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Protein

Phosphoglycerate mutase 1

Gene

PGAM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111Tele-phosphohistidine intermediate
Sitei62 – 621Interaction with carboxyl group of phosphoglycerates
Active sitei186 – 1861

GO - Molecular functioni

  • bisphosphoglycerate 2-phosphatase activity Source: UniProtKB-EC
  • bisphosphoglycerate mutase activity Source: UniProtKB-EC
  • phosphoglycerate mutase activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • canonical glycolysis Source: Reactome
  • carbohydrate metabolic process Source: Reactome
  • gluconeogenesis Source: Reactome
  • glucose metabolic process Source: Reactome
  • glycolytic process Source: UniProtKB
  • regulation of glycolytic process Source: UniProtKB
  • regulation of pentose-phosphate shunt Source: UniProtKB
  • respiratory burst Source: UniProtKB
  • small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciMetaCyc:HS10286-MONOMER.
BRENDAi5.4.2.11. 2681.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RKP18669.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PGAM1
Synonyms:PGAMA
ORF Names:CDABP0006
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:8888. PGAM1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33225.

Polymorphism and mutation databases

BioMutaiPGAM1.
DMDMi130348.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 254253Phosphoglycerate mutase 1PRO_0000179825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Phosphoserine4 Publications
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei26 – 261PhosphotyrosineBy similarity
Modified residuei31 – 311Phosphoserine1 Publication
Modified residuei106 – 1061N6-acetyllysineBy similarity
Modified residuei251 – 2511N6-acetyllysine; alternate1 Publication
Modified residuei251 – 2511N6-succinyllysine; alternateBy similarity
Modified residuei253 – 2531N6-acetyllysine1 Publication
Modified residuei254 – 2541N6-acetyllysine1 Publication

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP18669.
PaxDbiP18669.
PRIDEiP18669.

2D gel databases

DOSAC-COBS-2DPAGEP18669.
OGPiP18669.
SWISS-2DPAGEP18669.
UCD-2DPAGEP18669.

PTM databases

DEPODiP18669.
PhosphoSiteiP18669.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP18669.
CleanExiHS_PGAM1.
ExpressionAtlasiP18669. baseline and differential.
GenevestigatoriP18669.

Organism-specific databases

HPAiHPA042528.
HPA049237.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PCNAP120042EBI-717905,EBI-358311

Protein-protein interaction databases

BioGridi111244. 18 interactions.
IntActiP18669. 12 interactions.
MINTiMINT-3008987.
STRINGi9606.ENSP00000359991.

Structurei

Secondary structure

1
254
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Turni15 – 206Combined sources
Helixi32 – 4716Combined sources
Beta strandi53 – 575Combined sources
Helixi61 – 7313Combined sources
Beta strandi81 – 833Combined sources
Helixi85 – 873Combined sources
Helixi93 – 953Combined sources
Helixi100 – 1078Combined sources
Helixi109 – 1179Combined sources
Helixi133 – 1375Combined sources
Helixi140 – 1423Combined sources
Turni147 – 1493Combined sources
Helixi156 – 17015Combined sources
Helixi172 – 1765Combined sources
Beta strandi181 – 1855Combined sources
Helixi187 – 19812Combined sources
Helixi202 – 2076Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi216 – 2205Combined sources
Beta strandi226 – 2283Combined sources
Helixi236 – 2427Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP18669.
SMRiP18669. Positions 2-243.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18669.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi122 – 13110Pro-rich

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
HOVERGENiHBG027528.
InParanoidiP18669.
KOiK01834.
OMAiDRVLPYW.
OrthoDBiEOG7XM2ZV.
PhylomeDBiP18669.
TreeFamiTF300007.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18669-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY
60 70 80 90 100
EFDICFTSVQ KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK
110 120 130 140 150
AETAAKHGEA QVKIWRRSYD VPPPPMEPDH PFYSNISKDR RYADLTEDQL
160 170 180 190 200
PSCESLKDTI ARALPFWNEE IVPQIKEGKR VLIAAHGNSL RGIVKHLEGL
210 220 230 240 250
SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR KAMEAVAAQG

KAKK
Length:254
Mass (Da):28,804
Last modified:January 23, 2007 - v2
Checksum:i6DC0852BEBB22409
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7458.1.
PIRiA31782. PMHUYB.
RefSeqiNP_002620.1. NM_002629.2.
UniGeneiHs.632918.

Genome annotation databases

EnsembliENST00000334828; ENSP00000359991; ENSG00000171314.
GeneIDi5223.
KEGGihsa:5223.
UCSCiuc001knh.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7458.1.
PIRiA31782. PMHUYB.
RefSeqiNP_002620.1. NM_002629.2.
UniGeneiHs.632918.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP18669.
SMRiP18669. Positions 2-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111244. 18 interactions.
IntActiP18669. 12 interactions.
MINTiMINT-3008987.
STRINGi9606.ENSP00000359991.

PTM databases

DEPODiP18669.
PhosphoSiteiP18669.

Polymorphism and mutation databases

BioMutaiPGAM1.
DMDMi130348.

2D gel databases

DOSAC-COBS-2DPAGEP18669.
OGPiP18669.
SWISS-2DPAGEP18669.
UCD-2DPAGEP18669.

Proteomic databases

MaxQBiP18669.
PaxDbiP18669.
PRIDEiP18669.

Protocols and materials databases

DNASUi5223.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334828; ENSP00000359991; ENSG00000171314.
GeneIDi5223.
KEGGihsa:5223.
UCSCiuc001knh.3. human.

Organism-specific databases

CTDi5223.
GeneCardsiGC10P099176.
H-InvDBHIX0036336.
HIX0120028.
HGNCiHGNC:8888. PGAM1.
HPAiHPA042528.
HPA049237.
MIMi172250. gene.
neXtProtiNX_P18669.
PharmGKBiPA33225.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
HOVERGENiHBG027528.
InParanoidiP18669.
KOiK01834.
OMAiDRVLPYW.
OrthoDBiEOG7XM2ZV.
PhylomeDBiP18669.
TreeFamiTF300007.

Enzyme and pathway databases

BioCyciMetaCyc:HS10286-MONOMER.
BRENDAi5.4.2.11. 2681.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RKP18669.

Miscellaneous databases

ChiTaRSiPGAM1. human.
EvolutionaryTraceiP18669.
GenomeRNAii5223.
NextBioi20192.
PROiP18669.
SOURCEiSearch...

Gene expression databases

BgeeiP18669.
CleanExiHS_PGAM1.
ExpressionAtlasiP18669. baseline and differential.
GenevestigatoriP18669.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "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.

Entry informationi

Entry nameiPGAM1_HUMAN
AccessioniPrimary (citable) accession number: P18669
Secondary accession number(s): Q9BWC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 182 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.