Phosphoglycerate mutase 1 - Homo sapiens (Human)

Contribute

Send feedback

Read comments (?) or add your own

P18669 (PGAM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 160. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phosphoglycerate mutase 1
EC=3.1.3.13
EC=5.4.2.1
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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Catalytic activity	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.
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.
Sequence similarities	Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Ontologies

Keywords
Biological process	Glycolysis
Molecular function	Hydrolase Isomerase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Traceable author statement. Source: Reactome glycolysis Traceable author statement. Source: Reactome 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_component	cytosol Inferred from direct assay PubMed 12189148. Source: UniProtKB
Molecular_function	bisphosphoglycerate 2-phosphatase activity Inferred from electronic annotation. Source: EC bisphosphoglycerate mutase activity Inferred from electronic annotation. Source: EC phosphoglycerate mutase activity Inferred from mutant phenotype PubMed 12189148. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 254

254

Phosphoglycerate mutase 1

PRO_0000179825

Regions

Compositional bias

122 – 131

Pro-rich

Sites

Active site

Tele-phosphohistidine intermediate

Active site

186

Site

Interaction with carboxyl group of phosphoglycerates

Amino acid modifications

Modified residue

Phosphoserine Ref.8 Ref.9 Ref.11

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphoserine Ref.7

Modified residue

118

Phosphoserine By similarity

Modified residue

251

N6-acetyllysine Ref.12

Modified residue

253

N6-acetyllysine Ref.12

Modified residue

254

N6-acetyllysine Ref.12

Secondary structure

254

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P18669 [UniParc].

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

FASTA

254

28,804

        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' referencesShow '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.
[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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.

IPI

IPI00549725.

PIR

PMHUYB. A31782.

RefSeq

NP_002620.1. NM_002629.2.

UniGene

Hs.632918.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P18669.

ModBase

Search...

Protein-protein interaction databases

IntAct

P18669. 10 interactions.

MINT

MINT-3008987.

STRING

9606.ENSP00000359991.

PTM databases

PhosphoSite

P18669.

Polymorphism databases

DMDM

130348.

2D gel databases

DOSAC-COBS-2DPAGE

P18669.

OGP

P18669.

SWISS-2DPAGE

P18669.

UCD-2DPAGE

P18669.

Proteomic databases

PaxDb

P18669.

PRIDE

P18669.

Protocols and materials databases

DNASU

5223.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000334828; ENSP00000359991; ENSG00000171314.

GeneID

5223.

KEGG

hsa:5223.

UCSC

uc001knh.3. human.

Organism-specific databases

CTD

5223.

GeneCards

GC10P099176.

H-InvDB

HIX0036336.
HIX0120028.

HGNC

HGNC:8888. PGAM1.

MIM

172250. gene.

neXtProt

NX_P18669.

PharmGKB

PA33225.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0588.

HOGENOM

HOG000221682.

HOVERGEN

HBG027528.

InParanoid

P18669.

K01834.

OMA

GQSDWNL.

OrthoDB

EOG4MCX10.

PhylomeDB

P18669.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P18669.

Gene expression databases

ArrayExpress

P18669.

Bgee

P18669.

CleanEx

HS_PGAM1.

Genevestigator

P18669.

GermOnline

ENSG00000171314. Homo sapiens.
ENSG00000198191. Homo sapiens.

Family and domain databases

InterPro

IPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]

PANTHER

PTHR11931. PTHR11931. 1 hit.

Pfam

PF00300. His_Phos_1. 1 hit.
[Graphical view]

SMART

SM00855. PGAM. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01258. pgm_1. 1 hit.

PROSITE

PS00175. PG_MUTASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PGAM1. human.

EvolutionaryTrace

P18669.

GenomeRNAi

5223.

NextBio

20192.

SOURCE

Search...

Entry information

Entry name

PGAM1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 160 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human chromosome 10

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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents