Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P18669 (PGAM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglycerate mutase 1

EC=3.1.3.13
EC=5.4.2.11
EC=5.4.2.4
Alternative name(s):
BPG-dependent PGAM 1
Phosphoglycerate mutase isozyme B
Short name=PGAM-B
Gene names
Name:PGAM1
Synonyms:PGAMA
ORF Names:CDABP0006
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity. HAMAP-Rule MF_01039

Catalytic activity

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

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

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

Subunit structure

Homodimer. Ref.13

Tissue specificity

In mammalian tissues there are two types of phosphoglycerate mutase isozymes: type-M in muscles and type-B in other tissues.

Post-translational modification

Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose condition. Acetylation increases catalytic activity. Under glucose restriction SIRT1 levels dramatically increase and it deacetylates the enzyme. Ref.12

Sequence similarities

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

Ontologies

Keywords
   Biological processGlycolysis
   Molecular functionHydrolase
Isomerase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

gluconeogenesis

Traceable author statement. Source: Reactome

glucose metabolic process

Traceable author statement. Source: Reactome

glycolysis

Inferred from direct assay PubMed 22590500. Source: UniProt

regulation of glycolysis

Inferred from direct assay PubMed 12189148. Source: UniProtKB

regulation of pentose-phosphate shunt

Inferred from direct assay PubMed 12189148. Source: UniProtKB

respiratory burst

Inferred from direct assay PubMed 12189148. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 22590500. Source: UniProt

cytosol

Inferred from direct assay PubMed 12189148. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

   Molecular_functionbisphosphoglycerate 2-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

bisphosphoglycerate mutase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphoglycerate mutase activity

Inferred from mutant phenotype PubMed 12189148. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 12189148. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PCNAP120042EBI-717905,EBI-358311

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 254253Phosphoglycerate mutase 1 HAMAP-Rule MF_01039
PRO_0000179825

Regions

Compositional bias122 – 13110Pro-rich HAMAP-Rule MF_01039

Sites

Active site111Tele-phosphohistidine intermediate
Active site1861
Site621Interaction with carboxyl group of phosphoglycerates

Amino acid modifications

Modified residue141Phosphoserine Ref.8 Ref.9 Ref.11
Modified residue261Phosphotyrosine By similarity
Modified residue311Phosphoserine Ref.7
Modified residue1061N6-acetyllysine By similarity
Modified residue2511N6-acetyllysine; alternate Ref.12
Modified residue2511N6-succinyllysine; alternate By similarity
Modified residue2531N6-acetyllysine Ref.12
Modified residue2541N6-acetyllysine Ref.12

Secondary structure

............................................. 254
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18669 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6DC0852BEBB22409

FASTA25428,804
        10         20         30         40         50         60 
MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY EFDICFTSVQ 

        70         80         90        100        110        120 
KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD 

       130        140        150        160        170        180 
VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKEGKR 

       190        200        210        220        230        240 
VLIAAHGNSL RGIVKHLEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR 

       250 
KAMEAVAAQG KAKK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a cDNA encoding the B isozyme of human phosphoglycerate mutase (PGAM) and characterization of the PGAM gene family."
Sakoda S., Shanske S., Dimauro S., Schon E.A.
J. Biol. Chem. 263:16899-16905(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Pediatric leukemia cDNA sequencing project."
Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Leukemia.
[3]"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: Brain, Liver, Lymph, Skin and Uterus.
[4]"Sequence of the human erythrocyte phosphoglycerate mutase by microsequencer and mass spectrometry."
Blouquit Y., Calvin M.C., Rosa R., Prome D., Prome J.-C., Pratbernou F., Cohen-Solal M., Rosa J.
J. Biol. Chem. 263:16906-16910(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-254, CLEAVAGE OF INITIATOR METHIONINE.
[5]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 11-39; 47-61; 91-100; 118-138; 142-157; 163-176; 181-191 AND 223-240, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[6]"Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2."
Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S.
Electrophoresis 18:588-598(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 91-100.
Tissue: Mammary carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Regulation of glycolytic enzyme phosphoglycerate mutase-1 by Sirt1 protein-mediated deacetylation."
Hallows W.C., Yu W., Denu J.M.
J. Biol. Chem. 287:3850-3858(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-251; LYS-253 AND LYS-254, DEACETYLATION BY SIRT1.
[13]"Crystal structure of human B-type phosphoglycerate mutase bound with citrate."
Wang Y., Wei Z., Liu L., Cheng Z., Lin Y., Ji F., Gong W.
Biochem. Biophys. Res. Commun. 331:1207-1215(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH CITRATE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04173 mRNA. Translation: AAA60071.1.
AY007118 mRNA. Translation: AAG01990.1.
BC010038 mRNA. Translation: AAH10038.1.
BC011678 mRNA. Translation: AAH11678.1.
BC053356 mRNA. Translation: AAH53356.1.
BC066959 mRNA. Translation: AAH66959.1.
BC073742 mRNA. Translation: AAH73742.1.
PIRPMHUYB. A31782.
RefSeqNP_002620.1. NM_002629.2.
UniGeneHs.632918.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LJDmodel-A1-254[»]
1YFKX-ray2.70A/B1-254[»]
1YJXX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-254[»]
4GPIX-ray2.08B/C1-254[»]
4GPZX-ray1.65A/B1-254[»]
ProteinModelPortalP18669.
SMRP18669. Positions 2-243.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111244. 14 interactions.
IntActP18669. 12 interactions.
MINTMINT-3008987.
STRING9606.ENSP00000359991.

PTM databases

PhosphoSiteP18669.

Polymorphism databases

DMDM130348.

2D gel databases

DOSAC-COBS-2DPAGEP18669.
OGPP18669.
SWISS-2DPAGEP18669.
UCD-2DPAGEP18669.

Proteomic databases

PaxDbP18669.
PRIDEP18669.

Protocols and materials databases

DNASU5223.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334828; ENSP00000359991; ENSG00000171314.
GeneID5223.
KEGGhsa:5223.
UCSCuc001knh.3. human.

Organism-specific databases

CTD5223.
GeneCardsGC10P099176.
H-InvDBHIX0036336.
HIX0120028.
HGNCHGNC:8888. PGAM1.
MIM172250. gene.
neXtProtNX_P18669.
PharmGKBPA33225.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
HOVERGENHBG027528.
InParanoidP18669.
KOK01834.
OMASYYLGDQ.
OrthoDBEOG7XM2ZV.
PhylomeDBP18669.
TreeFamTF300007.

Enzyme and pathway databases

BioCycMetaCyc:HS10286-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP18669.

Gene expression databases

BgeeP18669.
CleanExHS_PGAM1.
GenevestigatorP18669.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
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]
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPGAM1. human.
EvolutionaryTraceP18669.
GenomeRNAi5223.
NextBio20192.
PROP18669.
SOURCESearch...

Entry information

Entry namePGAM1_HUMAN
AccessionPrimary (citable) accession number: P18669
Secondary accession number(s): Q9BWC0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 170 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 chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM