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UniProtKB/Swiss-Prot entry P07738


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PMGE_HUMAN
Primary accession number P07738
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 94)
Name and origin of the protein
Protein name Bisphosphoglycerate mutase
Synonyms BPGM
EC 5.4.2.4
2,3-bisphosphoglycerate mutase, erythrocyte
2,3-bisphosphoglycerate synthase
EC 5.4.2.1
EC 3.1.3.13
BPG-dependent PGAM
Gene name
Name: BPGM
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
PRELIMINARY PROTEIN SEQUENCE OF 2-259.
PubMed=6313356 [NCBI, ExPASy, EBI, Israel, Japan]
Haggarty N.W., Dunbar B., Fothergill L.A.;
"The complete amino acid sequence of human erythrocyte diphosphoglycerate mutase.";
EMBO J. 2:1213-1220(1983).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3023066 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Molecular cloning and sequencing of the human erythrocyte 2,3-bisphosphoglycerate mutase cDNA: revised amino acid sequence.";
EMBO J. 5:2275-2283(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3036106 [NCBI, ExPASy, EBI, Israel, Japan]
Cohen-Solal M., Joulin V., Romeo P.-H., Rosa R., Valentin C., Garel M.-C., Rosa J.;
"Molecular cloning of the human 2,3-bisphosphoglycerate mutase cDNA and revised amino acid sequence.";
Biomed. Biochim. Acta 46:S126-S130(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2844822 [NCBI, ExPASy, EBI, Israel, Japan]
Joulin V., Garel M.-C., le Boulch P., Valentin C., Rosa R., Rosa J., Cohen-Solal M.;
"Isolation and characterization of the human 2,3-bisphosphoglycerate mutase gene.";
J. Biol. Chem. 263:15785-15790(1988).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
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, AND ABSENCE OF GLYCATION AT LYS-29; LYS-46; LYS-143; LYS-181; LYS-246; LYS-247; LYS-253; LYS-258 AND LYS-259.
PubMed=9832630 [NCBI, ExPASy, EBI, Israel, Japan]
Fujita T., Suzuki K., Tada T., Yoshihara Y., Hamaoka R., Uchida K., Matuo Y., Sasaki T., Hanafusa T., Taniguchi N.;
"Human erythrocyte bisphosphoglycerate mutase: inactivation by glycation in vivo and in vitro.";
J. Biochem. 124:1237-1244(1998).
[7]
PROTEIN SEQUENCE OF 104-114.
PubMed=8440681 [NCBI, ExPASy, EBI, Israel, Japan]
Stafforini D.M., Rollins E.N., Prescott S.M., McIntyre T.M.;
"The platelet-activating factor acetylhydrolase from human erythrocytes. Purification and properties.";
J. Biol. Chem. 268:3857-3865(1993).
[8]
3D-STRUCTURE MODELING.
DOI=10.1016/0300-9084(92)90149-9; PubMed=1387804 [NCBI, ExPASy, EBI, Israel, Japan]
Craescu C.T., Schaad O., Garel M.-C., Rosa R., Edelstein S.J.;
"Structural modeling of the human erythrocyte bisphosphoglycerate mutase.";
Biochimie 74:519-526(1992).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X04327; CAA27858.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M23068; AAA51840.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M23067; AAA51840.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC017050; AAH17050.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A31999; PMHUBM.
RefSeq NP_001715.1; -.
NP_954655.1; -.
UniGene Hs.198365
3D structure databases
PDB
1T8P; X-ray; 2.50 A; A/B=1-259.[ExPASy / RCSB / EBI]
2A9J; X-ray; 2.00 A; A/B=1-259.[ExPASy / RCSB / EBI]
2F90; X-ray; 2.00 A; A/B=1-259.[ExPASy / RCSB / EBI]
2H4X; X-ray; 1.85 A; A/B=1-259.[ExPASy / RCSB / EBI]
2H4Z; X-ray; 2.00 A; A/B=1-259.[ExPASy / RCSB / EBI]
2H52; X-ray; 2.00 A; A/B=1-259.[ExPASy / RCSB / EBI]
2HHJ; X-ray; 1.50 A; A/B=1-259.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1T8P; -.
