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Protein

Bisphosphoglycerate mutase

Gene

BPGM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11) activity.1 Publication

Catalytic activityi

3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.1 Publication
2-phospho-D-glycerate = 3-phospho-D-glycerate.1 Publication

Activity regulationi

At alkaline pH BPGM favors the synthase reaction; however, at lower pH the phosphatase reaction is dominant. Inhibited by citrate.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei11Tele-phosphohistidine intermediate1 Publication1
Binding sitei62Substrate1 Publication1
Active sitei89Proton donor/acceptor1 Publication1
Binding sitei100Substrate1 Publication1
Sitei188Transition state stabilizer1 Publication1

GO - Molecular functioni

GO - Biological processi

  • canonical glycolysis Source: Reactome
  • carbohydrate metabolic process Source: ProtInc
  • erythrocyte development Source: Ensembl
  • gluconeogenesis Source: GO_Central
  • glycolytic process Source: GO_Central
  • regulation of pentose-phosphate shunt Source: GO_Central
  • respiratory gaseous exchange Source: ProtInc

Keywordsi

Molecular functionHydrolase, Isomerase
Biological processGlycolysis

Enzyme and pathway databases

BioCyciMetaCyc:HS10491-MONOMER
BRENDAi3.1.3.13 2681
5.4.2.4 2681
ReactomeiR-HSA-70171 Glycolysis
SABIO-RKiP07738

Names & Taxonomyi

Protein namesi
Recommended name:
Bisphosphoglycerate mutase (EC:5.4.2.41 Publication)
Short name:
BPGM
Alternative name(s):
2,3-bisphosphoglycerate mutase, erythrocyte
2,3-bisphosphoglycerate synthase (EC:5.4.2.111 Publication)
2,3-diphosphoglycerate mutase
Short name:
DPGM
BPG-dependent PGAM
Gene namesi
Name:BPGM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000172331.11
HGNCiHGNC:1093 BPGM
MIMi613896 gene
neXtProtiNX_P07738

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Involvement in diseasei

Bisphosphoglycerate mutase deficiency (BPGMD)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis.
See also OMIM:222800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06536762R → Q in BPGMD. 1 PublicationCorresponds to variant dbSNP:rs751972865Ensembl.1
Natural variantiVAR_06536890R → C in BPGMD; mutation identified at protein level; marked decrease in synthase and mutase activities; no effect on phosphatase activity. 2 PublicationsCorresponds to variant dbSNP:rs121964925EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

DisGeNETi669
MalaCardsiBPGM
MIMi222800 phenotype
OpenTargetsiENSG00000172331
Orphaneti714 Hemolytic anemia due to diphosphoglycerate mutase deficiency
PharmGKBiPA25401

Polymorphism and mutation databases

BioMutaiBPGM
DMDMi130350

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00001798342 – 259Bisphosphoglycerate mutaseAdd BLAST258

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Glycosylationi3N-linked (Glc) (glycation) lysine; in vitro1 Publication1
Glycosylationi5N-linked (Glc) (glycation) lysine; in vitro1 Publication1
Glycosylationi18N-linked (Glc) (glycation) lysine; in vitro1 Publication1
Glycosylationi43N-linked (Glc) (glycation) lysine; in vitro1 Publication1
Modified residuei122PhosphothreonineCombined sources1
Glycosylationi159N-linked (Glc) (glycation) lysine1 Publication1
Glycosylationi197N-linked (Glc) (glycation) lysine; in vitro1 Publication1

Post-translational modificationi

Glycation of Lys-159 in diabetic patients inactivates the enzyme.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei29Not glycated1 Publication1
Sitei46Not glycated1 Publication1
Sitei143Not glycated1 Publication1
Sitei181Not glycated1 Publication1
Sitei246Not glycated1 Publication1
Sitei247Not glycated1 Publication1
Sitei253Not glycated1 Publication1
Sitei258Not glycated1 Publication1
Sitei259Not glycated1 Publication1

Keywords - PTMi

Acetylation, Glycation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP07738
MaxQBiP07738
PaxDbiP07738
PeptideAtlasiP07738
PRIDEiP07738
ProteomicsDBi52025

2D gel databases

REPRODUCTION-2DPAGEiIPI00215979

PTM databases

DEPODiP07738
iPTMnetiP07738
PhosphoSitePlusiP07738

Expressioni

Tissue specificityi

Expressed in red blood cells. Expressed in non-erythroid cells of the placenta; present in the syncytiotrophoblast layer of the placental villi at the feto-maternal interface (at protein level).3 Publications

Gene expression databases

BgeeiENSG00000172331 Expressed in 217 organ(s), highest expression level in secondary oocyte
CleanExiHS_BPGM
ExpressionAtlasiP07738 baseline and differential
GenevisibleiP07738 HS

Organism-specific databases

HPAiHPA016493
HPA028735

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi107137, 22 interactors
IntActiP07738, 9 interactors
STRINGi9606.ENSP00000342032

Structurei

Secondary structure

1259
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP07738
SMRiP07738
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07738

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni10 – 17Substrate binding1 Publication8
Regioni23 – 24Substrate binding1 Publication2
Regioni89 – 92Substrate binding1 Publication4
Regioni116 – 117Substrate binding1 Publication2
Regioni189 – 190Substrate binding1 Publication2

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0235 Eukaryota
COG0588 LUCA
GeneTreeiENSGT00390000016700
HOGENOMiHOG000221682
HOVERGENiHBG027528
InParanoidiP07738
KOiK01837
OMAiNLHAVGP
OrthoDBiEOG091G0GIS
PhylomeDBiP07738
TreeFamiTF300007

Family and domain databases

CDDicd07067 HP_PGM_like, 1 hit
Gene3Di3.40.50.1240, 1 hit
HAMAPiMF_01039 PGAM_GpmA, 1 hit
InterProiView protein in InterPro
IPR013078 His_Pase_superF_clade-1
IPR029033 His_PPase_superfam
IPR001345 PG/BPGM_mutase_AS
IPR005952 Phosphogly_mut1
PANTHERiPTHR11931 PTHR11931, 1 hit
PfamiView protein in Pfam
PF00300 His_Phos_1, 2 hits
SMARTiView protein in SMART
SM00855 PGAM, 1 hit
SUPFAMiSSF53254 SSF53254, 1 hit
TIGRFAMsiTIGR01258 pgm_1, 1 hit
PROSITEiView protein in PROSITE
PS00175 PG_MUTASE, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.iShow all

P07738-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF
60 70 80 90 100
EFDLVFTSVL NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR
110 120 130 140 150
EQMALNHGEE QVRLWRRSYN VTPPPIEESH PYYQEIYNDR RYKVCDVPLD
160 170 180 190 200
QLPRSESLKD VLERLLPYWN ERIAPEVLRG KTILISAHGN SSRALLKHLE
210 220 230 240 250
GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA IQAAIKKVED

QGKVKQAKK
Length:259
Mass (Da):30,005
Last modified:January 23, 2007 - v2
Checksum:iA2AF1D6F2985A3B5
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9JH23C9JH23_HUMAN
Phosphoglycerate mutase
BPGM
78Annotation score:

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06536762R → Q in BPGMD. 1 PublicationCorresponds to variant dbSNP:rs751972865Ensembl.1
Natural variantiVAR_06536890R → C in BPGMD; mutation identified at protein level; marked decrease in synthase and mutase activities; no effect on phosphatase activity. 2 PublicationsCorresponds to variant dbSNP:rs121964925EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04327 mRNA Translation: CAA27858.1
M23068, M23067 Genomic DNA Translation: AAA51840.1
AK315439 mRNA Translation: BAG37827.1
CH236950 Genomic DNA Translation: EAL24067.1
CH471070 Genomic DNA Translation: EAW83821.1
BC017050 mRNA Translation: AAH17050.1
CCDSiCCDS5833.1
PIRiA31999 PMHUBM
RefSeqiNP_001280014.1, NM_001293085.1
NP_001715.1, NM_001724.4
NP_954655.1, NM_199186.2
XP_011514829.1, XM_011516527.1
UniGeneiHs.198365

Genome annotation databases

EnsembliENST00000344924; ENSP00000342032; ENSG00000172331
ENST00000393132; ENSP00000376840; ENSG00000172331
ENST00000418040; ENSP00000399838; ENSG00000172331
GeneIDi669
KEGGihsa:669
UCSCiuc003vrv.4 human

