We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for Myoinositol (HMDB00211)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-03-12 10:53:38
Accession Number HMDB00211
Secondary Accession Numbers HMDB02256
Common Name Myoinositol
Description Inositol is a cyclic polyalcohol that plays an important role as a second messenger in a cell, in the form of inositol phosphates. It is found in many foods, particularly in cereals with high bran content. It is an isomer of glucose that has traditionally been considered to be a B vitamin although it has an uncertain status as a vitamin and a deficiency syndrome has not been identified in man. (From Martindale, The Extra Pharmacopoeia, 30th ed., p1379) Inositol phospholipids are important in signal transduction.
Synonyms
  1. MI
  2. Meat sugar
  3. Myo-Inositol
  4. Myoinosite
  5. Myoinositol
  6. Phaseomannite
  7. Rat antispectacled eye factor
  8. cis-1,2,3,5-trans-4,6-Cyclohexanehexol
  9. i-Inositol
  10. iso-Inositol
  11. meso-Inositol
Chemical IUPAC Name (1r,2R,3S,4s,5R,6S)-cyclohexane-1,2,3,4,5,6-hexol
Chemical Formula C6H12O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Alcohols and Polyols
Sub Class
  • Simple alcohols
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
Biofunction
  • Osmolyte
  • Second messenger
  • Component of Glycerophospholipid metabolism
  • Component of Inositol phosphate metabolism
  • Component of Streptomycin biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 180.156
Monoisotopic Molecular Weight 180.063385
Isomeric SMILES O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@@H]1O
Canonical SMILES OC1C(O)C(O)C(O)C(O)C1O
KEGG Compound ID C00137 Link Image
BioCyc ID MYO-INOSITOL Link Image
BiGG ID 33990 Link Image
Wikipedia Link MI Link Image
NuGOwiki Link HMDB00211 Link Image
Metagene Link HMDB00211 Link Image
METLIN ID 5221 Link Image
PubChem Compound 892 Link Image
PubChem Substance 10355714 Link Image
ChEBI ID 17268 Link Image
CAS Registry Number 87-89-8
InChI Identifier InChI=1/C6H12O6/c7-1-2(8)4(10)6(12)5(11)3(1)9/h1-12H/t1-,2-,3-,4+,5-,6-
Synthesis Reference Iselin, Beat M. Synthesis of inositol-5-monophosphoric acid and scyllitol monophosphoric acid. Journal of the American Chemical Society (1949), 71 3822-5.
Melting Point (Experimental) 225 oC
Experimental Water Solubility 143 mg/mL at 19 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)]; 143.0 mg/mL at 19 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 485.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.08 [MEYLAN,WM & HOWARD,PH (1995)]; -2.59 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Basal Ganglia —
Brain —
Fibroblasts —
Intestine —
Kidney —
Myelin —
Nerve Cells —
Neuron —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 24.0 +/- 7.8 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 23.0 +/- 8.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 30.0 (21.0-49.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Huck JH, Verhoeven NM, Struys EA, Salomons GS, Jakobs C, van der Knaap MS: Ribose-5-phosphate isomerase deficiency: new inborn error in the pentose phosphate pathway associated with a slowly progressive leukoencephalopathy. Am J Hum Genet. 2004 Apr;74(4):745-51. Epub 2004 Feb 25. [PubMed Link Image]
Biofluid CSF
Value 158.8 +/- 46.07 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Huang W, Alexander GE, Daly EM, Shetty HU, Krasuski JS, Rapoport SI, Schapiro MB: High brain myo-inositol levels in the predementia phase of Alzheimer's disease in adults with Down's syndrome: a 1H MRS study. Am J Psychiatry. 1999 Dec;156(12):1879-86. [PubMed Link Image]
  • De Stefano N, Mortilla M, Federico A: Proton magnetic resonance spectroscopy of the brain in dementia. Ital J Neurol Sci. 1999;20(5 Suppl):S258-64. [PubMed Link Image]
  • Groenen PM, Peer PG, Wevers RA, Swinkels DW, Franke B, Mariman EC, Steegers-Theunissen RP: Maternal myo-inositol, glucose, and zinc status is associated with the risk of offspring with spina bifida. Am J Obstet Gynecol. 2003 Dec;189(6):1713-9. [PubMed Link Image]
  • Groenen PM, Klootwijk R, Schijvenaars MM, Straatman H, Mariman EC, Franke B, Steegers-Theunissen RP: Spina bifida and genetic factors related to myo-inositol, glucose, and zinc. Mol Genet Metab. 2004 Jun;82(2):154-61. [PubMed Link Image]
  • Dunne VG, Bhattachayya S, Besser M, Rae C, Griffin JL: Metabolites from cerebrospinal fluid in aneurysmal subarachnoid haemorrhage correlate with vasospasm and clinical outcome: a pattern-recognition 1H NMR study. NMR Biomed. 2005 Feb;18(1):24-33. [PubMed Link Image]
  • A J, Trygg J, Gullberg J, Johansson AI, Jonsson P, Antti H, Marklund SL, Moritz T: Extraction and GC/MS analysis of the human blood plasma metabolome. Anal Chem. 2005 Dec 15;77(24):8086-94. [PubMed Link Image]
  • Shoda J, Tanaka N, Osuga T, Matsuura K, Miyazaki H: Altered bile acid metabolism in liver disease: concurrent occurrence of C-1 and C-6 hydroxylated bile acid metabolites and their preferential excretion into urine. J Lipid Res. 1990 Feb;31(2):249-59. [PubMed Link Image]
  • Kusmierz J, DeGeorge JJ, Sweeney D, May C, Rapoport SI: Quantitative analysis of polyols in human plasma and cerebrospinal fluid. J Chromatogr. 1989 Dec 29;497:39-48. [PubMed Link Image]
  • Shoda J, Mahara R, Osuga T, Tohma M, Ohnishi S, Miyazaki H, Tanaka N, Matsuzaki Y: Similarity of unusual bile acids in human umbilical cord blood and amniotic fluid from newborns and in sera and urine from adult patients with cholestatic liver diseases. J Lipid Res. 1988 Jul;29(7):847-58. [PubMed Link Image]
