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Phosphoglycerate mutase 2 (EC 5.4.2.11) (EC 5.4.2.4) (BPG-dependent PGAM 2) (Muscle-specific phosphoglycerate mutase) (Phosphoglycerate mutase isozyme M) (PGAM-M)

 PGAM2_HUMAN             Reviewed;         253 AA.
P15259;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
18-JUL-2018, entry version 186.
RecName: Full=Phosphoglycerate mutase 2;
EC=5.4.2.11 {ECO:0000250|UniProtKB:P18669};
EC=5.4.2.4 {ECO:0000250|UniProtKB:P18669};
AltName: Full=BPG-dependent PGAM 2;
AltName: Full=Muscle-specific phosphoglycerate mutase;
AltName: Full=Phosphoglycerate mutase isozyme M;
Short=PGAM-M;
Name=PGAM2; Synonyms=PGAMM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2145198; DOI=10.1016/0378-1119(90)90092-6;
Castella-Escola J., Ojcius D.M., Leboulch P., Joulin V., Blouquit Y.,
Garel M.-C., Valentin C., Rosa R., Climent-Romeo F., Cohen-Solal M.;
"Isolation and characterization of the gene encoding the muscle-
specific isozyme of human phosphoglycerate mutase.";
Gene 91:225-232(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2549058;
Tsujino S., Sakoda S., Mizuno R., Kobayashi T., Suzuki T.,
Kishimoto S., Shanske S., Dimauro S., Schon E.A.;
"Structure of the gene encoding the muscle-specific subunit of human
phosphoglycerate mutase.";
J. Biol. Chem. 264:15334-15337(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=2822696;
Shanske S., Sakoda S., Hermodson M.A., Dimauro S., Schon E.A.;
"Isolation of a cDNA encoding the muscle-specific subunit of human
phosphoglycerate mutase.";
J. Biol. Chem. 262:14612-14617(1987).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
VARIANTS GSD10 ALA-89 AND TRP-90.
PubMed=8447317;
Tsujino S., Shanske S., Sakoda S., Fenichel G., Dimauro S.;
"The molecular genetic basis of muscle phosphoglycerate mutase (PGAM)
deficiency.";
Am. J. Hum. Genet. 52:472-477(1993).
[6]
VARIANT GSD10 ASP-97.
PubMed=10545043; DOI=10.1016/S0960-8966(99)00039-5;
Hadjigeorgiou G.M., Kawashima N., Bruno C., Andreu A.L., Sue C.M.,
Rigden D.J., Kawashima A., Shanske S., DiMauro S.;
"Manifesting heterozygotes in a Japanese family with a novel mutation
in the muscle-specific phosphoglycerate mutase (PGAM-M) gene.";
Neuromuscul. Disord. 9:399-402(1999).
-!- 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), but with a reduced
activity.
-!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
{ECO:0000250|UniProtKB:P18669}.
-!- CATALYTIC ACTIVITY: 3-phospho-D-glyceroyl phosphate = 2,3-
bisphospho-D-glycerate. {ECO:0000250|UniProtKB:P18669}.
-!- SUBUNIT: Homodimer. Interacts with ENO1.
{ECO:0000250|UniProtKB:O70250, ECO:0000250|UniProtKB:P18669}.
-!- TISSUE SPECIFICITY: Expressed in the heart and muscle. Not found
in the liver and brain. {ECO:0000269|PubMed:2822696}.
-!- DISEASE: Glycogen storage disease 10 (GSD10) [MIM:261670]: A
metabolic disorder characterized by myoglobinuria, increased serum
creatine kinase levels, decreased phosphoglycerate mutase
activity, myalgia, muscle pain, muscle cramps, exercise
intolerance. {ECO:0000269|PubMed:10545043,
ECO:0000269|PubMed:8447317}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
dependent PGAM subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M55674; AAA64238.1; -; Genomic_DNA.
EMBL; M55673; AAA64238.1; JOINED; Genomic_DNA.
EMBL; J05073; AAA60073.1; -; Genomic_DNA.
EMBL; M18172; AAA60072.1; -; mRNA.
EMBL; BC001904; AAH01904.1; -; mRNA.
EMBL; BC073741; AAH73741.1; -; mRNA.
CCDS; CCDS34624.1; -.
PIR; JQ0750; PMHUYM.
RefSeq; NP_000281.2; NM_000290.3.
UniGene; Hs.632642; -.
ProteinModelPortal; P15259; -.
SMR; P15259; -.
BioGrid; 111245; 13.
IntAct; P15259; 8.
STRING; 9606.ENSP00000297283; -.
DrugBank; DB04510; 3-Phosphoglyceric Acid.
DrugBank; DB01681; Benzene Hexacarboxylic Acid.
DEPOD; P15259; -.
iPTMnet; P15259; -.
PhosphoSitePlus; P15259; -.
BioMuta; PGAM2; -.
DMDM; 130353; -.
UCD-2DPAGE; P15259; -.
EPD; P15259; -.
MaxQB; P15259; -.
PaxDb; P15259; -.
PeptideAtlas; P15259; -.
PRIDE; P15259; -.
ProteomicsDB; 53121; -.
Ensembl; ENST00000297283; ENSP00000297283; ENSG00000164708.
GeneID; 5224; -.
KEGG; hsa:5224; -.
UCSC; uc003tjs.3; human.
CTD; 5224; -.
DisGeNET; 5224; -.
EuPathDB; HostDB:ENSG00000164708.5; -.
GeneCards; PGAM2; -.
HGNC; HGNC:8889; PGAM2.
HPA; HPA050314; -.
HPA; HPA060173; -.
