Phosphoglycerate mutase 2
Details
- Name
- Phosphoglycerate mutase 2
- Synonyms
- 3.1.3.13
- BPG-dependent PGAM 2
- Muscle-specific phosphoglycerate mutase
- PGAM-M
- PGAMM
- Phosphoglycerate mutase isozyme M
- Gene Name
- PGAM2
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0019575|Phosphoglycerate mutase 2 MATHRLVMVRHGESTWNQENRFCGWFDAELSEKGTEEAKRGAKAIKDAKMEFDICYTSVL KRAIRTLWAILDGTDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEEQVKIWRRSFD IPPPPMDEKHPYYNSISKERRYAGLKPGELPTCESLKDTIARALPFWNEEIVPQIKAGKR VLIAAHGNSLRGIVKHLEGMSDQAIMELNLPTGIPIVYELNKELKPTKPMQFLGDEETVR KAMEAVAAQGKAK
- Number of residues
- 253
- Molecular Weight
- 28765.96
- Theoretical pI
- Not Available
- GO Classification
- Functions2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity / bisphosphoglycerate 2-phosphatase activity / bisphosphoglycerate mutase activity / cofactor binding / phosphoglycerate mutase activityProcessescanonical glycolysis / carbohydrate metabolic process / gluconeogenesis / glucose metabolic process / glycolytic process / Notch signaling pathway / regulation of pentose-phosphate shunt / response to mercury ion / small molecule metabolic process / spermatogenesis / striated muscle contractionComponentscytosol / extracellular exosome / nucleus
- General Function
- Phosphoglycerate mutase 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.
- Pfam Domain Function
- His_Phos_1 (PF00300)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0019576|Phosphoglycerate mutase 2 (PGAM2) ATGGCCACTCACCGCCTCGTGATGGTCCGGCACGGCGAGAGCACATGGAACCAGGAGAAC CGTTTCTGTGGCTGGTTCGATGCAGAGCTGAGTGAAAAGGGGACCGAGGAGGCCAAGCGG GGAGCCAAGGCCATCAAGGATGCCAAGATGGAGTTTGACATCTGCTACACGTCAGTGCTG AAGCGGGCCATCCGCACCCTCTGGGCCATCCTGGACGGCACGGACCAGATGTGGCTGCCT GTGGTGCGCACTTGGCGCCTCAATGAGCGGCATTACGGGGGCCTCACAGGCCTCAACAAG GCAGAAACGGCCGCCAAGCACGGGGAGGAGCAGGTGAAGATCTGGAGGCGCTCCTTCGAC ATCCCGCCGCCCCCGATGGACGAGAAGCACCCCTACTACAACTCCATTAGCAAGGAGCGT CGGTACGCAGGCCTGAAGCCCGGGGAACTCCCCACCTGCGAGAGCCTCAAGGACACCATT GCCCGGGCCCTGCCCTTCTGGAACGAGGAGATTGTTCCCCAGATCAAGGCCGGCAAGCGA GTGCTCATTGCAGCCCACGGGAACAGCCTGCGGGGCATTGTCAAGCACCTGGAAGGGATG TCAGACCAGGCGATCATGGAGCTGAACCTGCCCACGGGGATCCCCATTGTGTATGAGCTG AACAAGGAGCTGAAGCCCACCAAGCCCATGCAGTTCCTGGGTGATGAGGAAACGGTGCGG AAGGCCATGGAGGCTGTGGCTGCCCAGGGCAAGGCCAAGTGA
- Chromosome Location
- 7
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P15259 UniProtKB Entry Name PGAM2_HUMAN HGNC ID HGNC:8889 - General References
- Castella-Escola J, Ojcius DM, LeBoulch P, Joulin V, Blouquit Y, Garel MC, Valentin C, Rosa R, Climent-Romeo F, Cohen-Solal M: Isolation and characterization of the gene encoding the muscle-specific isozyme of human phosphoglycerate mutase. Gene. 1990 Jul 16;91(2):225-32. [Article]
- Tsujino S, Sakoda S, Mizuno R, Kobayashi T, Suzuki T, Kishimoto S, Shanske S, DiMauro S, Schon EA: Structure of the gene encoding the muscle-specific subunit of human phosphoglycerate mutase. J Biol Chem. 1989 Sep 15;264(26):15334-7. [Article]
- Shanske S, Sakoda S, Hermodson MA, DiMauro S, Schon EA: Isolation of a cDNA encoding the muscle-specific subunit of human phosphoglycerate mutase. J Biol Chem. 1987 Oct 25;262(30):14612-7. [Article]
- 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. [Article]
- Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D: Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry. Proteomics. 2007 Mar;7(6):868-74. [Article]
- Tsujino S, Shanske S, Sakoda S, Fenichel G, DiMauro S: The molecular genetic basis of muscle phosphoglycerate mutase (PGAM) deficiency. Am J Hum Genet. 1993 Mar;52(3):472-7. [Article]
- Hadjigeorgiou GM, Kawashima N, Bruno C, Andreu AL, Sue CM, Rigden DJ, Kawashima A, Shanske S, DiMauro S: Manifesting heterozygotes in a Japanese family with a novel mutation in the muscle-specific phosphoglycerate mutase (PGAM-M) gene. Neuromuscul Disord. 1999 Oct;9(6-7):399-402. [Article]