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Human Metabolome Database Version 2.5

 

Showing metabocard for 1D-myo-Inositol 3-phosphate (HMDB06814)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2008-08-12 14:58:54
Update Date 2009-05-05 21:01:14
Accession Number HMDB06814
Secondary Accession Numbers Not Available
Common Name 1D-myo-Inositol 3-phosphate
Description 1D-myo-Inositol 3-phosphate is involved in the inositol phosphate metabolism and the phosphatidylinositol signaling systems. With regards to the inositol phosphate metabolism system, 1D-myo-Inositol 3-phosphate is created from D-myo-Inositol 3,4-bisphosphate by inositol polyphosphate-4-phosphatase (EC:3.1.3.66) and is converted to myo-Inositol by myo-inositol-1(or 4)-monophosphatase (EC:3.1.3.25). Within the phosphatidylinositol signaling system, 1D-myo-Inositol 3-phosphate is created from D-myo-Inositol 3,4-bisphosphate by inositol polyphosphate-4-phosphatase (EC:3.1.3.66) and is converted to myo-Inositol by myo-inositol-1(or 4)-monophosphatase (EC:3.1.3.25).
Synonyms
  1. D-myo-Inositol 3-phosphate
  2. myo-Inositol 3-phosphate
  3. Inositol 3-phosphate
  4. 1D-myo-Inositol 3-monophosphate
  5. D-myo-Inositol 3-monophosphate
  6. myo-Inositol 3-monophosphate
  7. Inositol 3-monophosphate
  8. 1L-myo-Inositol 1-phosphate
  9. L-myo-Inositol 1-phosphate
Chemical IUPAC Name Not Available
Chemical Formula C6H13O9P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Sugar Phosphates
Sub Class
  • Inositol phosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • phosphoric acid ester
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 260.136
Monoisotopic Molecular Weight 260.029724
Isomeric SMILES OC1[C@H](O)[C@H](O)C(OP(O)(O)=O)[C@@H](O)[C@@H]1O
Canonical SMILES OC1C(O)C(O)C(OP(O)(O)=O)C(O)C1O
KEGG Compound ID C04006 Link Image
BioCyc ID Not Available
BiGG ID 42948 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB06814 Link Image
Metagene Link HMDB06814 Link Image
METLIN ID Not Available
PubChem Compound 440194 Link Image
PubChem Substance 6716 Link Image
ChEBI ID 18169 Link Image
CAS Registry Number 2831-74-5
InChI Identifier InChI=1/C6H13O9P/c7-1-2(8)4(10)6(5(11)3(1)9)15-16(12,13)14/h1-11H,(H2,12,13,14)/t1?,2-,3+,4-,5-,6?/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 39.5 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.98 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Inositol Metabolism SMP00011 Link Image map00562 Link Image
Inositol Phosphate Metabolism SMP00462 Link Image map00562 Link Image
General References Not Available
Metabolic Enzymes
  1. Inositol monophosphatase 1
  2. Inositol monophosphatase 2
  3. Type II inositol-3,4-bisphosphate 4-phosphatase
  4. Inositol-3-phosphate synthase 1
  5. Type I inositol-3,4-bisphosphate 4-phosphatase
  6. cDNA, FLJ93260, Homo sapiens inositol(myo)-1(or 4)-monophosphatase 1 (IMPA1), mRNA (Inositol(Myo)-1(Or 4)-monophosphatase 1, isoform CRA_a)
  7. Inositol monophosphatase 2 variant 1 (Inositol(Myo)-1(Or 4)-monophosphatase 2, isoform CRA_b)
Enzyme 1 [top]
Enzyme 1 ID 6145
Enzyme 1 Name Inositol monophosphatase 1
Enzyme 1 Synonyms
  1. IMP 1
  2. IMPase 1
  3. Inositol-1(or 4)-monophosphatase 1
  4. Lithium-sensitive myo-inositol monophosphatase A1
Enzyme 1 Gene Name IMPA1
Enzyme 1 Protein Sequence >Inositol monophosphatase 1 
MADPWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSPVDLVTATDQKVEKMLISSIKE
KYPSHSFIGEESVAAGEKSILTDNPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFG
VVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRTPETVRMVLSNME
KLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTG
GPFDLMSRRVIAANNRILAERIAKEIQVIPLQRDDED
Enzyme 1 Number of Residues 277
Enzyme 1 Molecular Weight 30188.6
Enzyme 1 Theoretical pI 4.91
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
—
Component
—
Enzyme 1 General Function Involved in inositol or phosphatidylinositol phosphatase activity
Enzyme 1 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. Can use myo-inositol monophosphates, myo- inositol-1,3-diphosphate, myo-inositol-1,4-diphosphate, scyllo- inositol-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates
Enzyme 1 Pathways
Enzyme 1 Reactions
  • myo-inositol phosphate + H2O = myo-inositol + phosphate [RN:R07343]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 395340 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P29218 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name IMPA1_HUMAN Link Image
Enzyme 1 PDB ID 1IMB Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >834 bp 
ATGGCTGATCCTTGGCAGGAATGCATGGATTATGCAGTAACTCTAGCAAGACAAGCTGGA
GAGGTAGTTTGTGAAGCTATAAAAAATGAAATGAATGTTATGCTGAAAAGTTCTCCAGTT
GATTTGGTAACTGCTACGGACCAAAAAGTTGAAAAAATGCTTATCTCTTCCATAAAGGAA
AAGTATCCATCTCACAGTTTCATTGGTGAAGAATCTGTGGCAGCTGGGGAAAAAAGTATC
TTAACCGACAACCCCACATGGATCATTGACCCTATTGATGGAACAACTAACTTTGTACAT
AGATTTCCTTTTGTAGCTGTTTCAATTGGCTTTGCTGTAAATAAAAAGATAGAATTTGGA
GTTGTGTACAGTTGTGTGGAAGGCAAGATGTACACTGCCAGAAAAGGAAAAGGGGCCTTT
TGTAATGGTCAAAAACTACAAGTTTCACAACAAGAAGATATTACCAAATCTCTCTTGGTG
ACTGAGTTGGGCTCTTCTAGAACACCAGAGACTGTGAGAATGGTTCTTTCTAATATGGAA
AAGCTTTTTTGCATTCCTGTTCATGGGATCCGGAGTGTTGGAACAGCAGCTGTTAATATG
TGCCTTGTGGCAACTGGCGGAGCAGATGCATATTATGAAATGGGAATTCACTGCTGGGAT
GTTGCAGGAGCTGGCATTATTGTTACTGAAGCTGGTGGCGTGCTAATGGATGTTACAGGT
GGACCATTTGATTTGATGTCACGAAGAGTAATTGCTGCAAATAATAGAATATTAGCAGAA
AGGATAGCTAAAGAAATTCAGGTTATACCTTTGCAACGAGACGACGAAGATTAA
Enzyme 1 GenBank Gene ID X66922 Link Image
Enzyme 1 GeneCard ID IMPA1 Link Image
Enzyme 1 GenAtlas ID IMPA1 Link Image
Enzyme 1 HGNC ID HGNC:6050 Link Image
Enzyme 1 Chromosome Location 8
Enzyme 1 Locus 8q21.13-q21.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. 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 Link Image]
  5. Ohnishi T, Ohba H, Seo KC, Im J, Sato Y, Iwayama Y, Furuichi T, Chung SK, Yoshikawa T: Spatial expression patterns and biochemical properties distinguish a second myo-inositol monophosphatase IMPA2 from IMPA1. J Biol Chem. 2007 Jan 5;282(1):637-46. Epub 2006 Oct 26. [PubMed Link Image]
  6. 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]
  7. Bone R, Frank L, Springer JP, Atack JR: Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis. Biochemistry. 1994 Aug 16;33(32):9468-76. [PubMed Link Image]
  8. Ganzhorn AJ, Lepage P, Pelton PD, Strasser F, Vincendon P, Rondeau JM: The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase. Biochemistry. 1996 Aug 20;35(33):10957-66. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6411
Enzyme 2 Name Inositol monophosphatase 2
Enzyme 2 Synonyms
  1. IMP 2
  2. IMPase 2
  3. Inositol-1(or 4)-monophosphatase 2
  4. Myo-inositol monophosphatase A2
Enzyme 2 Gene Name IMPA2
Enzyme 2 Protein Sequence >Inositol monophosphatase 2 
MKPSGEDQAALAAGPWEECFQAAVQLALRAGQIIRKALTEEKRVSTKTSAADLVTETDHL
VEDLIISELRERFPSHRFIAEEAAASGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSI
GFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVLTEIGPKRDP
ATLKLFLSNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIR
EAGGIVIDTSGGPLDLMACRVVAASTREMAMLIAQALQTINYGRDDEK
Enzyme 2 Number of Residues 288
Enzyme 2 Molecular Weight 31320.5
Enzyme 2 Theoretical pI 6.59
Enzyme 2 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
—
Component
—
Enzyme 2 General Function Involved in inositol or phosphatidylinositol phosphatase activity
Enzyme 2 Specific Function Can use myo-inositol monophosphates, scylloinositol 1,4- diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'- AMP as substrates. Has been implicated as the pharmacological target for lithium Li(+) action in brain
Enzyme 2 Pathways
Enzyme 2 Reactions
  • myo-inositol phosphate + H2O = myo-inositol + phosphate [RN:R07343]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 2406666 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O14732 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name IMPA2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >867 bp 
ATGAAGCCGAGCGGCGAGGACCAGGCGGCGCTGGCGGCCGGCCCCTGGGAGGAGTGCTTC
CAGGCGGCCGTGCAGCTGGCGCTGCGGGCAGGACAGATCATCAGAAAAGCCCTTACTGAG
GAAAAACGTGTCTCAACAAAAACATCAGCTGCAGATCTTGTGACAGAAACAGATCACCTT
GTGGAAGATTTAATTATTTCTGAGTTGCGAGAGAGGTTTCCTTCACACAGGTTCATTGCA
GAAGAGGCCGCGGCTTCTGGGGCCAAGTGTGTGCTCACCCACAGCCCGACGTGGATCATC
GACCCCATCGACGGCACCTGCAATTTTGTGCACAGATTCCCGACTGTGGCGGTTAGCATT
GGATTTGCTGTTCGACAAGAGCTTGAATTCGGAGTGATTTACCACTGCACAGAGGAGCGG
CTGTACACGGGCCGGCGGGGTCGGGGCGCCTTCTGCAATGGCCAGCGGCTCCGGGTCTCC
GGGGAGACAGATCTCTCAAAGGCCTTGGTTCTGACAGAAATTGGCCCCAAACGTGACCCT
GCGACCCTGAAGCTGTTCCTGAGTAACATGGAGCGGCTGCTGCATGCCAAGGCGCATGGG
GTCCGAGTGATTGGAAGCTCCACATTGGCACTCTGCCACCTGGCCTCAGGGGCCGCGGAT
GCCTATTACCAGTTTGGCCTGCACTGCTGGGATCTGGCGGCTGCCACAGTCATCATCAGA
GAAGCAGGCGGCATCGTGATAGACACTTCGGGTGGACCCCTCGACCTCATGGCTTGCAGA
GTGGTTGCGGCCAGCACCCGGGAGATGGCGATGCTCATAGCTCAGGCCTTACAGACCATT
AACTATGGGCGGGATGATGAGAAGTGA
Enzyme 2 GenBank Gene ID AF014398 Link Image
Enzyme 2 GeneCard ID IMPA2 Link Image
Enzyme 2 GenAtlas ID IMPA2 Link Image
Enzyme 2 HGNC ID HGNC:6051 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 18p11.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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]
  3. 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 Link Image]
  4. Seelan RS, Parthasarathy LK, Parthasarathy RN: Lithium modulation of the human inositol monophosphatase 2 (IMPA2) promoter. Biochem Biophys Res Commun. 2004 Nov 26;324(4):1370-8. [PubMed Link Image]
  5. Ohnishi T, Ohba H, Seo KC, Im J, Sato Y, Iwayama Y, Furuichi T, Chung SK, Yoshikawa T: Spatial expression patterns and biochemical properties distinguish a second myo-inositol monophosphatase IMPA2 from IMPA1. J Biol Chem. 2007 Jan 5;282(1):637-46. Epub 2006 Oct 26. [PubMed Link Image]
  6. Arai R, Ito K, Ohnishi T, Ohba H, Akasaka R, Bessho Y, Hanawa-Suetsugu K, Yoshikawa T, Shirouzu M, Yokoyama S: Crystal structure of human myo-inositol monophosphatase 2, the product of the putative susceptibility gene for bipolar disorder, schizophrenia, and febrile seizures. Proteins. 2007 May 15;67(3):732-42. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 8851
Enzyme 3 Name Type II inositol-3,4-bisphosphate 4-phosphatase
Enzyme 3 Synonyms
  1. Inositol polyphosphate 4-phosphatase type II
Enzyme 3 Gene Name INPP4B
Enzyme 3 Protein Sequence >Type II inositol-3,4-bisphosphate 4-phosphatase 
MEIKEEGASEEGQHFLPTAQANDPGDCQFTSIQKTPNEPQLEFILACKDLVAPVRDRKLN
TLVQISVIHPVEQSLTRYSSTEIVEGTRDPLFLTGVTFPSEYPIYEETKIKLTVYDVKDK
SHDTVRTSVLPEHKDPPPEVGRSFLGYASFKVGELLKSKEQLLVLSLRTSDGGKVVGTIE
VSVVKMGEIEDGEADHITTDVQGQKCALVCECTAPESVSGKDNLPFLNSVLKNPVCKLYR
FPTSDNKWMRIREQMSESILSFHIPKELISLHIKEDLCRNQEIKELGELSPHWDNLRKNV
LTHCDQMVNMYQDILTELSKETGSSFKSSSSKGEKTLEFVPINLHLQRMQVHSPHLKDAL
YDVITVGAPAAHFQGFKNGGLRKLLHRFETERRNTGYQFIYYSPENTAKAKEVLSNINQL
QPLIATHADLLLNSASQHSPDSLKNSLKMLSEKTELFVHAFKDQLVRSALLALYTARPGG
ILKKPPSPKSSTEESSPQDQPPVMRGQDSIPHHSDYDEEEWDRVWANVGKSLNCIIAMVD
