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Human Metabolome Database Version 2.5

 

Showing metabocard for Inositol 1,4,5-trisphosphate (HMDB01498)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:49
Accession Number HMDB01498
Secondary Accession Numbers Not Available
Common Name Inositol 1,4,5-trisphosphate
Description Intracellular messenger formed by the action of phospholipase C on phosphatidylinositol 4,5-bisphosphate, which is one of the phospholipids that make up the cell membrane. Inositol 1,4,5-trisphosphate is released into the cytoplasm where it releases calcium ions from internal stores within the cell's endoplasmic reticulum. These calcium ions stimulate the activity of B kinase or calmodulin. (PubChem) Inositol 1,4,5-trisphosphate (InsP3) is traditionally considered to be the messenger that initiates the increase and spreading of the activating Ca2+ wave. In line with this hypothesis, recent evidence suggests that the penetrating sperm delivers into mammalian eggs a novel isoform of phospholipase C (PLC), which promotes the formation of InsP3. The mechanism by which the interacting sperm triggers the production of NAADP and subsequently that of InsP3 remains obscure. (PMID: 15362223)
Synonyms
  1. 1D-myo-Inositol 1,4,5-trisphosphate
  2. D-myo-Inositol 1,4,5-trisphosphate
  3. Inositol 1,4,5-trisphosphate
  4. Inositol 1,4,5-trisphosphic acid
Chemical IUPAC Name (2,3,6-trihydroxy-4,5-diphosphonooxy-cyclohexoxy)phosphonic acid
Chemical Formula C6H15O15P3
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
  • Second messenger
  • Component of Inositol phosphate metabolism
Application
Source
  • Endogenous
Average Molecular Weight 420.096
Monoisotopic Molecular Weight 419.962372
Isomeric SMILES O[C@@H]1[C@H](O)[C@@H](OP(O)(O)=O)[C@H](OP(O)(O)=O)[C@@H](O)[C@@H]1OP(O)(O)=O
Canonical SMILES OC1C(O)C(OP(O)(O)=O)C(OP(O)(O)=O)C(O)C1OP(O)(O)=O
KEGG Compound ID C01245 Link Image
BioCyc ID inositol_1,4,5-trisphosphate Link Image
BiGG ID 1485108 Link Image
Wikipedia Link Inositol 1,4,5-trisphosphate Link Image
NuGOwiki Link HMDB01498 Link Image
Metagene Link HMDB01498 Link Image
METLIN ID 6282 Link Image
PubChem Compound 439456 Link Image
PubChem Substance 8143490 Link Image
ChEBI ID 16595 Link Image
CAS Registry Number 88269-39-0
InChI Identifier InChI=1/C6H15O15P3/c7-1-2(8)5(20-23(13,14)15)6(21-24(16,17)18)3(9)4(1)19-22(10,11)12/h1-9H,(H2,10,11,12)(H2,13,14,15)(H2,16,17,18)/t1-,2+,3+,4-,5-,6-/m1/s1
Synthesis Reference Cooke, Allan M.; Potter, Barry V. L.; Gigg, Roy. Synthesis of DL-myo-inositol 1,4,5-trisphosphate. Tetrahedron Letters (1987), 28(20), 2305-8.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 14.8 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -6
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.86 [Predicted by ALOGPS]; -7.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
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
  • nucleus
Biofluid Location Not Available
Tissue Location
Tissue References
Epidermis
Neuron
Pancreas
Platelet
Spleen
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
Phosphatidylinositol Phosphate Metabolism SMP00463 Link Image map00562 Link Image
General References
  1. Nibbering PH, Zomerdijk TP, van Haastert PJ, van Furth R: A competition binding assay for determination of the inositol (1,4,5)-trisphosphate content of human leucocytes. Biochem Biophys Res Commun. 1990 Jul 31;170(2):755-62. [PubMed Link Image]
  2. Brann JH, Dennis JC, Morrison EE, Fadool DA: Type-specific inositol 1,4,5-trisphosphate receptor localization in the vomeronasal organ and its interaction with a transient receptor potential channel, TRPC2. J Neurochem. 2002 Dec;83(6):1452-60. [PubMed Link Image]
  3. Poeckel D, Tausch L, Altmann A, Feisst C, Klinkhardt U, Graff J, Harder S, Werz O: Induction of central signalling pathways and select functional effects in human platelets by beta-boswellic acid. Br J Pharmacol. 2005 Oct;146(4):514-24. [PubMed Link Image]
  4. Koizumi H, Tanaka H, Ohkawara A: beta-Adrenergic stimulation induces activation of protein kinase C and inositol 1,4,5-trisphosphate increase in epidermis. Exp Dermatol. 1997 Jun;6(3):128-32. [PubMed Link Image]
  5. Eberhard M, Erne P: Inositol 1,4,5-trisphosphate-induced calcium release in permeabilized platelets is coupled to hydrolysis of inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate. Biochem Biophys Res Commun. 1993 Aug 31;195(1):19-24. [PubMed Link Image]
  6. Garlind A, Wiehager B, Winblad B, Fowler CJ: Intracellular inositol (1,4,5)-trisphosphate receptor levels are preserved in Alzheimer's disease platelets. Neurobiol Aging. 1997 Sep-Oct;18(5):559-61. [PubMed Link Image]
  7. Eberhard M, Erne P: Regulation of inositol 1,4,5-trisphosphate-induced calcium release by inositol 1,4,5-trisphosphate and calcium in human platelets. J Recept Signal Transduct Res. 1995 Jan-Mar;15(1-4):297-309. [PubMed Link Image]
  8. Petersen OH, Burdakov D, Tepikin AV: Polarity in intracellular calcium signaling. Bioessays. 1999 Oct;21(10):851-60. [PubMed Link Image]
  9. Arranz B, Rosel P, Sarro S, Ramirez N, Duenas R, Cano R, Maria Sanchez J, San L: Altered platelet serotonin 5-HT2A receptor density but not second messenger inositol trisphosphate levels in drug-free schizophrenic patients. Psychiatry Res. 2003 May 30;118(2):165-74. [PubMed Link Image]
  10. Smith RJ, Justen JM, Nidy EG, Sam LM, Bleasdale JE: Transmembrane signaling in human polymorphonuclear neutrophils: 15(S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid modulates receptor agonist-triggered cell activation. Proc Natl Acad Sci U S A. 1993 Aug 1;90(15):7270-4. [PubMed Link Image]
  11. Laffi G, Marra F, Failli P, Ruggiero M, Cecchi E, Carloni V, Giotti A, Gentilini P: Defective signal transduction in platelets from cirrhotics is associated with increased cyclic nucleotides. Gastroenterology. 1993 Jul;105(1):148-56. [PubMed Link Image]
  12. Kalra R, Singh SP, Kracko D, Matta SG, Sharp BM, Sopori ML: Chronic self-administration of nicotine in rats impairs T cell responsiveness. J Pharmacol Exp Ther. 2002 Sep;302(3):935-9. [PubMed Link Image]
  13. Vanags DM, Lloyd JV, Rodgers SE, Bochner F: ADP, adrenaline and serotonin stimulate inositol 1,4,5-trisphosphate production in human platelets. Eur J Pharmacol. 1998 Sep 25;358(1):93-100. [PubMed Link Image]
  14. Saito H, Nishida A, Shimizu M, Motohashi N, Yamawaki S: Decreased inositol 1,4,5-trisphosphate-specific binding in platelets from alcoholic subjects. Biol Psychiatry. 1996 Nov 1;40(9):886-91. [PubMed Link Image]
  15. Suganuma A, Nakashima S, Okano Y, Nozawa Y: Mass contents of inositol 1,4,5-trisphosphate and 1,2-diacylglycerol in human platelets stimulated with a thromboxane analogue and thrombin. Thromb Haemost. 1992 Sep 7;68(3):341-5. [PubMed Link Image]
  16. Dwivedi Y, Janicak PG, Pandey GN: Elevated [3H]inositol 1,4,5-trisphosphate binding sites and expressed inositol 1,4,5-trisphosphate receptor protein level in platelets of depressed patients. Psychopharmacology (Berl). 1998 Jul;138(1):47-54. [PubMed Link Image]
  17. Willets JM, Nahorski SR, Challiss RA: Roles of phosphorylation-dependent and -independent mechanisms in the regulation of M1 muscarinic acetylcholine receptors by G protein-coupled receptor kinase 2 in hippocampal neurons. J Biol Chem. 2005 May 13;280(19):18950-8. Epub 2005 Mar 2. [PubMed Link Image]
  18. Goncalves I, Hughan SC, Schoenwaelder SM, Yap CL, Yuan Y, Jackson SP: Integrin alpha IIb beta 3-dependent calcium signals regulate platelet-fibrinogen interactions under flow. Involvement of phospholipase C gamma 2. J Biol Chem. 2003 Sep 12;278(37):34812-22. Epub 2003 Jun 27. [PubMed Link Image]
  19. Wikipedia Link Image
Metabolic Enzymes
  1. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
  2. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4
  3. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2
  4. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
  5. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
  6. Type I inositol-1,4,5-trisphosphate 5-phosphatase
  7. Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
  8. Inositol polyphosphate 5-phosphatase K
  9. Inositol-trisphosphate 3-kinase B
  10. Inositol-trisphosphate 3-kinase A
  11. Inositol polyphosphate multikinase
  12. Inositol 1,4,5-trisphosphate receptor type 1
  13. Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2
  14. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
  15. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
  16. Multiple inositol polyphosphate phosphatase 1
  17. Inositol 1,4,5-trisphosphate receptor type 2
  18. Inositol 1,4,5-trisphosphate receptor type 3
  19. Phospholipase C, beta 3 (Phosphatidylinositol-specific) (Phospholipase C, beta 3 (Phosphatidylinositol-specific), isoform CRA_a)
  20. Phospholipase C, gamma 1
  21. cDNA FLJ35540 fis, clone SPLEN2002493, highly similar to Phosphatidylinositol 4,5-bisphosphate5-phosphatase A (EC 3.1.3.56)
  22. cDNA, FLJ92960, Homo sapiens skeletal muscle and kidney enriched inositolphosphatase (SKIP), transcript variant 2, mRNA (Skeletal muscle and kidney enriched inositol phosphatase, isoform CRA_a)
  23. cDNA FLJ33455 fis, clone BRAMY2000354, highly similar to 1-phosphatidylinositol-4,5-bisphosphatephosphodiesterase delta 1 (EC 3.1.4.11)
Enzyme 1 [top]
Enzyme 1 ID 5454
Enzyme 1 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
Enzyme 1 Synonyms
  1. PLC-154
  2. Phosphoinositide phospholipase C-beta-1
  3. Phospholipase C-I
  4. PLC-I
  5. Phospholipase C-beta-1
  6. PLC-beta-1
Enzyme 1 Gene Name PLCB1
Enzyme 1 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKE
TELLDLSLVKDARCGRHAKAPKDPKLRELLDVGNIGRLEQRMITVVYGPDLVNISHLNLV
AFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSA
DRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYL
TVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLARKGQISVDGFMRYLS
GEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCV
ELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQ
QAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKK
KLSEQASNTYSDSSSMFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEM
SNLVNYIQPVKFESFEISKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPK
GTRVDSSNYMPQLFWNAGCQMVALNFQTMDLAMQINMGMYEYNGKSGYRLKPEFMRRPDK
HFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQG
NAVNPVWEEEPIVFKKVVLPTLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNER
NQPLTLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKK
EADPGETPSEAPSEARTTPAENGVNHTTTLTPKPPSQALHSQPAPGSVKAPAKTEDLIQS
VLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYL
RRRAALEKSAKKDSKKKSEPSSPDHGSSTIEQDLAALDAEMTQKLIDLKDKQQQQLLNLR
QEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKI
TEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHKEIRQQILDEKP
KLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKVNHKTPSS
EELGGDIPGKEFDTPL
Enzyme 1 Number of Residues 1216
Enzyme 1 Molecular Weight 138565.8
Enzyme 1 Theoretical pI 6.12
Enzyme 1 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 1 General Function Involved in calcium ion binding
Enzyme 1 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 12083581 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9NQ66 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PLCB1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >3651 bp
ATGGCCGGGGCTCAACCCGGAGTGCACGCCTTGCAACTCAAGCCCGTGTGCGTGTCCGAC
AGCCTCAAGAAGGGCACCAAATTCGTCAAGTGGGATGATGACTCAACTATTGTTACTCCA
ATTATTTTGAGGACTGACCCTCAGGGATTTTTCTTTTACTGGACAGATCAAAACAAGGAG
ACAGAGCTACTGGATCTCAGCCTTGTCAAAGATGCCAGATGTGGGAGACACGCCAAAGCT
CCCAAGGACCCCAAATTACGTGAACTTTTGGATGTGGGGAACATCGGGCGCCTGGAGCAG
CGCATGATCACAGTGGTGTATGGGCCTGACCTCGTGAACATCTCCCATTTGAATCTCGTG
GCTTTCCAAGAAGAAGTGGCCAAGGAATGGACAAATGAGGTTTTCAGTTTGGCAACAAAC
CTGCTGGCCCAAAACATGTCCAGGGATGCATTTCTGGAAAAAGCCTATACTAAACTTAAG
CTGCAAGTCACTCCAGAAGGGCGTATTCCTCTCAAAAACATATATCGCTTGTTTTCAGCA
GATCGGAAGCGAGTTGAAACTGCTTTAGAGGCTTGTAGTCTTCCATCTTCAAGGAATGAT
TCAATACCTCAAGAAGATTTCACTCCAGAAGTGTACAGAGTTTTCCTCAACAACCTTTGC
CCTCGACCTGAAATTGATAACATCTTTTCAGAATTTGGTGCAAAAAGCAAACCATATCTT
ACCGTTGATCAGATGATGGATTTTATCAACCTTAAGCAGCGAGATCCTCGGCTTAATGAA
ATACTTTATCCACCTCTAAAACAAGAGCAAGTCCAAGTATTGATTGAGAAGTATGAACCC
AACAACAGCCTCGCCAGAAAAGGACAAATATCAGTGGATGGGTTCATGCGCTATCTGAGT
GGAGAAGAAAACGGAGTCGTTTCACCTGAGAAACTGGATTTGAATGAAGACATGTCTCAG
CCCCTTTCTCACTATTTCATTAATTCCTCGCACAACACCTACCTCACAGCTGGCCAACTG
GCTGGAAACTCCTCTGTTGAGATGTATCGCCAAGTGCTCCTGTCTGGTTGTCGCTGTGTG
GAGCTGGACTGCTGGAAGGGACGGACTGCAGAAGAGGAACCTGTCATCACCCATGGCTTC
ACCATGACAACTGAAATATCTTTCAAGGAAGTGATAGAAGCAATTGCGGAGTGTGCATTT
AAGACTTCACCTTTTCCAATTCTCCTTTCGTTTGAGAACCATGTGGATTCCCCAAAGCAG
CAAGCCAAGATGGCGGAGTACTGCCGACTGATCTTTGGGGATGCCCTTCTCATGGAGCCC
CTGGAAAAATATCCACTGGAATCTGGAGTTCCTCTTCCAAGCCCTATGGATTTAATGTAT
AAAATTTTGGTGAAAAATAAGAAGAAATCACACAAGTCATCAGAAGGAAGCGGCAAAAAG
AAGCTCTCAGAACAAGCCTCCAACACCTACAGTGACTCCTCCAGCATGTTCGAGCCCTCA
TCCCCAGGAGCCGGAGAAGCTGATACGGAAAGTGACGACGACGATGATGATGATGACTGT
AAAAAATCTTCAATGGATGAGGGGACTGCTGGAAGTGAGGCTATGGCCACAGAAGAAATG
TCTAATCTGGTGAACTATATTCAGCCAGTCAAGTTTGAGTCATTTGAAATTTCAAAAAAA
AGAAATAAAAGTTTTGAAATGTCTTCCTTCGTGGAAACCAAAGGACTTGAACAACTCACC
