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Reviewed, UniProtKB/Swiss-Prot P07738 (PMGE_HUMAN)

Last modified July 7, 2009. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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=5.4.2.1
    EC=3.1.3.13
    BPG-dependent PGAM
Gene names
Name: BPGM
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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General annotation (Comments)

Function

Plays a major role in regulating hemoglobin oxygen affinity as a consequence of controlling 2,3-BPG concentration. Can also catalyze the reaction of EC 5.4.2.1 (mutase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.

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.

Sequence similarities

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

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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
Glycosylation51N-linked (Glc) (glycation); in vitro
Glycosylation181N-linked (Glc) (glycation); in vitro
Glycosylation431N-linked (Glc) (glycation); in vitro
Glycosylation1591N-linked (Glc) (glycation)
Glycosylation1971N-linked (Glc) (glycation); in vitro

Secondary structure

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

Details...

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Sequences

Sequence LengthMass (Da)Tools
P07738-1 [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

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References

« Hide 'large scale' references
[1]"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.
[2]"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].
[3]"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].
[4]"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].
[5]"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.
[6]"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, ABSENCE OF GLYCATION AT LYS-29; LYS-46; LYS-143; LYS-181; LYS-246; LYS-247; LYS-253; LYS-258 AND LYS-259.
[7]"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.
[8]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]"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.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X04327 mRNA. Translation: CAA27858.1.
M23068, M23067 Genomic DNA. Translation: AAA51840.1.
BC017050 mRNA. Translation: AAH17050.1.
IPIIPI00215979.
PIRPMHUBM. A31999.
RefSeqNP_001715.1.
NP_954655.1.
UniGeneHs.198365

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP07738. 2 interactions.

PTM databases

PhosphoSiteP07738.

2-D gel databases

REPRODUCTION-2DPAGEIPI00215979.

Proteomic databases

PeptideAtlasP07738.
PRIDEP07738.

Genome annotation databases

EnsemblENSG00000172331. Homo sapiens. [Contig view]
GeneID669.
KEGGhsa:669.
UCSCuc003vrv.1. human.

Organism-specific databases

GeneCardsGC07P133982.
H-InvDBHIX0007103.
HGNCHGNC:1093. BPGM.
HPAHPA016493.
MIM222800. gene+phenotype.
Orphanet714. Diphosphoglycerate mutase deficiency of erythrocyte.
98426. Erythrocytosis.
PharmGKBPA25401.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP07738.
HOVERGENP07738.
OMAP07738. SDRRYKV.

Enzyme and pathway databases

BRENDA3.1.3.13. 247.
5.4.2.1. 247.
5.4.2.4. 247.

Gene expression databases

ArrayExpressP07738.
BgeeP07738.
CleanExHS_BPGM.
GermOnlineENSG00000172331. Homo sapiens.

Family and domain databases

InterProIPR001345. PG/BPGM_mutase.
IPR013078. PG_mutase.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. Phosphogly_mut1. 1 hit.
PfamPF00300. PGAM. 1 hit.
[Graphical view]
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio2738.
SOURCESearch...

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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: July 7, 2009
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 7

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

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents