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Protein

Bisphosphoglycerate mutase

Gene

BPGM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 5.4.2.1) activity.

Catalytic activityi

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

Enzyme 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

  • carbohydrate metabolic process Source: ProtInc
  • erythrocyte development Source: Ensembl
  • gluconeogenesis Source: GO_Central
  • glucose metabolic process Source: Reactome
  • glycolytic process Source: GO_Central
  • regulation of pentose-phosphate shunt Source: GO_Central
  • respiratory gaseous exchange Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciMetaCyc:HS10491-MONOMER.
ZFISH:HS10491-MONOMER.
BRENDAi3.1.3.13. 2681.
5.4.2.4. 2681.
ReactomeiR-HSA-70326. Glucose metabolism.
SABIO-RKP07738.

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

HGNCiHGNC:1093. BPGM.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Bisphosphoglycerate mutase deficiency (BPGMD)2 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 rs751972865dbSNPEnsembl.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 rs121964925dbSNPEnsembl.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); in vitro1 Publication1
Glycosylationi5N-linked (Glc) (glycation); in vitro1 Publication1
Glycosylationi18N-linked (Glc) (glycation); in vitro1 Publication1
Glycosylationi43N-linked (Glc) (glycation); in vitro1 Publication1
Modified residuei122PhosphothreonineCombined sources1
Glycosylationi159N-linked (Glc) (glycation)1 Publication1
Glycosylationi197N-linked (Glc) (glycation); 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.

2D gel databases

REPRODUCTION-2DPAGEIPI00215979.

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.
CleanExiHS_BPGM.
ExpressionAtlasiP07738. baseline and differential.
GenevisibleiP07738. HS.

Organism-specific databases

HPAiHPA016493.
HPA028735.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi107137. 21 interactors.
IntActiP07738. 8 interactors.
STRINGi9606.ENSP00000342032.

Structurei

Secondary structure

1259
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi15 – 18Combined sources4
Helixi32 – 47Combined sources16
Beta strandi53 – 57Combined sources5
Helixi61 – 74Combined sources14
Beta strandi81 – 83Combined sources3
Helixi85 – 87Combined sources3
Helixi93 – 95Combined sources3
Helixi100 – 107Combined sources8
Helixi109 – 117Combined sources9
Helixi133 – 137Combined sources5
Helixi140 – 142Combined sources3
Beta strandi144 – 147Combined sources4
Helixi149 – 151Combined sources3
Helixi158 – 172Combined sources15
Helixi174 – 178Combined sources5
Beta strandi183 – 187Combined sources5
Helixi189 – 200Combined sources12
Helixi206 – 209Combined sources4
Beta strandi218 – 222Combined sources5
Beta strandi228 – 230Combined sources3
Helixi238 – 250Combined sources13

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...

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.
OMAiKEAQNCG.
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.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 2 hits.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06536762R → Q in BPGMD. 1 PublicationCorresponds to variant rs751972865dbSNPEnsembl.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 rs121964925dbSNPEnsembl.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.

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. 21 interactors.
IntActiP07738. 8 interactors.
STRINGi9606.ENSP00000342032.

PTM databases

DEPODiP07738.
iPTMnetiP07738.
PhosphoSitePlusiP07738.

Polymorphism and mutation databases

BioMutaiBPGM.
DMDMi130350.

2D gel databases

REPRODUCTION-2DPAGEIPI00215979.

Proteomic databases

EPDiP07738.
MaxQBiP07738.
PaxDbiP07738.
PeptideAtlasiP07738.
PRIDEiP07738.

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.
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.
OMAiKEAQNCG.
OrthoDBiEOG091G0GIS.
PhylomeDBiP07738.
TreeFamiTF300007.

Enzyme and pathway databases

BioCyciMetaCyc:HS10491-MONOMER.
ZFISH:HS10491-MONOMER.
BRENDAi3.1.3.13. 2681.
5.4.2.4. 2681.
ReactomeiR-HSA-70326. Glucose metabolism.
SABIO-RKP07738.

Miscellaneous databases

ChiTaRSiBPGM. human.
EvolutionaryTraceiP07738.
GenomeRNAii669.
PROiP07738.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000172331.
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.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 2 hits.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPMGE_HUMAN
AccessioniPrimary (citable) accession number: P07738
Secondary accession number(s): A4D1N9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 177 of the entry and version 2 of the sequence. [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

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.