AAGTCTCCAGTGGAATTTGTAGAATATAACAAAATGCAGCTTAGCAGGATATATCCAAAA
GGAACACGTGTGGATTCATCCAACTATATGCCTCAGCTCTTCTGGAATGCAGGTTGTCAG
ATGGTGGCACTTAATTTCCAGACAATGGACCTGGCTATGCAAATAAATATGGGGATGTAT
GAATACAACGGGAAGAGTGGCTACAGATTGAAGCCAGAGTTCATGAGGAGGCCTGACAAG
CATTTTGATCCATTTACTGAAGGCATCGTAGATGGGATAGTGGCAAACACTTTGTCTGTT
AAGATTATTTCAGGTCAGTTTCTTTCTGATAAGAAAGTTGGGACTTACGTGGAAGTAGAT
ATGTTTGGTTTGCCTGTGGATACAAGGAGGAAGGCATTTAAGACCAAAACATCCCAAGGA
AATGCTGTGAATCCTGTCTGGGAAGAAGAACCTATTGTGTTCAAAAAGGTGGTTCTTCCT
ACTCTGGCCTGTTTGAGAATAGCAGTTTATGAAGAAGGAGGTAAATTCATTGGCCACCGT
ATCTTGCCAGTGCAAGCCATTCGGCCAGGCTATCACTATATCTGTCTAAGGAATGAAAGG
AACCAGCCTCTGACGCTGCCTGCTGTCTTTGTCTACATAGAAGTGAAAGACTATGTGCCA
GACACATATGCAGATGTCATCGAAGCTTTATCAAACCCAATCCGATATGTGAACCTGATG
GAACAGAGAGCTAAGCAATTGGCTGCTTTGACACTGGAAGATGAAGAAGAAGTAAAGAAA
GAGGCTGATCCTGGAGAAACACCATCAGAGGCTCCAAGTGAAGCGAGAACGACTCCAGCA
GAAAATGGGGTGAATCACACTACAACCCTGACACCCAAGCCACCCTCCCAGGCTCTCCAC
AGCCAGCCAGCTCCAGGTTCTGTAAAGGCACCTGCCAAAACAGAAGATCTTATTCAGAGT
GTCTTAACAGAAGTGGAAGCACAGACCATCGAAGAACTAAAGCAACAGAAATCGTTTGTG
AAACTTCAAAAGAAACACTACAAAGAAATGAAAGACCTGGTTAAGAGACACCACAAGAAA
ACCACTGACCTTATCAAAGAACACACTACCAAGTATAATGAAATTCAGAATGACTACTTG
AGAAGGAGAGCCGCTTTGGAAAAGTCCGCCAAAAAGGACAGTAAGAAAAAATCGGAACCC
AGCAGCCCTGATCATGGTTCATCAACGATTGAGCAAGACCTCGCTGCTCTGGATGCTGAA
ATGACCCAAAAGTTAATAGACTTGAAGGACAAACAACAGCAGCAGCTGCTTAATCTTCGG
CAAGAACAGTATTATAGTGAAAAATACCAGAAGCGAGAACATATTAAACTGCTTATTCAA
AAGTTGACGGATGTCGCAGAAGAGTGTCAGAACAATCAGTTAAAGAAGCTCAAAGAAATC
TGTGAGAAAGAAAAGAAAGAATTAAAGAAGAAAATGGATAAAAAGAGGCAGGAGAAGATA
ACAGAAGCTAAATCCAAAGACAAAAGTCAGATGGAAGAGGAGAAGACAGAGATGATCCGG
TCATATATCCAGGAAGTGGTGCAGTATATCAAGAGGCTAGAAGAAGCGCAAAGTAAACGG
CAAGAAAAACTCGTAGAGAAACACAAGGAAATACGTCAGCAGATCCTGGATGAAAAGCCC
AAGCTGCAGGTGGAGCTGGAGCAAGAATACCAAGACAAATTCAAAAGACTGCCCCTCGAG
ATTTTGGAATTCGTGCAGGAAGCCATGAAAGGAAAGATCAGTGAAGACAGCAATCACGGT
TCTGCCCCTCTCTCCCTGTCCTCAGACCCTGGAAAAGTGAACCACAAGACTCCCTCCAGT
GAGGAGCTGGGAGGAGACATCCCAGGAAAAGAATTTGATACTCCTCTGTGA
Enzyme 1 GenBank Gene ID NM_015192.2 Link Image
Enzyme 1 GeneCard ID PLCB1 Link Image
Enzyme 1 GenAtlas ID PLCB1 Link Image
Enzyme 1 HGNC ID HGNC:15917 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 20p12
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Caricasole A, Sala C, Roncarati R, Formenti E, Terstappen GC: Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1). Biochim Biophys Acta. 2000 Dec 15;1517(1):63-72. [PubMed Link Image]
  2. Peruzzi D, Calabrese G, Faenza I, Manzoli L, Matteucci A, Gianfrancesco F, Billi AM, Stuppia L, Palka G, Cocco L: Identification and chromosomal localisation by fluorescence in situ hybridisation of human gene of phosphoinositide-specific phospholipase C beta(1). Biochim Biophys Acta. 2000 Apr 12;1484(2-3):175-82. [PubMed Link Image]
  3. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  4. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  5. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  6. 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]
  7. 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]
  8. 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]
  9. Tabellini G, Bortul R, Santi S, Riccio M, Baldini G, Cappellini A, Billi AM, Berezney R, Ruggeri A, Cocco L, Martelli AM: Diacylglycerol kinase-theta is localized in the speckle domains of the nucleus. Exp Cell Res. 2003 Jul 1;287(1):143-54. [PubMed Link Image]
  10. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  11. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  12. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5455
Enzyme 2 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4
Enzyme 2 Synonyms
  1. Phosphoinositide phospholipase C-beta-4
  2. Phospholipase C-beta-4
  3. PLC-beta-4
Enzyme 2 Gene Name PLCB4
Enzyme 2 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4
MAKPYEFNWQKEVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWRSEGKEGQVL
ECSLINSIRSGAIPKDPKILAALEAVGKSENDLEGRIVCVCSGTDLVNISFTYMVAENPE
VTKQWVEGLRSIIHNFRANNVSPMTCLKKHWMKLAFMTNTNGKIPVRSITRTFASGKTEK
VIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVD
QLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE
NAPVFLDRLELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELD
CWDGKGEDQEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKM
SKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRLKPEVEKKQLEALRSM
MEAGESASPANILEDDNEEEIESADQEEEAHPEFKFGNELSADDLGHKEAVANSVKKGLV
TVEDEQAWMASYKYVGATTNIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVG
LGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQL
NQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSETPVDGVIAATCSVQVISGQFLSDKKIGT
YVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNK
LIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKK
FLSITEKRADQMRAMGIETSDIADVPSDTSKNDKKGKANTAKANVTPQSSSELRPTTTAA
LASGVEAKKGIELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQ
VDKIVAQYDKEKSTHEKILEKAMKKKGGSNCLEMKKETEIKIQTLTSDHKSKVKEIVAQH
TKEWSEMINTHSAEEQEIRDLHLSQQCELLKKLLINAHEQQTQQLKLSHDRESKEMRAHQ
AKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQ
LEHLEFLEKQNEQAKEMQQMVKLEAEMDRRPATVV
Enzyme 2 Number of Residues 1175
Enzyme 2 Molecular Weight 134462.6
Enzyme 2 Theoretical pI 6.90
Enzyme 2 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 2 General Function Involved in calcium ion binding
Enzyme 2 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 57284038 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q15147 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PLCB4_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >3528 bp
ATGGCCAAACCTTATGAATTTAACTGGCAGAAGGAAGTTCCCTCCTTTTTGCAAGAAGGA
GCAGTTTTTGACAGATACGAGGAGGAATCCTTTGTGTTTGAACCCAACTGCCTCTTCAAA
GTGGATGAGTTTGGCTTCTTTCTGACATGGAGAAGTGAAGGCAAGGAAGGACAGGTGCTA
GAATGCTCCCTCATCAACAGTATTCGGTCGGGAGCCATACCAAAGGATCCCAAAATCTTG
GCTGCTCTTGAAGCTGTTGGAAAATCAGAAAATGATCTGGAAGGGCGGATAGTTTGTGTC
TGCAGTGGCACAGATCTAGTGAACATTAGTTTTACCTACATGGTGGCTGAAAATCCAGAA
GTAACTAAGCAATGGGTAGAAGGCCTGAGATCAATCATACACAACTTCAGGGCCAACAAC
GTCAGTCCAATGACATGCCTCAAGAAACACTGGATGAAATTGGCATTTATGACCAACACA
AATGGTAAAATTCCAGTTAGGAGTATTACTAGAACATTTGCATCGGGAAAAACAGAAAAG
GTGATCTTTCAAGCACTCAAGGAGTTAGGTCTTCCCAGTGGAAAGAATGATGAAATTGAG
CCCACAGCATTTTCTTATGAAAAGTTCTATGAACTGACACAAAAGATTTGTCCTCGGACA
GATATAGAAGATCTTTTCAAAAAAATCAATGGAGACAAAACTGATTATTTAACGGTAGAC
CAATTAGTGAGCTTTCTAAATGAACATCAACGAGATCCTCGATTGAATGAAATTTTATTT
CCATTTTATGATGCCAAAAGGGCAATGCAGATCATTGAGATGTATGAACCTGATGAAGAT
TTGAAGAAAAAAGGCCTTATATCAAGTGATGGGTTTTGCAGATATCTGATGTCAGATGAA
AACGCCCCAGTCTTCCTAGATCGTTTAGAACTTTACCAAGAAATGGACCATCCTCTGGCT
CACTACTTCATCAGTTCTTCCCATAACACTTATCTCACTGGCAGACAGTTCGGCGGGAAG
TCTTCGGTAGAAATGTACAGACAGGTTCTCCTGGCTGGTTGCAGATGTGTTGAACTTGAC
TGCTGGGATGGAAAAGGTGAAGACCAAGAACCAATAATAACTCATGGAAAAGCAATGTGT
ACAGATATCCTTTTTAAGGATGTAATTCAAGCCATCAAGGAAACTGCATTTGTCACATCA
GAATATCCTGTAATTCTCTCCTTTGAAAATCACTGCAGCAAATATCAACAGTACAAGATG
TCCAAATATTGCGAAGATCTATTTGGGGATCTCCTGTTGAAACAAGCACTTGAATCACAT
CCACTTGAACCAGGCAGGGCTTTGCCATCCCCCAATGACCTCAAAAGAAAAATACTCATA
AAAAACAAGCGGCTGAAACCTGAAGTTGAAAAAAAACAGCTGGAAGCTTTGAGAAGCATG
ATGGAAGCTGGAGAATCTGCCTCCCCAGCAAACATCTTAGAGGACGATAATGAAGAGGAG
ATCGAAAGTGCTGACCAAGAGGAGGAAGCTCACCCCGAATTCAAATTTGGAAATGAACTT
TCTGCTGATGACTTGGGTCACAAGGAAGCTGTTGCAAATAGCGTCAAGAAGGGCCTGGTC
ACTGTAGAAGATGAGCAGGCGTGGATGGCATCTTATAAATATGTAGGTGCTACCACTAAT
ATCCATCCATATTTGTCCACAATGATCAACTACGCCCAGCCTGTAAAGTTTCAAGGTTTC
CATGTGGCAGAAGAACGCAATATTCATTATAACATGTCTTCTTTTAATGAATCAGTCGGT
CTTGGCTACTTGAAGACACATGCAATTGAATTTGTCAATTATAACAAACGGCAAATGAGT
CGCATTTACCCCAAGGGAGGCCGAGTCGATTCCAGTAATTACATGCCTCAGATTTTCTGG
AACGCTGGCTGCCAGATGGTTTCACTGAACTATCAAACCCCAGATTTAGCGATGCAATTG
AATCAGGGAAAATTTGAGTATAATGGATCGTGCGGGTACCTTCTCAAACCAGATTTCATG
AGGCGGCCTGATCGAACATTTGACCCCTTCTCTGAAACTCCTGTTGATGGTGTTATTGCA
GCCACTTGCTCAGTGCAGGTTATATCAGGTCAATTCTTATCAGATAAGAAAATTGGCACC
TACGTAGAGGTGGATATGTATGGGTTGCCCACTGACACCATACGTAAGGAATTCCGAACT
CGCATGGTTATGAATAATGGACTCAATCCAGTTTACAATGAAGAGTCATTTGTATTTCGG
AAGGTGATCCTGCCGGACCTGGCTGTCTTGAGAATAGCTGTGTATGATGATAACAACAAG
CTGATTGGCCAGAGGATCCTCCCGCTTGATGGCCTCCAAGCCGGATATCGACACATTTCC
CTTCGAAATGAGGGAAATAAACCATTATCACTACCAACAATTTTCTGCAATATTGTTCTT
AAAACATATGTGCCTGATGGATTTGGAGATATCGTGGATGCTTTATCAGATCCAAAGAAA
TTTCTCTCAATTACAGAAAAGAGAGCAGACCAAATGAGAGCTATGGGCATTGAAACTAGT
GACATAGCCGACGTGCCCAGTGACACTTCCAAAAATGACAAGAAAGGAAAGGCCAACACC
GCCAAAGCAAATGTGACCCCTCAGAGTAGCTCTGAGCTCAGACCAACCACCACGGCTGCC
CTGGCCTCTGGTGTGGAAGCCAAGAAAGGTATTGAACTTATCCCTCAAGTAAGGATAGAA
GACTTAAAGCAGATGAAGGCTTACTTGAAGCATTTAAAGAAACAGCAGAAGGAGCTAAAT
TCTTTAAAGAAGAAACATGCAAAGGAACACAGTACCATGCAGAAGTTACACTGCACGCAA
GTTGACAAAATTGTGGCACAGTATGACAAAGAGAAGTCGACTCATGAGAAAATCCTAGAG
AAGGCAATGAAGAAGAAGGGGGGAAGTAATTGTCTCGAAATGAAAAAAGAAACAGAAATC
AAAATTCAGACGCTGACATCAGATCACAAATCTAAGGTCAAAGAGATTGTAGCACAGCAC
ACAAAGGAATGGTCAGAAATGATCAATACCCACAGTGCTGAGGAGCAAGAAATCCGAGAC
CTGCACCTCAGCCAGCAGTGTGAGCTGCTGAAAAAGCTACTCATCAATGCCCACGAGCAG
CAAACCCAGCAGCTGAAACTGTCCCATGACAGGGAAAGCAAGGAAATGCGAGCACACCAG
GCTAAGATTTCTATGGAAAATAGCAAAGCCATCAGCCAAGATAAATCTATCAAGAATAAA
GCAGAACGGGAAAGGCGAGTCAGGGAGTTAAACAGCAGCAACACTAAAAAGTTTCTGGAA
GAAAGAAAGAGACTTGCCATGAAGCAGTCCAAAGAAATGGATCAGTTGAAAAAAGTCCAG
CTTGAACATCTAGAATTCCTAGAGAAACAGAATGAGCAGGCGAAGGAGATGCAGCAGATG
GTGAAATTGGAAGCCGAGATGGACCGCAGACCAGCAACAGTAGTATGA
Enzyme 2 GenBank Gene ID AL023805 Link Image
Enzyme 2 GeneCard ID PLCB4 Link Image
Enzyme 2 GenAtlas ID PLCB4 Link Image
Enzyme 2 HGNC ID HGNC:9059 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 20p12
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Alvarez RA, Ghalayini AJ, Xu P, Hardcastle A, Bhattacharya S, Rao PN, Pettenati MJ, Anderson RE, Baehr W: cDNA sequence and gene locus of the human retinal phosphoinositide-specific phospholipase-C beta 4 (PLCB4). Genomics. 1995 Sep 1;29(1):53-61. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [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. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  5. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5456
Enzyme 3 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2
Enzyme 3 Synonyms
  1. Phosphoinositide phospholipase C-beta-2
  2. Phospholipase C-beta-2
  3. PLC-beta-2
Enzyme 3 Gene Name PLCB2
Enzyme 3 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2
MSLLNPVLLPPKVKAYLSQGERFIKWDDETTVASPVILRVDPKGYYLYWTYQSKEMEFLD
ITSIRDTRFGKFAKMPKSQKLRDVFNMDFPDNSFLLKTLTVVSGPDMVDLTFHNFVSYKE
NVGKAWAEDVLALVKHPLTANASRSTFLDKILVKLKMQLNSEGKIPVKNFFQMFPADRKR
VEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSYHAKAKPYMTKEH
LTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPEN
SVLAQDKLLLHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDC
WKGKPPDEEPIITHGFTMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVDSPRQQAKM
AEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKNQFSGPTSSSKDTGGE
AEGSSPPSAPAGEGTVWAGEEGTELEEEEVEEEEEEESGNLDEEEIKKMQSDEGTAGLEV
TAYEEMSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQM
SRIYPKGTRMDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEF
MRRPDKQFNPFSVDRIDVVVATTLSITVISGQFLSERSVRTYVEVELFGLPGDPKRRYRT
KLSPSTNSINPVWKEEPFVFEKILMPELASLRVAVMEEGNKFLGHRIIPINALNSGYHHL
CLHSESNMPLTMPALFIFLEMKDYIPGAWADLTVALANPIKFFSAHDTKSVKLKEAMGGL
PEKPFPLASPVASQVNGALAPTSNGSPAARAGAREEAMKEAAEPRTASLEELRELKGVVK
LQRRHEKELRELERRGARRWEELLQRGAAQLAELGPPGVGGVGACKLGPGKGSRKKRSLP
REESAGAAPGEGPEGVDGRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMEL
AREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNSHI
QEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAEVKE
SVRACLRTCFPSEAKDKPERACECPPELCEQDPLIAKADAQESRL
Enzyme 3 Number of Residues 1185
Enzyme 3 Molecular Weight 134023.2
Enzyme 3 Theoretical pI 6.21
Enzyme 3 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 3 General Function Involved in calcium ion binding
Enzyme 3 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 3 Pathways
Enzyme 3 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 95147333 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q00722 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PLCB2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >3558 bp
ATGTCTCTGCTCAACCCTGTCCTGCTGCCCCCCAAGGTGAAGGCCTATCTGAGCCAAGGG
GAGCGCTTCATCAAATGGGATGATGAAACTACAGTTGCCTCTCCAGTTATCCTCCGTGTG
GATCCTAAGGGCTACTACTTATACTGGACGTATCAAAGTAAGGAGATGGAGTTTCTGGAT
ATCACCAGCATCCGGGATACTCGCTTTGGGAAGTTTGCCAAGATGCCCAAGAGCCAGAAG
CTCCGGGACGTCTTCAACATGGACTTTCCTGATAACAGTTTCCTGCTGAAGACACTCACG
GTGGTGTCCGGCCCGGACATGGTGGACCTCACCTTCCACAACTTCGTCTCCTACAAGGAG
AACGTGGGCAAGGCCTGGGCTGAGGACGTACTGGCCCTAGTCAAACATCCGCTGACGGCC
AACGCCTCCCGCAGCACCTTCCTGGACAAGATCCTTGTGAAGCTCAAGATGCAGCTCAAC
TCTGAAGGGAAGATTCCGGTGAAGAACTTTTTCCAGATGTTTCCTGCTGACCGCAAGCGG
GTGGAAGCTGCTCTCAGTGCCTGCCACCTCCCCAAAGGCAAAAATGACGCCATCAATCCT
GAGGACTTCCCAGAACCTGTCTACAAGAGTTTCCTCATGAGCCTCTGTCCTCGGCCAGAA
ATAGATGAGATCTTCACTTCTTACCATGCTAAGGCCAAACCCTACATGACGAAGGAGCAC
CTGACCAAATTCATCAACCAGAAACAGCGGGACTCCCGGCTTAACTCCCTGCTGTTCCCG
CCAGCACGGCCTGACCAGGTGCAGGGCCTCATCGACAAGTATGAGCCCAGTGGCATCAAT
GCACAGAGGGGCCAGCTGTCACCTGAAGGCATGGTCTGGTTTCTCTGTGGGCCAGAGAAC
AGCGTGCTGGCCCAGGACAAGCTGCTGCTCCACCACGACATGACGCAGCCACTCAATCAT
TACTTCATCAACTCGTCCCACAACACCTACCTGACAGCCGGCCAGTTCTCAGGCCTCTCC
TCGGCTGAGATGTACCGCCAGGTGCTGCTCTCTGGCTGCCGTTGCGTGGAGCTAGACTGC
TGGAAGGGGAAACCCCCTGACGAGGAGCCCATTATCACCCATGGCTTCACCATGACCACA
GACATCTTCTTCAAAGAAGCAATTGAGGCTATTGCAGAAAGCGCCTTTAAGACCTCCCCC
