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P18669

- PGAM1_HUMAN

UniProt

P18669 - PGAM1_HUMAN

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Protein

Phosphoglycerate mutase 1

Gene

PGAM1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. bisphosphoglycerate 2-phosphatase activity Source: UniProtKB-EC
  2. bisphosphoglycerate mutase activity Source: UniProtKB-EC
  3. phosphoglycerate mutase activity Source: UniProtKB
  4. protein kinase binding Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. gluconeogenesis Source: Reactome
  3. glucose metabolic process Source: Reactome
  4. glycolytic process Source: UniProt
  5. regulation of glycolytic process Source: UniProtKB
  6. regulation of pentose-phosphate shunt Source: UniProtKB
  7. respiratory burst Source: UniProtKB
  8. 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.
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: Chromosome 10

Organism-specific databases

HGNCiHGNC:8888. PGAM1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProt
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33225.

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 – 141Phosphoserine3 Publications
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

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.
GenevestigatoriP18669.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111244. 19 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 – 107
Turni15 – 206
Helixi32 – 4716
Beta strandi53 – 575
Helixi61 – 7313
Beta strandi81 – 833
Helixi85 – 873
Helixi93 – 953
Helixi100 – 1078
Helixi109 – 1179
Helixi133 – 1375
Helixi140 – 1423
Turni147 – 1493
Helixi156 – 17015
Helixi172 – 1765
Beta strandi181 – 1855
Helixi187 – 19812
Helixi202 – 2076
Beta strandi212 – 2143
Beta strandi216 – 2205
Beta strandi226 – 2283
Helixi236 – 2427

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiIKEWRRS.
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:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi130348.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS7458.1.
PIRi A31782. PMHUYB.
RefSeqi NP_002620.1. NM_002629.2.
UniGenei Hs.632918.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LJD model - A 1-254 [» ]
1YFK X-ray 2.70 A/B 1-254 [» ]
1YJX X-ray 2.80 A/B/C/D/E/F/G/H/I/J/K/L 1-254 [» ]
4GPI X-ray 2.08 B/C 1-254 [» ]
4GPZ X-ray 1.65 A/B 1-254 [» ]
ProteinModelPortali P18669.
SMRi P18669. Positions 2-243.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111244. 19 interactions.
IntActi P18669. 12 interactions.
MINTi MINT-3008987.
STRINGi 9606.ENSP00000359991.

PTM databases

PhosphoSitei P18669.

Polymorphism databases

DMDMi 130348.

2D gel databases

DOSAC-COBS-2DPAGE P18669.
OGPi P18669.
SWISS-2DPAGE P18669.
UCD-2DPAGE P18669.

Proteomic databases

MaxQBi P18669.
PaxDbi P18669.
PRIDEi P18669.

Protocols and materials databases

DNASUi 5223.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000334828 ; ENSP00000359991 ; ENSG00000171314 .
GeneIDi 5223.
KEGGi hsa:5223.
UCSCi uc001knh.3. human.

Organism-specific databases

CTDi 5223.
GeneCardsi GC10P099176.
H-InvDB HIX0036336.
HIX0120028.
HGNCi HGNC:8888. PGAM1.
MIMi 172250. gene.
neXtProti NX_P18669.
PharmGKBi PA33225.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0588.
HOGENOMi HOG000221682.
HOVERGENi HBG027528.
InParanoidi P18669.
KOi K01834.
OMAi IKEWRRS.
OrthoDBi EOG7XM2ZV.
PhylomeDBi P18669.
TreeFami TF300007.

Enzyme and pathway databases

BioCyci MetaCyc:HS10286-MONOMER.
Reactomei REACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RK P18669.

Miscellaneous databases

ChiTaRSi PGAM1. human.
EvolutionaryTracei P18669.
GenomeRNAii 5223.
NextBioi 20192.
PROi P18669.
SOURCEi Search...

Gene expression databases

Bgeei P18669.
CleanExi HS_PGAM1.
ExpressionAtlasi P18669. baseline.
Genevestigatori P18669.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
HAMAPi MF_01039. PGAM_GpmA.
InterProi IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view ]
PANTHERi PTHR11931. PTHR11931. 1 hit.
Pfami PF00300. His_Phos_1. 1 hit.
[Graphical view ]
SMARTi SM00855. PGAM. 1 hit.
[Graphical view ]
SUPFAMi SSF53254. SSF53254. 1 hit.
TIGRFAMsi TIGR01258. pgm_1. 1 hit.
PROSITEi PS00175. PG_MUTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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: October 29, 2014
This is version 176 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