Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoglycerate mutase 1

Gene

PGAM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
  • neutrophil degranulation Source: Reactome
  • regulation of glycolytic process Source: UniProtKB
  • regulation of pentose-phosphate shunt Source: UniProtKB
  • respiratory burst Source: UniProtKB

Keywordsi

Molecular functionHydrolase, Isomerase
Biological processGlycolysis

Enzyme and pathway databases

BioCyciMetaCyc:HS10286-MONOMER
BRENDAi5.4.2.11 2681
ReactomeiR-HSA-6798695 Neutrophil degranulation
R-HSA-70171 Glycolysis
R-HSA-70263 Gluconeogenesis
SABIO-RKiP18669
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

EuPathDBiHostDB:ENSG00000171314.8
HGNCiHGNC:8888 PGAM1
MIMi172250 gene
neXtProtiNX_P18669

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
ProteomicsDBi53605
TopDownProteomicsiP18669

2D gel databases

DOSAC-COBS-2DPAGEiP18669
OGPiP18669
SWISS-2DPAGEiP18669
UCD-2DPAGEiP18669

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
HPA060483

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, 46 interactors
IntActiP18669, 16 interactors
MINTiP18669
STRINGi9606.ENSP00000359991

Chemistry databases

BindingDBiP18669

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
OMAiRMLPYWY
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
InterProiView protein in InterPro
IPR013078 His_Pase_superF_clade-1
IPR029033 His_PPase_superfam
IPR001345 PG/BPGM_mutase_AS
IPR005952 Phosphogly_mut1
PANTHERiPTHR11931 PTHR11931, 1 hit
PfamiView protein in Pfam
PF00300 His_Phos_1, 2 hits
SMARTiView protein in SMART
SM00855 PGAM, 1 hit
SUPFAMiSSF53254 SSF53254, 1 hit
TIGRFAMsiTIGR01258 pgm_1, 1 hit
PROSITEiView protein in PROSITE
PS00175 PG_MUTASE, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiPGAM1_HUMAN
AccessioniPrimary (citable) accession number: P18669
Secondary accession number(s): Q9BWC0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 212 of the entry and version 2 of the sequence. See 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health