TATCCCATCATCCTGTCGTTTGAGAACCATGTGGACTCACCCCGCCAGCAGGCTAAGATG
GCTGAGTATTGCCGGACGATCTTTGGGGATATGCTGCTCACAGAGCCCCTGGAAAAGTTC
CCACTAAAACCAGGTGTCCCCCTGCCCAGCCCTGAGGATCTCAGGGGCAAGATCCTCATC
AAGAACAAGAAGAACCAGTTTTCTGGCCCCACCTCCTCCAGTAAGGATACTGGTGGGGAG
GCTGAGGGCAGCAGCCCACCCAGTGCCCCTGCAGGTGAGGGCACAGTGTGGGCTGGCGAG
GAAGGGACTGAGCTGGAGGAGGAGGAGGTGGAAGAGGAAGAGGAGGAGGAGTCAGGAAAC
CTGGATGAAGAAGAGATTAAGAAGATGCAGTCGGATGAGGGCACAGCGGGCCTGGAAGTG
ACGGCTTATGAGGAGATGTCCAGCCTAGTCAATTACATCCAGCCCACCAAGTTCGTCTCC
TTTGAGTTCTCTGCCCAAAAGAACCGAAGTTATGTCATCTCGTCCTTCACAGAGCTCAAG
GCATATGACCTGCTCTCCAAGGCCTCGGTGCAGTTTGTGGACTACAACAAGCGCCAGATG
AGCCGCATTTACCCCAAGGGAACCCGCATGGACTCCTCCAACTACATGCCCCAGATGTTC
TGGAATGCTGGATGCCAGATGGTTGCCCTCAACTTCCAGACGATGGACTTGCCCATGCAG
CAGAACATGGCAGTATTTGAGTTCAACGGGCAGAGCGGCTACCTCCTCAAGCATGAGTTC
ATGCGCCGGCCGGACAAGCAGTTCAACCCCTTCTCAGTGGACCGCATCGACGTGGTGGTG
GCCACCACCCTTTCCATTACGGTGATCTCTGGGCAGTTCCTGTCAGAACGCAGCGTGCGC
ACCTATGTAGAAGTGGAGCTGTTTGGCCTTCCTGGGGACCCCAAGAGGCGCTATCGAACT
AAGCTGTCACCCAGTACTAACTCCATCAATCCTGTCTGGAAGGAGGAGCCCTTTGTCTTT
GAGAAGATCTTGATGCCTGAGCTGGCCTCCCTCAGAGTGGCTGTGATGGAGGAAGGCAAC
AAGTTTCTTGGACACCGCATCATCCCCATCAATGCCCTAAATTCTGGGTACCACCACCTG
TGCCTGCACAGTGAGAGCAACATGCCCCTCACCATGCCTGCGCTCTTCATCTTCCTGGAG
ATGAAGGACTACATACCTGGTGCTTGGGCAGATCTCACTGTGGCCCTCGCCAACCCCATT
AAGTTCTTCAGTGCCCATGACACGAAGTCTGTGAAGCTCAAGGAGGCCATGGGAGGTCTG
CCTGAGAAGCCCTTCCCACTGGCGAGTCCAGTTGCCAGCCAGGTCAATGGGGCGTTGGCC
CCAACGAGCAATGGGTCACCAGCAGCCAGGGCCGGGGCCAGGGAAGAGGCTATGAAAGAA
GCTGCGGAGCCGCGGACCGCCAGCCTGGAGGAGCTCCGGGAGCTAAAGGGCGTGGTGAAG
CTGCAGCGGCGGCACGAGAAGGAGCTGCGAGAGTTGGAGCGGCGCGGAGCGCGGCGCTGG
GAGGAGCTGCTGCAGCGGGGCGCGGCGCAGCTGGCGGAGCTCGGGCCACCGGGCGTGGGG
GGCGTCGGGGCCTGCAAGCTCGGTCCCGGCAAGGGCTCTCGCAAGAAGAGGAGCCTGCCC
CGCGAGGAGAGCGCCGGAGCCGCGCCGGGCGAGGGCCCTGAGGGCGTGGACGGGCGCGTG
CGGGAGCTGAAAGACAGGCTGGAGCTGGAGCTGCTGCGGCAGGGCGAGGAGCAGTACGAG
TGCGTTCTGAAGCGCAAGGAGCAGCACGTGGCCGAGCAAATCTCCAAAATGATGGAGCTG
GCCAGAGAGAAACAGGCGGCAGAGCTGAAGGCCCTGAAGGAGACGTCGGAGAACGACACC
AAAGAGATGAAGAAAAAGCTGGAGACAAAGAGACTGGAGCGGATCCAGGGCATGACCAAA
GTCACCACAGACAAGATGGCCCAGGAGAGGTTGAAGAGAGAGATTAACAACTCCCACATC
CAGGAAGTAGTGCAGGTGATCAAGCAGATGACGGAGAACTTGGAGAGGCACCAGGAGAAG
CTGGAGGAGAAGCAGGCGGCTTGCCTGGAACAGATACGGGAGATGGAAAAGCAGTTCCAG
AAGGAGGCGCTGGCAGAGTACGAGGCCAGGATGAAGGGTCTGGAGGCAGAGGTGAAGGAG
TCGGTGAGGGCCTGCCTCAGGACCTGCTTTCCCTCCGAGGCCAAGGACAAGCCTGAGAGG
GCCTGCGAGTGCCCCCCAGAGCTGTGTGAGCAGGACCCACTCATAGCAAAGGCAGATGCC
CAGGAGAGCCGCCTCTGA
Enzyme 3 GenBank Gene ID NM_004573.2 Link Image
Enzyme 3 GeneCard ID PLCB2 Link Image
Enzyme 3 GenAtlas ID PLCB2 Link Image
Enzyme 3 HGNC ID HGNC:9055 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 15q15
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Park D, Jhon DY, Kriz R, Knopf J, Rhee SG: Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2. J Biol Chem. 1992 Aug 15;267(23):16048-55. [PubMed Link Image]
  2. 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]
  3. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  4. Jezyk MR, Snyder JT, Gershberg S, Worthylake DK, Harden TK, Sondek J: Crystal structure of Rac1 bound to its effector phospholipase C-beta2. Nat Struct Mol Biol. 2006 Dec;13(12):1135-40. Epub 2006 Nov 19. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5460
Enzyme 4 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
Enzyme 4 Synonyms
  1. Phosphoinositide phospholipase C-beta-3
  2. Phospholipase C-beta-3
  3. PLC-beta-3
Enzyme 4 Gene Name PLCB3
Enzyme 4 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
MAGAQPGVHALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNME
VDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNF
MAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFS
ADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPY
LTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYL
GGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRC
VELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAK
QQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDS
AGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGD
EGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPV
KFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYM
PQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIV
DGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEP
FDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLI
YTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQL
GSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGH
KALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVED
TKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQF
KRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLE
EAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLG
DGPLVACASNGHAPGSSGHLSGADSESQEENTQL
Enzyme 4 Number of Residues 1234
Enzyme 4 Molecular Weight 138797.7
Enzyme 4 Theoretical pI 5.66
Enzyme 4 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 4 General Function Involved in calcium ion binding
Enzyme 4 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 4 Pathways
Enzyme 4 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 148745659 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q01970 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PLCB3_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >3705 bp
ATGGCGGGCGCCCAGCCCGGCGTCCACGCGCTGCAGTTGGAGCCGCCCACCGTGGTGGAG
ACCCTGCGGCGCGGGAGTAAGTTCATCAAATGGGACGAGGAGACCTCCAGTCGGAACCTG
GTGACCCTGCGTGTGGACCCCAATGGCTTCTTCTTGTACTGGACGGGCCCCAACATGGAG
GTGGACACACTGGACATCAGTTCCATCAGGGACACACGGACAGGCCGGTACGCCCGCCTG
CCCAAGGACCCCAAGATCCGGGAAGTTCTGGGCTTTGGGGGTCCCGATGCCCGGCTGGAG
GAGAAGCTGATGACGGTGGTGTCTGGGCCAGACCCGGTGAACACAGTGTTCTTGAACTTC
ATGGCCGTGCAGGATGACACAGCCAAGGTCTGGTCTGAGGAGCTATTCAAGCTGGCTATG
AACATCCTGGCTCAGAACGCCTCCCGGAACACCTTCCTGCGCAAAGCATACACGAAGCTG
AAGCTGCAGGTGAACCAGGATGGTCGGATCCCCGTCAAGAACATCCTGAAGATGTTCTCA
GCAGACAAGAAGCGGGTGGAGACTGCGCTGGAATCCTGTGGCCTCAAATTCAACCGGAGT
GAGTCCATCCGGCCTGATGAGTTTTCCTTGGAAATCTTTGAGCGGTTCCTGAACAAGCTG
TGTCTGCGGCCGGACATTGACAAGATCCTGCTGGAGATAGGCGCCAAGGGCAAGCCATAC
CTGACGCTGGAGCAGCTCATGGACTTCATCAACCAGAAGCAACGCGACCCGAGACTCAAC
GAAGTGCTGTACCCGCCCCTGCGGCCCTCCCAGGCCCGGCTGCTCATCGAAAAGTATGAG
CCCAACCAGCAGTTTCTGGAGCGAGACCAGATGTCCATGGAGGGCTTTAGCCGCTACCTG
GGAGGCGAGGAGAATGGCATCCTGCCCCTGGAAGCCCTGGATCTGAGCACGGACATGACC
CAGCCACTGAGTGCCTACTTCATCAACTCCTCGCATAACACCTATCTCACTGCGGGGCAG
CTGGCTGGGACCTCGTCGGTGGAGATGTACCGCCAGGCACTACTATGGGGCTGCCGCTGC
GTGGAGCTGGACGTGTGGAAGGGACGGCCGCCTGAGGAGGAACCCTTCATTACCCACGGC
TTCACCATGACCACAGAGGTGCCTCTGCGCGACGTGCTGGAGGCCATTGCCGAGACTGCC
TTCAAGACCTCGCCCTACCCCGTCATCCTCTCCTTCGAGAACCATGTGGACTCGGCAAAG
CAACAGGCAAAGATGGCTGAGTACTGCCGCTCCATCTTTGGAGACGCGCTACTCATCGAG
CCTCTGGACAAGTACCCGCTGGCCCCAGGCGTTCCCCTGCCCAGCCCCCAGGACCTGATG
GGCCGTATCCTGGTGAAGAACAAGAAGCGGCACCGACCCAGCGCAGGTGGCCCAGACAGC
GCCGGGCGCAAGCGGCCCCTGGAGCAGAGCAATTCTGCCCTGAGCGAGAGCTCCGCGGCC
ACCGAGCCCTCCTCCCCGCAGCTGGGGTCTCCCAGCTCTGACAGCTGCCCAGGCCTGAGC
AATGGGGAGGAGGTAGGGCTTGAGAAGCCCAGCCTGGAGCCTCAGAAGTCTCTGGGTGAC
GAGGGCCTGAACCGAGGCCCCTATGTTCTTGGACCTGCTGACCGTGAGGATGAGGAGGAA
GATGAGGAAGAGGAGGAACAGACAGACCCCAAAAAGCCAACTACAGATGAGGGCACAGCC
AGCAGCGAGGTGAATGCCACTGAGGAGATGTCCACGCTTGTCAACTACATCGAACCTGTC
AAGTTCAAGTCCTTTGAGGCTGCTCGAAAGAGGAACAAATGCTTCGAGATGTCGTCCTTT
GTGGAGACCAAGGCCATGGAGCAACTGACCAAGAGCCCCATGGAGTTTGTGGAATACAAC
AAGCAGCAGCTCAGCCGCATCTACCCCAAGGGCACCCGCGTGGACTCCTCCAACTACATG
CCCCAGCTCTTCTGGAACGTAGGGTGCCAGCTTGTTGCGCTCAACTTCCAGACCCTCGAT
GTGGCGATGCAGCTCAACGCGGGCGTTTTTGAGTACAACGGGCGCAGCGGGTACCTGCTC
AAGCCGGAGTTCATGCGGCGGCCGGACAAGTCCTTCGACCCCTTCACTGAGGTCATCGTG
GATGGCATCGTGGCCAATGCCTTGCGGGTCAAGGTGATCTCAGGGCAGTTCCTGTCCGAC
AGGAAGGTGGGCATCTACGTGGAGGTGGACATGTTTGGCCTCCCTGTTGATACGCGGCGC
AAGTACCGCACCCGGACCTCTCAGGGGAACTCGTTCAACCCCGTGTGGGACGAAGAGCCC
TTCGACTTCCCCAAGGTGGTGCTGCCCACGCTGGCTTCACTTCGCATTGCAGCCTTTGAG
GAGGGGGGTAAATTCGTAGGGCACCGGATCCTGCCTGTCTCTGCCATCCGCTCCGGATAC
CACTACGTCTGCCTGCGGAACGAGGCCAACCAACCGCTGTGCCTGCCGGCCCTGCTCATC
TACACCGAAGCCTCGGACTACATTCCTGACGACCACCAGGACTATGCGGAGGCCCTGATC
AACCCCATTAAGCACGTCAGCCTGATGGACCAGAGGGCCCGGCAGCTGGCCGCCCTCATT
GGGGAGAGTGAGGCTCAGGCTGGCCAAGAGACGTGCCAGGACACCCAGTCTCAGCAGCTG
GGGTCTCAGCCGTCCTCAAACCCCACCCCCAGCCCACTGGATGCCTCCCCCCGCCGGCCC
CCTGGCCCCACCACCTCCCCTGCCAGCACCTCCCTCAGCAGCCCAGGGCAGCGTGATGAT
CTCATCGCCAGCATCCTCTCAGAGGTGGCCCCCACCCCGCTGGATGAGCTCCGAGGTCAC
AAGGCTCTGGTCAAGCTCCGGAGCCGGCAAGAGCGAGACCTGCGGGAGCTGCGCAAGAAG
CATCAGCGGAAGGCAGTCACCCTCACCCGCCGCCTGCTGGATGGCCTGGCTCAGGCACAG
GCTGAGGGCAGGTGCCGGCTGCGGCCAGGTGCCCTAGGTGGGGCCGCTGATGTGGAGGAC
ACGAAGGAGGGGGAGGACGAGGCAAAGCGGTATCAGGAGTTCCAGAACAGACAGGTGCAG
AGCCTGCTGGAGCTGCGGGAGGCCCAGGTGGACGCAGAGGCCCAGCGGAGGCTGGAACAC
CTGAGACAGGCTCTGCAGCGGCTCAGGGAGGTCGTCCTTGATGCAAACACAACTCAGTTC
AAGAGGCTGAAAGAGATGAACGAGAGGGAGAAGAAGGAGCTGCAGAAGATCCTGGACAGA
AAGCGCCATAACAGCATCTCGGAGGCCAAGATGAGGGACAAGCATAAGAAGGAGGCGGAA
CTGACGGAGATTAACCGTCGGCACATCACTGAGTCAGTCAACTCCATCCGTCGGCTGGAG
GAGGCCCAGAAGCAGCGGCATGACCGTCTTGTGGCTGGGCAGCAGCAGGTCCTGCAACAG
CTGGCAGAAGAGGAGCCCAAGCTGCTGGCCCAGCTGGCCCAGGAGTGTCAGGAGCAGCGG
GCGAGGCTCCCCCAGGAGATCCGCCGGAGCCTGCTGGGCGAGATGCCAGAGGGGCTGGGG
GACGGGCCTCTGGTGGCCTGTGCCAGCAACGGTCACGCACCCGGGAGCAGCGGGCACCTG
TCGGGCGCTGACTCGGAGAGCCAGGAGGAGAACACGCAGCTCTGA
Enzyme 4 GenBank Gene ID BC142681 Link Image
Enzyme 4 GeneCard ID PLCB3 Link Image
Enzyme 4 GenAtlas ID PLCB3 Link Image
Enzyme 4 HGNC ID HGNC:9056 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 11q13
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Mazuruk K, Schoen TJ, Chader GJ, Rodriguez IR: Structural organization and expression of the human phosphatidylinositol-specific phospholipase C beta-3 gene. Biochem Biophys Res Commun. 1995 Jul 6;212(1):190-5. [PubMed Link Image]
  2. Lagercrantz J, Carson E, Phelan C, Grimmond S, Rosen A, Dare E, Nordenskjold M, Hayward NK, Larsson C, Weber G: Genomic organization and complete cDNA sequence of the human phosphoinositide-specific phospholipase C beta 3 gene (PLCB3). Genomics. 1995 Apr 10;26(3):467-72. [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. Carozzi AJ, Kriz RW, Webster C, Parker PJ: Identification, purification and characterization of a novel phosphatidylinositol-specific phospholipase C, a third member of the beta subfamily. Eur J Biochem. 1992 Dec 1;210(2):521-9. [PubMed Link Image]
  5. Oh YS, Jo NW, Choi JW, Kim HS, Seo SW, Kang KO, Hwang JI, Heo K, Kim SH, Kim YH, Kim IH, Kim JH, Banno Y, Ryu SH, Suh PG: NHERF2 specifically interacts with LPA2 receptor and defines the specificity and efficiency of receptor-mediated phospholipase C-beta3 activation. Mol Cell Biol. 2004 Jun;24(11):5069-79. [PubMed Link Image]
  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  9. 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]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5462
Enzyme 5 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
Enzyme 5 Synonyms
  1. Phosphoinositide phospholipase C-gamma-2
  2. Phospholipase C-IV
  3. PLC-IV
  4. Phospholipase C-gamma-2
  5. PLC-gamma-2
Enzyme 5 Gene Name PLCG2
Enzyme 5 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
MSTTVNVDSLAEYEKSQIKRALELGTVMTVFSFRKSTPERRTVQVIMETRQVAWSKTADK
IEGFLDIMEIKEIRPGKNSKDFERAKAVRQKEDCCFTILYGTQFVLSTLSLAADSKEDAV
NWLSGLKILHQEAMNASTPTIIESWLRKQIYSVDQTRRNSISLRELKTILPLINFKVSSA
KFLKDKFVEIGAHKDELSFEQFHLFYKKLMFEQQKSILDEFKKDSSVFILGNTDRPDASA
VYLHDFQRFLIHEQQEHWAQDLNKVRERMTKFIDDTMRETAEPFLFVDEFLTYLFSRENS
IWDEKYDAVDMQDMNNPLSHYWISSSHNTYLTGDQLRSESSPEAYIRCLRMGCRCIELDC
WDGPDGKPVIYHGWTRTTKIKFDDVVQAIKDHAFVTSSFPVILSIEEHCSVEQQRHMAKA
FKEVFGDLLLTKPTEASADQLPSPSQLREKIIIKHKKLGPRGDVDVNMEDKKDEHKQQGE
LYMWDSIDQKWTRHYCAIADAKLSFSDDIEQTMEEEVPQDIPPTELHFGEKWFHKKVEKR
TSAEKLLQEYCMETGGKDGTFLVRESETFPNDYTLSFWRSGRVQHCRIRSTMEGGTLKYY
LTDNLTFSSIYALIQHYRETHLRCAEFELRLTDPVPNPNPHESKPWYYDSLSRGEAEDML
MRIPRDGAFLIRKREGSDSYAITFRARGKVKHCRINRDGRHFVLGTSAYFESLVELVSYY
EKHSLYRKMRLRYPVTPELLERYNMERDINSLYDVSRMYVDPSEINPSMPQRTVKALYDY
KAKRSDELSFCRGALIHNVSKEPGGWWKGDYGTRIQQYFPSNYVEDISTADFEELEKQII
EDNPLGSLCRGILDLNTYNVVKAPQGKNQKSFVFILEPKQQGDPPVEFATDRVEELFEWF
QSIREITWKIDTKENNMKYWEKNQSIAIELSDLVVYCKPTSKTKDNLENPDFREIRSFVE
TKADSIIRQKPVDLLKYNQKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTADKY
MQMNHALFSLNGRTGYVLQPESMRTEKYDPMPPESQRKILMTLTVKVLGARHLPKLGRSI
ACPFVEVEICGAEYDNNKFKTTVVNDNGLSPIWAPTQEKVTFEIYDPNLAFLRFVVYEED
MFSDPNFLAHATYPIKAVKSGFRSVPLKNGYSEDIELASLLVFCEMRPVLESEEELYSSC
RQLRRRQEELNNQLFLYDTHQNLRNANRDALVKEFSVNENQLQLYQEKCNKRLREKRVSN
SKFYS
Enzyme 5 Number of Residues 1265
Enzyme 5 Molecular Weight 147868.7
Enzyme 5 Theoretical pI 6.60
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • molecular transducer activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • protein binding
  • signal transducer activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid catabolic process
  • phospholipid metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 5 General Function Involved in phosphoinositide phospholipase C activity
Enzyme 5 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling
Enzyme 5 Pathways
Enzyme 5 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 117320537 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P16885 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PLCG2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >3798 bp
ATGTCCACCACGGTCAATGTAGATTCCCTTGCGGAATATGAGAAGAGCCAGATCAAGAGA
GCCCTGGAGCTGGGGACGGTGATGACTGTGTTCAGCTTCCGCAAGTCCACCCCCGAGCGG
AGAACCGTCCAGGTGATCATGGAGACGCGGCAGGTGGCCTGGAGCAAGACCGCCGACAAG
