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P07738 (PMGE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bisphosphoglycerate mutase
Short name=BPGM
EC=5.4.2.4
Alternative name(s):
2,3-bisphosphoglycerate mutase, erythrocyte
2,3-bisphosphoglycerate synthase
EC=3.1.3.13
EC=5.4.2.1
2,3-diphosphoglycerate mutase
Short name=DPGM
BPG-dependent PGAM
Gene names
Name:BPGM
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length259 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities.

Catalytic activity

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

2-phospho-D-glycerate = 3-phospho-D-glycerate.

2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate.

Subunit structure

Homodimer.

Post-translational modification

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

Involvement in disease

Defects in BPGM are the cause of bisphosphoglycerate mutase deficiency (BPGMD) [MIM:222800]. A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis. Ref.1 Ref.11 Ref.12

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 259258Bisphosphoglycerate mutase
PRO_0000179834

Sites

Active site111Tele-phosphohistidine intermediate
Active site1881
Site291Not glycated
Site461Not glycated
Site621Interaction with carboxyl group of phosphoglycerates
Site1431Not glycated
Site1811Not glycated
Site2461Not glycated
Site2471Not glycated
Site2531Not glycated
Site2581Not glycated
Site2591Not glycated

Amino acid modifications

Glycosylation31N-linked (Glc) (glycation); in vitro Ref.7
Glycosylation51N-linked (Glc) (glycation); in vitro Ref.7
Glycosylation181N-linked (Glc) (glycation); in vitro Ref.7
Glycosylation431N-linked (Glc) (glycation); in vitro Ref.7
Glycosylation1591N-linked (Glc) (glycation) Ref.7
Glycosylation1971N-linked (Glc) (glycation); in vitro Ref.7

Natural variations

Natural variant621R → Q in BPGMD. Ref.12
VAR_065367
Natural variant901R → C in BPGMD; mutation identified at protein level; marked decrease in synthase and mutase activities; no effect on phosphatase activity. Ref.1 Ref.11
VAR_065368

Secondary structure

1 ............................................. 259
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07738 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A2AF1D6F2985A3B5

FASTA25930,005
        10         20         30         40         50         60 
MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL 

        70         80         90        100        110        120 
NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR EQMALNHGEE QVRLWRRSYN 

       130        140        150        160        170        180 
VTPPPIEESH PYYQEIYNDR RYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG 

       190        200        210        220        230        240 
KTILISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA 

