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Human Metabolome Database Version 2.5

 

Showing metabocard for 1-Phosphatidyl-1D-myo-inositol 3-phosphate (HMDB03850)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-13 06:57:54
Update Date 2009-05-05 20:59:45
Accession Number HMDB03850
Secondary Accession Numbers Not Available
Common Name 1-Phosphatidyl-1D-myo-inositol 3-phosphate
Description 1-Phosphatidyl-1D-myo-inositol 3-phosphate is a substrate for FYVE finger-containing phosphoinositide kinase and Neutrophil cytosol factor 4.
Synonyms
  1. 1-Phosphatidyl-1D-myo-inositol 3-phosphate
  2. 1-Phosphatidyl-1D-myo-inositol 3-phosphic acid
  3. Phosphatidylinositol 3-phosphate
Chemical IUPAC Name (2R)-2-[[hydroxy-[(1R,2S,3S,4R,5S,6R)-2,3,4,6-tetrahydroxy-5-phosphonooxy-cyclohexyl]oxy-phosphoryl]oxymethyl]butanedioic acid
Chemical Formula C11H20O16P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Sugar Phosphates
Sub Class
  • Inositol phosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • carboxylic acid
  • phosphoric acid ester
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 470.214
Monoisotopic Molecular Weight 470.022644
Isomeric SMILES O[C@H]1[C@H](O)[C@@H](OP(O)(O)=O)[C@@H](O)[C@@H](OP(O)(=O)OC[C@@H](CC(O)=O)C(O)=O)[C@@H]1O
Canonical SMILES OC1C(O)C(OP(O)(O)=O)C(O)C(OP(O)(=O)OCC(CC(O)=O)C(O)=O)C1O
KEGG Compound ID C04549 Link Image
BioCyc ID CPD-177 Link Image
BiGG ID 44024 Link Image
Wikipedia Link Phosphatidylinositol 3-phosphate Link Image
NuGOwiki Link HMDB03850 Link Image
Metagene Link HMDB03850 Link Image
METLIN ID 6985 Link Image
PubChem Compound 6857403 Link Image
PubChem Substance 8145274 Link Image
ChEBI ID 17283 Link Image
CAS Registry Number Not Available
InChI Identifier InChI=1/C11H20O16P2/c12-4(13)1-3(11(18)19)2-25-29(23,24)27-10-7(16)5(14)6(15)9(8(10)17)26-28(20,21)22/h3,5-10,14-17H,1-2H2,(H,12,13)(H,18,19)(H,23,24)(H2,20,21,22)/t3-,5+,6+,7-,8-,9-,10+/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 24.2 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -5
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.58 [Predicted by ALOGPS]; -6.3775 [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 (Predicted from LogP)
Biofluid Location Not Available
Tissue Location
Tissue References
Skeletal Muscle —
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
General References
  1. Buj-Bello A, Furling D, Tronchere H, Laporte J, Lerouge T, Butler-Browne GS, Mandel JL: Muscle-specific alternative splicing of myotubularin-related 1 gene is impaired in DM1 muscle cells. Hum Mol Genet. 2002 Sep 15;11(19):2297-307. [PubMed Link Image]
  2. Wikipedia Link Image
Metabolic Enzymes
  1. Type II inositol-3,4-bisphosphate 4-phosphatase
  2. Phosphatidylinositol 3-kinase catalytic subunit type 3
  3. Type I inositol-3,4-bisphosphate 4-phosphatase
Enzyme 1 [top]
Enzyme 1 ID 8851
Enzyme 1 Name Type II inositol-3,4-bisphosphate 4-phosphatase
Enzyme 1 Synonyms
  1. Inositol polyphosphate 4-phosphatase type II
Enzyme 1 Gene Name INPP4B
Enzyme 1 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 1 Number of Residues 924
Enzyme 1 Molecular Weight 104737.1
Enzyme 1 Theoretical pI 6.20
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Involved in phosphatidyl-inositol-4,5-bisphosphate 4-ph
Enzyme 1 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 1 Pathways
Enzyme 1 Reactions
  • 1-phosphatidyl-myo-inositol 3,4-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate [RN:R07299]
Enzyme 1 Pfam Domain Function Not Available