ATCGAGGGCTTCTTGGATATCATGGAAATAAAAGAAATCCGCCCAGGGAAGAACTCCAAA
GATTTCGAGCGAGCAAAAGCAGTTCGCCAGAAAGAAGACTGCTGCTTCACCATCCTATAT
GGCACTCAGTTCGTCCTCAGCACGCTCAGCTTGGCAGCTGACTCTAAAGAGGATGCAGTT
AACTGGCTCTCTGGCTTGAAAATCTTACACCAGGAAGCGATGAATGCGTCCACGCCCACC
ATTATCGAGAGTTGGCTGAGAAAGCAGATATATTCTGTGGATCAAACCAGAAGAAACAGC
ATCAGTCTCCGAGAGTTGAAGACCATCTTGCCCCTGATCAACTTTAAAGTGAGCAGTGCC
AAGTTCCTTAAAGATAAGTTTGTGGAAATAGGAGCACACAAAGATGAGCTCAGCTTTGAA
CAGTTCCATCTCTTCTATAAAAAACTTATGTTTGAACAGCAAAAATCGATTCTCGATGAA
TTCAAAAAGGATTCGTCCGTGTTCATCCTGGGGAACACTGACAGGCCGGATGCCTCTGCT
GTTTACCTGCATGACTTCCAGAGGTTTCTCATACATGAACAGCAGGAGCATTGGGCTCAG
GATCTGAACAAAGTCCGTGAGCGGATGACAAAGTTCATTGATGACACCATGCGTGAAACT
GCTGAGCCTTTCTTGTTTGTGGATGAGTTCCTCACGTACCTGTTTTCACGAGAAAACAGC
ATCTGGGATGAGAAGTATGACGCGGTGGACATGCAGGACATGAACAACCCCCTGTCTCAT
TACTGGATCTCCTCGTCACATAACACGTACCTTACAGGTGACCAGCTGCGGAGCGAGTCG
TCCCCAGAAGCTTACATCCGCTGCCTGCGCATGGGCTGTCGCTGCATTGAACTGGACTGC
TGGGACGGGCCCGATGGGAAGCCGGTCATCTACCATGGCTGGACGCGGACTACCAAGATC
AAGTTTGACGACGTCGTGCAGGCCATCAAAGACCACGCCTTTGTTACCTCGAGCTTCCCA
GTGATCCTGTCCATCGAGGAGCACTGCAGCGTGGAGCAACAGCGTCACATGGCCAAGGCC
TTCAAGGAAGTATTTGGCGACCTGCTGTTGACGAAGCCCACGGAGGCCAGTGCTGACCAG
CTGCCCTCGCCCAGCCAGCTGCGGGAGAAGATCATCATCAAGCATAAGAAGCTGGGCCCC
CGAGGCGATGTGGATGTCAACATGGAGGACAAGAAGGACGAACACAAGCAACAGGGGGAG
CTGTACATGTGGGATTCCATTGACCAGAAATGGACTCGGCACTACTGCGCCATTGCCGAT
GCCAAGCTGTCCTTCAGTGATGACATTGAACAGACTATGGAGGAGGAAGTGCCCCAGGAT
ATACCCCCTACAGAACTACATTTTGGGGAGAAATGGTTCCACAAGAAGGTGGAGAAGAGG
ACGAGTGCCGAGAAGTTGCTGCAGGAATACTGCATGGAGACGGGGGGCAAGGATGGCACC
TTCCTGGTTCGGGAGAGCGAGACCTTCCCCAATGACTACACCCTGTCCTTCTGGCGGTCA
GGCCGGGTCCAGCACTGCCGGATCCGCTCCACCATGGAGGGCGGGACCCTGAAATACTAC
TTGACTGACAACCTCACCTTCAGCAGCATCTATGCCCTCATCCAGCACTACCGCGAGACG
CACCTGCGCTGCGCCGAGTTCGAGCTGCGGCTCACGGACCCTGTGCCCAACCCCAACCCC
CACGAGTCCAAGCCGTGGTACTATGACAGCCTGAGCCGCGGAGAGGCAGAGGACATGCTG
ATGAGGATTCCCCGGGACGGGGCCTTCCTGATCCGGAAGCGAGAGGGGAGCGACTCCTAT
GCCATCACCTTCAGGGCTAGGGGCAAGGTAAAGCATTGTCGCATCAACCGGGACGGCCGG
CACTTTGTGCTGGGGACCTCCGCCTATTTTGAGAGTCTGGTGGAGCTCGTCAGTTACTAC
GAGAAGCATTCACTCTACCGAAAGATGAGACTGCGCTACCCCGTGACCCCCGAGCTCCTG
GAGCGCTACAATATGGAAAGAGATATAAACTCCCTCTACGACGTCAGCAGAATGTATGTG
GATCCCAGTGAAATCAATCCGTCCATGCCTCAGAGAACCGTGAAAGCTCTGTATGACTAC
AAAGCCAAGCGAAGCGATGAGCTGAGCTTCTGCCGTGGTGCCCTCATCCACAATGTCTCC
AAGGAGCCCGGGGGCTGGTGGAAAGGAGACTATGGAACCAGGATCCAGCAGTACTTCCCA
TCCAACTACGTCGAGGACATCTCAACTGCAGACTTCGAGGAGCTAGAAAAGCAGATTATT
GAAGACAATCCCTTAGGGTCTCTTTGCAGAGGAATATTGGACCTCAATACCTATAACGTC
GTGAAAGCCCCTCAGGGAAAAAACCAGAAGTCCTTTGTCTTCATCCTGGAGCCCAAGCAG
CAGGGCGATCCTCCGGTGGAGTTTGCCACAGACAGGGTGGAGGAGCTCTTTGAGTGGTTT
CAGAGCATCCGAGAGATCACCTGGAAGATTGACACCAAGGAGAACAACATGAAGTACTGG
GAGAAGAACCAGTCCATCGCCATCGAGCTCTCTGACCTGGTTGTCTACTGCAAACCAACC
AGCAAAACCAAGGACAACTTAGAAAATCCTGACTTCCGAGAAATCCGCTCCTTTGTGGAG
ACGAAGGCTGACAGCATCATCAGACAGAAGCCCGTCGACCTCCTGAAGTACAATCAAAAG
GGCCTGACCCGCGTCTACCCAAAGGGACAAAGAGTTGACTCTTCAAACTACGACCCCTTC
CGCCTCTGGCTGTGCGGTTCTCAGATGGTGGCACTCAATTTCCAGACGGCAGATAAGTAC
ATGCAGATGAATCACGCATTGTTTTCTCTCAATGGGCGCACGGGCTACGTTCTGCAGCCT
GAGAGCATGAGGACAGAGAAATATGACCCGATGCCACCCGAGTCCCAGAGGAAGATCCTG
ATGACGCTGACAGTCAAGGTTCTCGGTGCTCGCCATCTCCCCAAACTTGGACGAAGTATT
GCCTGTCCCTTTGTAGAAGTGGAGATCTGTGGAGCCGAGTATGACAACAACAAGTTCAAG
ACGACGGTTGTGAATGATAATGGCCTCAGCCCTATCTGGGCTCCAACACAGGAGAAGGTG
ACATTTGAAATTTATGACCCAAACCTGGCATTTCTGCGCTTTGTGGTTTATGAAGAAGAT
ATGTTCAGCGATCCCAACTTTCTTGCTCATGCCACTTACCCCATTAAAGCAGTCAAATCA
GGATTCAGGTCCGTTCCTCTGAAGAATGGGTACAGCGAGGACATAGAGCTGGCTTCCCTC
CTGGTTTTCTGTGAGATGCGGCCAGTCCTGGAGAGCGAAGAGGAACTTTACTCCTCCTGT
CGCCAGCTGAGGAGGCGGCAAGAAGAACTGAACAACCAGCTCTTTCTGTATGACACACAC
CAGAACTTGCGCAATGCCAACCGGGATGCCCTGGTTAAAGAGTTCAGTGTTAATGAGAAC
CAGCTCCAGCTGTACCAGGAGAAATGCAACAAGAGGTTAAGAGAGAAGAGAGTCAGCAAC
AGCAAGTTTTACTCATAG
Enzyme 5 GenBank Gene ID NM_002661.2 Link Image
Enzyme 5 GeneCard ID PLCG2 Link Image
Enzyme 5 GenAtlas ID PLCG2 Link Image
Enzyme 5 HGNC ID HGNC:9066 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 16q24.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Ohta S, Matsui A, Nazawa Y, Kagawa Y: Complete cDNA encoding a putative phospholipase C from transformed human lymphocytes. FEBS Lett. 1988 Dec 19;242(1):31-5. [PubMed Link Image]
  2. Kemmer D, Podowski RM, Arenillas D, Lim J, Hodges E, Roth P, Sonnhammer EL, Hoog C, Wasserman WW: NovelFam3000--uncharacterized human protein domains conserved across model organisms. BMC Genomics. 2006 Mar 13;7:48. [PubMed Link Image]
  3. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [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. Ozdener F, Dangelmaier C, Ashby B, Kunapuli SP, Daniel JL: Activation of phospholipase Cgamma2 by tyrosine phosphorylation. Mol Pharmacol. 2002 Sep;62(3):672-9. [PubMed Link Image]
  6. Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC: Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. Anal Chem. 2004 May 15;76(10):2763-72. [PubMed Link Image]
  7. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  8. 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 5597
Enzyme 6 Name Type I inositol-1,4,5-trisphosphate 5-phosphatase
Enzyme 6 Synonyms
  1. 5PTase
Enzyme 6 Gene Name INPP5A
Enzyme 6 Protein Sequence >Type I inositol-1,4,5-trisphosphate 5-phosphatase
MAGKAAAPGTAVLLVTANVGSLFDDPENLQKNWLREFYQVVHTHKPHFMALHCQEFGGKN
YEASMSHVDKFVKELLSSDAMKEYNRARVYLDENYKSQEHFTALGSFYFLHESLKNIYQF
DFKAKKYRKVAGKEIYSDTLESTPMLEKEKFPQDYFPECKWSRKGFIRTRWCIADCAFDL
VNIHLFHDASNLVAWETSPSVYSGIRHKALGYVLDRIIDQRFEKVSYFVFGDFNFRLDSK
SVVETLCTKATMQTVRAADTNEVVKLIFRESDNDRKVMLQLEKKLFDYFNQEVFRDNNGT
ALLEFDKELSVFKDRLYELDISFPPSYPYSEDARQGEQYMNTRCPAWCDRILMSPSAKEL
VLRSESEEKVVTYDHIGPNVCMGDHKPVFLAFRIMPGAGKPHAHVHKCCVVQ
Enzyme 6 Number of Residues 412
Enzyme 6 Molecular Weight 47819.2
Enzyme 6 Theoretical pI 7.04
Enzyme 6 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 6 General Function Involved in inositol or phosphatidylinositol phosphatase activity
Enzyme 6 Specific Function Major isoenzyme hydrolyzing the calcium-mobilizing second messenger Ins(1,4,5)P3, this is a signal-terminating reaction
Enzyme 6 Pathways
Enzyme 6 Reactions
  • (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate [RN:R03394]
  • (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate [RN:R03430]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 57209040 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q14642 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name I5P1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1239 bp
ATGGCGGGGAAGGCGGCCGCCCCGGGCACCGCGGTGCTGCTGGTCACGGCCAACGTGGGC
TCGCTCTTCGACGACCCAGAAAACCTGCAGAAGAACTGGCTTCGGGAATTTTACCAGGTC
GTGCACACACACAAGCCGCACTTCATGGCCTTGCACTGTCAGGAGTTTGGAGGGAAGAAC
TACGAGGCCTCCATGTCCCACGTGGACAAGTTCGTCAAAGAACTATTGTCGAGTGATGCG
ATGAAAGAATATAACAGGGCTCGAGTCTACCTGGATGAAAACTACAAATCCCAGGAGCAC
TTCACGGCACTAGGAAGCTTTTATTTTCTTCATGAGTCCTTAAAAAACATCTACCAGTTT
GACTTTAAAGCTAAGAAGTATAGAAAGGTCGCTGGCAAAGAGATCTACTCGGATACCTTA
GAGAGCACGCCCATGCTGGAGAAGGAGAAGTTTCCGCAGGACTACTTCCCCGAGTGCAAA
TGGTCAAGAAAAGGCTTCATCCGGACGAGGTGGTGCATTGCAGACTGTGCCTTTGACTTG
GTGAATATCCATCTTTTCCATGATGCTTCCAATCTGGTCGCCTGGGAAACAAGCCCTTCC
GTGTACTCGGGAATCCGGCACAAGGCACTGGGCTACGTGCTGGACAGAATCATTGATCAG
CGATTCGAGAAGGTTTCCTACTTTGTATTTGGTGATTTCAACTTCCGGCTGGATTCCAAG
TCCGTCGTGGAGACGCTCTGCACAAAAGCCACCATGCAGACGGTCCGGGCCGCCGACACC
AATGAAGTGGTGAAGCTCATATTTCGTGAGTCGGACAACGACCGGAAGGTTATGCTCCAG
TTAGAAAAGAAACTCTTCGACTACTTCAACCAGGAGGTTTTCCGAGACAACAACGGCACC
GCGCTCTTGGAGTTTGACAAGGAGTTGTCTGTCTTTAAGGACAGACTGTATGAACTGGAC
ATCTCGTTCCCTCCCAGCTACCCGTACAGTGAGGACGCCCGCCAGGGTGAGCAGTACATG
AACACCCGGTGCCCAGCCTGGTGTGACCGCATCCTCATGTCCCCGTCTGCCAAGGAGCTG
GTGCTGCGGTCGGAGAGCGAGGAGAAGGTTGTCACCTATGACCACATTGGGCCCAACGTC
TGCATGGGAGACCACAAGCCCGTGTTCCTGGCCTTCCGAATCATGCCCGGGGCAGGTAAA
CCTCATGCCCATGTGCACAAGTGTTGTGTCGTGCAGTGA
Enzyme 6 GenBank Gene ID AL356603 Link Image
Enzyme 6 GeneCard ID INPP5A Link Image
Enzyme 6 GenAtlas ID INPP5A Link Image
Enzyme 6 HGNC ID HGNC:6076 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 10q26.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. De Smedt F, Verjans B, Mailleux P, Erneux C: Cloning and expression of human brain type I inositol 1,4,5-trisphosphate 5-phosphatase. High levels of mRNA in cerebellar Purkinje cells. FEBS Lett. 1994 Jun 20;347(1):69-72. [PubMed Link Image]
  2. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [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. Laxminarayan KM, Chan BK, Tetaz T, Bird PI, Mitchell CA: Characterization of a cDNA encoding the 43-kDa membrane-associated inositol-polyphosphate 5-phosphatase. J Biol Chem. 1994 Jun 24;269(25):17305-10. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5599
Enzyme 7 Name Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
Enzyme 7 Synonyms
  1. Inositol polyphosphate 5-phosphatase J
Enzyme 7 Gene Name INPP5J
Enzyme 7 Protein Sequence >Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
MEGQSSRGSRRPGTRAGLGSLPMPQGVAQTGAPSKVDSSFQLPAKKNAALGPSEPRLALA
PVGPRAAMSASSEGPRLALASPRPILAPLCTPEGQKTATAHRSSSLAPTSVGQLVMSASA
GPKPPPATTGSVLAPTSLGLVMPASAGPRSPPVTLGPNLAPTSRDQKQEPPASVGPKPTL
AASGLSLALASEEQPPELPSTPSPVPSPVLSPTQEQALAPASTASGAASVGQTSARKRDA
PAPRPLPASEGHLQPPAQTSGPTGSPPCIQTSPDPRLSPSFRARPEALHSSPEDPVLPRP
PQTLPLDVGQGPSEPGTHSPGLLSPTFRPGAPSGQTVPPPLPKPPRSPSRSPSHSPNRSP
CVPPAPDMALPRLGTQSTGPGRCLSPNLQAQEAPAPVTTSSSTSTLSSSPWSAQPTWKSD
PGFRITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGADMIAIGLQEVNSMLNKRLKDALFT
DQWSELFMDALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNK
GGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFQGPGAQGILDHDLVFW
FGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKF
DVGTNKYDTSAKKRKPAWTDRILWKVKAPGGGPSPSGRKSHRLQVTQHSYRSHMEYTVSD
HKPVAAQFLLQFAFRDDMPLVRLEVADEWVRPEQAVVRYRMETVFARSSWDWIGLYRVGF
RHCKDYVAYVWAKHEDVDGNTYQVTFSEESLPKGHGDFILGYYSHNHSILIGITEPFQIS
LPSSELASSSTDSSGTSSEGEDDSTLELLAPKSRSPSPGKSKRHRSRSPGLARFPGLALR
PSSRERRGASRSPSPQSRRLSRVAPDRSSNGSSRGSSEEGPSGLPGPWAFPPAVPRSLGL
LPALRLETVDPGGGGSWGPDREALAPNSLSPSPQGHRGLEEGGLGP
Enzyme 7 Number of Residues 1006
Enzyme 7 Molecular Weight 107195.7
Enzyme 7 Theoretical pI 9.53
Enzyme 7 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 7 General Function Involved in inositol or phosphatidylinositol phosphatase activity
Enzyme 7 Specific Function Inositol 5-phosphatase, which converts inositol 1,4,5- trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4- phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate- binding proteins that are present at membranes ruffles
Enzyme 7 Pathways
Enzyme 7 Reactions
  • (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate [RN:R03394]
  • (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate [RN:R03430]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 50726960 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q15735 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PI5PA_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 Not Available
Enzyme 7 GeneCard ID INPP5J Link Image
Enzyme 7 GenAtlas ID INPP5J Link Image
Enzyme 7 HGNC ID HGNC:8956 Link Image
Enzyme 7 Chromosome Location 2
Enzyme 7 Locus 22q12.2
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. 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]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  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]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5600
Enzyme 8 Name Inositol polyphosphate 5-phosphatase K
Enzyme 8 Synonyms
  1. Skeletal muscle and kidney-enriched inositol phosphatase
Enzyme 8 Gene Name INPP5K
Enzyme 8 Protein Sequence >Inositol polyphosphate 5-phosphatase K
MSSRKLSGPKGRRLSIHVVTWNVASAAPPLDLSDLLQLNNRNLNLDIYVIGLQELNSGII
SLLSDAAFNDSWSSFLMDVLSPLSFIKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPT
GLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFDRILEMQNCEGRDIPN
ILDHDLIIWFGDMNFRIEDFGLHFVRESIKNRCYGGLWEKDQLSIAKKHDPLLREFQEGR
LLFPPTYKFDRNSNDYDTSEKKRKPAWTDRILWRLKRQPCAGPDTPIPPASHFSLSLRGY
SSHMTYGISDHKPVSGTFDLELKPLVSAPLIVLMPEDLWTVENDMMVSYSSTSDFPSSPW
DWIGLYKVGLRDVNDYVSYAWVGDSKVSCSDNLNQVYIDISNIPTTEDEFLLCYYSNSLR
SVVGISRPFQIPPGSLREDPLGEAQPQI
Enzyme 8 Number of Residues 448
Enzyme 8 Molecular Weight 51089.8
Enzyme 8 Theoretical pI 6.51
Enzyme 8 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 8 General Function Involved in inositol or phosphatidylinositol phosphatase activity
Enzyme 8 Specific Function Inositol 5-phosphatase which acts on inositol 1,4,5- trisphosphate, inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-triphosphate. Has 6-fold higher affinity for phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5- trisphosphate. May negatively regulate assembly of the actin cytoskeleton
Enzyme 8 Pathways
Enzyme 8 Reactions
  • (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate [RN:R03394]
  • (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate [RN:R03430]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 7209855 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9BT40 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name INP5K_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1347 bp
ATGAGCTCGCGGAAGCTGAGCGGGCCGAAAGGCAGGAGGCTCAGCATACACGTCGTGACT
TGGAACGTGGCTTCGGCAGCGCCCCCTCTAGATCTCAGTGACCTGCTTCAGCTGAACAAC
CGGAACCTCAATCTTGACATATATGTTATTGGTTTGCAGGAATTGAACTCTGGGATCATA
AGCCTCCTTTCCGATGCTGCCTTTAATGACTCGTGGAGCAGTTTCCTCATGGATGTGCTT
TCCCCTCTGAGCTTCATCAAGGTCTCCCATGTCCGTATGCAGGGGATCCTCTTACTGGTC
TTTGCCAAGTATCAGCATTTGCCCTATATCCAGATTCTGTCTACTAAATCCACCCCCACT
GGCCTGTTTGGGTACTGGGGGAACAAAGGTGGAGTCAACATCTGCCTGAAGCTTTATGGC
TACTATGTCAGCATCATCAACTGCCACCTGCCTCCCCACATTTCCAACAATTACCAGCGG
CTGGAGCACTTTGACCGGATCCTGGAGATGCAGAATTGTGAGGGGCGAGACATCCCAAAC
ATCCTGGACCACGACCTCATTATCTGGTTTGGAGACATGAACTTTCGGATCGAGGACTTT
GGGTTGCACTTTGTTCGGGAATCCATTAAAAATCGGTGCTACGGTGGCCTGTGGGAGAAG
GACCAGCTCAGCATTGCCAAGAAACATGACCCGCTGCTCCGGGAGTTCCAGGAGGGCCGC
CTACTCTTCCCGCCCACCTACAAGTTTGATAGGAACTCCAACGACTATGACACCAGTGAG
AAAAAACGCAAGCCTGCATGGACCGATCGCATCCTGTGGAGGCTGAAGCGGCAGCCCTGT
GCTGGCCCCGACACTCCCATACCGCCGGCGTCACACTTCTCCTTGTCTCTGAGGGGCTAC
AGCAGCCACATGACGTACGGCATCAGCGACCACAAGCCTGTCTCCGGCACGTTCGACTTG
GAGCTGAAGCCATTGGTGTCTGCTCCGCTGATCGTCCTGATGCCCGAGGACCTGTGGACC
GTGGAAAATGACATGATGGTCAGCTACTCTTCAACCTCGGACTTCCCCAGCAGCCCGTGG
GACTGGATTGGACTGTACAAGGTGGGGCTGCGGGACGTTAATGACTACGTGTCCTATGCC
TGGGTCGGGGACAGCAAGGTCTCCTGCAGCGACAACCTGAACCAGGTTTACATCGACATC
AGCAATATCCCTACCACTGAAGATGAGTTTCTCCTCTGTTACTACAGAAACAGTCTGCGT
TCTGTGGTGGGGATAAGAAGACCCTTCCAGATCCCGCCTGGCTCCTTGAGGGAGGACCCA
CTGGGTGAAGCACAGCCACAGATCTGA
Enzyme 8 GenBank Gene ID AB036829 Link Image
Enzyme 8 GeneCard ID INPP5K Link Image
Enzyme 8 GenAtlas ID INPP5K Link Image
Enzyme 8 HGNC ID HGNC:33882 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 17p13.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Ijuin T, Mochizuki Y, Fukami K, Funaki M, Asano T, Takenawa T: Identification and characterization of a novel inositol polyphosphate 5-phosphatase. J Biol Chem. 2000 Apr 14;275(15):10870-5. [PubMed Link Image]
  2. 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]
  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. Gurung R, Tan A, Ooms LM, McGrath MJ, Huysmans RD, Munday AD, Prescott M, Whisstock JC, Mitchell CA: Identification of a novel domain in two mammalian inositol-polyphosphate 5-phosphatases that mediates membrane ruffle localization. The inositol 5-phosphatase skip localizes to the endoplasmic reticulum and translocates to membrane ruffles following epidermal growth factor stimulation. J Biol Chem. 2003 Mar 28;278(13):11376-85. Epub 2003 Jan 20. [PubMed Link Image]
  5. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6271
Enzyme 9 Name Inositol-trisphosphate 3-kinase B
Enzyme 9 Synonyms
  1. Inositol 1,4,5-trisphosphate 3-kinase B
  2. IP3 3-kinase B
  3. IP3K B
  4. InsP 3-kinase B
Enzyme 9 Gene Name ITPKB
Enzyme 9 Protein Sequence >Inositol-trisphosphate 3-kinase B
MAVYCYALNSLVIMNSANEMKSGGGPGPSGSETPPPPRRAVLSPGSVFSPGRGASFLFPP
AESLSPEEPRSPGGWRSGRRRLNSSSGSGSGSSGSSVSSPSWAGRLRGDRQQVVAAGTLS
PPGPEEAKRKLRILQRELQNVQVNQKVGMFEAHIQAQSSAIQAPRSPRLGRARSPSPCPF
RSSSQPPGRVLVQGARSEERRTKSWGEQCPETSGTDSGRKGGPSLCSSQVKKGMPPLPGR
AAPTGSEAQGPSAFVRMEKGIPASPRCGSPTAMEIDKRGSPTPGTRSCLAPSLGLFGASL
TMATEVAARVTSTGPHRPQDLALTEPSGRARELEDLQPPEALVERQGQFLGSETSPAPER
GGPRDGEPPGKMGKGYLPCGMPGSGEPEVGKRPEETTVSVQSAESSDSLSWSRLPRALAS
VGPEEARSGAPVGGGRWQLSDRVEGGSPTLGLLGGSPSAQPGTGNVEAGIPSGRMLEPLP
CWDAAKDLKEPQCPPGDRVGVQPGNSRVWQGTMEKAGLAWTRGTGVQSEGTWESQRQDSD
ALPSPELLPQDPDKPFLRKACSPSNIPAVIITDMGTQEDGALEETQGSPRGNLPLRKLSS
SSASSTGFSSSYEDSEEDISSDPERTLDPNSAFLHTLDQQKPRVSKSWRKIKNMVHWSPF
VMSFKKKYPWIQLAGHAGSFKAAANGRILKKHCESEQRCLDRLMVDVLRPFVPAYHGDVV
KDGERYNQMDDLLADFDSPCVMDCKMGIRTYLEEELTKARKKPSLRKDMYQKMIEVDPEA
PTEEEKAQRAVTKPRYMQWRETISSTATLGFRIEGIKKEDGTVNRDFKKTKTREQVTEAF
REFTKGNHNILIAYRDRLKAIRTTLEVSPFFKCHEVIGSSLLFIHDKKEQAKVWMIDFGK
TTPLPEGQTLQHDVPWQEGNREDGYLSGLNNLVDILTEMSQDAPLA
Enzyme 9 Number of Residues 946
Enzyme 9 Molecular Weight 102375.3
Enzyme 9 Theoretical pI 8.56
Enzyme 9 GO Classification
Function
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • inositol trisphosphate 3-kinase activity
  • inositol trisphosphate kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
Component
Enzyme 9 General Function Involved in inositol trisphosphate 3-kinase activity
Enzyme 9 Specific Function ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
Enzyme 9 Pathways
Enzyme 9 Reactions
  • ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate [RN:R03433]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 14329672 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P27987 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name IP3KB_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >2841 bp
ATGGCTGTGTACTGCTATGCGCTCAATAGCCTGGTGATCATGAATAGCGCCAACGAGATG
AAGAGCGGCGGCGGCCCGGGGCCCAGTGGCAGCGAGACGCCCCCGCCCCCGAGGAGGGCA
GTGCTGAGCCCCGGCAGCGTTTTCAGCCCCGGGAGAGGCGCCTCTTTCCTCTTCCCCCCA
GCCGAGTCGCTGTCCCCCGAGGAGCCCCGGAGCCCCGGGGGCTGGCGGAGCGGCCGGCGC
AGGCTGAATAGTAGCAGCGGCAGTGGCAGCGGCAGCAGCGGCAGTAGCGTGAGCAGCCCA
AGTTGGGCTGGTCGCCTGCGAGGGGACCGGCAGCAGGTGGTGGCAGCCGGTACCCTCTCC
CCGCCAGGGCCGGAGGAGGCCAAGAGGAAGCTGCGGATCTTGCAGCGCGAGTTGCAGAAC
GTGCAGGTGAACCAGAAAGTGGGCATGTTTGAGGCGCACATCCAGGCACAGAGCTCCGCC
ATTCAAGCGCCCCGCAGCCCGCGTTTGGGCAGGGCTCACTCGCCCTCCCCGTGCCCCTTC
CGCAGCAGCAGTCAGCCCCCTGGAAGGGTCCTGGTTCAGGGCGCCCGGAGCGAGGAACGG
AGGACAAAGTCCTGGGGGGAGCAATGTTCAGAGACTTCAGGAACCGACTCCGGGAGGAAA
GGAGGGCCCAGCCTATGCTCCTCGCAGGTGAAGAAAGGAATGCCACCTCTTCCCGGCCGG
GCTGCCCCTACAGGATCAGAGGCTCAGGGTCCATCCGCTTTTGTAAGGATGGAGAAGGGT
ATCCCTGCCAGTCCCCGCTGTGGCTCACCCACAGCTATGGAAATTGACAAAAGGGGCTCT
CCTACCCCGGGAACTCGGAGCTGCCTAGCTCCCTCATTGGGGCTGTTCGCCCCTAGCTTC
CCGATGGCCACGGAAGTGGCAGCGAGAGTTACATCCACTGGGCCACACCGTCCACAGGAT
CTTGCCCTCACTGAGCCGTCTGGGAGAGCCCGTGAGCTTGAGGACCTGCAGCCCCCAGAG
GCCCTGGTGGAGAGGCAGGGGCAGTTTCTGGGCAGTGAGACAAGCCCAGCCCCAGAAAGG
GGCGGGCCCCGCGATGGAGAACCCCCTGGGAAGATGGGGAAAGGATATCTGCCCTGTGGC
ATGCCGGGCTCTGGGGAGCCTGAAGTGGGCAAAAGGCCAGAGGAGACGACTGTGAGCGTG
CAAAGCGCAGAGTCCTCTGATTCCCTGAGCTGGTCCAGGCTGCCCAGGGCCCTGGCCTCC
GTAGGCCCTGAGGAGGCCCGAAGTGGGGCCCCCGTGGGCGGGGGGCGTTGGCAGCTCTCC
GACAGAGTGGAGGGAGGGTCCCCAACGCTGGGCTTGCTTGGGGGCAGCCCCTCAGCACAG
CCGGGGACCGGGAATGTGGAGGCGGGAATTCCTTCTGGCAGAATGCTGGAGCCTTTGCCC
TGTTGGGACGCTGCGAAAGATCTGAAAGAACCTCAGTGCCCTCCTGGGGACAGGGTGGGT
GTGCAGCCTGGGAACTCCAGGGTTTGGCAGGGCACCATGGAGAAAGCCGGTTTGGCTTGG
ACGCGTGGCACAGGGGTGCAATCAGAGGGGACTTGGGAAAGCCAGCGGCAGGACAGTGAT
GCCCTCCCAAGTCCGGAGCTGCTACCCCAAGATCAGGACAAGCCTTTCCTGAGGAAGGCC
TGCAGCCCCAGCAACATACCTGCTGTCATCATTACAGACATGGGCACCCAGGAGGATGGG
GCCTTGGAGGAGACGCAGGGAAGCCCTCGGGGCAACCTGCCCCTGAGGAAACTGTCCTCT
TCCTCGGCCTCCTCCACGGGCTTCTCCTCATCCTACGAAGACTCAGAGGAGGACATCTCC
AGTGACCCTGAGCGCACCCTGGACCCCAACTCAGCTTTCCTGCATACCCTGGACCAGCAG
AAACCTAGAGTGAGCAAATCATGGAGGAAGATAAAAAACATGGTGCACTGGTCTCCCTTC
GTCATGTCCTTCAAGAAGAAGTACCCCTGGATCCAGCTGGCAGGACACGCAGGGAGTTTC
AAGGCAGCTGCCAATGGCAGGATCCTGAAGAAGCACTGTGAGTCAGAGCAGCGCTGCCTG
GACCGGCTGATGGTGGATGTGCTGAGGCCCTTCGTACCTGCCTACCATGGGGATGTGGTG
AAGGACGGGGAGCGCTACAACCAGATGGACGACCTGCTGGCCGACTTCGACTCGCCCTGT
GTGATGGACTGCAAGATGGGAATCAGGACCTACCTGGAGGAGGAGCTCACGAAGGCCCGG
AAGAAGCCCAGCCTGCGGAAGGACATGTACCAGAAGATGATCGAGGTGGACCCCGAGGCC
CCCACCGAGGAGGAAAAAGCACAGCGGGCTGTGACCAAGCCACGGTACATGCAGTGGCGG
GAGACCATCAGCTCCACGGCCACCCTGGGGTTCAGGATCGAGGGAATCAAGAAAGAAGAC
GGCACCGTGAACCGGGACTTCAAGAAGACCAAAACGAGGGAGCAGGTCACCGAGGCCTTC
AGAGAGTTCACTAAAGGAAACCATAACATCCTGATCGCCTATCGGGACCGGCTGAAGGCC
ATTCGAACCACTCTAGAAGTTTCTCCCTTCTTCAAGTGCCACGAGGTCATTGGCAGCTCC
CTCCTCTTCATCCACGACAAGAAGGAACAGGCCAAAGTGTGGATGATCGACTTTGGGAAA
ACCACGCCCCTGCCTGAGGGCCAGACCCTGCAGCATGACGTCCCCTGGCAGGAGGGGAAC
CGGGAGGATGGCTACCTCTCGGGGCTCAATAACCTCGTCGACATCCTGACCGAGATGTCC
CAGGATGCCCCACTCGCCTGA
Enzyme 9 GenBank Gene ID AJ242780 Link Image
Enzyme 9 GeneCard ID ITPKB Link Image
Enzyme 9 GenAtlas ID ITPKB Link Image
Enzyme 9 HGNC ID HGNC:6179 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 1q42.13
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Dewaste V, Roymans D, Moreau C, Erneux C: Cloning and expression of a full-length cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase B. Biochem Biophys Res Commun. 2002 Feb 22;291(2):400-5. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [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. Takazawa K, Perret J, Dumont JE, Erneux C: Molecular cloning and expression of a new putative inositol 1,4,5-trisphosphate 3-kinase isoenzyme. Biochem J. 1991 Sep 15;278 ( Pt 3):883-6. [PubMed Link Image]
  5. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. 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 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6272
Enzyme 10 Name Inositol-trisphosphate 3-kinase A
Enzyme 10 Synonyms
  1. Inositol 1,4,5-trisphosphate 3-kinase A
  2. IP3 3-kinase A
  3. IP3K A
  4. InsP 3-kinase A
Enzyme 10 Gene Name ITPKA
Enzyme 10 Protein Sequence >Inositol-trisphosphate 3-kinase A
MTLPGGPTGMARPGGARPCSPGLERAPRRSVGELRLLFEARCAAVAAAAAAGEPRARGAK
RRGGQVPNGLPRAPPAPVIPQLTVTAEEPDVPPTSPGPPERERDCLPAAGSSHLQQPRRL
STSSVSSTGSSSLLEDSEDDLLSDSESRSRGNVQLEAGEDVGQKNHWQKIRTMVNLPVIS
PFKKRYAWVQLAGHTGSFKAAGTSGLILKRCSEPERYCLARLMADALRGCVPAFHGVVER
DGESYLQLQDLLDGFDGPCVLDCKMGVRTYLEEELTKARERPKLRKDMYKKMLAVDPEAP
TEEEHAQRAVTKPRYMQWREGISSSTTLGFRIEGIKKADGSCSTDFKTTRSREQVLRVFE
EFVQGDEEVLRRYLNRLQQIRDTLEVSEFFRRHEVIGSSLLFVHDHCHRAGVWLIDFGKT
TPLPDGQILDHRRPWEEGNREDGYLLGLDNLIGILASLAER
Enzyme 10 Number of Residues 461
Enzyme 10 Molecular Weight 51008.3
Enzyme 10 Theoretical pI 7.72
Enzyme 10 GO Classification
Function
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • inositol trisphosphate 3-kinase activity
  • inositol trisphosphate kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
Component
Enzyme 10 General Function Involved in inositol trisphosphate 3-kinase activity
Enzyme 10 Specific Function ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate [RN:R03433]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 32105 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P23677 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name IP3KA_HUMAN Link Image
Enzyme 10 PDB ID 1W2F Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1386 bp
ATGACCCTGCCCGGGGGCCCAACGGGCATGGCGCGGCCGGGGGGCGCGAGGCCCTGCAGC
CCGGGGCTGGAGCGGGCCCCGCGCCGGAGTGTCGGGGAGCTGCGCCTGCTCTTCGAGGCG
CGCTGTGCGGCGGTCGCTGCGGCCGCCGCCGCGGGGGAGCCCCGGGCCCGCGGGGCCAAG
CGGCGTGGGGGACAGGTCCCCAACGGGCTTCCGCGGGCTCCCCCGGCCCCGGTGATCCCT
CAGCTGACCGTGACAGCCGAGGAGCCCGACGTGCCCCCGACCAGCCCTGGGCCGCCGGAG
CGGGAGAGGGACTGCCTCCCGGCAGCGGGCTCTTCGCACCTGCAGCAGCCGCGCCGCCTT
TCCACCTCGTCGGTCTCCTCCACTGGCTCCTCGTCGCTGCTCGAGGACTCGGAGGACGAC
CTGCTGAGCGACAGTGAGAGCCGGAGCCGCGGCAACGTGCAGCTGGAAGCGGGCGAGGAC
GTGGGTCAGAAAAACCACTGGCAGAAGATCCGGACCATGGTCAATCTGCCGGTCATAAGC
CCTTTCAAGAAGCGCTACGCCTGGGTGCAGCTGGCAGGGCACACTGGGAGTTTTAAGGCG
GCGGGCACCAGCGGGCTGATCCTGAAGCGCTGCTCGGAGCCGGAGCGCTACTGCCTGGCG
CGGCTGATGGCTGACGCGCTGCGCGGCTGCGTGCCTGCCTTCCACGGCGTGGTGGAGCGC
GACGGCGAAAGCTACCTGCAGCTGCAGGACCTGCTCGATGGCTTCGACGGACCTTGTGTG
CTCGACTGCAAAATGGGCGTCAGGACTTACCTAGAGGAGGAGCTGACCAAGGCCCGTGAG
CGGCCCAAGCTGCGGAAGGACATGTACAAGAAAATGCTGGCGGTGGATCCTGAAGCTCCC
ACGGAGGAGGAGCACGCGCAGCGCGCCGTCACCAAGCCGCGCTACATGCAGTGGCGGGAA
GGCATCAGCTCCAGCACCACCCTCGGCTTCCGCATCGAGGGCATCAAGAAAGCGGACGGC
TCCTGCAGCACCGACTTCAAGACTACGCGAAGCCGAGAGCAGGTGCTTCGCGTCTTTGAA
GAGTTTGTGCAAGGAGATGAGGAAGTGCTGAGGCGGTATCTGAACCGCCTGCAGCAGATC
CGGGACACCCTGGAGGTATCCGAGTTCTTCAGGAGGCACGAGGTGATCGGCAGCTCGCTC
CTCTTTGTGCACGATCACTGCCATCGCGCCGGCGTGTGGCTCATCGACTTCGGCAAGACC
ACGCCCCTCCCCGATGGCCAGATCCTGGACCACCGGCGGCCCTGGGAGGAGGGCAACCGC
GAGGACGGCTATTTGCTGGGGCTGGACAATCTCATTGGCATCCTGGCCAGCCTGGCTGAG
AGATGA
Enzyme 10 GenBank Gene ID X54938 Link Image
Enzyme 10 GeneCard ID ITPKA Link Image
Enzyme 10 GenAtlas ID ITPKA Link Image
Enzyme 10 HGNC ID HGNC:6178 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 15q15.1
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Takazawa K, Perret J, Dumont JE, Erneux C: Molecular cloning and expression of a human brain inositol 1,4,5-trisphosphate 3-kinase. Biochem Biophys Res Commun. 1991 Jan 31;174(2):529-35. [PubMed Link Image]
  2. Takazawa K, Perret J, Dumont JE, Erneux C: Human brain inositol 1,4,5-trisphosphate 3-kinase cDNA sequence. Nucleic Acids Res. 1990 Dec 11;18(23):7141. [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. Gonzalez B, Schell MJ, Letcher AJ, Veprintsev DB, Irvine RF, Williams RL: Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase. Mol Cell. 2004 Sep 10;15(5):689-701. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6582
Enzyme 11 Name Inositol polyphosphate multikinase
Enzyme 11 Synonyms
  1. Inositol 1,3,4,6-tetrakisphosphate 5-kinase
Enzyme 11 Gene Name IPMK
Enzyme 11 Protein Sequence >Inositol polyphosphate multikinase
MATEPPSPLRVEAPGPPEMRTSPAIESTPEGTPQPAGGRLRFLNGCVPLSHQVAGHMYGK
DKVGILQHPDGTVLKQLQPPPRGPRELEFYNMVYAADCFDGVLLELRKYLPKYYGIWSPP
TAPNDLYLKLEDVTHKFNKPCIMDVKIGQKSYDPFASSEKIQQQVSKYPLMEEIGFLVLG
MRVYHVHSDSYETENQHYGRSLTKETIKDGVSRFFHNGYCLRKDAVAASIQKIEKILQWF
ENQKQLNFYASSLLFVYEGSSQPTTTKLNDRTLAEKFLSKGQLSDTEVLEYNNNFHVLSS
TANGKIESSVGKSLSKMYARHRKIYTKKHHSQTSLKVENLEQDNGWKSMSQEHLNGNVLS
QLEKVFYHLPTGCQEIAEVEVRMIDFAHVFPSNTIDEGYVYGLKHLISVLRSILDN
Enzyme 11 Number of Residues 416
Enzyme 11 Molecular Weight 47221.5
Enzyme 11 Theoretical pI 7.71
Enzyme 11 GO Classification
Function
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • inositol trisphosphate 3-kinase activity
  • inositol trisphosphate kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
Component
Enzyme 11 General Function Involved in inositol trisphosphate 3-kinase activity
Enzyme 11 Specific Function Inositol phosphate kinase with a broad substrate specificity. Has a preference for inositol-1,4,5-trisphosphate (Ins(1,4,5)P3) and inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4)
Enzyme 11 Pathways
Enzyme 11 Reactions
  • (1) (1a) ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate [RN:R05800]
  • (2) (1b) ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate [RN:R05801]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 22532105 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q8NFU5 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name IPMK_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1251 bp
ATGGCAACAGAGCCACCATCCCCCCTCCGGGTCGAGGCGCCGGGCCCCCCAGAAATGCGG
ACCTCACCGGCGATCGAGTCCACCCCTGAGGGCACCCCGCAGCCGGCGGGCGGCAGACTC
CGCTTCCTCAACGGCTGCGTGCCCCTCTCGCATCAGGTGGCCGGGCACATGTACGGGAAG
GACAAAGTGGGTATACTGCAACATCCAGATGGCACAGTTTTGAAACAGTTACAACCACCT
CCAAGGGGCCCAAGAGAGCTGGAATTCTATAATATGGTTTATGCTGCTGACTGTTTTGAT
GGTGTTCTTCTAGAGCTACGAAAATATTTGCCAAAATATTATGGCATCTGGTCACCTCCC
ACTGCACCAAACGATTTATACCTAAAACTGGAAGATGTGACCCATAAATTTAATAAGCCC
TGTATAATGGATGTAAAGATAGGGCAAAAAAGCTATGATCCTTTTGCCTCATCTGAGAAG
ATTCAGCAACAGGTCAGCAAGTACCCATTAATGGAAGAGATTGGGTTCTTGGTGCTTGGC
ATGAGGGTTTATCATGTTCATTCCGATAGCTATGAGACAGAAAACCAGCATTACGGAAGA
AGCTTAACAAAAGAAACTATAAAGGATGGAGTCTCCAGATTTTTTCATAATGGGTACTGC
TTAAGAAAAGATGCTGTTGCTGCCAGTATTCAGAAGATTGAGAAAATTCTGCAGTGGTTT
GAAAACCAGAAGCAGCTTAATTTTTACGCAAGTTCATTACTCTTTGTTTATGAAGGTTCA
TCTCAGCCAACCACTACAAAATTGAATGACAGAACTTTGGCAGAAAAGTTTTTGTCCAAA
GGACAACTGTCAGACACAGAAGTACTAGAGTACAATAATAACTTTCATGTGTTAAGTTCC
ACAGCTAATGGAAAAATAGAGTCTTCAGTGGGCAAAAGCTTGTCCAAGATGTATGCGCGT
CACAGGAAAATATATACAAAAAAGCATCACAGTCAGACTTCATTGAAAGTTGAAAATCTG
GAGCAAGACAATGGGTGGAAAAGCATGTCACAGGAACATTTAAATGGAAATGTACTTTCC
CAACTGGAAAAAGTTTTCTACCATCTTCCCACTGGTTGCCAAGAGATTGCTGAAGTAGAA
GTGCGAATGATAGATTTTGCTCATGTGTTCCCTAGCAACACAATAGATGAGGGATATGTT
TATGGGCTAAAGCATTTAATTTCTGTACTTCGAAGTATTTTAGACAATTGA
Enzyme 11 GenBank Gene ID AF432853 Link Image
Enzyme 11 GeneCard ID IPMK Link Image
Enzyme 11 GenAtlas ID IPMK Link Image
Enzyme 11 HGNC ID HGNC:20739 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 10q21.1
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Nalaskowski MM, Deschermeier C, Fanick W, Mayr GW: The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization. Biochem J. 2002 Sep 1;366(Pt 2):549-56. [PubMed Link Image]
  2. Chang SC, Miller AL, Feng Y, Wente SR, Majerus PW: The human homolog of the rat inositol phosphate multikinase is an inositol 1,3,4,6-tetrakisphosphate 5-kinase. J Biol Chem. 2002 Nov 15;277(46):43836-43. Epub 2002 Sep 9. [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. 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]
  5. 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 8356
Enzyme 12 Name Inositol 1,4,5-trisphosphate receptor type 1
Enzyme 12 Synonyms
  1. IP3 receptor isoform 1
  2. IP3R 1
  3. InsP3R1
  4. Type 1 inositol 1,4,5-trisphosphate receptor
  5. Type 1 InsP3 receptor
Enzyme 12 Gene Name ITPR1
Enzyme 12 Protein Sequence >Inositol 1,4,5-trisphosphate receptor type 1
MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPETGDLNNPPKKFRDCLFKL
CPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNV
IQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGD
KVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVV
RLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWN
SLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPE
GNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGT
SPVKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDL
VYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEE
LGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLH
NNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPT
NADILIETKLVLSRFEFEGVSSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDA
KEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRA
SFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEF
VEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVH
VTTIFPISKMAKGEENKGNNDVEKLKSSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAA
PEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQTSE
TSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMH
DYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSE
LWVYKGQGPDETMDGASGENEHKKTEEGNNKPQKHESTSSYNYRVVKEILIRLSKLCVQE
SASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQ
NQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIK
FLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSP
LMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCY
VDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFF
SSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAI
PVDLDSQVNNLFLKSHSIVQKTAMNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSAL
EDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKL
CIKVLQTLREMMTKDRGYGEKLISIDELDNAELPPAPDSENSTEELEPSPPLRQLEDHKR
GEALRQVLVNRYYGNVRPSGRRESLTSFGNGPLSAGGPGKPGGGGGGSGSSSMSRGEMSL
AEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKK
SEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEV
RDQLLEASAATRKAFTTFRREADPDDHYQPGEGTQATADKAKDDLEMSAVITIMQPILRF
LQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVAL
INQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNA
SKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNV
GHNIYILAHQLARHNKELQSMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPV
PSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARN
MSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHG
IRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEF
LYHLLYLVICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILV
YLFSIVGYLFFKDDFILEVDRLPNETAVPETGESLASEFLFSDVCRVESGENCSSPAPRE
ELVPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLL
FFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHI
KEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIKERNLDWFPRMRAMSLVSSDSEGEQ
NELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA
Enzyme 12 Number of Residues 2758
Enzyme 12 Molecular Weight 313942.4
Enzyme 12 Theoretical pI 5.91
Enzyme 12 GO Classification
Function
  • calcium channel activity
  • cation channel activity
  • inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity
  • intracellular ligand-gated ion channel activity
  • ion channel activity
  • ion transmembrane transporter activity
  • ligand-gated ion channel activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • calcium ion transport
  • cation transport
  • di-, tri-valent inorganic cation transport
  • divalent metal ion transport
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • endoplasmic reticulum
  • intracellular membrane-bounded organelle
  • membrane
  • membrane-bounded organelle
  • organelle
Enzyme 12 General Function Involved in calcium channel activity
Enzyme 12 Specific Function Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5- trisphosphate
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 2283-2303 2315-2335 2362-2382 2406-2426 2449-2469 2578-2598
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 269954692 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q14643 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name ITPR1_HUMAN Link Image
Enzyme 12 PDB ID 1N4K Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >8088 bp
ATGTCTGACAAAATGTCTAGCTTCCTACATATTGGAGACATTTGTTCTCTGTACGCGGAG
GGATCGACAAATGGATTTATTAGCACCTTGGGCCTGGTTGATGATCGTTGTGTTGTACAG
CCAGAAACCGGGGACCTTAACAATCCACCTAAGAAATTCAGAGACTGCCTCTTTAAGCTA
TGTCCCATGAACCGCTACTCTGCCCAAAAGCAGTTCTGGAAAGCCGCTAAGCCTGGGGCC
AACAGCACCACAGACGCAGTGCTACTCAACAAACTGCACCACGCTGCAGACTTGGAAAAG
AAGCAGAATGAGACAGAAAACAGGAAATTGCTGGGGACCGTAATCCAGTATGGCAATGTG
ATCCAGCTCCTGCATTTGAAAAGTAATAAATACCTAACAGTGAATAAGAGGCTTCCTGCT
CTGTTGGAGAAGAATGCCATGAGAGTCACATTGGACGAGGCTGGAAATGAAGGGTCCTGG
TTTTATATTCAGCCATTCTACAAGCTGCGATCCATTGGAGACAGCGTGGTCATAGGTGAC
AAGGTGGTTCTGAACCCCGTCAATGCTGGTCAGCCCCTACATGCTAGCAGCCATCAACTG
GTAGATAACCCAGGCTGCAATGAGGTCAATTCCGTCAACTGCAATACAAGCTGGAAAATA
GTCCTTTTCATGAAATGGAGTGATAACAAAGACGACATATTAAAGGGGGGTGACGTGGTG
AGGCTGTTTCATGCTGAGCAGGAGAAGTTTCTCACCTGTGACGAACACAGGAAGAAGCAG
CACGTCTTCCTGAGAACCACGGGCCGGCAGTCGGCCACATCTGCCACCAGTTCAAAAGCC
CTGTGGGAGGTGGAGGTGGTCCAGCATGACCCATGTCGGGGCGGAGCAGGGTATTGGAAC
AGCCTTTTCCGTTTCAAGCATCTGGCCACGGGGCATTACTTGGCAGCAGAGGTGGACCCT
GATCAGGACGCCTCTCGAAGTAGGTTGCGGAATGCCCAAGAAAAGATGGTATACTCCCTG
GTCTCTGTGCCTGAAGGCAATGACATCTCCTCCATTTTCGAGCTAGATCCCACCACTCTG
CGTGGAGGTGACAGCCTTGTCCCAAGGAACTCTTATGTTCGGCTCAGACACCTATGTACT
AATACCTGGGTTCACAGCACAAATATTCCTATTGACAAGGAAGAAGAAAAGCCCGTGATG
CTGAAAATTGGCACCTCTCCTGTGAAGGAGGATAAGGAAGCATTTGCCATAGTTCCGGTT
TCTCCTGCTGAAGTTCGGGACCTGGACTTTGCCAATGATGCCAGCAAGGTGCTGGGCTCC
ATTGCTGGGAAGCTAGAGAAGGGCACCATCACCCAGAATGAAAGGAGGTCTGTAACCAAG
CTGCTAGAAGATTTGGTTTACTTCGTCACTGGTGGAACTAATTCTGGTCAAGATGTTCTC
GAAGTTGTCTTCTCCAAGCCCAACAGAGAACGGCAGAAACTGATGAGAGAACAGAATATT
CTCAAGCAGATCTTCAAGTTGTTACAAGCCCCATTCACAGACTGCGGTGATGGCCCAATG
CTTCGGCTGGAAGAGCTCGGGGACCAGCGGCACGCTCCTTTCAGACACATCTGCCGGCTC
TGCTACAGGGTGCTGAGACACTCGCAGCAAGACTACAGGAAGAACCAGGAGTATATAGCC
AAGCAGTTTGGCTTCATGCAGAAGCAGATTGGCTATGATGTGTTGGCTGAAGACACTATC
ACTGCCCTGCTCCACAATAATCGGAAACTCCTGGAAAAACACATTACCGCGGCAGAGATT
GACACATTTGTCAGCCTGGTGCGAAAGAACAGGGAGCCCAGATTCTTAGATTACCTCTCC
GACCTCTGTGTCTCCATGAACAAATCAATTCCAGTGACCCAGGAACTGATATGTAAAGCT
GTGCTGAACCCCACCAACGCTGACATCCTGATTGAGACCAAGTTGGTTCTTTCTCGTTTT
GAATTTGAAGGTGTCTCTTCCACTGGAGAGAATGCTCTGGAGGCAGGAGAAGACGAGGAA
GAGGTGTGGCTGTTTTGGAGGGACAGCAACAAAGAGATTCGCAGCAAGAGTGTGAGGGAA
TTGGCTCAGGATGCTAAAGAAGGGCAGAAGGAGGACCGAGACGTTCTCAGCTACTACAGA
TATCAGCTGAACCTCTTTGCGAGGATGTGTCTGGACCGCCAATACCTGGCCATCAACGAA
ATCTCAGGCCAGCTGGATGTCGATCTCATTCTCCGCTGCATGTCTGACGAGAACCTGCCC
TATGACCTCAGGGCGTCCTTCTGCCGCCTCATGCTTCACATGCATGTGGACCGAGATCCC
CAGGAACAAGTCACCCCCGTGAAATATGCCCGCCTCTGGTCGGAGATTCCCTCGGAGATC
GCCATTGACGACTATGATAGTAGTGGAGCTTCCAAAGATGAAATTAAGGAGAGATTTGCT
CAGACCATGGAGTTTGTGGAGGAGTATTTAAGAGATGTGGTTTGTCAGAGGTTCCCTTTC
TCTGATAAAGAGAAGAATAAGCTTACGTTTGAGGTTGTAAATTTAGCTAGGAATCTCATA
TACTTTGGTTTCTACAACTTCTCTGACCTTCTACGATTAACTAAGATCCTTCTGGCCATA
TTGGACTGTGTACATGTGACAACAATCTTCCCCATTAGCAAGATGGCGAAAGGAGAAGAG
AATAAAGGCAGTAACGTGATGAGATCTATTCATGGCGTGGGAGAGCTGATGACCCAGGTG
GTGCTCCGGGGAGGAGGCTTTTTGCCCATGACTCCCATGGCTGCTGCCCCTGAAGGCAAT
GTGAAGCAGGCAGAGCCTGAGAAGGAGGACATCATGGTCATGGACACCAAGCTGAAGATC
ATTGAGATACTCCAGTTTATTTTGAATGTGAGGTTGGATTATAGGATCTCCTGCCTCCTG
TGTATATTTAAGCGAGAGTTTGATGAAAGCAATTCCCAGACTTCAGAAACATCCTCCGGA
AACAGCAGCCAAGAAGGGCCAAGTAATGTACCAGGTGCTCTTGACTTTGAACACATTGAA
GAACAAGCAGAAGGCATCTTTGGAGGAAGTGAGGAGAACACCCCACTGGACTTGGATGAC
CACGGCGGCAGAACCTTTCTCCGTGTCCTGCTCCACTTGACGATGCATGACTACCCACCC
CTGGTGTCAGGGGCCCTGCAGCTCCTCTTCCGGCACTTCAGCCAGAGGCAGGAGGTGCTC
CAGGCCTTCAAACAGGTTCAACTGCTGGTTACCAGCCAAGATGTGGACAACTACAAACAG
ATCAAACAAGACTTGGATCAACTGAGGTCCATCGTGGAAAAGTCAGAGCTTTGGGTGTAC
AAAGGGCAGGGCCCCGATGAGACTATGGATGGTGCATCTGGAGAAAATGAACATAAGAAA
ACGGAGGAGGGAAATAACAAGCCACAAAAGCATGAAAGCACCAGCAGCTACAACTACAGA
GTGGTCAAAGAGATTTTGATTCGGCTTAGCAAACTCTGTGTTCAAGAGAGTGCCTCAGTG
AGAAAGAGCAGGAAGCAGCAACAGCGTCTGCTCCGGAACATGGGCGCGCACGCCGTGGTG
CTGGAGCTGCTGCAGATTCCCTATGAGAAGGCCGAAGATACCAAGATGCAAGAGATAATG
AGGTTGGCTCATGAATTTTTGCAGAATTTCTGCGCAGGCAACCAGCAGAATCAAGCTTTG
CTACATAAACACATAAACCTGTTTCTCAACCCAGGGATCCTGGAGGCAGTAACCATGCAG
CACATCTTCATGAACAATTTCCAGCTTTGCAGTGAGATCAACGAGAGAGTTGTTCAGCAC
TTCGTTCACTGCATAGAGACTCACGGTCGGAATGTCCAGTATATAAAGTTCTTACAGACA
ATTGTCAAGGCAGAAGGGAAATTTATTAAAAAATGCCAAGACATGGTTATGGCCGAGCTG
GTCAATTCGGGAGAGGATGTCCTCGTGTTCTACAACGACAGAGCCTCTTTCCAGACTCTG
ATCCAGATGATGCGGTCAGAACGGGATCGGATGGATGAGAACAGCCCTCTCATGTACCAC
ATCCACTTGGTCGAGCTCCTGGCTGTGTGCACGGAGGGTAAGAATGTCTACACAGAGATC
AAGTGCAACTCCCTGCTCCCGCTGGATGACATCGTTCGCGTGGTGACCCACGAGGACTGC
ATCCCTGAGGTTAAAATTGCATACATTAACTTCCTGAATCACTGCTATGTGGATACAGAG
GTGGAAATGAAGGAGATTTATACCAGCAATCACATGTGGAAATTGTTTGAGAATTTCCTT
GTAGACATCTGCAGGGCCTGTAACAACACTAGTGACAGGAAACATGCAGACTCGATTTTG
GAGAAGTATGTCACCGAAATCGTCATGAGTATTGTTACTACTTTCTTCAGCTCTCCCTTC
TCAGACCAGAGTACGACTTTGCAGACTCGCCAGCCTGTCTTTGTGCAACTGCTGCAAGGC
GTGTTCAGGGTTTACCACTGCAACTGGTTAATGCCAAGCCAAAAAGCCTCCGTGGAGAGC
TGTATTCGGGTGCTGTCTGATGTAGCCAAGAGCCGGGCCATTGCCATTCCCGTGGACCTG
GACAGCCAAGTCAACAACCTCTTTCTCAAGTCCCACAGCATTGTGCAGAAAACAGCCATG
AACTGGCGGCTCTCAGCCCGCAATGCCGCACGCAGGGACTCTGTTCTGGCAGCTTCCAGA
GACTACCGGAATATCATTGAGAGATTGCAGGACATCGTCTCCGCGCTGGAGGACCGTCTC
AGGCCCCTGGTGCAGGCAGAGTTATCTGTGCTCGTGGATGTTCTCCACAGACCCGAGCTG
CTTTTCCCAGAGAACACAGACGCCAGAAGGAAATGTGAAAGTGGCGGTTTCATTTGCAAG
TTAATAAAGCATACAAAACAGCTGCTAGAAGAAAATGAAGAGAAGCTCTGCATTAAGGTC
CTACAGACCCTGAGGGAAATGATGACCAAAGATAGAGGCTATGGAGAAAAGGGTGAGGCG
CTCAGGCAAGTTCTGGTCAACCGTTACTATGGAAACGTCAGACCTTCGGGACGAAGAGAG
AGCCTTACCAGCTTTGGCAATGGCCCACTGTCAGCAGGAGGACCCGGCAAGCCCGGGGGA
GGAGGGGGAGGTTCCGGATCCAGCTCTATGAGCAGGGGTGAGATGAGTCTGGCCGAGGTT
CAGTGTCACCTTGACAAGGAGGGGGCTTCCAATCTAGTTATCGACCTCATCATGAACGCA
TCCAGTGACCGAGTGTTCCATGAAAGCATTCTCCTGGCCATTGCCCTTCTGGAAGGAGGC
AACACCACCATCCAGCACTCCTTTTTCTGTCGCTTGACAGAAGATAAGAAGTCAGAGAAA
TTCTTTAAGGTGTTTTATGACCGGATGAAGGTGGCCCAGCAAGAAATCAAAGCAACAGTG
ACAGTGAACACCAGTGACTTGGGAAATAAAAAGAAAGACGATGAGGTAGACAGGGATGCC
CCATCACGGAAAAAAGCTAAAGAGCCCACAACACAGATAACAGAAGAGGTCCGGGATCAG
CTCCTGGAGGCCTCCGCTGCCACCAGGAAAGCCTTCACCACTTTCAGGAGGGAGGCTGAT
CCCGACGACCACTACCAGCCTGGAGAGGGCACCCAGGCCACTGCCGACAAGGCCAAGGAC
GACCTGGAGATGAGCGCGGTCATCACCATCATGCAGCCCATCCTCCGCTTCCTTCAGCTC
CTGTGTGAAAACCACAACCGAGACCTGCAGAACTTCCTCCGTTGCCAAAATAACAAGACC
AACTACAATTTGGTATGTGAGACCCTGCAGTTTCTGGACTGTATTTGTGGAAGCACAACT