  • Shetty HU, Schapiro MB, Holloway HW, Rapoport SI: Polyol profiles in Down syndrome. myo-Inositol, specifically, is elevated in the cerebrospinal fluid. J Clin Invest. 1995 Feb;95(2):542-6. [PubMed Link Image]
  • Shetty HU, Holloway HW, Schapiro MB: Cerebrospinal fluid and plasma distribution of myo-inositol and other polyols in Alzheimer disease. Clin Chem. 1996 Feb;42(2):298-302. [PubMed Link Image]
  • Acevedo LD, Holloway HW, Rapoport SI, Shetty HU: Application of stable isotope tracer combined with mass spectrometric detection for studying myo-inositol uptake by cultured neurons from fetal mouse: effect of trisomy 16. J Mass Spectrom. 1997 Apr;32(4):395-400. [PubMed Link Image]
  • Michaelis T, Videen JS, Linsey MS, Ross BD: Dialysis and transplantation affect cerebral abnormalities of end-stage renal disease. J Magn Reson Imaging. 1996 Mar-Apr;6(2):341-7. [PubMed Link Image]
Biofluid CSF
Value 133.0 (111.0-155.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shetty HU, Holloway HW, Rapoport SI: Capillary gas chromatography combined with ion trap detection for quantitative profiling of polyols in cerebrospinal fluid and plasma. Anal Biochem. 1995 Jan 1;224(1):279-85. [PubMed Link Image]
Biofluid CSF
Value 174.0 +/- 31.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 138.3 +/- 24.4 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shetty HU, Holloway HW, Schapiro MB: Cerebrospinal fluid and plasma distribution of myo-inositol and other polyols in Alzheimer disease. Clin Chem. 1996 Feb;42(2):298-302. [PubMed Link Image]
Biofluid CSF
Value 84 +/- 40 uM
Age N/A
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Lewis MJ, Morrissey JA, Flegel MD, Jeroncic K, Xiong Y, Cheng D, Eisner R, Gautam B, Tzur D, Sawhney S, Bamforth F, Greiner R, Li L: The human cerebrospinal fluid metabolome. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Aug 15;871(2):164-173. Epub 2008 May 8. [PubMed Link Image]
Biofluid Urine
Value 52.8 +/- 47.7 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 6.11 +/- 6.25 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 20.0 (23.0–24.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Ribose-5-phosphate isomerase deficiency
Comments Not Available
References
  • Huck JH, Verhoeven NM, Struys EA, Salomons GS, Jakobs C, van der Knaap MS: Ribose-5-phosphate isomerase deficiency: new inborn error in the pentose phosphate pathway associated with a slowly progressive leukoencephalopathy. Am J Hum Genet. 2004 Apr;74(4):745-51. Epub 2004 Feb 25. [PubMed Link Image]
Biofluid CSF
Value 158.8 +/- 27.2 uM
Age N/A
Sex N/A
Condition Alzheimer's disease
Comments Not Available
References
  • Shetty HU, Holloway HW, Schapiro MB: Cerebrospinal fluid and plasma distribution of myo-inositol and other polyols in Alzheimer disease. Clin Chem. 1996 Feb;42(2):298-302. [PubMed Link Image]
Biofluid CSF
Value 158.8 +/- 27.2 uM
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Shetty HU, Holloway HW, Schapiro MB: Cerebrospinal fluid and plasma distribution of myo-inositol and other polyols in Alzheimer disease. Clin Chem. 1996 Feb;42(2):298-302. [PubMed Link Image]
Biofluid Urine
Value 20.33 +/- 13.70 umol/mmol creatinine
Age Adult:>18 yrs old
Sex N/A
Condition Cachexia
Comments Not Available
References
Associated Disorders
Condition References
Alzheimer's disease
  • Shetty HU, Holloway HW, Schapiro MB: Cerebrospinal fluid and plasma distribution of myo-inositol and other polyols in Alzheimer disease. Clin Chem. 1996 Feb;42(2):298-302. [PubMed Link Image]
Cachexia —
Ribose-5-phosphate isomerase deficiency
  • Huck JH, Verhoeven NM, Struys EA, Salomons GS, Jakobs C, van der Knaap MS: Ribose-5-phosphate isomerase deficiency: new inborn error in the pentose phosphate pathway associated with a slowly progressive leukoencephalopathy. Am J Hum Genet. 2004 Apr;74(4):745-51. Epub 2004 Feb 25. [PubMed Link Image]
OMIM ID
  • 104300 Link Image (Alzheimer's disease)
  • 608611 Link Image (Ribose-5-phosphate isomerase deficiency)
Pathways
Name SMPDB Link KEGG Link
Galactose Metabolism SMP00043 Link Image map00052 Link Image
Inositol Metabolism SMP00011 Link Image map00562 Link Image
Inositol Phosphate Metabolism SMP00462 Link Image map00562 Link Image
Phosphatidylinositol Phosphate Metabolism SMP00463 Link Image map00562 Link Image
General References
  1. Gryz EA, Galicka-Latala D, Szczudlik A, Sieradzki J: [Etiopathogenesis of diabetic neuropathy] Przegl Lek. 2000;57(12):727-31. [PubMed Link Image]
  2. Kim MO, Im JH, Choi CG, Lee MC: Proton MR spectroscopic findings in paroxysmal kinesigenic dyskinesia. Mov Disord. 1998 May;13(3):570-5. [PubMed Link Image]
  3. Wuarin-Bierman L, Zahnd GR: Current aspects of research on the pathogenesis of diabetic neuropathy. Diabete Metab. 1986 Dec;12(6):319-24. [PubMed Link Image]
  4. Reznek RH, Salway JG, Thomas PK: Plasma-myoinositol concentrations in uraemic neuropathy. Lancet. 1977 Mar 26;1(8013):675-6. [PubMed Link Image]
  5. Scully SE, Stebner FC, Yoest SM: Magnetic resonance spectroscopic findings in neuro-Behcet disease. Neurologist. 2004 Nov;10(6):323-6. [PubMed Link Image]
  6. Cordoba J, Hinojosa C, Sampedro F, Alonso J, Rovira A, Quiroga S, Esteban R, Guardia J: Usefulness of magnetic resonance spectroscopy for diagnosis of hepatic encephalopathy in a patient with relapsing confusional syndrome. Dig Dis Sci. 2001 Nov;46(11):2451-5. [PubMed Link Image]
  7. Chang L, Ernst T, Leonido-Yee M, Witt M, Speck O, Walot I, Miller EN: Highly active antiretroviral therapy reverses brain metabolite abnormalities in mild HIV dementia. Neurology. 1999 Sep 11;53(4):782-9. [PubMed Link Image]
  8. Kusmierz J, DeGeorge JJ, Sweeney D, May C, Rapoport SI: Quantitative analysis of polyols in human plasma and cerebrospinal fluid. J Chromatogr. 1989 Dec 29;497:39-48. [PubMed Link Image]
  9. Ashwal S, Holshouser B, Tong K, Serna T, Osterdock R, Gross M, Kido D: Proton spectroscopy detected myoinositol in children with traumatic brain injury. Pediatr Res. 2004 Oct;56(4):630-8. Epub 2004 Aug 4. [PubMed Link Image]
  10. Servo C, Pitkanen E: Variation in polyol levels in cerebrospinal fluid and serum in diabetic patients. Diabetologia. 1975 Dec;11(6):575-80. [PubMed Link Image]
  11. Utriainen M, Komu M, Vuorinen V, Lehikoinen P, Sonninen P, Kurki T, Utriainen T, Roivainen A, Kalimo H, Minn H: Evaluation of brain tumor metabolism with [11C]choline PET and 1H-MRS. J Neurooncol. 2003 May;62(3):329-38. [PubMed Link Image]
  12. Grzelec H: [Pathogenesis and treatment of diabetic neuropathy] Neurol Neurochir Pol. 1991 Jul-Aug;25(4):477-84. [PubMed Link Image]
  13. Ernst T, Itti E, Itti L, Chang L: Changes in cerebral metabolism are detected prior to perfusion changes in early HIV-CMC: A coregistered (1)H MRS and SPECT study. J Magn Reson Imaging. 2000 Dec;12(6):859-65. [PubMed Link Image]
  14. Hallman M, Saugstad OD, Porreco RP, Epstein BL, Gluck L: Role of myoinositol in regulation of surfactant phospholipids in the newborn. Early Hum Dev. 1985 Jan;10(3-4):245-54. [PubMed Link Image]
  15. Chang L, Lee PL, Yiannoutsos CT, Ernst T, Marra CM, Richards T, Kolson D, Schifitto G, Jarvik JG, Miller EN, Lenkinski R, Gonzalez G, Navia BA: A multicenter in vivo proton-MRS study of HIV-associated dementia and its relationship to age. Neuroimage. 2004 Dec;23(4):1336-47. [PubMed Link Image]
  16. Rysz J, Bartnicki P, Blaszczak R, Kujawski K, Cialkowska-Rysz A, Olszewski R, Markuszewski L: [Anti-inflammatory action of myoinositol in renal insufficiency] Pol Merkur Lekarski. 2006 Feb;20(116):180-3. [PubMed Link Image]
  17. Lee PL, Yiannoutsos CT, Ernst T, Chang L, Marra CM, Jarvik JG, Richards TL, Kwok EW, Kolson DL, Simpson D, Tang CY, Schifitto G, Ketonen LM, Meyerhoff DJ, Lenkinski RE, Gonzalez RG, Navia BA: A multi-center 1H MRS study of the AIDS dementia complex: validation and preliminary analysis. J Magn Reson Imaging. 2003 Jun;17(6):625-33. [PubMed Link Image]
  18. Galasko GT, Bao Y, Broomfield SJ, Hooper NM, Turner AJ, Larner J: Circulating factors and insulin resistance. I. A novel myoinositol 1,2-cyclic phosphate phosphoglycan insulin antagonist from human plasma is elevated in noninsulin-dependent diabetes mellitus. J Clin Endocrinol Metab. 1995 Aug;80(8):2419-29. [PubMed Link Image]
  19. Shetty HU, Holloway HW, Rapoport SI: Capillary gas chromatography combined with ion trap detection for quantitative profiling of polyols in cerebrospinal fluid and plasma. Anal Biochem. 1995 Jan 1;224(1):279-85. [PubMed Link Image]
  20. Yiannoutsos CT, Ernst T, Chang L, Lee PL, Richards T, Marra CM, Meyerhoff DJ, Jarvik JG, Kolson D, Schifitto G, Ellis RJ, Swindells S, Simpson DM, Miller EN, Gonzalez RG, Navia BA: Regional patterns of brain metabolites in AIDS dementia complex. Neuroimage. 2004 Nov;23(3):928-35. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Alpha-galactosidase A precursor
  2. Inositol oxygenase
  3. Inositol monophosphatase
  4. Inositol monophosphatase 2
  5. MIOX protein
  6. Inositol monophosphatase 3
  7. cDNA FLJ77674, highly similar to Homo sapiens CDP-diacylglycerol-- inositol 3-phosphatidyltransferase (phosphatidylinositol synthase) (CDIPT), transcript variant 1, mRNA (CDP-diacylglycerol--inositol 3- phosphatidyltransferase (Phosphatidylinositol syntha
  8. cDNA, FLJ93260, Homo sapiens inositol(myo)-1(or 4)-monophosphatase 1 (IMPA1), mRNA (Inositol(Myo)-1(Or 4)-monophosphatase 1, isoform CRA_a)
  9. Inositol monophosphatase 2 variant 1 (Inositol(Myo)-1(Or 4)-monophosphatase 2, isoform CRA_b)
Enzyme 1 [top]
Enzyme 1 ID 5997
Enzyme 1 Name Alpha-galactosidase A precursor
Enzyme 1 Synonyms
  1. Melibiase
  2. Alpha-D- galactoside galactohydrolase
  3. Alpha-D-galactosidase A
  4. Agalsidase alfa
Enzyme 1 Gene Name GLA
Enzyme 1 Protein Sequence >Alpha-galactosidase A precursor 
MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEP
DSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQL
ANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENL
ADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIK
SILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDL
RHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIG
GPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENT
MQMSLKDLL
Enzyme 1 Number of Residues 429
Enzyme 1 Molecular Weight 48767
Enzyme 1 Theoretical pI 5.27
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Hydrolysis of terminal, non-reducing alpha-D- galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase
Enzyme 1 Pathways
Enzyme 1 Reactions
  • Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-31
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 757912 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P06280 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AGAL_HUMAN Link Image
Enzyme 1 PDB ID 1R47 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1290 bp 
ATGCAGCTGAGGAACCCAGAACTACATCTGGGCTGCGCGCTTGCGCTTCGCTTCCTGGCC