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04327 mRNA Translation: CAA27858.1
M23068, M23067 Genomic DNA Translation: AAA51840.1
AK315439 mRNA Translation: BAG37827.1
CH236950 Genomic DNA Translation: EAL24067.1
CH471070 Genomic DNA Translation: EAW83821.1
BC017050 mRNA Translation: AAH17050.1
CCDSiCCDS5833.1
PIRiA31999 PMHUBM
RefSeqiNP_001280014.1, NM_001293085.1
NP_001715.1, NM_001724.4
NP_954655.1, NM_199186.2
XP_011514829.1, XM_011516527.1
UniGeneiHs.198365

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T8PX-ray2.50A/B1-259[»]
2A9JX-ray2.00A/B1-259[»]
2F90X-ray2.00A/B1-259[»]
2H4XX-ray1.85A/B1-259[»]
2H4ZX-ray2.00A/B1-259[»]
2H52X-ray2.00A/B1-259[»]
2HHJX-ray1.50A/B1-259[»]
3NFYX-ray1.94A/B1-259[»]
ProteinModelPortaliP07738
SMRiP07738
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107137, 22 interactors
IntActiP07738, 9 interactors
STRINGi9606.ENSP00000342032

PTM databases

DEPODiP07738
iPTMnetiP07738
PhosphoSitePlusiP07738

Polymorphism and mutation databases

BioMutaiBPGM
DMDMi130350

2D gel databases

REPRODUCTION-2DPAGEiIPI00215979

Proteomic databases

EPDiP07738
MaxQBiP07738
PaxDbiP07738
PeptideAtlasiP07738
PRIDEiP07738
ProteomicsDBi52025

Protocols and materials databases

DNASUi669
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344924; ENSP00000342032; ENSG00000172331
ENST00000393132; ENSP00000376840; ENSG00000172331
ENST00000418040; ENSP00000399838; ENSG00000172331
GeneIDi669
KEGGihsa:669
UCSCiuc003vrv.4 human

Organism-specific databases

CTDi669
DisGeNETi669
EuPathDBiHostDB:ENSG00000172331.11
GeneCardsiBPGM
HGNCiHGNC:1093 BPGM
HPAiHPA016493
HPA028735
MalaCardsiBPGM
MIMi222800 phenotype
613896 gene
neXtProtiNX_P07738
OpenTargetsiENSG00000172331
Orphaneti714 Hemolytic anemia due to diphosphoglycerate mutase deficiency
PharmGKBiPA25401
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0235 Eukaryota
COG0588 LUCA
GeneTreeiENSGT00390000016700
HOGENOMiHOG000221682
HOVERGENiHBG027528
InParanoidiP07738
KOiK01837
OMAiNLHAVGP
OrthoDBiEOG091G0GIS
PhylomeDBiP07738
TreeFamiTF300007

Enzyme and pathway databases

BioCyciMetaCyc:HS10491-MONOMER
BRENDAi3.1.3.13 2681
5.4.2.4 2681
ReactomeiR-HSA-70171 Glycolysis
SABIO-RKiP07738

Miscellaneous databases

ChiTaRSiBPGM human
EvolutionaryTraceiP07738
GenomeRNAii669
PROiPR:P07738
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000172331 Expressed in 217 organ(s), highest expression level in secondary oocyte
CleanExiHS_BPGM
ExpressionAtlasiP07738 baseline and differential
GenevisibleiP07738 HS

Family and domain databases

CDDicd07067 HP_PGM_like, 1 hit
Gene3Di3.40.50.1240, 1 hit
HAMAPiMF_01039 PGAM_GpmA, 1 hit
InterProiView protein in InterPro
IPR013078 His_Pase_superF_clade-1
IPR029033 His_PPase_superfam
IPR001345 PG/BPGM_mutase_AS
IPR005952 Phosphogly_mut1
PANTHERiPTHR11931 PTHR11931, 1 hit
PfamiView protein in Pfam
PF00300 His_Phos_1, 2 hits
SMARTiView protein in SMART
SM00855 PGAM, 1 hit
SUPFAMiSSF53254 SSF53254, 1 hit
TIGRFAMsiTIGR01258 pgm_1, 1 hit
PROSITEiView protein in PROSITE
PS00175 PG_MUTASE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPMGE_HUMAN
AccessioniPrimary (citable) accession number: P07738
Secondary accession number(s): A4D1N9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: September 12, 2018
This is version 189 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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