KLIERDGGSEGSGGNNDGEKEPSLTDAIPSHPREDWYEQLYPLILTLKDCMGEVVNRAKQ
SLTFVLLQELAYSLPQCLMLTLRRDIVFSQALAGLVCGFIIKLQTSLYDPGFLQQLHTVG
LIVQYEGLLSTYSDEIGMLEDMAVGISDLKKVAFKIIEAKSNDVLPVITGRREHYVVEVK
LPARMFESLPLQIKEGQLLHVYPVLFNVGINEQQTLAERFGDVSLQESINQENFELLQEY
YKIFMEKMPPDYISHFQEQNDLKALLENLLQNIQSKKRKNVEIMWLAATICRKLNGIRFT
CCKSAKDRTSMSVTLEQCSILRDEHQLHKDFFIRALDCMRREGCRIENVLKNIKCRKYAF
NMLQLMAFPKYYRPPEGTYGKADT
Enzyme 3 Number of Residues 924
Enzyme 3 Molecular Weight 104737.1
Enzyme 3 Theoretical pI 6.20
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Involved in phosphatidyl-inositol-4,5-bisphosphate 4-ph
Enzyme 3 Specific Function Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4- trisphosphate and inositol 1,4-bisphosphate
Enzyme 3 Pathways
Enzyme 3 Reactions
  • 1-phosphatidyl-myo-inositol 3,4-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate [RN:R07299]
Enzyme 3 Pfam Domain Function Not Available
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 156104897 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O15327 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name INP4B_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2775 bp 
ATGGAAATTAAAGAGGAAGGGGCATCAGAAGAAGGGCAGCACTTTCTTCCTACAGCCCAG
GCCAATGATCCCGGGGACTGTCAGTTCACAAGTATCCAGAAGACTCCAAATGAACCGCAG
TTGGAATTCATCCTTGCATGCAAGGATCTCGTGGCTCCTGTCCGTGATCGTAAACTGAAT
ACACTGGTGCAGATCTCCGTAATCCACCCCGTGGAGCAGAGTCTGACAAGATACTCCAGC
ACCGAAATTGTGGAGGGAACAAGGGACCCACTGTTTTTGACTGGTGTCACATTCCCATCT
GAGTATCCCATCTATGAGGAGACCAAAATAAAACTAACAGTCTATGATGTCAAGGATAAG
TCTCATGACACCGTTCGAACCAGTGTCCTACCAGAACATAAGGATCCCCCGCCAGAAGTT
GGGCGAAGTTTCTTGGGCTATGCCAGTTTTAAAGTGGGAGAGCTGCTGAAGTCAAAGGAG
CAATTGCTGGTCCTGAGCCTGAGAACTTCAGATGGTGGCAAAGTGGTTGGCACCATAGAA
GTCAGTGTCGTGAAGATGGGGGAGATTGAGGATGGGGAAGCCGACCACATCACCACAGAT
GTACAGGGACAAAAGTGTGCCCTGGTATGTGAATGTACAGCCCCGGAAAGTGTGAGCGGA
AAAGATAACTTACCTTTTTTGAATTCAGTGTTAAAGAACCCAGTATGTAAATTATATAGA
TTTCCCACATCTGACAATAAGTGGATGCGAATTCGAGAGCAGATGTCAGAGAGCATTCTT
TCCTTTCATATTCCTAAGGAATTGATTTCCCTTCACATTAAAGAAGATTTGTGCAGAAAC
CAGGAGATAAAAGAACTTGGTGAGCTTTCTCCACATTGGGACAATCTGCGAAAAAATGTC
CTTACTCACTGTGATCAAATGGTGAATATGTACCAAGACATTCTGACAGAACTTAGCAAG
GAAACAGGGTCCTCTTTCAAATCAAGCAGCAGCAAAGGAGAGAAAACATTAGAATTTGTT
CCAATAAATCTACATCTGCAAAGAATGCAGGTACACAGCCCTCACTTGAAAGATGCTCTC
TACGATGTCATCACTGTGGGAGCCCCAGCTGCCCATTTTCAGGGATTTAAGAATGGTGGT
CTTCGGAAGCTACTCCATAGATTTGAAACAGAAAGAAGAAATACCGGATACCAGTTTATT
TACTATTCACCTGAAAACACAGCCAAAGCAAAGGAAGTTCTCAGCAACATCAATCAACTA
CAACCTCTTATAGCAACCCATGCAGACCTACTGCTTAATTCTGCAAGCCAGCATTCTCCA
GACAGCTTGAAGAATTCTTTAAAGATGCTTTCAGAAAAAACAGAGCTTTTTGTACATGCC
TTCAAGGATCAACTTGTCAGGAGTGCTCTTTTAGCACTCTACACTGCAAGGCCAGGAGGC
ATTCTTAAGAAGCCACCCTCTCCTAAGAGCAGCACAGAGGAGAGCAGTCCCCAAGACCAA
CCCCCAGTGATGAGAGGGCAGGACTCCATACCACATCATTCAGACTATGATGAGGAAGAG
TGGGACAGGGTGTGGGCCAATGTGGGGAAGAGCCTGAACTGCATTATTGCTATGGTGGAC
AAACTGATTGAAAGAGATGGTGGCAGTGAAGGCAGTGGCGGCAACAATGATGGAGAAAAG
GAACCTTCATTAACAGATGCCATTCCCTCTCACCCAAGAGAGGACTGGTATGAACAGTTG
TATCCCCTCATCCTTACCCTGAAGGACTGCATGGGAGAAGTGGTGAACCGAGCCAAGCAG
TCCCTGACATTTGTGCTCCTTCAGGAACTTGCGTACAGCTTGCCCCAGTGTCTGATGCTG
ACGCTAAGAAGAGACATCGTCTTCAGCCAAGCACTTGCTGGATTGGTTTGTGGTTTTATC
ATCAAATTACAGACAAGTCTGTATGACCCAGGCTTCCTACAGCAGCTTCACACAGTGGGG
TTGATAGTACAATATGAAGGACTGCTAAGTACATACAGCGATGAAATTGGAATGCTAGAG
GACATGGCCGTTGGCATTTCCGATTTAAAGAAAGTTGCATTTAAAATAATTGAAGCCAAA
TCCAATGATGTGTTGCCAGTTATAACAGGAAGACGAGAACATTACGTGGTAGAGGTCAAG
CTTCCAGCCAGAATGTTTGAGTCACTACCTCTACAGATTAAAGAAGGACAGTTGCTTCAT
GTGTATCCAGTACTTTTTAATGTTGGAATCAATGAACAGCAAACTCTGGCTGAAAGGTTT
GGAGATGTCTCTTTGCAAGAAAGTATTAATCAGGAAAACTTCGAACTTCTACAAGAATAT
TACAAGATATTTATGGAAAAGATGCCTCCTGATTATATTTCACATTTTCAGGAACAAAAT
GATTTAAAAGCATTGCTAGAAAATCTCCTTCAAAATATCCAATCCAAAAAAAGAAAGAAT
