PGAM2_HUMAN
ID PGAM2_HUMAN Reviewed; 253 AA.
AC P15259;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Phosphoglycerate mutase 2;
DE EC=5.4.2.11 {ECO:0000250|UniProtKB:P18669};
DE EC=5.4.2.4 {ECO:0000250|UniProtKB:P18669};
DE AltName: Full=BPG-dependent PGAM 2;
DE AltName: Full=Muscle-specific phosphoglycerate mutase;
DE AltName: Full=Phosphoglycerate mutase isozyme M;
DE Short=PGAM-M;
GN Name=PGAM2; Synonyms=PGAMM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2145198; DOI=10.1016/0378-1119(90)90092-6;
RA Castella-Escola J., Ojcius D.M., Leboulch P., Joulin V., Blouquit Y.,
RA Garel M.-C., Valentin C., Rosa R., Climent-Romeo F., Cohen-Solal M.;
RT "Isolation and characterization of the gene encoding the muscle-specific
RT isozyme of human phosphoglycerate mutase.";
RL Gene 91:225-232(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2549058; DOI=10.1016/s0021-9258(19)84831-7;
RA Tsujino S., Sakoda S., Mizuno R., Kobayashi T., Suzuki T., Kishimoto S.,
RA Shanske S., Dimauro S., Schon E.A.;
RT "Structure of the gene encoding the muscle-specific subunit of human
RT phosphoglycerate mutase.";
RL J. Biol. Chem. 264:15334-15337(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=2822696; DOI=10.1016/s0021-9258(18)47840-4;
RA Shanske S., Sakoda S., Hermodson M.A., Dimauro S., Schon E.A.;
RT "Isolation of a cDNA encoding the muscle-specific subunit of human
RT phosphoglycerate mutase.";
RL J. Biol. Chem. 262:14612-14617(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP VARIANTS GSD10 ALA-89 AND TRP-90.
RX PubMed=8447317;
RA Tsujino S., Shanske S., Sakoda S., Fenichel G., Dimauro S.;
RT "The molecular genetic basis of muscle phosphoglycerate mutase (PGAM)
RT deficiency.";
RL Am. J. Hum. Genet. 52:472-477(1993).
RN [6]
RP VARIANT GSD10 ASP-97.
RX PubMed=10545043; DOI=10.1016/s0960-8966(99)00039-5;
RA Hadjigeorgiou G.M., Kawashima N., Bruno C., Andreu A.L., Sue C.M.,
RA Rigden D.J., Kawashima A., Shanske S., DiMauro S.;
RT "Manifesting heterozygotes in a Japanese family with a novel mutation in
RT the muscle-specific phosphoglycerate mutase (PGAM-M) gene.";
RL Neuromuscul. Disord. 9:399-402(1999).
CC -!- FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-
CC bisphosphoglycerate as the primer of the reaction. Can also catalyze
CC the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000250|UniProtKB:P18669};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-
CC bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4;
CC Evidence={ECO:0000250|UniProtKB:P18669};
CC -!- SUBUNIT: Homodimer. Interacts with ENO1. {ECO:0000250|UniProtKB:O70250,
CC ECO:0000250|UniProtKB:P18669}.
CC -!- INTERACTION:
CC P15259; P07738: BPGM; NbExp=4; IntAct=EBI-2511669, EBI-2115835;
CC P15259; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-2511669, EBI-12357161;
CC P15259; Q9Y6G9: DYNC1LI1; NbExp=3; IntAct=EBI-2511669, EBI-2556107;
CC P15259; Q9BW62: KATNAL1; NbExp=3; IntAct=EBI-2511669, EBI-743591;
CC P15259; P15259: PGAM2; NbExp=3; IntAct=EBI-2511669, EBI-2511669;
CC -!- TISSUE SPECIFICITY: Expressed in the heart and muscle. Not found in the
CC liver and brain. {ECO:0000269|PubMed:2822696}.
CC -!- DISEASE: Glycogen storage disease 10 (GSD10) [MIM:261670]: A metabolic
CC disorder characterized by myoglobinuria, increased serum creatine
CC kinase levels, decreased phosphoglycerate mutase activity, myalgia,
CC muscle pain, muscle cramps, exercise intolerance.
CC {ECO:0000269|PubMed:10545043, ECO:0000269|PubMed:8447317}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; M55674; AAA64238.1; -; Genomic_DNA.
DR EMBL; M55673; AAA64238.1; JOINED; Genomic_DNA.
DR EMBL; J05073; AAA60073.1; -; Genomic_DNA.
DR EMBL; M18172; AAA60072.1; -; mRNA.
DR EMBL; BC001904; AAH01904.1; -; mRNA.
DR EMBL; BC073741; AAH73741.1; -; mRNA.
DR CCDS; CCDS34624.1; -.
DR PIR; JQ0750; PMHUYM.
DR RefSeq; NP_000281.2; NM_000290.3.
DR AlphaFoldDB; P15259; -.
DR SMR; P15259; -.
DR BioGRID; 111245; 68.
DR IntAct; P15259; 12.
DR STRING; 9606.ENSP00000297283; -.
DR DrugBank; DB04510; 3-phospho-D-glyceric acid.
DR DrugBank; DB01681; Benzene Hexacarboxylic Acid.
DR DEPOD; PGAM2; -.
DR iPTMnet; P15259; -.
DR PhosphoSitePlus; P15259; -.
DR BioMuta; PGAM2; -.
DR DMDM; 130353; -.
DR UCD-2DPAGE; P15259; -.
DR EPD; P15259; -.
DR jPOST; P15259; -.
DR MassIVE; P15259; -.
DR MaxQB; P15259; -.
DR PaxDb; P15259; -.
DR PeptideAtlas; P15259; -.
DR PRIDE; P15259; -.
DR ProteomicsDB; 53121; -.
DR Antibodypedia; 26984; 373 antibodies from 27 providers.
DR DNASU; 5224; -.
DR Ensembl; ENST00000297283.4; ENSP00000297283.3; ENSG00000164708.6.
DR GeneID; 5224; -.
DR KEGG; hsa:5224; -.
DR MANE-Select; ENST00000297283.4; ENSP00000297283.3; NM_000290.4; NP_000281.2.
DR UCSC; uc003tjs.3; human.
DR CTD; 5224; -.
DR DisGeNET; 5224; -.
DR GeneCards; PGAM2; -.
DR HGNC; HGNC:8889; PGAM2.
DR HPA; ENSG00000164708; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR MalaCards; PGAM2; -.
DR MIM; 261670; phenotype.
DR MIM; 612931; gene.
DR neXtProt; NX_P15259; -.
DR OpenTargets; ENSG00000164708; -.
DR Orphanet; 97234; Glycogen storage disease due to phosphoglycerate mutase deficiency.
DR PharmGKB; PA33226; -.
DR VEuPathDB; HostDB:ENSG00000164708; -.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00950000182926; -.
DR HOGENOM; CLU_033323_1_1_1; -.
DR InParanoid; P15259; -.
DR OMA; MATHRVV; -.
DR OrthoDB; 804949at2759; -.
DR PhylomeDB; P15259; -.
DR TreeFam; TF300007; -.
DR BioCyc; MetaCyc:HS09121-MON; -.
DR BRENDA; 5.4.2.11; 2681.
DR PathwayCommons; P15259; -.
DR Reactome; R-HSA-70171; Glycolysis.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR SignaLink; P15259; -.
DR SIGNOR; P15259; -.
DR BioGRID-ORCS; 5224; 15 hits in 1075 CRISPR screens.
DR ChiTaRS; PGAM2; human.
DR GenomeRNAi; 5224; -.
DR Pharos; P15259; Tbio.
DR PRO; PR:P15259; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P15259; protein.
DR Bgee; ENSG00000164708; Expressed in apex of heart and 122 other tissues.
DR Genevisible; P15259; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:Ensembl.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IMP:UniProtKB.
DR GO; GO:0061621; P:canonical glycolysis; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR GO; GO:0006096; P:glycolytic process; IMP:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0046689; P:response to mercury ion; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0006941; P:striated muscle contraction; IMP:UniProtKB.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW Disease variant; Glycogen storage disease; Glycolysis; Hydrolase;
KW Isomerase; Phosphoprotein; Reference proteome.
FT CHAIN 1..253
FT /note="Phosphoglycerate mutase 2"
FT /id="PRO_0000179829"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 23..24
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT SITE 186
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70250"
FT MOD_RES 132
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 133
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16290"
FT VARIANT 89
FT /note="E -> A (in GSD10; dbSNP:rs104894030)"
FT /evidence="ECO:0000269|PubMed:8447317"
FT /id="VAR_006088"
FT VARIANT 90
FT /note="R -> W (in GSD10; dbSNP:rs104894034)"
FT /evidence="ECO:0000269|PubMed:8447317"
FT /id="VAR_006089"
FT VARIANT 97
FT /note="G -> D (in GSD10; dbSNP:rs77938727)"
FT /evidence="ECO:0000269|PubMed:10545043"
FT /id="VAR_013103"
FT CONFLICT 14
FT /note="S -> T (in Ref. 3; AAA60072)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="R -> P (in Ref. 2; AAA60073)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="W -> C (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="L -> F (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="L -> F (in Ref. 3; AAA60072)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..114
FT /note="KI -> RS (in Ref. 3; AAA60072)"
FT /evidence="ECO:0000305"
SQ 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
