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 1D-Myo-inositol 3,4-bisphosphate (HMDB06235)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2007-05-22 19:41:52
Update Date 2009-05-05 21:00:52
Accession Number HMDB06235
Secondary Accession Numbers Not Available
Common Name 1D-Myo-inositol 3,4-bisphosphate
Description 1D-myo-Inositol 3,4-bisphosphate is an intermediate in inositol phosphate metabolism. 1D-myo-Inositol 3,4-bisphosphate is converted from 1D-myo-inositol-3-phosphate via inositol polyphosphate-4-phosphatase [EC:3.1.3.66].
Synonyms
  1. 1D-myo-inositol 3,4-bis(dihydrogen phosphate)
  2. D-myo-Inositol 3,4-bisphosphate
  3. Inositol 3,4-bisphosphate
Chemical IUPAC Name [(1S,2R,3S,4S,5S,6S)-2,3,4,5-tetrahydroxy-6-phosphonooxy-cyclohexyl]oxyphosphonic acid
Chemical Formula C6H14O12P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Alcohol Phosphates
Sub Class
  • Inositol phosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • phosphoric acid ester
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 340.116
Monoisotopic Molecular Weight 339.996063
Isomeric SMILES O[C@H]1[C@H](O)[C@@H](O)[C@H](OP(O)(O)=O)[C@@H](OP(O)(O)=O)[C@H]1O
Canonical SMILES OC1C(O)C(O)C(OP(O)(O)=O)C(OP(O)(O)=O)C1O
KEGG Compound ID C04063 Link Image
BioCyc ID PHOSPHATIDYLINOSITOL-345-TRIPHOSPHATE Link Image
BiGG ID 43066 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB06235 Link Image
Metagene Link HMDB06235 Link Image
METLIN ID Not Available
PubChem Compound 440211 Link Image
PubChem Substance 10298560 Link Image
ChEBI ID 28858 Link Image
CAS Registry Number 103597-56-4
InChI Identifier InChI=1/C6H14O12P2/c7-1-2(8)4(10)6(18-20(14,15)16)5(3(1)9)17-19(11,12)13/h1-10H,(H2,11,12,13)(H2,14,15,16)/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 23.699999 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.31 [Predicted by ALOGPS]; -5.6 [Predicted by PubChem via XLOGP] 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
  • Cytoplasm
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 polyphosphate 1-phosphatase
  2. Type II inositol-3,4-bisphosphate 4-phosphatase
  3. Type I inositol-3,4-bisphosphate 4-phosphatase
Enzyme 1 [top]
Enzyme 1 ID 5598
Enzyme 1 Name Inositol polyphosphate 1-phosphatase
Enzyme 1 Synonyms
  1. IPP
  2. IPPase
Enzyme 1 Gene Name INPP1
Enzyme 1 Protein Sequence >Inositol polyphosphate 1-phosphatase 
MSDILRELLCVSEKAANIARACRQQEALFQLLIEEKKEGEKNKKFAVDFKTLADVLVQEV
IKQNMENKFPGLEKNIFGEESNEFTNDWGEKITLRLCSTEEETAELLSKVLNGNKVASEA
LARVVHQDVAFTDPTLDSTEINVPQDILGIWVDPIDSTYQYIKGSADIKSNQGIFPCGLQ
CVTILIGVYDIQTGVPLMGVINQPFVSRDPNTLRWKGQCYWGLSYMGTNMHSLQLTISRR
NGSETHTGNTGSEAAFSPSFSAVISTSEKETIKAALSRVCGDRIFGAAGAGYKSLCVVQG
LVDIYIFSEDTTFKWDSCAAHAILRAMGGGIVDLKECLERNPETGLDLPQLVYHVENEGA
AGVDRWANKGGLIAYRSRKRLETFLSLLVQNLAPAETHT
Enzyme 1 Number of Residues 399
Enzyme 1 Molecular Weight 43997.6
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 1D-myo-inositol 1,4-bisphosphate + H(2)O = 1D- myo-inositol 4-phosphate + phosphate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate [RN:R03393]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID P49441 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name INPP_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1200 bp 
ATGTCAGATATCCTCCGGGAGCTGCTCTGTGTCTCTGAGAAGGCTGCTAACATTGCCCGG
GCGTGCAGACAGCAGGAAGCCCTCTTCCAGCTGCTGATCGAAGAAAAGAAAGAGGGAGAA
AAGAACAAGAAGTTTGCAGTTGACTTCAAGACTCTGGCTGATGTACTGGTACAGGAAGTT
ATAAAACAGAATATGGAGAACAAGTTTCCAGGCTTGGAAAAAAATATTTTTGGAGAAGAA
TCCAATGAGTTTACTAATGACTGGGGGGAAAAGATTACCTTGAGGTTGTGTTCAACAGAG
GAAGAAACAGCAGAGCTTCTTAGCAAAGTCCTCAATGGTAACAAGGTAGCATCTGAAGCA
TTAGCCAGGGTTGTTCATCAGGATGTTGCCTTTACTGACCCAACTCTGGATTCCACAGAG
ATCAATGTTCCACAGGACATTTTGGGAATTTGGGTGGACCCCATAGATTCAACTTATCAG
TATATAAAAGGTTCTGCTGACATTAAATCCAACCAGGGAATCTTCCCCTGTGGACTTCAG
TGTGTCACCATTTTAATTGGTGTCTATGACATACAGACAGGGGTTCCCCTGATGGGAGTC
ATCAATCAACCTTTTGTGTCACGAGATCCAAACACCCTCAGGTGGAAAGGACAGTGCTAT
TGGGGCCTTTCTTACATGGGGACCAACATGCATTCACTACAGCTCACCATCTCTAGAAGA
AACGGCAGTGAAACACACACTGGAAACACCGGCTCTGAGGCAGCATTCTCCCCCAGTTTT
TCAGCCGTAATTAGTACAAGTGAAAAGGAGACTATCAAAGCTGCATTGTCACGTGTGTGT
GGAGATCGCATATTTGGGGCAGCTGGGGCTGGTTATAAGAGCCTATGTGTTGTCCAAGGC
CTCGTTGACATTTACATCTTTTCAGAAGATACCACATTCAAATGGGACTCTTGTGCTGCT
CATGCCATACTGCGGGCCATGGGTGGGGGAATAGTAGACTTGAAAGAATGCTTAGAAAGA
AATCCAGAAACAGGGCTTGATTTGCCACAGTTGGTGTACCACGTGGAAAATGAGGGTGCT
GCTGGGGTGGATCGGTGGGCCAACAAGGGAGGACTCATTGCATACAGATCCAGGAAGCGG
CTGGAGACATTCCTGAGCCTCCTGGTCCAAAACCTGGCACCTGCAGAGACGCATACCTAG
Enzyme 1 GenBank Gene ID L08488 Link Image
Enzyme 1 GeneCard ID INPP1 Link Image
Enzyme 1 GenAtlas ID INPP1 Link Image
Enzyme 1 HGNC ID HGNC:6071 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2q32
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. York JD, Veile RA, Donis-Keller H, Majerus PW: Cloning, heterologous expression, and chromosomal localization of human inositol polyphosphate 1-phosphatase. Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5833-7. [PubMed Link Image]
  2. Lovlie R, Gulbrandsen AK, Molven A, Steen VM: Genomic structure and sequence analysis of a human inositol polyphosphate 1-phosphatase gene (INPP1). Pharmacogenetics. 1999 Aug;9(4):517-28. [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. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  5. Steen VM, Lovlie R, Osher Y, Belmaker RH, Berle JO, Gulbrandsen AK: The polymorphic inositol polyphosphate 1-phosphatase gene as a candidate for pharmacogenetic prediction of lithium-responsive manic-depressive illness. Pharmacogenetics. 1998 Jun;8(3):259-68. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 8851
Enzyme 2 Name Type II inositol-3,4-bisphosphate 4-phosphatase
Enzyme 2 Synonyms
  1. Inositol polyphosphate 4-phosphatase type II
Enzyme 2 Gene Name INPP4B
Enzyme 2 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 2 Number of Residues 924
Enzyme 2 Molecular Weight 104737.1
Enzyme 2 Theoretical pI 6.20
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Involved in phosphatidyl-inositol-4,5-bisphosphate 4-ph
Enzyme 2 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 2 Pathways
Enzyme 2 Reactions
  • 1-phosphatidyl-myo-inositol 3,4-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate [RN:R07299]
Enzyme 2 Pfam Domain Function Not Available
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 156104897 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O15327 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name INP4B_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID NM_001101669.1 Link Image
Enzyme 2 GeneCard ID INPP4B Link Image
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location 4
Enzyme 2 Locus 4q31.21
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 11758
Enzyme 3 Name Type I inositol-3,4-bisphosphate 4-phosphatase
Enzyme 3 Synonyms
  1. Inositol polyphosphate 4-phosphatase type I
Enzyme 3 Gene Name INPP4A
Enzyme 3 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 3 Number of Residues 977
Enzyme 3 Molecular Weight 109954.7
Enzyme 3 Theoretical pI 6.96
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 3,4-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 197116359 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q96PE3 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name INP4A_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 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 3 GenBank Gene ID NM_001134224.1 Link Image
Enzyme 3 GeneCard ID INPP4A Link Image
Enzyme 3 GenAtlas ID INPP4A Link Image
Enzyme 3 HGNC ID HGNC:6074 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2q11.2
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available