GTAGAAATTATGTGGCTGGCTGCAACGATTTGCCGCAAACTGAATGGTATTCGTTTCACC
TGTTGTAAAAGTGCCAAAGACAGGACATCGATGTCAGTGACACTTGAACAATGCTCAATC
TTGAGAGATGAGCACCAGTTACACAAGGACTTCTTTATCCGAGCGCTGGATTGCATGAGA
AGAGAAGGATGCCGCATAGAGAATGTACTGAAGAATATCAAATGCAGAAAGTATGCTTTC
AACATGCTACAGCTGATGGCTTTCCCCAAGTACTACAGACCTCCAGAGGGGACTTATGGA
AAAGCTGACACCTAA
Enzyme 3 GenBank Gene ID NM_001101669.1 Link Image
Enzyme 3 GeneCard ID INPP4B Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location 4
Enzyme 3 Locus 4q31.21
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Norris FA, Atkins RC, Majerus PW: The cDNA cloning and characterization of inositol polyphosphate 4-phosphatase type II. Evidence for conserved alternative splicing in the 4-phosphatase family. J Biol Chem. 1997 Sep 19;272(38):23859-64. [PubMed Link Image]
  2. 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 Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 11503
Enzyme 4 Name Inositol-3-phosphate synthase 1
Enzyme 4 Synonyms
  1. IPS 1
  2. Myo-inositol 1-phosphate synthase A1
  3. hINO1
  4. Myo-inositol-1-phosphate synthase
  5. MI-1-P synthase
  6. MIP synthase
  7. hIPS
Enzyme 4 Gene Name ISYNA1
Enzyme 4 Protein Sequence >Inositol-3-phosphate synthase 1 
MEAAAQFFVESPDVVYGPEAIEAQYEYRTTRVSREGGVLKVHPTSTRFTFRTARQVPRLG
VMLVGWGGNNGSTLTAAVLANRLRLSWPTRSGRKEANYYGSLTQAGTVSLGLDAEGQEVF
VPFSAVLPMVAPNDLVFDGWDISSLNLAEAMRRAKVLDWGLQEQLWPHMEALRPRPSVYI
PEFIAANQSARADNLIPGSRAQQLEQIRRDIRDFRSSAGLDKVIVLWTANTERFCEVIPG
LNDTAENLLRTIELGLEVSPSTLFAVASILEGCAFLNGSPQNTLVPGALELAWQHRVFVG
GDDFKSGQTKVKSVLVDFLIGSGLKTMSIVSYNHLGNNDGENLSAPLQFRSKEVSKSNVV
DDMVQSNPVLYTPGEEPDHCVVIKYVPYVGDSKRALDEYTSELMLGGTNTLVLHNTCEDS
LLAAPIMLDLALLTELCQRVSFCTDMDPEPQTFHPVLSLLSFLFKAPLVPPGSPVVNALF
RQRSCIENILRACVGLPPQNHMLLEHKMERPGPSLKRVGPVAATYPMLNKKGPVPAATNG
CTGDANGHLQEEPPMPTT
Enzyme 4 Number of Residues 558
Enzyme 4 Molecular Weight 61067.3
Enzyme 4 Theoretical pI 5.51
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • inositol-3-phosphate synthase activity
  • intramolecular lyase activity
  • isomerase activity
Process
  • alcohol metabolic process
  • inositol biosynthetic process
  • inositol metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid biosynthetic process
  • phospholipid metabolic process
  • polyol metabolic process
  • small molecule metabolic process
Component
—
Enzyme 4 General Function Involved in inositol-3-phosphate synthase activity
Enzyme 4 Specific Function Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the synthesis of all inositol-containing compounds
Enzyme 4 Pathways
Enzyme 4 Reactions
  • D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate [RN:R07324]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 7705558 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9NPH2 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name INO1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1677 bp 
ATGGAGGCCGCCGCCCAGTTCTTCGTCGAGAGCCCGGACGTGGTCTACGGCCCCGAGGCC
ATCGAGGCGCAATACGAGTACCGGACGACGCGCGTCAGCCGCGAGGGTGGCGTTCTCAAG
GTGCACCCCACGTCCACGCGCTTCACCTTCCGGACCGCCCGGCAGGTGCCCCGGCTCGGG
GTCATGCTTGTCGGCTGGGGCGGGAACAACGGCTCCACACTCACCGCCGCGGTGCTGGCC
AATCGACTGCGTTTGTCCTGGCCCACGCGCAGCGGCCGCAAGGAGGCCAACTACTACGGC
TCGCTGACTCAGGCGGGCACCGTGAGCCTGGGCCTGGACGCCGAGGGCCAGGAGGTGTTC
GTACCCTTCAGCGCGGTGCTGCCCATGGTGGCGCCCAACGACCTCGTGTTCGATGGCTGG
GACATCTCGTCGCTGAACCTGGCCGAGGCGATGCGGCGCGCGAAGGTGCTGGACTGGGGG
CTGCAGGAGCAACTGTGGCCGCACATGGAGGCCCTGCGGCCCCGGCCTTCTGTTTACATC
CCCGAATTCATCGCGGCCAACCAGAGCGCGCGCGCGGACAACCTCATCCCAGGCTCGCGT
GCGCAGCAGCTGGAGCAGATCCGCAGGGACATCCGAGACTTCCGGTCTAGCGCGGGGCTG
GACAAAGTCATAGTGCTGTGGACGGCGAACACGGAGCGCTTCTGTGAGGTGATTCCAGGC
CTCAACGACACAGCCGAGAACCTGCTGCGCACCATTGAGCTCGGTCTGGAGGTGTCGCCC
TCCACGCTCTTCGCCGTGGCCAGCATCCTGGAGGGCTGTGCCTTCCTCAATGGGTCTCCG
CAGAACACCCTGGTGCCCGGAGCTCTTGAGCTCGCGTGGCAGCACCGGGTTTTTGTGGGC
GGAGATGACTTCAAGTCAGGCCAGACCAAAGTCAAGTCCGTGCTTGTGGACTTCCTCATT
GGCTCCGGCCTCAAGACCATGTCCATCGTGAGTTACAACCACCTGGGCAACAACGATGGG
GAGAACCTATCGGCGCCATTGCAGTTCCGCTCTAAGGAGGTGTCCAAGAGCAACGTGGTG
GACGACATGGTGCAGAGCAACCCAGTGCTCTATACGCCCGGCGAAGAGCCTGACCACTGC
GTGGTCATCAAGTATGTGCCGTACGTGGGTGACAGCAAGCGCGCGCTGGATGAGTATACC
TCGGAGCTGATGCTGGGCGGAACCAACACACTGGTGCTGCACAACACGTGTGAGGACTCG
CTGCTGGCCGCACCCATCATGCTGGACCTAGCGCTGCTGACCGAGCTGTGCCAGCGCGTG
AGCTTCTGCACTGACATGGACCCCGAGCCGCAGACCTTCCACCCCGTGCTGTCCCTGCTC
AGCTTCCTCTTCAAGGCGCCACTAGTGCCGCCCGGCAGCCCGGTGGTCAATGCGCTTTTC
CGCCAGCGCAGCTGCATCGAGAACATCCTCAGGGCCTGCGTGGGGCTCCCGCCACAGAAC
CACATGCTCCTGGAACACAAAATGGAGCGCCCAGGGCCCAGCCTCAAGCGAGTTGGACCC
GTGGCTGCCACCTACCCTATGTTGAACAAGAAAGGACCGGTACCCGCTGCCACCAATGGC
TGCACCGGTGATGCCAATGGGCATCTGCAAGAGGAGCCCCCAATGCCCACCACCTGA
Enzyme 4 GenBank Gene ID NM_016368.4 Link Image
Enzyme 4 GeneCard ID ISYNA1 Link Image
Enzyme 4 GenAtlas ID ISYNA1 Link Image
Enzyme 4 HGNC ID HGNC:29821 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 19p13.11
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Guan G, Dai P, Shechter I: cDNA cloning and gene expression analysis of human myo-inositol 1-phosphate synthase. Arch Biochem Biophys. 2003 Sep 15;417(2):251-9. [PubMed Link Image]
  2. Parthasarathy LK, Seelan RS, Tobias C, Casanova MF, Parthasarathy RN: Mammalian inositol 3-phosphate synthase: its role in the biosynthesis of brain inositol and its clinical use as a psychoactive agent. Subcell Biochem. 2006;39:293-314. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. 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 Link Image]
  6. Seelan RS, Parthasarathy LK, Parthasarathy RN: E2F1 regulation of the human myo-inositol 1-phosphate synthase (ISYNA1) gene promoter. Arch Biochem Biophys. 2004 Nov 1;431(1):95-106. [PubMed Link Image]
  7. Ju S, Shaltiel G, Shamir A, Agam G, Greenberg ML: Human 1-D-myo-inositol-3-phosphate synthase is functional in yeast. J Biol Chem. 2004 May 21;279(21):21759-65. Epub 2004 Mar 15. [PubMed Link Image]
  8. Shamir A, Shaltiel G, Mark S, Bersudsky Y, Belmaker RH, Agam G: Human MIP synthase splice variants in bipolar disorder. Bipolar Disord. 2007 Nov;9(7):766-71. [PubMed Link Image]
  9. Shaltiel G, Mark S, Kofman O, Belmaker RH, Agam G: Effect of valproate derivatives on human brain myo-inositol-1-phosphate (MIP) synthase activity and amphetamine-induced rearing. Pharmacol Rep. 2007 Jul-Aug;59(4):402-7. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 11758
Enzyme 5 Name Type I inositol-3,4-bisphosphate 4-phosphatase
Enzyme 5 Synonyms
  1. Inositol polyphosphate 4-phosphatase type I
Enzyme 5 Gene Name INPP4A
Enzyme 5 Protein Sequence >Type I inositol-3,4-bisphosphate 4-phosphatase 
MTAREHSPRHGARARAMQRASTIDVAADMLGLSLAGNIQDPDEPILEFSLACSELHTPSL
DRKPNSFVAVSVTTPPQAFWTKHAQTEIIEGTNNPIFLSSIAFFQDSLINQMTQVKLSVY
DVKDRSQGTMYLLGSGTFIVKDLLQDRHHRLHLTLRSAESDRVGNITVIGWQMEEKSDQR
PPVTRSVDTVNGRMVLPVDESLTEALGIRSKYASLRKDTLLKSVFGGAICRMYRFPTTDG
NHLRILEQMAESVLSLHVPRQFVKLLLEEDAARVCELEELGELSPCWESLRRQIVTQYQT
IILTYQENLTDLHQYRGPSFKASSLKADKKLEFVPTNLHIQRMRVQDDGGSDQNYDIVTI
GAPAAHCQGFKSGGLRKKLHKFEETKKHFEECCTSSGCQSIIYIPQDVVRAKEIIAQINT
LKTQVSYYAERLSRAAKDRSATGLERTLAILADKTRQLVTVCDCKLLANSIHGLNAARPD
YIASKASPTSTEEEQVMLRNDQDTLMARWTGRNSRSSLQVDWHEEEWEKVWLNVDKSLEC
IIQRVDKLLQKERLHGEGCEDVFPCAGSCTSKKGNPDSHAYWIRPEDPFCDVPSSPCPST
MPSTACHPHLTTHCSPPPEESSPGEWSEALYPLLTTLTDCVAMMSDKAKKAMVFLLMQDS
APTIATYLSLQYRRDVVFCQTLTALICGFIIKLRNCLHDDGFLRQLYTIGLLAQFESLLS
TYGEELAMLEDMSLGIMDLRNVTFKVTQATSSASADMLPVITGNRDGFNVRVPLPGPLFD
ALPREIQSGMLLRVQPVLFNVGINEQQTLAERFGDTSLQEVINVESLVRLNSYFEQFKEV
LPEDCLPRSRSQTCLPELLRFLGQNVHARKNKNVDILWQAAEICRRLNGVRFTSCKSAKD
RTAMSVTLEQCLILQHEHGMAPQVFTQALECMRSEGCRRENTMKNVGSRKYAFNSLQLKA
FPKHYRPPEGTYGKVET
Enzyme 5 Number of Residues 977
Enzyme 5 Molecular Weight 109954.7
Enzyme 5 Theoretical pI 6.96
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Involved in phosphatidyl-inositol-4,5-bisphosphate 4-ph
Enzyme 5 Specific Function Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4- trisphosphate and inositol 3,4-bisphosphate
Enzyme 5 Pathways
Enzyme 5 Reactions
  • 1-phosphatidyl-myo-inositol 3,4-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate [RN:R07299]
Enzyme 5 Pfam Domain Function Not Available
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 197116359 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q96PE3 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name INP4A_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2934 bp 
ATGACAGCAAGAGAGCACAGCCCTCGCCATGGTGCCAGGGCCCGTGCAATGCAGCGGGCT
TCCACCATCGACGTGGCGGCCGACATGCTGGGCCTCTCTCTGGCAGGAAATATACAAGAC
CCAGATGAGCCCATTTTAGAATTTAGCTTAGCTTGCAGTGAGCTGCATACTCCATCGCTA
GATCGAAAGCCAAATAGTTTTGTTGCGGTGAGTGTCACCACCCCTCCTCAGGCATTCTGG
ACGAAGCATGCACAGACGGAGATCATTGAGGGAACCAACAATCCTATATTTCTAAGCAGT
ATTGCCTTCTTTCAAGACTCTCTTATCAATCAGATGACACAAGTCAAACTCTCCGTGTAT
GATGTCAAAGATAGATCTCAGGGAACAATGTATTTACTGGGCTCTGGAACGTTCATTGTC
AAAGATCTGCTCCAGGACAGGCATCATAGGTTGCATTTAACACTAAGGTCTGCAGAGAGT
GACCGTGTAGGTAACATCACCGTGATTGGCTGGCAGATGGAGGAGAAGTCAGACCAACGG
CCCCCTGTGACCCGGTCTGTGGACACTGTCAATGGGAGGATGGTTCTTCCTGTCGATGAG
AGCTTGACGGAGGCGTTAGGAATCCGATCCAAATACGCTTCATTGCGAAAGGACACTTTG
CTGAAATCGGTGTTCGGTGGTGCCATCTGCCGCATGTACCGGTTTCCAACCACTGATGGT
AACCATTTGCGGATCCTGGAGCAGATGGCAGAGAGCGTGCTCTCCCTGCACGTGCCCCGG
CAGTTCGTGAAGCTCCTACTAGAGGAAGATGCAGCCAGAGTGTGTGAGCTGGAGGAGCTG
GGAGAGCTGTCCCCTTGCTGGGAGAGCCTCCGGCGCCAAATTGTCACCCAGTACCAGACC
ATCATCCTCACATACCAGGAGAACCTGACCGACCTCCATCAGTACAGAGGGCCCTCGTTT
AAAGCAAGCAGTTTGAAAGCAGATAAAAAGTTAGAATTTGTTCCCACAAACTTGCACATA
CAAAGGATGAGAGTTCAAGACGATGGAGGATCAGATCAGAACTACGACATCGTCACCATT
GGGGCGCCAGCAGCACACTGCCAAGGTTTTAAGTCAGGAGGTCTCCGCAAAAAGCTGCAC
AAATTTGAAGAGACCAAGAAACATTTTGAGGAGTGTTGTACATCATCTGGCTGCCAGTCC
ATAATCTACATACCCCAGGATGTTGTCAGAGCCAAGGAGATCATCGCCCAGATCAACACC
CTGAAAACCCAAGTGAGTTACTACGCAGAGCGGCTGTCAAGGGCAGCCAAGGACAGGTCT
GCCACTGGCCTTGAGAGGACACTCGCCATCTTGGCAGACAAGACACGGCAGCTGGTCACG
GTCTGCGACTGCAAGCTCCTGGCCAACTCCATCCATGGGCTGAACGCTGCACGGCCTGAC
TACATTGCCTCCAAGGCCTCTCCCACTTCGACTGAGGAGGAGCAGGTGATGCTTAGAAAT
GACCAGGACACCCTCATGGCCCGGTGGACAGGGAGAAACAGCCGATCTTCCCTGCAGGTG
GACTGGCACGAGGAGGAGTGGGAGAAAGTGTGGCTGAACGTGGACAAGAGCCTAGAGTGC
ATCATTCAGCGTGTGGACAAGCTGCTGCAGAAGGAGCGGCTGCATGGCGAGGGCTGTGAG
GATGTCTTCCCCTGTGCAGGCAGCTGCACCAGCAAGAAAGGTAACCCGGACAGCCACGCC
TACTGGATCAGACCAGAAGACCCCTTCTGTGATGTCCCCTCCTCACCATGCCCCTCCACC
ATGCCCTCCACTGCATGCCATCCTCATCTGACCACACATTGCAGTCCCCCTCCTGAAGAG
TCCAGCCCAGGTGAATGGAGTGAGGCCCTTTACCCGCTGCTGACCACTCTCACCGACTGC
GTGGCCATGATGAGTGACAAGGCCAAGAAGGCCATGGTATTCCTGCTCATGCAGGACAGC
GCGCCCACCATAGCCACCTACCTGAGCCTGCAGTACCGCCGTGACGTGGTCTTCTGCCAG
ACGCTGACCGCCCTCATCTGCGGCTTCATCATTAAGCTGAGGAACTGCCTGCATGACGAC
GGCTTCCTGCGCCAGCTCTACACCATCGGGCTGCTGGCCCAGTTCGAGAGCCTGCTGAGC
ACCTACGGGGAGGAGCTGGCAATGCTGGAGGACATGAGCCTTGGGATCATGGACTTGAGG
AACGTGACCTTCAAAGTCACTCAGGCCACTTCCAGCGCCTCCGCAGACATGCTGCCCGTC
ATCACAGGAAATCGCGACGGGTTTAACGTGCGGGTCCCTCTGCCGGGCCCGCTGTTTGAC
GCCTTGCCCCGGGAGATCCAGAGTGGCATGCTGCTGCGAGTGCAGCCCGTCCTCTTCAAC
GTGGGCATCAATGAGCAGCAGACACTGGCCGAGAGGTTTGGCGATACGTCTTTACAAGAA
GTCATCAACGTGGAGAGTTTGGTGCGGTTAAATTCCTACTTTGAGCAGTTTAAGGAAGTT
TTGCCTGAGGATTGCCTGCCTCGGTCTCGCAGTCAGACGTGCCTGCCAGAGCTGCTGCGG
TTTCTGGGTCAGAACGTGCATGCCCGGAAGAATAAGAACGTCGACATTCTCTGGCAAGCT
GCTGAGATCTGCCGCCGCCTTAATGGGGTCCGGTTCACCAGCTGCAAGAGCGCTAAGGAC
CGTACAGCCATGTCGGTGACACTGGAGCAGTGCCTGATCCTGCAACACGAGCATGGCATG
GCCCCGCAGGTCTTCACCCAGGCCCTGGAGTGCATGCGCAGTGAGGGTTGTCGAAGAGAA
AATACAATGAAGAATGTTGGAAGTCGCAAATATGCATTTAATTCCCTGCAGCTGAAGGCT
TTCCCCAAGCATTACAGGCCTCCCGAAGGGACTTACGGAAAAGTTGAAACGTGA
Enzyme 5 GenBank Gene ID NM_001134224.1 Link Image
Enzyme 5 GeneCard ID INPP4A Link Image
Enzyme 5 GenAtlas ID INPP4A Link Image
Enzyme 5 HGNC ID HGNC:6074 Link Image
Enzyme 5 Chromosome Location 2
Enzyme 5 Locus 2q11.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Norris FA, Auethavekiat V, Majerus PW: The isolation and characterization of cDNA encoding human and rat brain inositol polyphosphate 4-phosphatase. J Biol Chem. 1995 Jul 7;270(27):16128-33. [PubMed Link Image]
  2. Norris FA, Atkins RC, Majerus PW: The cDNA cloning and characterization of inositol polyphosphate 4-phosphatase type II. Evidence for conserved alternative splicing in the 4-phosphatase family. J Biol Chem. 1997 Sep 19;272(38):23859-64. [PubMed Link Image]
  3. Shearn CT, Walker J, Norris FA: Identification of a novel spliceoform of inositol polyphosphate 4-phosphatase type Ialpha expressed in human platelets: structure of human inositol polyphosphate 4-phosphatase type I gene. Biochem Biophys Res Commun. 2001 Aug 10;286(1):119-25. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. 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 Link Image]
  6. 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. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 16514
Enzyme 6 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 6 Synonyms Not Available
Enzyme 6 Gene Name IMPA1
Enzyme 6 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 6 Number of Residues 277
Enzyme 6 Molecular Weight 30189
Enzyme 6 Theoretical pI 4.91
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 Carbohydrate transport and metabolism
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID B2R733 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name B2R733_HUMAN Link Image
Enzyme 6 PDB ID 1IMB Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID AK312823 Link Image
Enzyme 6 GeneCard ID B2R733 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
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 16515
Enzyme 7 Name Inositol monophosphatase 2 variant 1 (Inositol(Myo)-1(Or 4)-monophosphatase 2, isoform CRA_b)
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name IMPA2
Enzyme 7 Protein Sequence >Inositol monophosphatase 2 variant 1 (Inositol(Myo)-1(Or 4)-monophosphatase 2, isoform CRA_b) 
MKPSGEDQAALAAGPWEECFQAAVQLALRAGQIIRKALTEEKRVSTKTSAADLVTETDHL
VEDLIISELRERFPSHRFIAEEAAASGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSI
GFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVLTEIGPKRDP
ATLKLFLSNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIR
EAGGIVIDTSGGPLDLMACRVVAASTREMAMLIAQALQTINYGRDDEK
Enzyme 7 Number of Residues 288
Enzyme 7 Molecular Weight 31321
Enzyme 7 Theoretical pI 6.59
Enzyme 7 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 7 General Function Carbohydrate transport and metabolism
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID B0YJ29 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name B0YJ29_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID EF444990 Link Image
Enzyme 7 GeneCard ID B0YJ29 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location 18
Enzyme 7 Locus 18p11.2
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available