GGAGGCCTTGGTCTTCTGGGCTTGTATATAAATGAAAAGAACGTAGCGCTTATCAACCAA
ACCCTGGAAAGTCTGACCGAATACTGTCAAGGACCTTGCCATGAGAACCAGAACTGCATA
GCCACCCATGAATCCAATGGCATTGACATCATCACAGCCCTGATCCTCAATGATATCAAT
CCTTTGGGAAAGAAGAGGATGGACCTTGTGTTAGAACTGAAGAACAATGCCTCGAAGTTG
CTCCTGGCCATCATGGAAAGCAGGCACGACAGTGAAAACGCAGAGAGGATACTTTATAAC
ATGAGGCCCAAGGAACTGGTGGAAGTGATCAAGAAAGCCTACATGCAAGGTGAAGTGGAA
TTTGAGGATGGAGAAAACGGTGAGGATGGGGCGGCGTCCCCCAGGAACGTGGGGCACAAC
ATCTACATATTAGCCCATCAGTTGGCTCGGCATAACAAAGAACTTCAGAGCATGCTGAAA
CCTGGTGGCCAAGTGGACGGAGATGAAGCCCTGGAGTTTTATGCCAAGCACACGGCGCAG
ATAGAGATTGTCAGATTAGACCGAACAATGGAACAGATAGTCTTTCCCGTGCCCAGCATA
TGTGAATTCCTAACCAAGGAGTCAAAACTACGAATTTACTATACTACAGAGAGAGACGAA
CAAGGCAGCAAAATCAATGATTTCTTTCTGCGGTCTGAAGACCTCTTCAATGAAATGAAT
TGGCAGAAGAAACTGAGAGCCCAGCCCGTGTTGTACTGGTGTGCCCGCAACATGTCTTTC
TGGAGCAGCATTTCGTTTAACCTGGCCGTCCTGATGAACCTGCTGGTGGCGTTTTTCTAC
CCGTTTAAGGGAGTCCGAGGAGGAACCCTGGAGCCCCACTGGTCGGGACTCCTGTGGACA
GCCATGCTCATCTCTCTGGCCATCGTCATTGCCCTCCCCAAGCCCCATGGCATCCGGGCC
TTAATTGCCTCCACAATTCTACGACTGATATTTTCAGTCGGGTTACAACCCACGTTGTTT
CTTCTGGGCGCTTTCAATGTATGCAATAAAATCATCTTTCTAATGAGCTTTGTGGGCAAC
TGTGGGACATTCACAAGAGGCTACCGAGCCATGGTTCTGGATGTTGAGTTCCTCTATCAT
TTGTTGTATCTGGTGATCTGTGCCATGGGGCTCTTTGTCCATGAATTCTTCTACAGTCTG
CTGCTTTTTGATTTAGTGTACAGAGAAGAGACTTTGCTTAATGTCATTAAAAGTGTCACT
CGCAATGGACGGTCCATCATCCTGACAGCAGTTCTGGCTCTGATCCTCGTTTACCTGTTC
TCAATAGTGGGCTATCTTTTCTTCAAGGATGACTTTATCTTGGAAGTAGATAGGCTGCCC
AATGAAACAGCTGTTCCAGAAACCGGCGAGAGTTTGGCAAGCGAGTTCCTGTTCTCCGAT
GTGTGTAGGGTGGAGAGTGGGGAGAACTGCTCCTCTCCTGCACCCAGAGAAGAGCTGGTC
CCTGCAGAAGAGACGGAACAGGATAAAGAGCACACATGTGAGACGCTGCTGATGTGCATT
GTCACTGTGCTGAGTCACGGGCTGCGGAGCGGGGGTGGAGTAGGAGATGTACTCAGGAAG
CCGTCCAAAGAGGAACCCCTGTTTGCTGCTAGAGTTATTTATGACCTCTTGTTCTTCTTC
ATGGTCATCATCATTGTTCTTAACCTGATTTTTGGGGTTATCATTGACACTTTTGCTGAC
CTGAGGAGTGAGAAGCAGAAGAAGGAAGAGATCTTGAAGACCACGTGCTTTATCTGTGGC
TTGGAAAGAGACAAGTTTGACAACAAGACTGTCACCTTTGAAGAGCACATCAAGGAAGAA
CACAACATGTGGCACTATCTGTGCTTCATCGTCCTGGTGAAAGTAAAGGACTCCACCGAA
TATACTGGGCCTGAGAGTTACGTGGCAGAAATGATCAAGGAAAGAAACCTTGACTGGTTC
CCCAGGATGAGAGCCATGTCATTGGTCAGCAGTGATTCTGAAGGAGAACAGAATGAGCTG
AGAAACCTGCAGGAGAAGCTGGAGTCCACCATGAAACTTGTCACGAACCTTTCTGGCCAG
CTGTCGGAATTAAAGGATCAGATGACAGAACAAAGGAAGCAGAAACAAAGAATTGGTCTT
CTAGGACATCCTCCTCACATGAATGTCAACCCACAACAACCAGCATAA
Enzyme 12 GenBank Gene ID Not Available
Enzyme 12 GeneCard ID ITPR1 Link Image
Enzyme 12 GenAtlas ID ITPR1 Link Image
Enzyme 12 HGNC ID HGNC:6180 Link Image
Enzyme 12 Chromosome Location 3
Enzyme 12 Locus 3p26.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Yamada N, Makino Y, Clark RA, Pearson DW, Mattei MG, Guenet JL, Ohama E, Fujino I, Miyawaki A, Furuichi T, et al.: Human inositol 1,4,5-trisphosphate type-1 receptor, InsP3R1: structure, function, regulation of expression and chromosomal localization. Biochem J. 1994 Sep 15;302 ( Pt 3):781-90. [PubMed Link Image]
  2. Harnick DJ, Jayaraman T, Ma Y, Mulieri P, Go LO, Marks AR: The human type 1 inositol 1,4,5-trisphosphate receptor from T lymphocytes. Structure, localization, and tyrosine phosphorylation. J Biol Chem. 1995 Feb 10;270(6):2833-40. [PubMed Link Image]
  3. Nucifora FC Jr, Li SH, Danoff S, Ullrich A, Ross CA: Molecular cloning of a cDNA for the human inositol 1,4,5-trisphosphate receptor type 1, and the identification of a third alternatively spliced variant. Brain Res Mol Brain Res. 1995 Sep;32(2):291-6. [PubMed Link Image]
  4. Yan J, Khanna KK, Lavin MF: Induction of inositol 1,4,5 trisphosphate receptor genes by ionizing radiation. Int J Radiat Biol. 1996 May;69(5):539-46. [PubMed Link Image]
  5. Yang J, McBride S, Mak DO, Vardi N, Palczewski K, Haeseleer F, Foskett JK: Identification of a family of calcium sensors as protein ligands of inositol trisphosphate receptor Ca(2+) release channels. Proc Natl Acad Sci U S A. 2002 May 28;99(11):7711-6. [PubMed Link Image]
  6. Kasri NN, Holmes AM, Bultynck G, Parys JB, Bootman MD, Rietdorf K, Missiaen L, McDonald F, De Smedt H, Conway SJ, Holmes AB, Berridge MJ, Roderick HL: Regulation of InsP3 receptor activity by neuronal Ca2+-binding proteins. EMBO J. 2004 Jan 28;23(2):312-21. Epub 2003 Dec 18. [PubMed Link Image]
  7. Higo T, Hattori M, Nakamura T, Natsume T, Michikawa T, Mikoshiba K: Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44. Cell. 2005 Jan 14;120(1):85-98. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Antl M, von Bruhl ML, Eiglsperger C, Werner M, Konrad I, Kocher T, Wilm M, Hofmann F, Massberg S, Schlossmann J: IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation. Blood. 2007 Jan 15;109(2):552-9. Epub 2006 Sep 21. [PubMed Link Image]
  10. van de Leemput J, Chandran J, Knight MA, Holtzclaw LA, Scholz S, Cookson MR, Houlden H, Gwinn-Hardy K, Fung HC, Lin X, Hernandez D, Simon-Sanchez J, Wood NW, Giunti P, Rafferty I, Hardy J, Storey E, Gardner RJ, Forrest SM, Fisher EM, Russell JT, Cai H, Singleton AB: Deletion at ITPR1 underlies ataxia in mice and spinocerebellar ataxia 15 in humans. PLoS Genet. 2007 Jun;3(6):e108. Epub 2007 May 16. [PubMed Link Image]
  11. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  12. 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]
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  14. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  15. 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 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 8839
Enzyme 13 Name Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2
Enzyme 13 Synonyms
  1. Inositol polyphosphate phosphatase-like protein 1
  2. INPPL-1
  3. Protein 51C
  4. SH2 domain-containing inositol-5'-phosphatase 2
  5. SH2 domain-containing inositol phosphatase 2
  6. SHIP-2
Enzyme 13 Gene Name INPPL1
Enzyme 13 Protein Sequence >Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2
MASACGAPGPGGALGSQAPSWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCV
LYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVEGE
REPDPPDDRDASDGEDEKPPLPPRSGSTSISAPTGPSSPLPAPETPTAPAAESAPNGLST
VSHDYLKGSYGLDLEAVRGGASHLPHLTRTLATSCRRLHSEVDKVLSGLEILSKVFDQQS
SPMVTRLLQQQNLPQTGEQELESLVLKLSVLKDFLSGIQKKALKALQDMSSTAPPAPQPS
TRKAKTIPVQAFEVKLDVTLGDLTKIGKSQKFTLSVDVEGGRLVLLRRQRDSQEDWTTFT
HDRIRQLIKSQRVQNKLGVVFEKEKDRTQRKDFIFVSARKREAFCQLLQLMKNKHSKQDE
PDMISVFIGTWNMGSVPPPKNVTSWFTSKGLGKTLDEVTVTIPHDIYVFGTQENSVGDRE
WLDLLRGGLKELTDLDYRPIAMQSLWNIKVAVLVKPEHENRISHVSTSSVKTGIANTLGN
KGAVGVSFMFNGTSFGFVNCHLTSGNEKTARRNQNYLDILRLLSLGDRQLNAFDISLRFT
HLFWFGDLNYRLDMDIQEILNYISRKEFEPLLRVDQLNLEREKHKVFLRFSEEEISFPPT
YRYERGSRDTYAWHKQKPTGVRTNVPSWCDRILWKSYPETHIICNSYGCTDDIVTSDHSP
VFGTFEVGVTSQFISKKGLSKTSDQAYIEFESIEAIVKTASRTKFFIEFYSTCLEEYKKS
FENDAQSSDNINFLKVQWSSRQLPTLKPILADIEYLQDQHLLLTVKSMDGYESYGECVVA
LKSMIGSTAQQFLTFLSHRGEETGNIRGSMKVRVPTERLGTRERLYEWISIDKDEAGAKS
KAPSVSRGSQEPRSGSRKPAFTEASCPLSRLFEEPEKPPPTGRPPAPPRAAPREEPLTPR
LKPEGAPEPEGVAAPPPKNSFNNPAYYVLEGVPHQLLPPEPPSPARAPVPSATKNKVAIT
VPAPQLGHHRHPRVGEGSSSDEESGGTLPPPDFPPPPLPDSAIFLPPSLDPLPGPVVRGR
GGAEARGPPPPKAHPRPPLPPGPSPASTFLGEVASGDDRSCSVLQMAKTLSEVDYAPAGP
ARSALLPGPLELQPPRGLPSDYGRPLSFPPPRIRESIQEDLAEEAPCLQGGRASGLGEAG
MSAWLRAIGLERYEEGLVHNGWDDLEFLSDITEEDLEEAGVQDPAHKRLLLDTLQLSK
Enzyme 13 Number of Residues 1258
Enzyme 13 Molecular Weight 138597.5
Enzyme 13 Theoretical pI 6.49
Enzyme 13 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphatase activity
  • phosphoric ester hydrolase activity
  • protein binding
Process
Component
Enzyme 13 General Function Involved in inositol or phosphatidylinositol phosphatase activity
Enzyme 13 Specific Function Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol- 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling. Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 222136583 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID O15357 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name SHIP2_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >3777 bp
ATGGCCTCGGCCTGCGGGGCGCCGGGCCCGGGGGGCGCCCTGGGCAGCCAGGCCCCCTCC
TGGTACCACCGCGACCTGAGCCGGGCGGCCGCGGAGGAGCTGCTGGCCCGGGCGGGCCGC
GATGGCAGCTTCCTGGTCCGAGACAGCGAGAGCGTGGCGGGGGCCTTCGCGCTCTGCGTC
CTGTATCAGAAGCATGTGCACACGTATCGCATTCTGCCTGATGGAGAAGATTTCTTGGCT
GTGCAGACCTCGCAGGGTGTGCCTGTGCGCCGCTTCCAGACCCTGGGTGAGCTCATCGGC
CTGTACGCCCAGCCCAACCAGGGCCTTGTGTGCGCCCTGCTTCTTCCTGTAGAGGGTGAG
CGAGAGCCGGACCCACCGGATGACCGGGATGCCTCAGATGGGGAGGATGAGAAGCCCCCG
CTGCCCCCGCGCTCTGGCTCCACCAGCATTTCTGCCCCCACTGGGCCCAGCAGTCCCCTG
CCAGCTCCTGAGACTCCCACAGCTCCAGCTGCTGAGAGTGCTCCCAATGGGCTGAGCACC
GTCTCGCACGACTACCTGAAAGGCAGCTATGGGCTGGACCTGGAAGCTGTGAGGGGTGGA
GCCAGCCACCTGCCCCACCTCACCCGTACCCTCGCTACCTCATGCCGGAGGCTGCACAGT
GAGGTGGACAAGGTCCTGTCAGGCCTGGAGATCCTGTCCAAGGTGTTTGACCAGCAGAGC
TCGCCCATGGTGACCCGCCTTTTGCAGCAGCAGAACCTGCCACAGACAGGGGAGCAGGAA
CTAGAGAGCCTGGTGCTGAAGCTGTCAGTGCTAAAGGACTTCCTGTCAGGCATCCAGAAG
AAGGCCCTGAAGGCCCTACAGGACATGAGCTCCACAGCACCCCCAGCTCCGCAGCCATCC
ACACGTAAGGCCAAGACCATCCCCGTGCAGGCCTTTGAGGTGAAGCTAGATGTGACCCTG
GGTGACCTGACCAAGATTGGGAAGTCACAGAAGTTCACGCTGAGCGTGGATGTGGAGGGT
GGGCGGCTGGTGCTGCTGCGGAGACAGCGGGACTCCCAGGAGGACTGGACCACCTTCACG
CACGACCGCATCCGCCAGCTCATTAAGTCCCAGCGTGTCCAGAACAAGCTGGGTGTTGTG
TTTGAGAAGGAGAAGGACCGGACTCAGCGCAAGGACTTCATCTTTGTCAGTGCCCGGAAG
CGGGAGGCCTTCTGCCAGCTGTTGCAGCTCATGAAGAACAAGCACTCCAAGCAGGACGAG
CCCGACATGATCTCAGTCTTCATAGGCACCTGGAACATGGGAAGTGTACCACCTCCAAAA
AACGTGACATCCTGGTTCACATCGAAGGGTCTGGGGAAGACCCTGGACGAGGTCACAGTG
ACCATACCCCATGACATCTATGTCTTTGGGACCCAGGAGAACTCAGTGGGCGACCGCGAG
TGGCTGGACCTACTGCGCGGGGGCCTCAAGGAGCTTACGGATCTGGATTACCGCCCGATT
GCCATGCAATCACTGTGGAATATCAAGGTGGCAGTGCTGGTCAAGCCAGAGCACGAGAAC
CGTATCAGCCATGTCAGTACGTCCAGTGTGAAGACTGGCATCGCCAACACCCTGGGGAAC
AAGGGGGCTGTGGGCGTCTCCTTCATGTTTAATGGCACCTCATTTGGCTTTGTGAATTGT
CACCTCACCTCGGGAAATGAGAAGACGGCTCGGAGGAACCAAAACTACTTGGACATCCTG
CGGCTGCTCTCGCTGGGCGACCGGCAGCTCAATGCCTTTGACATCTCTCTGCGTTTCACA
CACCTCTTCTGGTTTGGGGACCTCAACTACCGCCTGGACATGGATATCCAGGAGATCCTG
AACTACATCAGCAGGAAAGAGTTTGAGCCCCTCCTCAGGGTGGACCAGCTCAACCTGGAG
CGGGAGAAGCACAAGGTCTTCCTTCGATTCAGTGAGGAGGAGATCTCCTTCCCACCCACC
TACCGCTATGAGCGGGGTTCCCGGGACACATATGCCTGGCACAAGCAGAAGCCAACTGGG
GTCCGGACCAATGTGCCCTCATGGTGTGACCGGATTCTGTGGAAATCCTACCCTGAAACT
CACATCATCTGCAATTCTTATGGTTGCACTGATGACATCGTCACCAGCGACCATTCCCCC
GTGTTTGGGACATTTGAGGTTGGAGTTACCTCCCAGTTCATCTCCAAGAAAGGGCTCTCA
AAGACTTCAGACCAGGCCTACATTGAGTTTGAGAGCATCGAGGCCATTGTGAAGACAGCC
AGCCGCACCAAGTTCTTCATCGAGTTCTACTCTACCTGCCTGGAGGAATACAAGAAGAGC
TTTGAGAATGATGCCCAGAGCAGTGACAACATCAACTTCCTCAAAGTGCAGTGGTCTTCA
CGCCAGCTGCCCACGCTCAAACCAATTCTGGCTGATATCGAGTACCTGCAGGACCAGCAC
CTCCTGCTCACAGTCAAGTCCATGGATGGCTATGAATCCTATGGGGAGTGTGTGGTTGCA
CTCAAATCCATGATCGGCAGCACGGCCCAACAGTTCCTGACCTTCCTATCCCACCGTGGC
GAGGAGACAGGCAATATCAGAGGCTCCATGAAGGTGCGGGTGCCCACGGAGCGCCTGGGC
ACCCGTGAGCGGCTCTACGAGTGGATCAGCATTGATAAGGATGAGGCAGGAGCAAAGAGC
AAAGCCCCCTCTGTGTCCCGAGGGAGCCAGGAGCCCAGGTCAGGGAGCCGCAAGCCAGCC
TTCACAGAGGCCTCCTGCCCGCTCTCCAGGTTATTTGAAGAACCAGAGAAACCGCCACCA
ACGGGGAGGCCCCCAGCCCCACCCCGAGCAGCTCCCCGGGAGGAGCCCTTGACCCCCAGG
TTGAAGCCAGAGGGAGCTCCTGAACCAGAAGGGGTGGCGGCCCCCCCACCCAAGAACAGC
TTCAATAACCCTGCCTACTACGTCCTTGAAGGGGTCCCGCACCAGCTGCTGCCCCCGGAG
CCACCCTCGCCTGCCAGGGCCCCTGTCCCATCTGCCACCAAGAACAAAGTGGCCATTACA
GTGCCTGCTCCACAGCTTGGGCACCACCGGCACCCTCGTGTGGGAGAGGGGAGTTCTTCA
GATGAGGAGTCTGGAGGCACACTGCCCCCTCCAGACTTTCCACCTCCACCACTGCCGGAC
TCAGCCATCTTCCTGCCCCCCAGCCTGGATCCTTTACCAGGGCCAGTGGTCCGGGGCCGT
GGTGGGGCTGAGGCCCGTGGCCCACCACCTCCCAAGGCCCATCCAAGGCCTCCACTGCCC
CCAGGCCCCTCACCAGCCAGCACTTTCCTGGGGGAAGTGGCCAGTGGGGATGACCGGTCC
TGCTCGGTGCTGCAGATGGCCAAGACGCTGAGCGAGGTGGACTATGCCCCTGCTGGGCCT
GCACGCTCAGCGCTCCTCCCAGGCCCCCTGGAGCTGCAGCCCCCCCGGGGACTGCCCTCG
GACTATGGCCGGCCCCTCAGCTTCCCTCCACCCCGCATCCGGGAGAGCATCCAGGAAGAC
CTGGCAGAGGAGGCTCCGTGCCTGCAGGGCGGGCGGGCCAGCGGGCTGGGCGAGGCAGGC
ATGAGTGCCTGGCTGCGGGCCATCGGCTTGGAGCGCTATGAGGAGGGCCTGGTGCATAAT
GGCTGGGACGACCTGGAGTTTCTCAGTGACATCACCGAGGAGGACTTGGAGGAGGCTGGG
GTGCAGGACCCGGCTCACAAGCGCCTCCTTCTGGACACCCTGCAGCTCAGCAAGTGA
Enzyme 13 GenBank Gene ID NM_001567.3 Link Image
Enzyme 13 GeneCard ID INPPL1 Link Image
Enzyme 13 GenAtlas ID INPPL1 Link Image
Enzyme 13 HGNC ID HGNC:6080 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 11q23
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Hejna JA, Saito H, Merkens LS, Tittle TV, Jakobs PM, Whitney MA, Grompe M, Friedberg AS, Moses RE: Cloning and characterization of a human cDNA (INPPL1) sharing homology with inositol polyphosphate phosphatases. Genomics. 1995 Sep 1;29(1):285-7. [PubMed Link Image]
  2. Pesesse X, Deleu S, De Smedt F, Drayer L, Erneux C: Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP. Biochem Biophys Res Commun. 1997 Oct 29;239(3):697-700. [PubMed Link Image]
  3. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [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. Habib T, Hejna JA, Moses RE, Decker SJ: Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein. J Biol Chem. 1998 Jul 17;273(29):18605-9. [PubMed Link Image]
  6. Wisniewski D, Strife A, Swendeman S, Erdjument-Bromage H, Geromanos S, Kavanaugh WM, Tempst P, Clarkson B: A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells. Blood. 1999 Apr 15;93(8):2707-20. [PubMed Link Image]
  7. Bruhns P, Vely F, Malbec O, Fridman WH, Vivier E, Daeron M: Molecular basis of the recruitment of the SH2 domain-containing inositol 5-phosphatases SHIP1 and SHIP2 by fcgamma RIIB. J Biol Chem. 2000 Dec 1;275(48):37357-64. [PubMed Link Image]
