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Identification
HMDB Protein ID HMDBP00269
Secondary Accession Numbers
  • 5501
Name Phosphoglycerate mutase 1
Synonyms
  1. BPG-dependent PGAM 1
  2. PGAM-B
  3. Phosphoglycerate mutase isozyme B
Gene Name PGAM1
Protein Type Enzyme
Biological Properties
General Function Involved in catalytic activity
Specific 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.
Pathways
  • Fanconi-bickel syndrome
  • Fructose-1,6-diphosphatase deficiency
  • Gluconeogenesis
  • Glycine, serine and threonine metabolism
  • Glycogen Storage Disease Type 1A (GSD1A) or Von Gierke Disease
  • Glycogenosis, Type IA. Von gierke disease
  • Glycogenosis, Type IB
  • Glycogenosis, Type IC
  • Glycogenosis, Type VII. Tarui disease
  • Glycolysis
  • Glycolysis / Gluconeogenesis
  • Phosphoenolpyruvate carboxykinase deficiency 1 (PEPCK1)
  • Triosephosphate isomerase
Reactions
2-Phospho-D-glyceric acid → 3-Phosphoglyceric acid details
Glyceric acid 1,3-biphosphate → 2,3-Diphosphoglyceric acid details
2,3-Diphosphoglyceric acid + Water → 3-Phosphoglyceric acid + Phosphoric acid details
GO Classification
Biological Process
small molecule metabolic process
regulation of glycolysis
glycolysis
gluconeogenesis
regulation of pentose-phosphate shunt
respiratory burst
Cellular Component
cytosol
Function
catalytic activity
isomerase activity
intramolecular transferase activity
intramolecular transferase activity, phosphotransferases
Molecular Function
bisphosphoglycerate 2-phosphatase activity
bisphosphoglycerate mutase activity
phosphoglycerate mutase activity
Process
metabolic process
small molecule metabolic process
alcohol metabolic process
monosaccharide metabolic process
hexose metabolic process
glucose metabolic process
glucose catabolic process
glycolysis
Cellular Location Not Available
Gene Properties
Chromosome Location 10
Locus 10q25.3
SNPs PGAM1
Gene Sequence
>765 bp
ATGGCCGCCTACAAACTGGTGCTGATCCGGCACGGCGAGAGCGCATGGAACCTGGAGAAC
CGCTTCAGCGGCTGGTACGACGCCGACCTGAGCCCGGCGGGCCACGAGGAGGCGAAGCGC
GGCGGGCAGGCGCTACGAGATGCTGGCTATGAGTTTGACATCTGCTTCACCTCAGTGCAG
AAGAGAGCGATCCGGACCCTCTGGACAGTGCTAGATGCCATTGATCAGATGTGGCTGCCA
GTGGTGAGGACTTGGCGCCTCAATGAGCGGCACTATGGGGGTCTAACCGGTCTCAATAAA
GCAGAAACTGCTGCAAAGCATGGTGAGGCCCAGGTGAAGATCTGGAGGCGCTCCTATGAT
GTCCCACCACCTCCGATGGAGCCCGACCATCCTTTCTACAGCAACATCAGTAAGGATCGC
AGGTATGCAGACCTCACAGAAGATCAGCTACCCTCCTGTGAGAGTCTGAAGGATACTATT
GCCAGAGCTCTGCCCTTCTGGAATGAAGAAATAGTTCCCCAGATCAAGGAGGGGAAACGT
GTACTGATTGCAGCCCATGGCAACAGCCTCCGGGGCATTGTCAAGCATCTGGAGGGTCTC
TCTGAAGAGGCTATCATGGAGCTGAACCTGCCGACTGGTATTCCCATTGTCTATGAATTG
GACAAGAACTTGAAGCCTATCAAGCCCATGCAGTTTCTGGGGGATGAAGAGACGGTGCGC
AAAGCCATGGAAGCTGTGGCTGCCCAGGGCAAGGCCAAGAAGTGA
Protein Properties
Number of Residues 254
Molecular Weight 28803.675
Theoretical pI 7.182
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Phosphoglycerate mutase 1
MAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQ
KRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYD
VPPPPMEPDHPFYSNISKDRRYADLTEDQLPSCESLKDTIARALPFWNEEIVPQIKEGKR
VLIAAHGNSLRGIVKHLEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVR
KAMEAVAAQGKAKK
GenBank ID Protein 9956014
UniProtKB/Swiss-Prot ID P18669
UniProtKB/Swiss-Prot Entry Name PGAM1_HUMAN
PDB IDs
GenBank Gene ID AY007118
GeneCard ID PGAM1
GenAtlas ID PGAM1
HGNC ID HGNC:8888
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed:15592455 ]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  6. 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 JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed:18083107 ]
  7. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. doi: 10.1021/pr900044c. [PubMed:19534553 ]
  8. Sakoda S, Shanske S, DiMauro S, Schon EA: Isolation of a cDNA encoding the B isozyme of human phosphoglycerate mutase (PGAM) and characterization of the PGAM gene family. J Biol Chem. 1988 Nov 15;263(32):16899-905. [PubMed:2846553 ]
  9. Blouquit Y, Calvin MC, Rosa R, Prome D, Prome JC, Pratbernou F, Cohen-Solal M, Rosa J: Sequence of the human erythrocyte phosphoglycerate mutase by microsequencer and mass spectrometry. J Biol Chem. 1988 Nov 15;263(32):16906-10. [PubMed:2846554 ]
  10. Rasmussen RK, Ji H, Eddes JS, Moritz RL, Reid GE, Simpson RJ, Dorow DS: Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. Electrophoresis. 1997 Mar-Apr;18(3-4):588-98. [PubMed:9150946 ]
  11. Wang Y, Wei Z, Liu L, Cheng Z, Lin Y, Ji F, Gong W: Crystal structure of human B-type phosphoglycerate mutase bound with citrate. Biochem Biophys Res Commun. 2005 Jun 17;331(4):1207-15. [PubMed:15883004 ]