CTCGTTTCCTGGGACATCCCTGGGGCTAGAGCACTGGACAATGGATTGGCAAGGACGCCT
ACCATGGGCTGGCTGCACTGGGAGCGCTTCATGTGCAACCTTGACTGCCAGGAAGAGCCA
GATTCCTGCATCAGTGAGAAGCTCTTCATGGAGATGGCAGAGCTCATGGTCTCAGAAGGC
TGGAAGGATGCAGGTTATGAGTACCTCTGCATTGATGACTGTTGGATGGCTCCCCAAAGA
GATTCAGAAGGCAGACTTCAGGCAGACCCTCAGCGCTTTCCTCATGGGATTCGCCAGCTA
GCTAATTATGTTCACAGCAAAGGACTGAAGCTAGGGATTTATGCAGATGTTGGAAATAAA
ACCTGCGCAGGCTTCCCTGGGAGTTTTGGATACTACGACATTGATGCCCAGACCTTTGCT
GACTGGGGAGTAGATCTGCTAAAATTTGATGGTTGTTACTGTGACAGTTTGGAAAATTTG
GCAGATGGTTATAAGCACATGTCCTTGGCCCTGAATAGGACTGGCAGAAGCATTGTGTAC
TCCTGTGAGTGGCCTCTTTATATGTGGCCCTTTCAAAAGCCCAATTATACAGAAATCCGA
CAGTACTGCAATCACTGGCGAAATTTTGCTGACATTGATGATTCCTGGAAAAGTATAAAG
AGTATCTTGGACTGGACATCTTTTAACCAGGAGAGAATTGTTGATGTTGCTGGACCAGGG
GGTTGGAATGACCCAGATATGTTAGTGATTGGCAACTTTGGCCTCAGCTGGAATCAGCAA
GTAACTCAGATGGCCCTCTGGGCTATCATGGCTGCTCCTTTATTCATGTCTAATGACCTC
CGACACATCAGCCCTCAAGCCAAAGCTCTCCTTCAGGATAAGGACGTAATTGCCATCAAT
CAGGACCCCTTGGGCAAGCAAGGGTACCAGCTTAGACAGGGAGACAACTTTGAAGTGTGG
GAACGACCTCTCTCAGGCTTAGCCTGGGCTGTAGCTATGATAAACCGGCAGGAGATTGGT
GGACCTCGCTCTTATACCATCGCAGTTGCTTCCCTGGGTAAAGGAGTGGCCTGTAATCCT
GCCTGCTTCATCACACAGCTCCTCCCTGTGAAAAGGAAGCTAGGGTTCTATGAATGGACT
TCAAGGTTAAGAAGTCACATAAATCCCACAGGCACTGTTTTGCTTCAGCTAGAAAATACA
ATGCAGATGTCATTAAAAGACTTACTTTAA
Enzyme 1 GenBank Gene ID X05790 Link Image
Enzyme 1 GeneCard ID GLA Link Image
Enzyme 1 GenAtlas ID GLA Link Image
Enzyme 1 HGNC ID HGNC:4296 Link Image
Enzyme 1 Chromosome Location X
Enzyme 1 Locus Xq22
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Tsuji S, Martin BM, Kaslow DC, Migeon BR, Choudary PV, Stubbleflied BK, Mayor JA, Murray GJ, Barranger JA, Ginns EI: Signal sequence and DNA-mediated expression of human lysosomal alpha-galactosidase A. Eur J Biochem. 1987 Jun 1;165(2):275-80. [PubMed Link Image]
  2. Kornreich R, Desnick RJ, Bishop DF: Nucleotide sequence of the human alpha-galactosidase A gene. Nucleic Acids Res. 1989 Apr 25;17(8):3301-2. [PubMed Link Image]
  3. Oeltjen JC, Liu X, Lu J, Allen RC, Muzny D, Belmont JW, Gibbs RA: Sixty-nine kilobases of contiguous human genomic sequence containing the alpha-galactosidase A and Bruton's tyrosine kinase loci. Mamm Genome. 1995 May;6(5):334-8. [PubMed Link Image]
  4. Bishop DF, Calhoun DH, Bernstein HS, Hantzopoulos P, Quinn M, Desnick RJ: Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding the mature enzyme. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4859-63. [PubMed Link Image]
  5. Quinn M, Hantzopoulos P, Fidanza V, Calhoun DH: A genomic clone containing the promoter for the gene encoding the human lysosomal enzyme, alpha-galactosidase A. Gene. 1987;58(2-3):177-88. [PubMed Link Image]
  6. Bishop DF, Kornreich R, Desnick RJ: Structural organization of the human alpha-galactosidase A gene: further evidence for the absence of a 3' untranslated region. Proc Natl Acad Sci U S A. 1988 Jun;85(11):3903-7. [PubMed Link Image]
  7. Novo FJ, Kruszewski A, MacDermot KD, Goldspink G, Gorecki DC: Editing of human alpha-galactosidase RNA resulting in a pyrimidine to purine conversion. Nucleic Acids Res. 1995 Jul 25;23(14):2636-40. [PubMed Link Image]
  8. Eng CM, Desnick RJ: Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene. Hum Mutat. 1994;3(2):103-11. [PubMed Link Image]
  9. Koide T, Ishiura M, Iwai K, Inoue M, Kaneda Y, Okada Y, Uchida T: A case of Fabry's disease in a patient with no alpha-galactosidase A activity caused by a single amino acid substitution of Pro-40 by Ser. FEBS Lett. 1990 Jan 1;259(2):353-6. [PubMed Link Image]
  10. von Scheidt W, Eng CM, Fitzmaurice TF, Erdmann E, Hubner G, Olsen EG, Christomanou H, Kandolf R, Bishop DF, Desnick RJ: An atypical variant of Fabry's disease with manifestations confined to the myocardium. N Engl J Med. 1991 Feb 7;324(6):395-9. [PubMed Link Image]
  11. Sakuraba H, Oshima A, Fukuhara Y, Shimmoto M, Nagao Y, Bishop DF, Desnick RJ, Suzuki Y: Identification of point mutations in the alpha-galactosidase A gene in classical and atypical hemizygotes with Fabry disease. Am J Hum Genet. 1990 Nov;47(5):784-9. [PubMed Link Image]
  12. Bernstein HS, Bishop DF, Astrin KH, Kornreich R, Eng CM, Sakuraba H, Desnick RJ: Fabry disease: six gene rearrangements and an exonic point mutation in the alpha-galactosidase gene. J Clin Invest. 1989 Apr;83(4):1390-9. [PubMed Link Image]
  13. Ishii S, Sakuraba H, Suzuki Y: Point mutations in the upstream region of the alpha-galactosidase A gene exon 6 in an atypical variant of Fabry disease. Hum Genet. 1992 Apr;89(1):29-32. [PubMed Link Image]
  14. Eng CM, Resnick-Silverman LA, Niehaus DJ, Astrin KH, Desnick RJ: Nature and frequency of mutations in the alpha-galactosidase A gene that cause Fabry disease. Am J Hum Genet. 1993 Dec;53(6):1186-97. [PubMed Link Image]
  15. Davies JP, Winchester BG, Malcolm S: Mutation analysis in patients with the typical form of Anderson-Fabry disease. Hum Mol Genet. 1993 Jul;2(7):1051-3. [PubMed Link Image]
  16. Davies J, Christomanou H, Winchester B, Malcolm S: Detection of 8 new mutations in the alpha-galactosidase A gene in Fabry disease. Hum Mol Genet. 1994 Apr;3(4):667-9. [PubMed Link Image]
  17. Eng CM, Niehaus DJ, Enriquez AL, Burgert TS, Ludman MD, Desnick RJ: Fabry disease: twenty-three mutations including sense and antisense CpG alterations and identification of a deletional hot-spot in the alpha-galactosidase A gene. Hum Mol Genet. 1994 Oct;3(10):1795-9. [PubMed Link Image]
  18. Okumiya T, Ishii S, Takenaka T, Kase R, Kamei S, Sakuraba H, Suzuki Y: Galactose stabilizes various missense mutants of alpha-galactosidase in Fabry disease. Biochem Biophys Res Commun. 1995 Sep 25;214(3):1219-24. [PubMed Link Image]
  19. Okumiya T, Ishii S, Kase R, Kamei S, Sakuraba H, Suzuki Y: Alpha-galactosidase gene mutations in Fabry disease: heterogeneous expressions of mutant enzyme proteins. Hum Genet. 1995 May;95(5):557-61. [PubMed Link Image]
  20. Madsen KM, Hasholt L, Sorensen SA, Fermer ML, Dahl N: Two novel mutations (L32P) and (G85N) among five different missense mutations in six Danish families with Fabry's disease. Hum Mutat. 1995;5(3):277-8. [PubMed Link Image]
  21. Nakao S, Takenaka T, Maeda M, Kodama C, Tanaka A, Tahara M, Yoshida A, Kuriyama M, Hayashibe H, Sakuraba H, et al.: An atypical variant of Fabry's disease in men with left ventricular hypertrophy. N Engl J Med. 1995 Aug 3;333(5):288-93. [PubMed Link Image]
  22. Davies JP, Eng CM, Hill JA, Malcolm S, MacDermot K, Winchester B, Desnick RJ: Fabry disease: fourteen alpha-galactosidase A mutations in unrelated families from the United Kingdom and other European countries. Eur J Hum Genet. 1996;4(4):219-24. [PubMed Link Image]
  23. Cariolou MA, Christodoulides M, Manoli P, Kokkofitou A, Tsambaos D: Novel trinucleotide deletion in Fabry's disease. Hum Genet. 1996 Apr;97(4):468-70. [PubMed Link Image]
  24. Germain D, Biasotto M, Tosi M, Meo T, Kahn A, Poenaru L: Fluorescence-assisted mismatch analysis (FAMA) for exhaustive screening of the alpha-galactosidase A gene and detection of carriers in Fabry disease. Hum Genet. 1996 Dec;98(6):719-26. [PubMed Link Image]
  25. Blanch LC, Meaney C, Morris CP: A sensitive mutation screening strategy for Fabry disease: detection of nine mutations in the alpha-galactosidase A gene. Hum Mutat. 1996;8(1):38-43. [PubMed Link Image]
  26. Redonnet-Vernhet I, Ploos van Amstel JK, Jansen RP, Wevers RA, Salvayre R, Levade T: Uneven X inactivation in a female monozygotic twin pair with Fabry disease and discordant expression of a novel mutation in the alpha-galactosidase A gene. J Med Genet. 1996 Aug;33(8):682-8. [PubMed Link Image]
  27. Takata T, Okumiya T, Hayashibe H, Shimmoto M, Kase R, Itoh K, Utsumi K, Kamei S, Sakuraba H: Screening and detection of gene mutations in Japanese patients with Fabry disease by non-radioactive single-stranded conformation polymorphism analysis. Brain Dev. 1997 Mar;19(2):111-6. [PubMed Link Image]
  28. Eng CM, Ashley GA, Burgert TS, Enriquez AL, D'Souza M, Desnick RJ: Fabry disease: thirty-five mutations in the alpha-galactosidase A gene in patients with classic and variant phenotypes. Mol Med. 1997 Mar;3(3):174-82. [PubMed Link Image]
  29. Miyazaki T, Kajita M, Ohmori S, Mizutani N, Niwa T, Murata Y, Seo H: A novel mutation (E358K) in the alpha-galactosidase A gene detected in a Japanese family with Fabry disease. Hum Mutat. 1998;Suppl 1:S139-40. [PubMed Link Image]
  30. Okumiya T, Kawamura O, Itoh K, Kase R, Ishii S, Kamei S, Sakuraba H: Novel missense mutation (M72V) of alpha-galactosidase gene and its expression product in an atypical Fabry hemizygote. Hum Mutat. 1998;Suppl 1:S213-6. [PubMed Link Image]
  31. Guffon N, Froissart R, Chevalier-Porst F, Maire I: Mutation analysis in 11 French patients with Fabry disease. Hum Mutat. 1998;Suppl 1:S288-90. [PubMed Link Image]
  32. Germain DP, Poenaru L: Fabry disease: identification of novel alpha-galactosidase A mutations and molecular carrier detection by use of fluorescent chemical cleavage of mismatches. Biochem Biophys Res Commun. 1999 Apr 21;257(3):708-13. [PubMed Link Image]
  33. Beyer EM, Karpova EA, Udalova OV, Ploos van Amstel JK, van Diggelen OP, Tsvetkova IV: The multiple cases of Fabry disease in a Russian family caused by an E341K amino acid substitution in the alpha-galactosidase A. Clin Chim Acta. 1999 Feb;280(1-2):81-9. [PubMed Link Image]
  34. Topaloglu AK, Ashley GA, Tong B, Shabbeer J, Astrin KH, Eng CM, Desnick RJ: Twenty novel mutations in the alpha-galactosidase A gene causing Fabry disease. Mol Med. 1999 Dec;5(12):806-11. [PubMed Link Image]
  35. Lee JK, Kim GH, Kim JS, Kim KK, Lee MC, Yoo HW: Identification of four novel mutations in five unrelated Korean families with Fabry disease. Clin Genet. 2000 Sep;58(3):228-33. [PubMed Link Image]
  36. Ashton-Prolla P, Tong B, Shabbeer J, Astrin KH, Eng CM, Desnick RJ: Fabry disease: twenty-two novel mutations in the alpha-galactosidase A gene and genotype/phenotype correlations in severely and mildly affected hemizygotes and heterozygotes. J Investig Med. 2000 Jul;48(4):227-35. [PubMed Link Image]
  37. Germain DP, Salard D, Fellmann F, Azibi K, Caillaud C, Bernard MC, Poenaru L: Identification of a novel de novo mutation (G373D) in the alpha-galactosidase A gene (GLA) in a patient affected with Fabry disease. Hum Mutat. 2001 Apr;17(4):353. [PubMed Link Image]
  38. Blaydon D, Hill J, Winchester B: Fabry disease: 20 novel GLA mutations in 35 families. Hum Mutat. 2001 Nov;18(5):459. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6121
Enzyme 2 Name Inositol oxygenase
Enzyme 2 Synonyms
  1. Myo-inositol oxygenase
  2. Aldehyde reductase-like 6
  3. Renal-specific oxidoreductase
  4. Kidney-specific protein 32
Enzyme 2 Gene Name MIOX
Enzyme 2 Protein Sequence >Inositol oxygenase 
MKVTVGPDPSLVYRPDVDPEVAKDKASFRNYTSGPLLDRVFTTYKLMHTHQTVDFVRSKH
AQFGGFSYKKMTVMEAVDLLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVG
LLHDLGKVLALFGEPQWAVVGDTFPVGCRPQASVVFCDSTFQDNPDLQDPRYSTELGMYQ
PHCGLDRVLMSWGHDEYMYQVMKFNKFSLPPEAFYMIRFHSFYPWHTGRDYQQLCSQQDL