MalaCards; PGAM2; -.
MIM; 261670; phenotype.
MIM; 612931; gene.
neXtProt; NX_P15259; -.
OpenTargets; ENSG00000164708; -.
Orphanet; 97234; Glycogen storage disease due to phosphoglycerate mutase deficiency.
PharmGKB; PA33226; -.
eggNOG; KOG0235; Eukaryota.
eggNOG; COG0588; LUCA.
GeneTree; ENSGT00390000016700; -.
HOGENOM; HOG000221682; -.
HOVERGEN; HBG027528; -.
InParanoid; P15259; -.
KO; K01834; -.
OMA; WTILDGT; -.
OrthoDB; EOG091G0GIS; -.
PhylomeDB; P15259; -.
TreeFam; TF300007; -.
BioCyc; MetaCyc:HS09121-MONOMER; -.
Reactome; R-HSA-70171; Glycolysis.
Reactome; R-HSA-70263; Gluconeogenesis.
GenomeRNAi; 5224; -.
PRO; PR:P15259; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000164708; -.
CleanEx; HS_PGAM2; -.
Genevisible; P15259; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IBA:GO_Central.
GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC.
GO; GO:0048037; F:cofactor binding; IEA:Ensembl.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0004619; F:phosphoglycerate mutase activity; IMP:UniProtKB.
GO; GO:0061621; P:canonical glycolysis; TAS:Reactome.
GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
GO; GO:0006096; P:glycolytic process; IMP:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:0043456; P:regulation of pentose-phosphate shunt; IBA:GO_Central.
GO; GO:0046689; P:response to mercury ion; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0006941; P:striated muscle contraction; IMP:UniProtKB.
CDD; cd07067; HP_PGM_like; 1.
Gene3D; 3.40.50.1240; -; 1.
HAMAP; MF_01039; PGAM_GpmA; 1.
InterPro; IPR013078; His_Pase_superF_clade-1.
InterPro; IPR029033; His_PPase_superfam.
InterPro; IPR001345; PG/BPGM_mutase_AS.
InterPro; IPR005952; Phosphogly_mut1.
PANTHER; PTHR11931; PTHR11931; 1.
Pfam; PF00300; His_Phos_1; 2.
SMART; SM00855; PGAM; 1.
SUPFAM; SSF53254; SSF53254; 1.
TIGRFAMs; TIGR01258; pgm_1; 1.
PROSITE; PS00175; PG_MUTASE; 1.
1: Evidence at protein level;
Complete proteome; Disease mutation; Glycogen storage disease;
Glycolysis; Hydrolase; Isomerase; Phosphoprotein; Reference proteome.
CHAIN 1 253 Phosphoglycerate mutase 2.
/FTId=PRO_0000179829.
REGION 10 17 Substrate binding.
{ECO:0000250|UniProtKB:P00950}.
REGION 23 24 Substrate binding.
{ECO:0000250|UniProtKB:P00950}.
REGION 89 92 Substrate binding.
{ECO:0000250|UniProtKB:P00950}.
REGION 116 117 Substrate binding.
{ECO:0000250|UniProtKB:P00950}.
REGION 187 188 Substrate binding.
{ECO:0000250|UniProtKB:P00950}.
COMPBIAS 122 125 Poly-Pro.
ACT_SITE 11 11 Tele-phosphohistidine intermediate.
{ECO:0000250|UniProtKB:P18669}.
ACT_SITE 89 89 Proton donor/acceptor.
{ECO:0000250|UniProtKB:P18669}.
BINDING 62 62 Substrate.
{ECO:0000250|UniProtKB:P00950}.
BINDING 100 100 Substrate.
{ECO:0000250|UniProtKB:P00950}.
SITE 186 186 Transition state stabilizer.
{ECO:0000250|UniProtKB:P00950}.
MOD_RES 3 3 Phosphothreonine.
{ECO:0000250|UniProtKB:P16290}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000250|UniProtKB:P16290}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000250|UniProtKB:O70250}.
MOD_RES 132 132 Phosphotyrosine.
{ECO:0000250|UniProtKB:P16290}.
MOD_RES 133 133 Phosphotyrosine.
{ECO:0000250|UniProtKB:P16290}.
MOD_RES 135 135 Phosphoserine.
{ECO:0000250|UniProtKB:P16290}.
MOD_RES 152 152 Phosphothreonine.
{ECO:0000250|UniProtKB:P16290}.
VARIANT 89 89 E -> A (in GSD10; dbSNP:rs104894030).
{ECO:0000269|PubMed:8447317}.
/FTId=VAR_006088.
VARIANT 90 90 R -> W (in GSD10; dbSNP:rs104894034).
{ECO:0000269|PubMed:8447317}.
/FTId=VAR_006089.
VARIANT 97 97 G -> D (in GSD10; dbSNP:rs77938727).
{ECO:0000269|PubMed:10545043}.
/FTId=VAR_013103.
CONFLICT 14 14 S -> T (in Ref. 3; AAA60072).
{ECO:0000305}.
CONFLICT 65 65 R -> P (in Ref. 2; AAA60073).
{ECO:0000305}.
CONFLICT 85 85 W -> C (in Ref. 2). {ECO:0000305}.
CONFLICT 87 87 L -> F (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 98 98 L -> F (in Ref. 3; AAA60072).
{ECO:0000305}.
CONFLICT 113 114 KI -> RS (in Ref. 3; AAA60072).
{ECO:0000305}.
SEQUENCE 253 AA; 28766 MW; 0FDC97631104FCF7 CRC64;
MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL
KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD
IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR
VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR
KAMEAVAAQG KAK


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