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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), 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei11Tele-phosphohistidine intermediate1 Publication1 Publication1
Binding sitei62SubstrateBy similarity1
Active sitei89Proton donor/acceptor1 Publication1
Binding sitei100Substrate2 Publications1
Sitei186Transition state stabilizerBy similarity1

GO - Molecular functioni

GO - Biological processi

  • canonical glycolysis Source: Reactome
  • gluconeogenesis Source: GO_Central
  • glycolytic process Source: UniProtKB
  • regulation of glycolytic process Source: UniProtKB
  • regulation of pentose-phosphate shunt Source: UniProtKB
  • respiratory burst Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciMetaCyc:HS10286-MONOMER.
ZFISH:HS10286-MONOMER.
BRENDAi5.4.2.11. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-70171. Glycolysis.
R-HSA-70263. Gluconeogenesis.
SABIO-RKP18669.
SIGNORiP18669.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate mutase 1 (EC:5.4.2.111 Publication, EC:5.4.2.41 Publication)
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
Proteomesi
  • UP000005640 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
  • myelin sheath Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi5223.
OpenTargetsiENSG00000171314.
PharmGKBiPA33225.

Chemistry databases

ChEMBLiCHEMBL3334418.

Polymorphism and mutation databases

BioMutaiPGAM1.
DMDMi130348.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001798252 – 254Phosphoglycerate mutase 1Add BLAST253

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14PhosphoserineCombined sources1
Modified residuei23PhosphoserineCombined sources1
Modified residuei26Phosphotyrosine1 Publication1
Modified residuei31PhosphoserineCombined sources1
Modified residuei106N6-acetyllysineBy similarity1
Modified residuei118PhosphoserineBy similarity1
Modified residuei251N6-acetyllysine; alternate1 Publication1
Modified residuei251N6-succinyllysine; alternateBy similarity1
Modified residuei253N6-acetyllysine1 Publication1
Modified residuei254N6-acetyllysine1 Publication1

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

EPDiP18669.
PaxDbiP18669.
PeptideAtlasiP18669.
PRIDEiP18669.
TopDownProteomicsiP18669.

2D gel databases

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

PTM databases

DEPODiP18669.
iPTMnetiP18669.
PhosphoSitePlusiP18669.
SwissPalmiP18669.

Expressioni

Tissue specificityi

Expressed in the liver and brain. Not found in the muscle.1 Publication

Gene expression databases

BgeeiENSG00000171314.
CleanExiHS_PGAM1.
ExpressionAtlasiP18669. baseline and differential.
GenevisibleiP18669. HS.

Organism-specific databases

HPAiHPA042528.
HPA049237.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

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

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111244. 39 interactors.
IntActiP18669. 14 interactors.
MINTiMINT-3008987.
STRINGi9606.ENSP00000359991.

Structurei

Secondary structure

1254
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Turni15 – 20Combined sources6
Helixi32 – 47Combined sources16
Beta strandi53 – 57Combined sources5
Helixi61 – 73Combined sources13
Beta strandi81 – 83Combined sources3
Helixi85 – 87Combined sources3
Helixi93 – 95Combined sources3
Helixi100 – 107Combined sources8
Helixi109 – 117Combined sources9
Helixi133 – 137Combined sources5
Helixi140 – 142Combined sources3
Turni147 – 149Combined sources3
Helixi156 – 170Combined sources15
Helixi172 – 176Combined sources5
Beta strandi181 – 185Combined sources5
Helixi187 – 198Combined sources12
Helixi202 – 207Combined sources6
Beta strandi212 – 214Combined sources3
Beta strandi216 – 220Combined sources5
Beta strandi226 – 228Combined sources3
Helixi236 – 242Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18669.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni10 – 17Substrate binding2 Publications8
Regioni23 – 24Substrate binding2 Publications2
Regioni89 – 92Substrate binding1 Publication4
Regioni116 – 117Substrate binding1 Publication2
Regioni187 – 188Substrate bindingBy similarity2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi122 – 131Pro-rich10

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0235. Eukaryota.
COG0588. LUCA.
GeneTreeiENSGT00390000016700.
HOGENOMiHOG000221682.
HOVERGENiHBG027528.
InParanoidiP18669.
KOiK01834.
OMAiVKNQGKK.
OrthoDBiEOG091G0GIS.
PhylomeDBiP18669.
TreeFamiTF300007.

Family and domain databases

CDDicd07067. HP_PGM_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA. 1 hit.
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. 2 hits.
[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_002629.3.
UniGeneiHs.632918.

Genome annotation databases

EnsembliENST00000334828; ENSP00000359991; ENSG00000171314.
GeneIDi5223.
KEGGihsa:5223.

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_002629.3.
UniGeneiHs.632918.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111244. 39 interactors.
IntActiP18669. 14 interactors.
MINTiMINT-3008987.
STRINGi9606.ENSP00000359991.

Chemistry databases

ChEMBLiCHEMBL3334418.

PTM databases

DEPODiP18669.
iPTMnetiP18669.
PhosphoSitePlusiP18669.
SwissPalmiP18669.

Polymorphism and mutation databases

BioMutaiPGAM1.
DMDMi130348.

2D gel databases

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

Proteomic databases

EPDiP18669.
PaxDbiP18669.
PeptideAtlasiP18669.
PRIDEiP18669.
TopDownProteomicsiP18669.

Protocols and materials databases

DNASUi5223.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334828; ENSP00000359991; ENSG00000171314.
GeneIDi5223.
KEGGihsa:5223.

Organism-specific databases

CTDi5223.
DisGeNETi5223.
GeneCardsiPGAM1.
H-InvDBHIX0036336.
HIX0120028.
HGNCiHGNC:8888. PGAM1.
HPAiHPA042528.
HPA049237.
MIMi172250. gene.
neXtProtiNX_P18669.
OpenTargetsiENSG00000171314.
PharmGKBiPA33225.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0235. Eukaryota.
COG0588. LUCA.
GeneTreeiENSGT00390000016700.
HOGENOMiHOG000221682.
HOVERGENiHBG027528.
InParanoidiP18669.
KOiK01834.
OMAiVKNQGKK.
OrthoDBiEOG091G0GIS.
PhylomeDBiP18669.
TreeFamiTF300007.

Enzyme and pathway databases

BioCyciMetaCyc:HS10286-MONOMER.
ZFISH:HS10286-MONOMER.
BRENDAi5.4.2.11. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-70171. Glycolysis.
R-HSA-70263. Gluconeogenesis.
SABIO-RKP18669.
SIGNORiP18669.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000171314.
CleanExiHS_PGAM1.
ExpressionAtlasiP18669. baseline and differential.
GenevisibleiP18669. HS.

Family and domain databases

CDDicd07067. HP_PGM_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA. 1 hit.
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. 2 hits.
[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...

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: November 30, 2016
This is version 199 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

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 one 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.