       250 
IQAAIKKVED QGKVKQAKK

« Hide

References

« Hide 'large scale' references
[1]"Isolation, characterization, and structure of a mutant 89 ArgTO: bisphosphoglycerate mutase. Implication of the active site in the mutation."
Rosa R., Blouquit Y., Calvin M.C., Prome D., Prome J.C., Rosa J.
J. Biol. Chem. 264:7837-7843(1989) [PubMed: 2542247] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, IDENTIFICATION OF VARIANT BPGMD CYS-90, CHARACTERIZATION OF VARIANT BPGMD CYS-90.
[2]"The complete amino acid sequence of human erythrocyte diphosphoglycerate mutase."
Haggarty N.W., Dunbar B., Fothergill L.A.
EMBO J. 2:1213-1220(1983) [PubMed: 6313356] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-259.
[3]"Molecular cloning and sequencing of the human erythrocyte 2,3-bisphosphoglycerate mutase cDNA: revised amino acid sequence."
Joulin V., Peduzzi J., Romeo P.-H., Rosa R., Valentin C., Dubart A., Lapeyre B., Blouquit Y., Garel M.-C., Goossens M., Rosa J., Cohen-Solal M.
EMBO J. 5:2275-2283(1986) [PubMed: 3023066] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Molecular cloning of the human 2,3-bisphosphoglycerate mutase cDNA and revised amino acid sequence."
Cohen-Solal M., Joulin V., Romeo P.-H., Rosa R., Valentin C., Garel M.-C., Rosa J.
Biomed. Biochim. Acta 46:S126-S130(1987) [PubMed: 3036106] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Isolation and characterization of the human 2,3-bisphosphoglycerate mutase gene."
Joulin V., Garel M.-C., le Boulch P., Valentin C., Rosa R., Rosa J., Cohen-Solal M.
J. Biol. Chem. 263:15785-15790(1988) [PubMed: 2844822] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon.
[7]"Human erythrocyte bisphosphoglycerate mutase: inactivation by glycation in vivo and in vitro."
Fujita T., Suzuki K., Tada T., Yoshihara Y., Hamaoka R., Uchida K., Matuo Y., Sasaki T., Hanafusa T., Taniguchi N.
J. Biochem. 124:1237-1244(1998) [PubMed: 9832630] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-46; 144-168 AND 182-206, GLYCATION AT LYS-3; LYS-5; LYS-18; LYS-43; LYS-159 AND LYS-197, LACK OF GLYCATION AT LYS-29; LYS-46; LYS-143; LYS-181; LYS-246; LYS-247; LYS-253; LYS-258 AND LYS-259.
[8]"The platelet-activating factor acetylhydrolase from human erythrocytes. Purification and properties."
Stafforini D.M., Rollins E.N., Prescott S.M., McIntyre T.M.
J. Biol. Chem. 268:3857-3865(1993) [PubMed: 8440681] [Abstract]
Cited for: PROTEIN SEQUENCE OF 104-114.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Structural modeling of the human erythrocyte bisphosphoglycerate mutase."
Craescu C.T., Schaad O., Garel M.-C., Rosa R., Edelstein S.J.
Biochimie 74:519-526(1992) [PubMed: 1387804] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[11]"Compound heterozygosity in a complete erythrocyte bisphosphoglycerate mutase deficiency."
Lemarchandel V., Joulin V., Valentin C., Rosa R., Galacteros F., Rosa J., Cohen-Solal M.
Blood 80:2643-2649(1992) [PubMed: 1421379] [Abstract]
Cited for: VARIANT BPGMD CYS-90.
[12]"Erythrocytosis due to bisphosphoglycerate mutase deficiency with concurrent glucose-6-phosphate dehydrogenase (G-6-PD) deficiency."
Hoyer J.D., Allen S.L., Beutler E., Kubik K., West C., Fairbanks V.F.
Am. J. Hematol. 75:205-208(2004) [PubMed: 15054810] [Abstract]
Cited for: VARIANT BPGMD GLN-62.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X04327 mRNA. Translation: CAA27858.1.
M23068, M23067 Genomic DNA. Translation: AAA51840.1.
BC017050 mRNA. Translation: AAH17050.1.
IPIIPI00215979.
PIRPMHUBM. A31999.
RefSeqNP_001715.1. NM_001724.4.
NP_954655.1. NM_199186.2.
UniGeneHs.198365.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T8PX-ray2.50A/B1-259[»]
2A9JX-ray2.00A/B1-258[»]
2F90X-ray2.00A/B1-259[»]
2H4XX-ray1.85A/B1-258[»]
2H4ZX-ray2.00A/B1-258[»]
2H52X-ray2.00A/B1-258[»]
2HHJX-ray1.50A/B1-258[»]
3NFYX-ray1.94A/B1-259[»]
ProteinModelPortalP07738.
SMRP07738. Positions 2-256.
ModBaseSearch...

Protein-protein interaction databases

IntActP07738. 8 interactions.
STRINGP07738.

PTM databases

PhosphoSiteP07738.

Polymorphism databases

DMDM130350.

2D gel databases

REPRODUCTION-2DPAGEIPI00215979.

Proteomic databases

PeptideAtlasP07738.
PRIDEP07738.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344924; ENSP00000342032; ENSG00000172331.
ENST00000393132; ENSP00000376840; ENSG00000172331.
ENST00000418040; ENSP00000399838; ENSG00000172331.
GeneID669.
KEGGhsa:669.
UCSCuc003vrv.1. human.

Organism-specific databases

CTD669.
GeneCardsGC07P134331.
H-InvDBHIX0007103.
HGNCHGNC:1093. BPGM.
HPAHPA016493.
HPA028735.
MIM222800. phenotype.
613896. gene.
neXtProtNX_P07738.
Orphanet714. Hemolytic anemia due to diphosphoglycerate mutase deficiency.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG658938.
HOVERGENHBG027528.
InParanoidP07738.
OMANLHAVGP.
OrthoDBEOG454908.
PhylomeDBP07738.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15292.

Gene expression databases

ArrayExpressP07738.
BgeeP07738.
CleanExHS_BPGM.
GenevestigatorP07738.
GermOnlineENSG00000172331. Homo sapiens.

Family and domain databases

InterProIPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
KOK01837.
PANTHERPTHR11931. Phosphogly_mut1. 1 hit.
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
TIGRFAMsTIGR01258. Pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio2738.
SOURCESearch...

Entry information

Entry namePMGE_HUMAN
AccessionPrimary (citable) accession number: P07738
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents