogenesis
Reference #:  P15259 (UniProtKB)
Alt. Names/Synonyms: BPG-dependent PGAM 2; GSD10; MGC88743; Muscle-specific phosphoglycerate mutase; PGAM-M; PGAM2; PGAMM; Phosphoglycerate mutase 2; phosphoglycerate mutase 2 (muscle); Phosphoglycerate mutase isozyme M
Gene Symbols: PGAM2
Molecular weight: 28,766 Da
Basal Isoelectric point: 8.99  Predict pI for various phosphorylation states
Select Structure to View Below

PGAM2
Protein Structure Not Found.


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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 1 K33-a FDAELSEkGTEEAkR
0 5 K39-a EkGTEEAkRGAKAIK
0 2 S58 EFDICYTSVLKRAIR
0 1 K61 ICYTSVLKRAIRTLW
0 2214 Y92-p WRLNERHyGGLtGLN
0 55 T96-p ERHyGGLtGLNkAET
0 23 K100-a GGLtGLNkAETAAKH
0 15 K100-u GGLtGLNkAETAAKH
0 3 K106 NkAETAAKHGEEQVK
0 1 K113 KHGEEQVKIWRRSFD
0 1 S118 QVKIWRRSFDIPPPP
0 1 K129 PPPPMDEKHPyyNsI
0 22 Y132-p PMDEKHPyyNsIsKE
0 5 Y133-p MDEKHPyyNsIsKER
0 3 N134 DEKHPyyNsIsKERR
0 13 S135-p EKHPyyNsIsKERRY
0 3 S137-p HPyyNsIsKERRYAG
0 2 K138 PyyNsIsKERRYAGL
0 1 K146 ERRYAGLKPGELPtC
0 1 T152-p LKPGELPtCESLKDT
0 1 K157 LPtCESLKDTIARAL
0 1 Q174 WNEEIVPQIKAGkRV
0 1 Q174 WNEEIVPQIKAGkRV
1 1 K179-u VPQIKAGkRVLIAAH
1 1 K195-u NSLRGIVkHLEGMSD
0 3 K241 GDEETVRKAMEAVAA
0 4 K251-u EAVAAQGkAK_____
  mouse

 
K33 FDAELSEKGAEEAKR
K39 EKGAEEAKRGATAIK
S58-p EFDICYTsVLkRAIR
K61-u ICYTsVLkRAIRTLW
Y92-p WRLNERHyGGLTGLN
T96 ERHyGGLTGLNkAET
K100-a GGLTGLNkAETAAkH
K100-u GGLTGLNkAETAAkH
K106-u NkAETAAkHGEEQVk
K113-u kHGEEQVkIWRRsFD
S118-p QVkIWRRsFDTPPPP
K129-u PPPPMDEkHNyytsI
Y132-p PMDEkHNyytsISkD
Y133-p MDEkHNyytsISkDR
T134-p DEkHNyytsISkDRR
S135-p EkHNyytsISkDRRY
S137 HNyytsISkDRRYAG
K138-u NyytsISkDRRYAGL
K146-u DRRYAGLkPEELPTC
T152 LkPEELPTCESLkDT
K157-u LPTCESLkDTIARAL
K174 WNEEIAPKIKAGQRV
K174-u WNEEIAPkIKAGQRV
Q179 APkIKAGQRVLIAAH
K195 NSLRGIVKHLEGMSD
K241-u GDEETVRkAMEAVAA
K251-u EAVAAQGkAK_____
  rat

 
K33 FDAELSEKGAEEAKR
K39 EKGAEEAKRGATAIK
S58 EFDICYTSVLKRAIR
K61 ICYTSVLKRAIRTLW
Y92-p WRLNERHyGGLTGLN
T96 ERHyGGLTGLNKAET
K100 GGLTGLNKAETAAKH
K100 GGLTGLNKAETAAKH
K106 NKAETAAKHGEEQVK
K113 KHGEEQVKIWRRSFD
S118 QVKIWRRSFDTPPPP
K129 PPPPMDEKHNYYASI
Y132 PMDEKHNYYASISKD
Y133 MDEKHNYYASISKDR
A134 DEKHNYYASISKDRR
S135 EKHNYYASISKDRRY
S137 HNYYASISKDRRYAG
K138 NYYASISKDRRYAGL
K146 DRRYAGLKPEELPTC
T152 LKPEELPTCESLKDT
K157 LPTCESLKDTIARAL
K174-m2 WNEEIAPkIKAGKRV
K174 WNEEIAPKIKAGKRV
K179 APkIKAGKRVLIAAH
K195 NSLRGIVKHLEGMSD
K241 GDEETVRKAMEAVAA
K251 EAVAAQGKAK_____
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