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 156104897 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O15327 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name INP4B_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID NM_001101669.1 Link Image
Enzyme 1 GeneCard ID INPP4B Link Image
Enzyme 1 GenAtlas ID Not Available
Enzyme 1 HGNC ID Not Available
Enzyme 1 Chromosome Location 4
Enzyme 1 Locus 4q31.21
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 9581
Enzyme 2 Name Phosphatidylinositol 3-kinase catalytic subunit type 3
Enzyme 2 Synonyms
  1. PI3-kinase type 3
  2. PI3K type 3
  3. PtdIns-3-kinase type 3
  4. Phosphatidylinositol 3-kinase p100 subunit
  5. Phosphoinositide-3-kinase class 3
  6. hVps34
Enzyme 2 Gene Name PIK3C3
Enzyme 2 Protein Sequence >Phosphatidylinositol 3-kinase catalytic subunit type 3 
MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVT
CQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAV
PVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTK
AHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDG
DESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIV
SYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDV
EDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKK
DSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLI
SRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRS
LLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVK
IRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRK
ENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAE
VMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLN
KEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVK
KVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK
Enzyme 2 Number of Residues 887
Enzyme 2 Molecular Weight 101548.6
Enzyme 2 Theoretical pI 6.79
Enzyme 2 GO Classification
Function
  • 1-phosphatidylinositol-3-kinase activity
  • binding
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • kinase activity
  • lipid kinase activity
  • phosphoinositide 3-kinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biological regulation
  • glycerophospholipid metabolic process
  • intracellular signal transduction
  • metabolic process
  • organophosphate metabolic process
  • phosphoinositide metabolic process
  • phosphoinositide phosphorylation
  • phosphoinositide-mediated signaling
  • phospholipid metabolic process
  • regulation of biological process
  • regulation of cellular process
  • second-messenger-mediated signaling
  • signal transduction
Component
  • macromolecular complex
  • phosphoinositide 3-kinase complex
  • protein complex
Enzyme 2 General Function Involved in binding
Enzyme 2 Specific Function Catalytic subunit of the PI3K complex. Involved in the transport of lysosomal enzyme precursors to lysosomes
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate [RN:R03362]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 987948 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q8NEB9 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PK3C3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2664 bp 
ATGGGGGAAGCAGAGAAGTTTCACTACATCTATAGTTGTGACCTGGATATCAACGTCCAG
CTTAAGATAGGAAGCTTGGAAGGGAAGAGAGAACAAAAGAGTTATAACGCTGTCCTGGAA
GACCCAATGTTGAAGTTCTCAGGACTATATCAAGAGACATGCTCTGATCTTTATGTTACT
TGTCAAGTTTTTGCAGAAGGGAAGCCTTCGGCCTTGCCAGTGAGAACATCCTACAAAGCA
TTTAGTACAAGATGGAACTGGAATGAATGGCTGAAACTACCAGTAAAATACCCTGACCTG
CCCAGGAATGCCCAAGTGGCCCTCACCATATGGGATGTGTATGGTCCCGGAAAAGCAGTG
CCTGTAGGAGGAACAACGGTTTCGCTCTTTGGAAAATACGGCATGTCTCGCCAAGGGATG
