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P07738 (PMGE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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=5.4.2.11
2,3-diphosphoglycerate mutase
Short name=DPGM
BPG-dependent PGAM
Gene names
Name:BPGM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities. HAMAP-Rule MF_01039

Catalytic activity

3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate. HAMAP-Rule MF_01039

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01039

2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate. HAMAP-Rule MF_01039

Enzyme regulation

At alkaline pH BPGM favors the synthase reaction; however, at lower pH the phosphatase reaction is dominant. Inhibited by citrate. Ref.12 Ref.18

Subunit structure

Homodimer. Ref.17

Tissue specificity

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). Ref.2 Ref.3 Ref.13

Post-translational modification

Glycation of Lys-159 in diabetic patients inactivates the enzyme. HAMAP-Rule MF_01039

Involvement in disease

Bisphosphoglycerate mutase deficiency (BPGMD) [MIM:222800]: A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.19 Ref.20

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 Ref.2 Ref.10 Ref.15
Chain2 – 259258Bisphosphoglycerate mutase HAMAP-Rule MF_01039
PRO_0000179834

Regions

Region23 – 2422,3-bisphospho-D-glycerate binding HAMAP-Rule MF_01039
Region89 – 9242,3-bisphospho-D-glycerate binding HAMAP-Rule MF_01039
Region116 – 11722,3-diphosphoglyceric acid binding HAMAP-Rule MF_01039
Region188 – 19032,3-bisphospho-D-glycerate binding HAMAP-Rule MF_01039

Sites

Active site111Tele-phosphohistidine intermediate Ref.17
Active site1881 Ref.17
Binding site1712,3-bisphospho-D-glycerate
Binding site6212,3-bisphospho-D-glycerate
Binding site10012,3-bisphospho-D-glycerate
Site291Not glycated
Site461Not glycated
Site1431Not glycated
Site1811Not glycated
Site2461Not glycated
Site2471Not glycated
Site2531Not glycated
Site2581Not glycated
Site2591Not glycated

Amino acid modifications

Modified residue21N-acetylserine Ref.15
Glycosylation31N-linked (Glc) (glycation); in vitro Ref.10
Glycosylation51N-linked (Glc) (glycation); in vitro Ref.10
Glycosylation181N-linked (Glc) (glycation); in vitro Ref.10
Glycosylation431N-linked (Glc) (glycation); in vitro Ref.10
Glycosylation1591N-linked (Glc) (glycation) Ref.10
Glycosylation1971N-linked (Glc) (glycation); in vitro Ref.10

Natural variations

Natural variant621R → Q in BPGMD. Ref.20
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.19
VAR_065368

Secondary structure

............................................. 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] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-259, CLEAVAGE OF INITIATOR METHIONINE, TISSUE SPECIFICITY.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.
[7]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon.
[10]"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] [Europe PMC] [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.
[11]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 104-114.
[12]"Model of 2,3-bisphosphoglycerate metabolism in the human erythrocyte based on detailed enzyme kinetic equations: equations and parameter refinement."
Mulquiney P.J., Kuchel P.W.
Biochem. J. 342:581-596(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[13]"Novel placental expression of 2,3-bisphosphoglycerate mutase."
Pritlove D.C., Gu M., Boyd C.A., Randeva H.S., Vatish M.
Placenta 27:924-927(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[14]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[16]"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] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[17]"Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase."
Wang Y., Liu L., Wei Z., Cheng Z., Lin Y., Gong W.
J. Biol. Chem. 281:39642-39648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-258 IN COMPLEXES WITH 3-PHOSPHO-D-GLYCERATE AND 2,3-BISPHOSPHO-D-GLYCERATE, SUBUNIT, ACTIVE SITE.
[18]"Unliganded structure of human bisphosphoglycerate mutase reveals side-chain movements induced by ligand binding."
Patterson A., Price N.C., Nairn J.
Acta Crystallogr. F 66:1415-1420(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), ENZYME REGULATION.
[19]"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] [Europe PMC] [Abstract]
Cited for: VARIANT BPGMD CYS-90.
[20]"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] [Europe PMC] [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.
AK315439 mRNA. Translation: BAG37827.1.
CH236950 Genomic DNA. Translation: EAL24067.1.
CH471070 Genomic DNA. Translation: EAW83821.1.
BC017050 mRNA. Translation: AAH17050.1.
CCDSCCDS5833.1.
PIRPMHUBM. A31999.
RefSeqNP_001715.1. NM_001724.4.
NP_954655.1. NM_199186.2.
XP_006716159.1. XM_006716096.1.
UniGeneHs.198365.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP07738.
SMRP07738. Positions 2-256.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107137. 10 interactions.
IntActP07738. 8 interactions.
STRING9606.ENSP00000342032.

PTM databases

PhosphoSiteP07738.

Polymorphism databases

DMDM130350.

2D gel databases

REPRODUCTION-2DPAGEIPI00215979.

Proteomic databases

MaxQBP07738.
PaxDbP07738.
PeptideAtlasP07738.
PRIDEP07738.

Protocols and materials databases

DNASU669.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344924; ENSP00000342032; ENSG00000172331.
ENST00000393132; ENSP00000376840; ENSG00000172331.
ENST00000418040; ENSP00000399838; ENSG00000172331.
GeneID669.
KEGGhsa:669.
UCSCuc003vrv.3. human.

Organism-specific databases

CTD669.
GeneCardsGC07P134331.
HGNCHGNC:1093. BPGM.
HPAHPA016493.
HPA028735.
MIM222800. phenotype.
613896. gene.
neXtProtNX_P07738.
Orphanet714. Hemolytic anemia due to diphosphoglycerate mutase deficiency.
PharmGKBPA25401.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
HOVERGENHBG027528.
InParanoidP07738.
KOK01837.
OMAIKEAQNC.
OrthoDBEOG7XM2ZV.
PhylomeDBP07738.
TreeFamTF300007.

Enzyme and pathway databases

BioCycMetaCyc:HS10491-MONOMER.
SABIO-RKP07738.

Gene expression databases

ArrayExpressP07738.
BgeeP07738.
CleanExHS_BPGM.
GenevestigatorP07738.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. PTHR11931. 1 hit.
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMSSF53254. SSF53254. 1 hit.
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBPGM. human.
EvolutionaryTraceP07738.
GenomeRNAi669.
NextBio2738.
PROP07738.
SOURCESearch...

Entry information

Entry namePMGE_HUMAN
AccessionPrimary (citable) accession number: P07738
Secondary accession number(s): A4D1N9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 153 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

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