2A9J; -.
2F90; -.
2H4X; -.
2H4Z; -.
2H52; -.
2HHJ; -.
ModBase P07738.
PTM databases
PhosphoSite P07738; -.
2D gel databases
REPRODUCTION-2DPAGE IPI00215979; -.
Organism-specific databases
H-InvDB HIX0007103; -.
HGNC HGNC:1093; BPGM.
GenAtlas BPGM.
HPA HPA016493; -.
MIM 222800; gene+phenotype. [NCBI / EBI]
Orphanet 714; Diphosphoglycerate mutase deficiency of erythrocyte.
PharmGKB PA25401; -.
GeneCards P07738.
Gene expression databases
ArrayExpress P07738; -.
CleanEx HS_BPGM; -.
GermOnline ENSG00000172331; Homo sapiens.
Ontologies
GO
GO:0004082; Molecular function: bisphosphoglycerate mutase activity (traceable author statement from ProtInc).
GO:0005975; Biological process: carbohydrate metabolic process (non-traceable author statement from ProtInc).
GO:0007585; Biological process: respiratory gaseous exchange (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001345; PG/BPGM_mutase.
IPR013078; PG_mutase.
IPR005952; Phosphogly_mut1.
Graphical view of domain structure.
PANTHER PTHR11931; Phosphogly_mut1; 1.
Pfam PF00300; PGAM; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01258; pgm_1; 1.
PROSITE PS00175; PG_MUTASE; 1.
BLOCKS P07738.
ProtoNet P07738.
Proteomic databases
PeptideAtlas P07738; -.
Genome annotation databases
Ensembl ENSG00000172331; Homo sapiens. [Contig view]
GeneID 669; -.
KEGG hsa:669; -.
Phylogenomic databases
HOGENOM P07738; -.
HOVERGEN P07738; -.
Other
NextBio 2738; -.
SOURCE BPGM; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Glycation; Glycolysis; Glycoprotein; Hydrolase; Isomerase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   259  258     Bisphosphoglycerate mutase. PRO_0000179834
ACT_SITE   11    11        Tele-phosphohistidine intermediate. 
ACT_SITE   188   188         
SITE   29    29  1     Not glycated. 
SITE   46    46  1     Not glycated. 
SITE   62    62  1     Interaction with carboxyl group of phosphoglycerates. 
SITE   143   143  1     Not glycated. 
SITE   181   181  1     Not glycated. 
SITE   246   246  1     Not glycated. 
SITE   247   247  1     Not glycated. 
SITE   253   253  1     Not glycated. 
SITE   258   258  1     Not glycated. 
SITE   259   259  1     Not glycated. 
CARBOHYD   3     3        N-linked (Glc) (glycation); in vitro. 
CARBOHYD   5     5        N-linked (Glc) (glycation); in vitro. 
CARBOHYD   18    18        N-linked (Glc) (glycation); in vitro. 
CARBOHYD   43    43        N-linked (Glc) (glycation); in vitro. 
CARBOHYD   159   159        N-linked (Glc) (glycation). 
CARBOHYD   197   197        N-linked (Glc) (glycation); in vitro. 
STRAND   4    10  7      
HELIX   15    18  4      
HELIX   32    47  16      
STRAND   53    57  5      
HELIX   61    74  14      
STRAND   81    83  3      
HELIX   85    87  3      
HELIX   93    95  3      
HELIX   100   107  8      
HELIX   109   117  9      
HELIX   133   137  5      
HELIX   140   142  3      
STRAND   144   147  4      
HELIX   149   151  3      
HELIX   158   172  15      
HELIX   174   178  5      
STRAND   183   187  5      
HELIX   189   200  12      
HELIX   206   209  4      
STRAND   218   222  5      
STRAND   228   230  3      
HELIX   238   250  13      
Sequence information
Length: 259 AA [This is the length of the unprocessed precursor] Molecular weight: 30005 Da [This is the MW of the unprocessed precursor] CRC64: A2AF1D6F2985A3B5 [This is a checksum on the sequence]
        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 

P07738 in FASTA format

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