Reviewed, UniProtKB/Swiss-Prot P18669 (PGAM1_HUMAN)

Names and origin

Protein names

Recommended name:
    Phosphoglycerate mutase 1
    EC=5.4.2.1
    EC=5.4.2.4
    EC=3.1.3.13
Alternative name(s):
    Phosphoglycerate mutase isozyme B
      Short name=PGAM-B
    BPG-dependent PGAM 1

Gene names

Name:	PGAM1
Synonyms:	PGAMA
ORF Names:	CDABP0006

Organism

Homo sapiens (Human) [Complete 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.
Sequence processing	The displayed sequence is further processed into a mature form.
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.14
Tissue specificity	In mammalian tissues there are two types of phosphoglycerate mutase isozymes: type-M in muscles and type-B in other tissues.
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
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of glycolysis Inferred from direct assay. Source: UniProtKB regulation of pentose-phosphate shunt Inferred from direct assay. Source: UniProtKB respiratory burst Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	2,3-bisphospho-D-glycerate 2-phosphohydrolase activity Inferred from electronic annotation. Source: EC bisphosphoglycerate mutase activity Inferred from electronic annotation. Source: EC phosphoglycerate mutase activity Ref.4 Inferred from mutant phenotype. Source: UniProtKB protein kinase binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 254

253

Phosphoglycerate mutase 1

PRO_0000179825

Regions

Compositional bias

122 – 131

10

Pro-rich

Sites

Active site

11

1

Tele-phosphohistidine intermediate

Active site

186

1

Site

62

1

Interaction with carboxyl group of phosphoglycerates

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.11

Modified residue

14

1

Phosphoserine Ref.9 Ref.13

Modified residue

26

1

Phosphotyrosine Ref.13 Ref.7 Ref.8 Ref.12

Modified residue

31

1

Phosphoserine Ref.9

Modified residue

92

1

Phosphotyrosine Ref.13

Modified residue

118

1

Phosphoserine Ref.13

Secondary structure

1

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254

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Turn

15 – 20

6

Helix

32 – 48

17

Beta strand

53 – 57

5

Helix

61 – 73

13

Beta strand

81 – 83

3

Helix

85 – 87

3

Helix

93 – 95

3

Helix

100 – 107

8

Helix

109 – 117

9

Helix

133 – 137

5

Helix

140 – 142

3

Turn

147 – 149

3

Helix

156 – 176

21

Beta strand

181 – 185

5

Helix

187 – 198

12

Helix

202 – 206

5

Beta strand

212 – 214

3

Beta strand

216 – 220

5

Beta strand

226 – 228

3

Helix

236 – 243

8

Sequences

	Sequence		Length	Mass (Da)
	P18669-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6DC0852BEBB22409	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

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: 2846553] [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: 15489334] [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: 2846554] [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: 9150946] [Abstract] Cited for: PROTEIN SEQUENCE OF 91-100. Tissue: Mammary carcinoma.
[7]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-26, MASS SPECTROMETRY.
[8]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-26, MASS SPECTROMETRY.
[9]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-31, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[12]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-26, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[13]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; TYR-26; TYR-92 AND SER-118, MASS SPECTROMETRY. Tissue: T-cell.
[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: 15883004] [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.

UniGene

Hs.592599
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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P18669. 6 interactions.

STRING

P18669.

PTM databases

PhosphoSite

P18669.

2-D gel databases

SWISS-2DPAGE

P18669.

Aarhus/Ghent-2DPAGE

1107. IEF.
2132. IEF.

DOSAC-COBS-2DPAGE

P18669.

OGP

P18669.

Proteomic databases

PRIDE

P18669.

Genome annotation databases

Ensembl

ENST00000334828; ENSP00000359991; ENSG00000171314; Homo sapiens. [Genome view]

GeneID

5223.

KEGG

hsa:5223.

UCSC

uc001knh.1. human.

Organism-specific databases

CTD

5223.

GeneCards

GC10P099176.

H-InvDB

HIX0009089.
HIX0036336.
HIX0036843.

HGNC

HGNC:8888. PGAM1.

MIM

172250. gene.

PharmGKB

PA33225.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17698.

HOGENOM

HBG658938.

HOVERGEN

P18669.

InParanoid

P18669.

OMA

VPLTECL.

OrthoDB

EOG9R26D8.

PhylomeDB

P18669.

Enzyme and pathway databases

BRENDA

3.1.3.13. 247.
5.4.2.1. 247.
5.4.2.4. 247.

Reactome

REACT_1505. Integration of energy metabolism.
REACT_15380. Diabetes pathways.
REACT_474. Metabolism of carbohydrates.

Gene expression databases

Bgee

P18669.

CleanEx

HS_PGAM1.

Genevestigator

P18669.

GermOnline

ENSG00000171314. Homo sapiens.
ENSG00000198191. Homo sapiens.

Family and domain databases

InterPro

IPR001345. PG/BPGM_mutase_AS.
IPR013078. PG_mutase.
IPR005952. Phosphogly_mut1.
[Graphical view]

PANTHER

PTHR11931. Phosphogly_mut1. 1 hit.

Pfam

PF00300. PGAM. 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 Resources

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:	February 9, 2010
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.