CATGACTTGAAAGTCTGGCCTAATGTAGAAGCAGATGGATCAGAACCCACAAATACTCCT
GGCAGAACAAGTAGCACTCTCTCAGAAGATCAGATGAGCCGTCTTGCCAAGCTCACCAAA
GCTCATCGACAAGGACACATGGTGAAAGTAGATTGGCTGGATAGATTGACATTTAGAGAA
ATAGAAATGATAAATGAGAGTGTGAAACGAAGTTCTAATTTCATGTACCTGATGGGTGGA
TTTCGATGTGTCAAGTGTGATGATAAGGAATATGGTATTGTTTATTATGAAAAGGACGGT
GATGAATCATCTCCAATTTTAACAAGTTTTGAATTAGTGAAAGTTCCTGACCCCCAGATG
TCCCTGGAGAATTTAGTTGAGAGCAAACACCACAACCTTCCCCGGAGTTTAAGAAGTGGA
CCTTCTGACCACGATCTGAAACCCTATCCTTCCCCGAGAGATCAGTTAAAAAATATTGTG
AGTTATCCTCCATCCAAGCCACCCACATATGAAGAACAAGATCTTGTTTGGGAGTTTAGA
TATTATCTTACGAATCAAGATAAAGCCTTGACCAAAATCCTGACATCTGTTATTTGGGAT
CTACCTCAGGGGGCCAAACAGGCCTTGGCACTTCTGGGGAAATGGAACCCGATGGATGTA
GAGGACTCCTTGGAGCTGATATCCTCTCATTACACCAACCCAACTGTGAGGCGTTATGCT
GTTGCCCGGTTGCGACAGGCCGATGATGAGGATTTGTTGATGTACCTATCACAATTGGTC
CAGGCTCTCAAATATGAAAATTTTGATGATATAAAGAATGGATTGGAACCTACCAAGAAG
GATAGTCAGAGTTCAGTGTCAGGAAATGTGTCAAATTCTGGAATAAATTCTGCAGAAATA
GATAGCTCCCAAATTATAACCAGCCCCCTTCCTTCAGTCTCTTCACCTCCTCCTGCATCA
AAAACAAAAGAAGTTCCAGATGGCGAAAATCTGGAACAAGATCTCTGTACCTTCTTGATA
TCGAGAGCCTCCAAAAACTCAACACTGGCTAATTATTTATACTGGTATGTGATAGTGGAA
TGTGAAGATCAAGATACTCAGCAGAGAGATCCAAAGACCCATGAGATGTACTTGAACGTA
ATGAGAAGATTCAGCCAAGCATTGTTGAAGGGTGATAAGTCTGTCAGAGTTATGCGTTCT
TTGCTGGCTGCACAACAGACATTTGTAGATCGGTTGGTGCATCTAATGAAGGCAGTACAA
CGCGAAAGTGGAAATCGTAAGAAAAAGAATGAGAGACTACAGGCATTGCTTGGAGATAAT
GAAAAGATGAATTTGTCAGATGTGGAACTTATCCCGTTGCCTTTAGAACCCCAAGTGAAA
ATTAGAGGAATAATTCCGGAAACAGCTACACTGTTTAAAAGTGCCCTTATGCCTGCACAG
TTGTTTTTTAAGACGGAAGATGGAGGCAAATATCCAGTTATATTTAAGCATGGAGATGAT
TTACGTCAAGATCAACTTATTCTTCAAATCATTTCACTCATGGACAAGCTGTTACGGAAA
GAAAATCTGGACTTGAAATTGACACCTTATAAGGTGTTAGCCACCAGTACAAAACATGGC
TTCATGCAGTTTATCCAGTCAGTTCCTGTGGCTGAAGTTCTTGATACAGAGGGAAGCATT
CAGAACTTTTTTAGAAAATATGCACCAAGTGAGAATGGGCCAAATGGGATTAGTGCTGAG
GTCATGGACACTTACGTTAAAAGCTGTGCTGGATATTGCGTGATCACCTATATACTTGGA
GTTGGAGACAGGCACCTGGATAACCTTGTGCTAACAAAAACAGGCAAACTCTTCCACATA
GACTTTGGATATATTTTGGGTCGGGATCCAAAGCCTCTTCCTCCACCAATGAAGCTGAAT
AAAGAAATGGTAGAAGGAATGGGGGGCACACAGAGTGAGCAGTACCAAGAGTTCCGTAAA
CAGTGTTACACGGCTTTCCTCCACCTGCGGAGGTATTCTAATCTGATTTTGAACTTGTTT
TCCTTGATGGTTGATCCAAACATTCCAGATATTGCACTTGAACCAGATAAAACTGTGAAA
AAGGTTCAGGATAAATTCCGCTTAGACCTGTCGGATGAAGAGGCTGTGCATTACATGCAG
AGTCTGATTGATGAGAGTGTCCATGCTCTTTTTGCTGCAGTGGTGGAACAGATTCACAAG
TTTGCCCAGTACTGGAGAAAATGA
Enzyme 2 GenBank Gene ID Z46973 Link Image
Enzyme 2 GeneCard ID PIK3C3 Link Image
Enzyme 2 GenAtlas ID PIK3C3 Link Image
Enzyme 2 HGNC ID HGNC:8974 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 18q12.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Volinia S, Dhand R, Vanhaesebroeck B, MacDougall LK, Stein R, Zvelebil MJ, Domin J, Panaretou C, Waterfield MD: A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system. EMBO J. 1995 Jul 17;14(14):3339-48. [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]
  3. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  4. Sun Q, Fan W, Chen K, Ding X, Chen S, Zhong Q: Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase. Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19211-6. Epub 2008 Dec 2. [PubMed Link Image]
  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  6. Matsunaga K, Saitoh T, Tabata K, Omori H, Satoh T, Kurotori N, Maejima I, Shirahama-Noda K, Ichimura T, Isobe T, Akira S, Noda T, Yoshimori T: Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages. Nat Cell Biol. 2009 Apr;11(4):385-96. Epub 2009 Mar 8. [PubMed Link Image]
  7. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [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