AMLPWVREFNKFDLYTKCPDLPDVDKLRPYYQGLIDKYCPGILSW
Enzyme 2 Number of Residues 285
Enzyme 2 Molecular Weight 33010
Enzyme 2 Theoretical pI 5.74
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Myo-inositol + O(2) = D-glucuronate + H(2)O
Enzyme 2 Pathways
Enzyme 2 Reactions
  • myo-inositol + O2 = D-glucuronate + H2O
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 17932582 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9UGB7 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name MIOX_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >858 bp 
ATGAAGGTGACGGTGGGCCCAGACCCTTCCCTGGTCTACCGACCTGATGTGGACCCAGAG
GTGGCCAAAGACAAGGCCAGCTTCCGGAACTACACGTCAGGTCCCCTCCTGGACCGTGTC
TTCACCACCTACAAGCTCATGCACACGCACCAGACAGTGGACTTCGTCAGGAGCAAGCAT
GCCCAGTTTGGGGGCTTCTCCTACAAGAAAATGACAGTCATGGAGGCCGTGGACCTGCTG
GATGGGCTGGTGGATGAGTCGGACCCGGACGTAGATTTCCCCAACTCCTTCCATGCCTTC
CAGACAGCGGAGGGCATCCGGAAGGCCCACCCAGACAAGGACTGGTTCCACCTCGTCGGG
CTCCTGCACGACCTGGGGAAGGTCCTGGCCCTGTTCGGGGAGCCCCAGTGGGCTGTCGTC
GGCGACACCTTCCCCGTCGGATGCCGTCCGCAGGCCTCCGTGGTTTTCTGCGACTCCACC
TTCCAGGACAACCCTGACCTCCAGGATCCTCGATACAGCACAGAGCTCGGGATGTATCAG
CCCCACTGTGGGCTCGACAGGGTCCTCATGTCCTGGGGCCATGATGAGTACATGTACCAG
GTGATGAAGTTTAACAAGTTCTCACTGCCCCCTGAGGCTTTCTACATGATCCGGTTCCAC
TCCTTCTACCCCTGGCACACGGGCCGCGACTACCAGCAGCTGTGCAGCCAGCAGGACCTG
GCCATGCTGCCCTGGGTGCGGGAGTTCAACAAGTTCGACCTCTACACCAAGTGCCCGGAC
CTGCCGGACGTGGACAAGCTGCGGCCCTACTACCAGGGGCTCATTGACAAGTACTGCCCT
GGCATCCTGAGCTGGTGA
Enzyme 2 GenBank Gene ID AY064416 Link Image
Enzyme 2 GeneCard ID MIOX Link Image
Enzyme 2 GenAtlas ID MIOX Link Image
Enzyme 2 HGNC ID HGNC:14522 Link Image
Enzyme 2 Chromosome Location 22
Enzyme 2 Locus 22q13.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Yang Q, Dixit B, Wada J, Tian Y, Wallner EI, Srivastva SK, Kanwar YS: Identification of a renal-specific oxido-reductase in newborn diabetic mice. Proc Natl Acad Sci U S A. 2000 Aug 29;97(18):9896-901. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6145
Enzyme 3 Name Inositol monophosphatase
Enzyme 3 Synonyms
  1. IMPase
  2. IMP
  3. Inositol-1(or 4-monophosphatase
  4. Lithium-sensitive myo-inositol monophosphatase A1
Enzyme 3 Gene Name IMPA1
Enzyme 3 Protein Sequence >Inositol monophosphatase 
MADPWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSPVDLVTATDQKVEKMLISSIKE
KYPSHSFIGEESVAAGEKSILTDNPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFG
VVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRTPETVRMVLSNME
KLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTG
GPFDLMSRRVIAANNRILAERIAKEIQVIPLQRDDED
Enzyme 3 Number of Residues 277
Enzyme 3 Molecular Weight 30189
Enzyme 3 Theoretical pI 4.91
Enzyme 3 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Carbohydrate transport and metabolism
Enzyme 3 Specific Function Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain
Enzyme 3 Pathways
Enzyme 3 Reactions
  • myo-inositol phosphate + H2O = myo-inositol + phosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 395340 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P29218 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name IMPA1_HUMAN Link Image
Enzyme 3 PDB ID 1IMB Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >834 bp 
ATGGCTGATCCTTGGCAGGAATGCATGGATTATGCAGTAACTCTAGCAAGACAAGCTGGA
GAGGTAGTTTGTGAAGCTATAAAAAATGAAATGAATGTTATGCTGAAAAGTTCTCCAGTT
GATTTGGTAACTGCTACGGACCAAAAAGTTGAAAAAATGCTTATCTCTTCCATAAAGGAA
AAGTATCCATCTCACAGTTTCATTGGTGAAGAATCTGTGGCAGCTGGGGAAAAAAGTATC
TTAACCGACAACCCCACATGGATCATTGACCCTATTGATGGAACAACTAACTTTGTACAT
AGATTTCCTTTTGTAGCTGTTTCAATTGGCTTTGCTGTAAATAAAAAGATAGAATTTGGA
GTTGTGTACAGTTGTGTGGAAGGCAAGATGTACACTGCCAGAAAAGGAAAAGGGGCCTTT
TGTAATGGTCAAAAACTACAAGTTTCACAACAAGAAGATATTACCAAATCTCTCTTGGTG
ACTGAGTTGGGCTCTTCTAGAACACCAGAGACTGTGAGAATGGTTCTTTCTAATATGGAA
AAGCTTTTTTGCATTCCTGTTCATGGGATCCGGAGTGTTGGAACAGCAGCTGTTAATATG
TGCCTTGTGGCAACTGGCGGAGCAGATGCATATTATGAAATGGGAATTCACTGCTGGGAT
GTTGCAGGAGCTGGCATTATTGTTACTGAAGCTGGTGGCGTGCTAATGGATGTTACAGGT
GGACCATTTGATTTGATGTCACGAAGAGTAATTGCTGCAAATAATAGAATATTAGCAGAA
AGGATAGCTAAAGAAATTCAGGTTATACCTTTGCAACGAGACGACGAAGATTAA
Enzyme 3 GenBank Gene ID X66922 Link Image
Enzyme 3 GeneCard ID IMPA1 Link Image
Enzyme 3 GenAtlas ID IMPA1 Link Image
Enzyme 3 HGNC ID HGNC:6050 Link Image
Enzyme 3 Chromosome Location 8
Enzyme 3 Locus 8q21.13-q21.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. McAllister G, Whiting P, Hammond EA, Knowles MR, Atack JR, Bailey FJ, Maigetter R, Ragan CI: cDNA cloning of human and rat brain myo-inositol monophosphatase. Expression and characterization of the human recombinant enzyme. Biochem J. 1992 Jun 15;284 ( Pt 3):749-54. [PubMed Link Image]
  2. Sjoholt G, Molven A, Lovlie R, Wilcox A, Sikela JM, Steen VM: Genomic structure and chromosomal localization of a human myo-inositol monophosphatase gene (IMPA). Genomics. 1997 Oct 1;45(1):113-22. [PubMed Link Image]
  3. Bone R, Springer JP, Atack JR: Structure of inositol monophosphatase, the putative target of lithium therapy. Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10031-5. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6411
Enzyme 4 Name Inositol monophosphatase 2
Enzyme 4 Synonyms
  1. IMPase 2
  2. IMP 2
  3. Inositol- 1(or 4-monophosphatase 2
  4. Myo-inositol monophosphatase A2
Enzyme 4 Gene Name IMPA2
Enzyme 4 Protein Sequence >Inositol monophosphatase 2 
MKPSGEDQAALAAGPWEECFQAAVQLALRAGQIIRKALTEEKRVSTKTSAADLVTETDHL
VEDLIISELRERFPSHRFIAEEAAASGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSI
GFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVLTEIGPKRDP
ATLKLFLSNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIR
EAGGIVIDTSGGPLDLMACRVVAASTREMAMLIAQALQTINYGRDDEK
Enzyme 4 Number of Residues 288
Enzyme 4 Molecular Weight 31321
Enzyme 4 Theoretical pI 6.59
Enzyme 4 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
—
Component
—
Enzyme 4 General Function Carbohydrate transport and metabolism
Enzyme 4 Specific Function Myo-inositol phosphate + H(2)O = myo-inositol + phosphate
Enzyme 4 Pathways
Enzyme 4 Reactions
  • myo-inositol phosphate + H2O = myo-inositol + phosphate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 2406666 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O14732 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name IMPA2_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >867 bp 
ATGAAGCCGAGCGGCGAGGACCAGGCGGCGCTGGCGGCCGGCCCCTGGGAGGAGTGCTTC
CAGGCGGCCGTGCAGCTGGCGCTGCGGGCAGGACAGATCATCAGAAAAGCCCTTACTGAG
GAAAAACGTGTCTCAACAAAAACATCAGCTGCAGATCTTGTGACAGAAACAGATCACCTT
GTGGAAGATTTAATTATTTCTGAGTTGCGAGAGAGGTTTCCTTCACACAGGTTCATTGCA
GAAGAGGCCGCGGCTTCTGGGGCCAAGTGTGTGCTCACCCACAGCCCGACGTGGATCATC
GACCCCATCGACGGCACCTGCAATTTTGTGCACAGATTCCCGACTGTGGCGGTTAGCATT
GGATTTGCTGTTCGACAAGAGCTTGAATTCGGAGTGATTTACCACTGCACAGAGGAGCGG
CTGTACACGGGCCGGCGGGGTCGGGGCGCCTTCTGCAATGGCCAGCGGCTCCGGGTCTCC
GGGGAGACAGATCTCTCAAAGGCCTTGGTTCTGACAGAAATTGGCCCCAAACGTGACCCT
GCGACCCTGAAGCTGTTCCTGAGTAACATGGAGCGGCTGCTGCATGCCAAGGCGCATGGG
GTCCGAGTGATTGGAAGCTCCACATTGGCACTCTGCCACCTGGCCTCAGGGGCCGCGGAT
GCCTATTACCAGTTTGGCCTGCACTGCTGGGATCTGGCGGCTGCCACAGTCATCATCAGA
GAAGCAGGCGGCATCGTGATAGACACTTCGGGTGGACCCCTCGACCTCATGGCTTGCAGA
GTGGTTGCGGCCAGCACCCGGGAGATGGCGATGCTCATAGCTCAGGCCTTACAGACCATT
AACTATGGGCGGGATGATGAGAAGTGA
Enzyme 4 GenBank Gene ID AF014398 Link Image
Enzyme 4 GeneCard ID IMPA2 Link Image
Enzyme 4 GenAtlas ID IMPA2 Link Image
Enzyme 4 HGNC ID HGNC:6051 Link Image
Enzyme 4 Chromosome Location 18
Enzyme 4 Locus 18p11.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Yoshikawa T, Turner G, Esterling LE, Sanders AR, Detera-Wadleigh SD: A novel human myo-inositol monophosphatase gene, IMP.18p, maps to a susceptibility region for bipolar disorder. Mol Psychiatry. 1997 Sep;2(5):393-7. [PubMed Link Image]
  2. Sjoholt G, Gulbrandsen AK, Lovlie R, Berle JO, Molven A, Steen VM: A human myo-inositol monophosphatase gene (IMPA2) localized in a putative susceptibility region for bipolar disorder on chromosome 18p11.2: genomic structure and polymorphism screening in manic-depressive patients. Mol Psychiatry. 2000 Mar;5(2):172-80. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 13064
Enzyme 5 Name MIOX protein
Enzyme 5 Synonyms
  1. Myo-inositol oxygenase, isoform CRA_d
  2. Myo-inositol oxygenase
Enzyme 5 Gene Name MIOX
Enzyme 5 Protein Sequence >MIOX protein 
MKVTVGPDPSLVYRPDVDPEVAKDKASFRNYTSGPLLDRVFTTYKLMHTHQTVDFVRSKH
AQFGGFSYKKMTVMEAVDLLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKVPNLPCP
SPSQTGSTSSGSCTTWGRSWPCSGSPSGLSSATPSPSDAVRRPPWFSATPPSRTTLTSRI
LDTAQSSGCISPTVGSTGSSCPGAMMQVRPLHQVPGPAGRGQAAALLPGAH
Enzyme 5 Number of Residues 231
Enzyme 5 Molecular Weight 24516
Enzyme 5 Theoretical pI 8.23
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 116283362 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q05DJ6 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q05DJ6_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID BC012025 Link Image
Enzyme 5 GeneCard ID Q05DJ6 Link Image
Enzyme 5 GenAtlas ID MIOX Link Image
Enzyme 5 HGNC ID HGNC:14522 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 14455
Enzyme 6 Name Inositol monophosphatase 3
Enzyme 6 Synonyms
  1. IMPase 3
  2. IMP 3
  3. Inositol- 1(or 4-monophosphatase 3
  4. Myo-inositol monophosphatase A3
  5. Inositol monophosphatase domain-containing protein 1
Enzyme 6 Gene Name IMPAD1
Enzyme 6 Protein Sequence >Inositol monophosphatase 3 
MAPMGIRLSPLGVAVFCLLGLGVLYHLYSGFLAGRFSLFGLGGEPGGGAAGPAAAADGGT
VDLREMLAVSVLAAVRGGDEVRRVRESNVLHEKSKGKTREGAEDKMTSGDVLSNRKMFYL
LKTAFPSVQINTEEHVDAADQEVILWDHKIPEDILKEVTTPKEVPAESVTVWIDPLDATQ
EYTEDLRKYVTTMVCVAVNGKPMLGVIHKPFSEYTAWAMVDGGSNVKARSSYNEKTPRIV
VSRSHSGMVKQVALQTFGNQTTIIPAGGAGYKVLALLDVPDKSQEKADLYIHVTYIKKWD
ICAGNAILKALGGHMTTLSGEEISYTGSDGIEGGLLASIRMNHQALVRKLPDLEKTGHK
Enzyme 6 Number of Residues 359
Enzyme 6 Molecular Weight 38682
Enzyme 6 Theoretical pI 6.86
Enzyme 6 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
—
Component
—
Enzyme 6 General Function Inorganic ion transport and metabolism
Enzyme 6 Specific Function Myo-inositol phosphate + H(2)O = myo-inositol + phosphate
Enzyme 6 Pathways
Enzyme 6 Reactions
  • myo-inositol phosphate + H2O = myo-inositol + phosphate [RN:R07343] ALL_REAC R07343 > R01185 R01186 R01187
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-24
Enzyme 6 Transmembrane Regions
  • 13-33
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 7020510 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9NX62 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name IMPA3_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1080 bp 
ATGGCCCCCATGGGCATCCGCCTTTCCCCACTGGGGGTGGCAGTGTTTTGTCTGCTGGGG
CTCGGCGTGCTCTACCACCTCTACTCGGGCTTCTTGGCCGGCCGCTTCAGCCTCTTCGGC
CTGGGCGGCGAGCCTGGCGGCGGCGCGGCGGGGCCCGCGGCCGCGGCCGATGGGGGCACC
GTGGACTTGCGCGAGATGCTGGCTGTGTCAGTGCTGGCCGCAGTCCGCGGCGGCGACGAG
GTGAGGCGCGTCCGCGAGAGCAACGTCCTCCACGAGAAGTCCAAGGGGAAGACGCGCGAG
GGAGCCGAGGACAAGATGACCAGCGGCGACGTGCTGTCCAACCGCAAGATGTTCTACCTG
CTCAAGACCGCCTTCCCCAGCGTCCAGATTAATACTGAGGAACACGTGGATGCAGCTGAT
CAGGAGGTTATCTTGTGGGATCATAAGATTCCTGAGGATATCCTAAAGGAAGTAACTACT
CCTAAAGAGGTACCAGCAGAAAGTGTTACTGTCTGGATTGACCCACTTGATGCTACACAG
GAATATACAGAGGATCTTCGAAAGTACGTCACTACTATGGTGTGTGTGGCTGTAAATGGT
AAACCCATGCTAGGAGTTATACATAAGCCATTTTCCGAATATACAGCTTGGGCAATGGTA
GATGGTGGTTCAAATGTGAAAGCCCGCTCTTCCTACAATGAGAAGACCCCAAGGATCGTT
GTGTCTCGTTCCCATTCAGGGATGGTCAAACAGGTCGCTCTTCAGACTTTTGGAAACCAG
ACTACAATTATCCCAGCTGGTGGTGCTGGTTATAAAGTTTTAGCACTTTTGGATGTGCCT
GATAAGAGTCAAGAAAAAGCTGATTTATACATCCATGTGACATACATCAAAAAGTGGGAT
ATATGTGCTGGTAATGCCATCTTAAAAGCCCTAGGGGGGCATATGACTACCCTGAGTGGT
GAAGAAATCAGTTACACTGGTTCAGACGGCATTGAAGGGGGACTCCTTGCTAGCATCAGA
ATGAACCACCAGGCCCTGGTCAGAAAACTCCCAGATCTAGAAAAGACAGGACATAAATGA
Enzyme 6 GenBank Gene ID AK000428 Link Image
Enzyme 6 GeneCard ID Q9NX62 Link Image
Enzyme 6 GenAtlas ID IMPAD1 Link Image
Enzyme 6 HGNC ID HGNC:26019 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 15204
Enzyme 7 Name cDNA FLJ77674, highly similar to Homo sapiens CDP-diacylglycerol-- inositol 3-phosphatidyltransferase (phosphatidylinositol synthase) (CDIPT), transcript variant 1, mRNA (CDP-diacylglycerol--inositol 3- phosphatidyltransferase (Phosphatidylinositol syntha
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name CDIPT
Enzyme 7 Protein Sequence >cDNA FLJ77674, highly similar to Homo sapiens CDP-diacylglycerol-- inositol 3-phosphatidyltransferase (phosphatidylinositol synthase) (CDIPT), transcript variant 1, mRNA (CDP-diacylglycerol--inositol 3- phosphatidyltransferase (Phosphatidylinositol synthase), isoform CRA_a) 
MPDENIFLFVPNLIGYARIVFAIISFYFMPCCPLTASSFYLLSGLLDAFDGHAARALNQG
TRFGAMLDMLTDRCSTMCLLVNLALLYPGATLFFQISMSLDVASHWLHLHSSVVRGSESH
KMIDLSGNPVLRIYYTSRPALFTLCAGNELFYCLLYLFHFSEGPLVGSVGLFRMGLWVTA
PIALLKSLISVIHLITAARNMAALDAADRAKKK
Enzyme 7 Number of Residues 213
Enzyme 7 Molecular Weight 23539
Enzyme 7 Theoretical pI 8.13
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Lipid transport and metabolism
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function Not Available
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 158254696 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID A8K3L7 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name A8K3L7_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >642 bp 
ATGCCAGACGAAAATATCTTCCTGTTCGTGCCCAACCTCATCGGTTATGCCCGGATTGTC
TTCGCCATCATTTCTTTCTACTTCATGCCCTGCTGCCCCCTCACGGCCTCCTCCTTCTAC
CTGCTCAGCGGCCTGCTGGACGCTTTCGATGGACACGCTGCTCGCGCTCTTAATCAAGGA
ACCCGGTTTGGGGCCATGCTGGACATGCTGACGGACCGCTGCTCCACCATGTGCCTGTTG
GTCAACCTGGCCCTGCTGTACCCTGGAGCCACGCTGTTCTTCCAAATCAGCATGAGTTTG
GATGTGGCCAGTCACTGGCTGCACCTCCACAGTTCTGTGGTCCGAGGCAGTGAGAGTCAC
AAGATGATCGACTTGTCCGGGAATCCGGTGCTTCGGATCTACTACACCTCGAGGCCTGCT
CTGTTCACCTTGTGTGCTGGGAATGAGCTCTTCTACTGCCTCCTCTACCTGTTCCATTTC
TCTGAGGGACCTTTAGTTGGCTCTGTGGGACTGTTCCGGATGGGCCTCTGGGTCACTGCC
CCCATCGCCTTGCTGAAGTCGCTCATCAGCGTCATCCACCTGATCACGGCCGCCCGCAAC
ATGGCTGCCCTGGACGCAGCAGACCGCGCCAAGAAGAAGTGA
Enzyme 7 GenBank Gene ID AK290632 Link Image
Enzyme 7 GeneCard ID A8K3L7 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location 16
Enzyme 7 Locus 16p11.2
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 16514
Enzyme 8 Name cDNA, FLJ93260, Homo sapiens inositol(myo)-1(or 4)-monophosphatase 1 (IMPA1), mRNA (Inositol(Myo)-1(Or 4)-monophosphatase 1, isoform CRA_a)
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name IMPA1
Enzyme 8 Protein Sequence >cDNA, FLJ93260, Homo sapiens inositol(myo)-1(or 4)-monophosphatase 1 (IMPA1), mRNA (Inositol(Myo)-1(Or 4)-monophosphatase 1, isoform CRA_a) 
MADPWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSPVDLVTATDQKVEKMLISSIKE
KYPSHSFIGEESVAAGEKSILTDNPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFG
VVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRTPETVRMVLSNME
KLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTG
GPFDLMSRRVIAANNRILAERIAKEIQVIPLQRDDED
Enzyme 8 Number of Residues 277
Enzyme 8 Molecular Weight 30189
Enzyme 8 Theoretical pI 4.91
Enzyme 8 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
—
Component
—
Enzyme 8 General Function Carbohydrate transport and metabolism
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID B2R733 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name B2R733_HUMAN Link Image
Enzyme 8 PDB ID 1IMB Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AK312823 Link Image
Enzyme 8 GeneCard ID B2R733 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 16515
Enzyme 9 Name Inositol monophosphatase 2 variant 1 (Inositol(Myo)-1(Or 4)-monophosphatase 2, isoform CRA_b)
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name IMPA2
Enzyme 9 Protein Sequence >Inositol monophosphatase 2 variant 1 (Inositol(Myo)-1(Or 4)-monophosphatase 2, isoform CRA_b) 
MKPSGEDQAALAAGPWEECFQAAVQLALRAGQIIRKALTEEKRVSTKTSAADLVTETDHL
VEDLIISELRERFPSHRFIAEEAAASGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSI
GFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVLTEIGPKRDP
ATLKLFLSNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIR
EAGGIVIDTSGGPLDLMACRVVAASTREMAMLIAQALQTINYGRDDEK
Enzyme 9 Number of Residues 288
Enzyme 9 Molecular Weight 31321
Enzyme 9 Theoretical pI 6.59
Enzyme 9 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
—
Component
—
Enzyme 9 General Function Carbohydrate transport and metabolism
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID B0YJ29 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name B0YJ29_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID EF444990 Link Image
Enzyme 9 GeneCard ID B0YJ29 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location 18
Enzyme 9 Locus 18p11.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available