  8. Pesesse X, Dewaste V, De Smedt F, Laffargue M, Giuriato S, Moreau C, Payrastre B, Erneux C: The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor (EGF) receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cells. J Biol Chem. 2001 Jul 27;276(30):28348-55. Epub 2001 May 10. [PubMed Link Image]
  9. Dyson JM, O'Malley CJ, Becanovic J, Munday AD, Berndt MC, Coghill ID, Nandurkar HH, Ooms LM, Mitchell CA: The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. J Cell Biol. 2001 Dec 10;155(6):1065-79. Epub 2001 Dec 10. [PubMed Link Image]
  10. Prasad N, Topping RS, Decker SJ: SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas) adapter protein and regulates cellular adhesion and spreading. Mol Cell Biol. 2001 Feb;21(4):1416-28. [PubMed Link Image]
  11. Steen H, Kuster B, Fernandez M, Pandey A, Mann M: Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway. J Biol Chem. 2002 Jan 11;277(2):1031-9. Epub 2001 Oct 30. [PubMed Link Image]
  12. Prasad N, Topping RS, Decker SJ: Src family tyrosine kinases regulate adhesion-dependent tyrosine phosphorylation of 5'-inositol phosphatase SHIP2 during cell attachment and spreading on collagen I. J Cell Sci. 2002 Oct 1;115(Pt 19):3807-15. [PubMed Link Image]
  13. Vandenbroere I, Paternotte N, Dumont JE, Erneux C, Pirson I: The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2. Biochem Biophys Res Commun. 2003 Jan 10;300(2):494-500. [PubMed Link Image]
  14. Dyson JM, Munday AD, Kong AM, Huysmans RD, Matzaris M, Layton MJ, Nandurkar HH, Berndt MC, Mitchell CA: SHIP-2 forms a tetrameric complex with filamin, actin, and GPIb-IX-V: localization of SHIP-2 to the activated platelet actin cytoskeleton. Blood. 2003 Aug 1;102(3):940-8. Epub 2003 Apr 3. [PubMed Link Image]
  15. Pengal RA, Ganesan LP, Fang H, Marsh CB, Anderson CL, Tridandapani S: SHIP-2 inositol phosphatase is inducibly expressed in human monocytes and serves to regulate Fcgamma receptor-mediated signaling. J Biol Chem. 2003 Jun 20;278(25):22657-63. Epub 2003 Apr 10. [PubMed Link Image]
  16. Salomon AR, Ficarro SB, Brill LM, Brinker A, Phung QT, Ericson C, Sauer K, Brock A, Horn DM, Schultz PG, Peters EC: Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry. Proc Natl Acad Sci U S A. 2003 Jan 21;100(2):443-8. Epub 2003 Jan 9. [PubMed Link Image]
  17. Vandeput F, Backers K, Villeret V, Pesesse X, Erneux C: The influence of anionic lipids on SHIP2 phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase activity. Cell Signal. 2006 Dec;18(12):2193-9. Epub 2006 May 23. [PubMed Link Image]
  18. Paternotte N, Zhang J, Vandenbroere I, Backers K, Blero D, Kioka N, Vanderwinden JM, Pirson I, Erneux C: SHIP2 interaction with the cytoskeletal protein Vinexin. FEBS J. 2005 Dec;272(23):6052-66. [PubMed Link Image]
  19. Prasad NK, Decker SJ: SH2-containing 5'-inositol phosphatase, SHIP2, regulates cytoskeleton organization and ligand-dependent down-regulation of the epidermal growth factor receptor. J Biol Chem. 2005 Apr 1;280(13):13129-36. Epub 2005 Jan 24. [PubMed Link Image]
  20. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  21. Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed Link Image]
  22. Koch A, Mancini A, El Bounkari O, Tamura T: The SH2-domian-containing inositol 5-phosphatase (SHIP)-2 binds to c-Met directly via tyrosine residue 1356 and involves hepatocyte growth factor (HGF)-induced lamellipodium formation, cell scattering and cell spreading. Oncogene. 2005 May 12;24(21):3436-47. [PubMed Link Image]
  23. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  24. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  25. Raaijmakers JH, Deneubourg L, Rehmann H, de Koning J, Zhang Z, Krugmann S, Erneux C, Bos JL: The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2 in a SAM domain-dependent manner. Cell Signal. 2007 Jun;19(6):1249-57. Epub 2007 Jan 20. [PubMed Link Image]
  26. Zhuang G, Hunter S, Hwang Y, Chen J: Regulation of EphA2 receptor endocytosis by SHIP2 lipid phosphatase via phosphatidylinositol 3-Kinase-dependent Rac1 activation. J Biol Chem. 2007 Jan 26;282(4):2683-94. Epub 2006 Nov 29. [PubMed Link Image]
  27. Artemenko Y, Gagnon A, Ibrahim S, Sorisky A: Regulation of PDGF-stimulated SHIP2 tyrosine phosphorylation and association with Shc in 3T3-L1 preadipocytes. J Cell Physiol. 2007 Jun;211(3):598-607. [PubMed Link Image]
  28. Marion E, Kaisaki PJ, Pouillon V, Gueydan C, Levy JC, Bodson A, Krzentowski G, Daubresse JC, Mockel J, Behrends J, Servais G, Szpirer C, Kruys V, Gauguier D, Schurmans S: The gene INPPL1, encoding the lipid phosphatase SHIP2, is a candidate for type 2 diabetes in rat and man. Diabetes. 2002 Jul;51(7):2012-7. [PubMed Link Image]
  29. Kaisaki PJ, Delepine M, Woon PY, Sebag-Montefiore L, Wilder SP, Menzel S, Vionnet N, Marion E, Riveline JP, Charpentier G, Schurmans S, Levy JC, Lathrop M, Farrall M, Gauguier D: Polymorphisms in type II SH2 domain-containing inositol 5-phosphatase (INPPL1, SHIP2) are associated with physiological abnormalities of the metabolic syndrome. Diabetes. 2004 Jul;53(7):1900-4. [PubMed Link Image]
  30. Kagawa S, Sasaoka T, Yaguchi S, Ishihara H, Tsuneki H, Murakami S, Fukui K, Wada T, Kobayashi S, Kimura I, Kobayashi M: Impact of SRC homology 2-containing inositol 5'-phosphatase 2 gene polymorphisms detected in a Japanese population on insulin signaling. J Clin Endocrinol Metab. 2005 May;90(5):2911-9. Epub 2005 Feb 1. [PubMed Link Image]
  31. Marcano AC, Burke B, Gungadoo J, Wallace C, Kaisaki PJ, Woon PY, Farrall M, Clayton D, Brown M, Dominiczak A, Connell JM, Webster J, Lathrop M, Caulfield M, Samani N, Gauguier D, Munroe PB: Genetic association analysis of inositol polyphosphate phosphatase-like 1 (INPPL1, SHIP2) variants with essential hypertension. J Med Genet. 2007 Sep;44(9):603-5. Epub 2007 Jun 8. [PubMed Link Image]
  32. Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM: Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5860-5. Epub 2007 Mar 26. [PubMed Link Image]
  33. 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]
  34. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  35. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 10047
Enzyme 14 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
Enzyme 14 Synonyms
  1. hPLCD4
  2. Phosphoinositide phospholipase C-delta-4
  3. Phospholipase C-delta-4
  4. PLC-delta-4
Enzyme 14 Gene Name PLCD4
Enzyme 14 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
MASLLQDQLTTDQDLLLMQEGMPMRKVRSKSWKKLRYFRLQNDGMTVWHARQARGSAKPS
FSISDVETIRNGHDSELLRSLAEELPLEQGFTIVFHGRRSNLDLMANSVEEAQIWMRGLQ
LLVDLVTSMDHQERLDQWLSDWFQRGDKNQDGKMSFQEVQRLLHLMNVEMDQEYAFSLFQ
AADTSQSGTLEGEEFVQFYKALTKRAEVQELFESFSADGQKLTLLEFLDFLQEEQKERDC
TSELALELIDRYEPSDSGKLRHVLSMDGFLSYLCSKDGDIFNPACLPIYQDMTQPLNHYF
ICSSHNTYLVGDQLCGQSSVEGYIRALKRGCRCVEVDVWDGPSGEPVVYHGHTLTSRILF
KDVVATVAQYAFQTSDYPVILSLETHCSWEQQQTMARHLTEILGEQLLSTTLDGVLPTQL
PSPEELRRKILVKGKKLTLEEDLEYEEEEAEPELEESELALESQFETEPEPQEQNLQNKD
KKKKSKPILCPALSSLVIYLKSVSFRSFTHSKEHYHFYEISSFSETKAKRLIKEAGNEFV
QHNTWQLSRVYPSGLRTDSSNYNPQELWNAGCQMVAMNMQTAGLEMDICDGHFRQNGGCG
YVLKPDFLRDIQSSFHPEKPISPFKAQTLLIQVISGQQLPKVDKTKEGSIVDPLVKVQIF
GVRLDTARQETNYVENNGFNPYWGQTLCFRVLVPELAMLRFVVMDYDWKSRNDFIGQYTL
PWTCMQQGYRHIHLLSKDGISLRPASIFVYICIQEGLEGDES
Enzyme 14 Number of Residues 762
Enzyme 14 Molecular Weight 87584.5
Enzyme 14 Theoretical pI 4.85
Enzyme 14 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 14 General Function Involved in calcium ion binding
Enzyme 14 Specific Function Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Required for acrosome reaction in sperm during fertilization, probably by acting as an important enzyme for intracellular Ca(2+) mobilization in the zona pellucida- induced acrosome reaction. May play a role in cell growth. Modulates the liver regeneration in cooperation with nuclear PKC. Overexpression upregulates the Erk signaling pathway and proliferation
Enzyme 14 Pathways
Enzyme 14 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 62897967 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q9BRC7 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name PLCD4_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >2289 bp
ATGGCGTCCCTGCTGCAAGACCAGCTGACCACTGATCAGGACTTGCTGCTGATGCAGGAA
GGCATGCCGATGCGCAAGGTGAGGTCCAAAAGCTGGAAGAAGCTAAGATACTTCAGACTT
CAGAATGACGGCATGACAGTCTGGCATGCACGGCAGGCCAGGGGCAGTGCCAAGCCCAGC
TTCTCAATCTCTGATGTGGAGACAATACGTAATGGCCATGATTCCGAGTTGCTGCGTAGC
CTGGCAGAGGAGCTCCCCCTGGAGCAGGGCTTCACCATTGTCTTCCATGGCCACCGCTCC
AACCTGGACCTGATGGCCAACAGTGTTGAGGAGGCCCAGATATGGATGCGAGGGCTCCAG
CTGTTGGTGGATCTTGTCACCAGCATGGACCATCAGGAGCGCCTGGACCAATGGCTGAGC
GATTGGTTTCAACGTGGAGACAAAAATCAGGATGGTAAGATGAGTTTCCAAGAAGTTCAG
CGGTTATTGCACCTAATGAATGTGGAAATGGACCAAGAATATGCCTTCAGTCTTTTTCAG
GCAGCAGACACGTCCCAGTCTGGAACCCTGGAAGGAGAAGAATTCGTACAGTTCTATAAG
GCATTGACTAAACGTGCTGAGGTGCAGGAACTGTTTGAAAGTTTTTCAGCTGATGGGCAG
AAGCTGACTCTGCTGGAATTTTTGGATTTCCTCCAAGAGGAGCAGAAGGAGAGAGACTGC
ACCTCTGAGCTTGCTCTGGAACTCATTGACCGCTATGAACCTTCAGACAGTGGCAAACTG
CGGCATGTGCTGAGTATGGATGGCTTCCTCAGCTACCTCTGCTCTAAGGATGGAGACATC
TTCAACCCAGCCTGCCTCCCCATCTATCAGGATATGACTCAACCCCTGAACCACTACTTC
ATCTGCTCTTCTCATAACACCTACCTAGTGGGGGACCAGCTTTGCGGCCAGAGCAGCGTC
GAGGGATATATACGGGCCCTGAAGCGGGGGTGCCGCTGCGTGGAGGTGGATGTATGGGAT
GGACCTAGCGGGGAACCTGTCGTTTACCACGGACACACCCTGACCTCCCGCATCCTGTTC
AAAGATGTCGTGGCCACAGTAGCACAGTATGCCTTCCAGACATCAGACTACCCAGTCATC
TTGTCCCTGGAGACCCACTGCAGCTGGGAGCAGCAGCAGACCATGGCCCGTCATCTGACT
GAGATCCTGGGGGAGCAGCTGCTGAGCACCACCTTGGATGGGGTGCTGCCCACTCAGCTG
CCCTCGCCTGAGGAGCTTCGGAGGAAGATCCTGGTGAAGGGGAAGAAGTTAACACTTGAG
GAAGACCTGGAATATGAGGAAGAGGAAGCAGAACCTGAGTTGGAAGAGTCAGAATTGGCG
CTGGAGTCCCAGTTTGAGACTGAGCCTGAGCCCCAGGAGCAGAACCTTCAGAATAAGGAC
AAAAAGAAGAAATCCAAGCCCATCTTGTGTCCAGCCCTCTCTTCCCTGGTTATCTACTTG
AAGTCTGTCTCATTCCGCAGCTTCACACATTCAAAGGAGCACTACCACTTCTACGAGATA
TCATCTTTCTCTGAAACCAAGGCCAAGCGCCTCATCAAGGAGGCTGGCAATGAGTTTGTG
CAGCACAATACTTGGCAGTTAAGCCGTGTGTATCCCAGCGGCCTGAGGACAGACTCTTCC
AACTACAACCCCCAGGAACTCTGGAATGCAGGCTGCCAGATGGTGGCCATGAATATGCAG
ACTGCAGGGCTTGAAATGGACATCTGTGATGGGCATTTCCGCCAGAATGGCGGCTGTGGC
TATGTGCTGAAGCCAGACTTCCTGCGTGATATCCAGAGTTCTTTCCACCCTGAGAAGCCC
ATCAGCCCTTTCAAAGCCCAGACTCTCTTAATCCAGGTGATCAGCGGTCAGCAACTCCCC
AAAGTGGACAAGACCAAAGAGGGGTCCATTGTGGATCCACTGGTGAAAGTGCAGATCTTT
GGCGTTCGTCTAGACACAGCACGGCAGGAGACCAACTATGTGGAGAACAATGGTTTTAAT
CCATACTGGGGGCAGACACTATGTTTCCGGGTGCTGGTGCCTGAACTTGCCATGCTGCGT
TTTGTGGTAATGGATTATGACTGGAAATCCCGAAATGACTTTATTGGTCAGTACACCCTG
CCTTGGACCTGCATGCAACAAGGTTACCGCCACATTCACCTGCTGTCCAAAGATGGCATC
AGCCTCCGCCCAGCTTCCATCTTTGTGTATATCTGCATCCAGGAAGGCCTGGAGGGGGAT
GAGTCCTGA
Enzyme 14 GenBank Gene ID AK223203 Link Image
Enzyme 14 GeneCard ID PLCD4 Link Image
Enzyme 14 GenAtlas ID PLCD4 Link Image
Enzyme 14 HGNC ID HGNC:9062 Link Image
Enzyme 14 Chromosome Location 2
Enzyme 14 Locus 2q35
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Leung DW, Tompkins C, Brewer J, Ball A, Coon M, Morris V, Waggoner D, Singer JW: Phospholipase C delta-4 overexpression upregulates ErbB1/2 expression, Erk signaling pathway, and proliferation in MCF-7 cells. Mol Cancer. 2004 May 13;3:15. [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. Kim H, Suh PG, Ryu SH, Park SH: Assignment of the human PLC delta4 gene (PLCD4) to human chromosome band 2q35 by fluorescence in situ hybridization. Cytogenet Cell Genet. 1999;87(3-4):254-5. [PubMed Link Image]
  4. Landreville S, Coulombe S, Carrier P, Gelb MH, Guerin SL, Salesse C: Expression of phospholipases A2 and C in human corneal epithelial cells. Invest Ophthalmol Vis Sci. 2004 Nov;45(11):3997-4003. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 10050
Enzyme 15 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
Enzyme 15 Synonyms
  1. Phosphoinositide phospholipase C-delta-3
  2. Phospholipase C-delta-3
  3. PLC-delta-3
Enzyme 15 Gene Name PLCD3
Enzyme 15 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
MLCGRWRRCRRPPEEPPVAAQVAAQVAAPVALPSPPTPSDGGTKRPGLRALKKMGLTEDE
DVRAMLRGSRLRKIRSRTWHKERLYRLQEDGLSVWFQRRIPRAPSQHIFFVQHIEAVREG
HQSEGLRRFGGAFAPARCLTIAFKGRRKNLDLAAPTAEEAQRWVRGLTKLRARLDAMSQR
ERLDHWIHSYLHRADSNQDSKMSFKEIKSLLRMVNVDMNDMYAYLLFKECDHSNNDRLEG
AEIEEFLRRLLKRPELEEIFHQYSGEDRVLSAPELLEFLEDQGEEGATLARAQQLIQTYE
LNETAKQHELMTLDGFMMYLLSPEGAALDNTHTCVFQDMNQPLAHYFISSSHNTYLTDSQ
IGGPSSTEAYVRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVVQAVRDHAFT
LSPYPVILSLENHCGLEQQAAMARHLCTILGDMLVTQALDSPNPEELPSPEQLKGRVLVK
GKKLPAARSEDGRALSDREEEEEDDEEEEEEVEAAAQRRLAKQISPELSALAVYCHATRL
RTLHPAPNAPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQ
EMWNSGCQLVALNFQTPGYEMDLNAGRFLVNGQCGYVLKPACLRQPDSTFDPEYPGPPRT
TLSIQVLTAQQLPKLNAEKPHSIVDPLVRIEIHGVPADCARQETDYVLNNGFNPRWGQTL
QFQLRAPELALVRFVVEDYDATSPNDFVGQFTLPLSSLKQGYRHIHLLSKDGASLSPATL
FIQIRIQRS
Enzyme 15 Number of Residues 789
Enzyme 15 Molecular Weight 89257.5
Enzyme 15 Theoretical pI 6.97
Enzyme 15 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 15 General Function Involved in calcium ion binding
Enzyme 15 Specific Function Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow
Enzyme 15 Pathways
Enzyme 15 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID Q8N3E9 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name PLCD3_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >2370 bp
ATGCTGTGCGGCCGCTGGAGGCGTTGCCGCCGCCCGCCCGAGGAGCCCCCGGTGGCCGCC
CAGGTCGCAGCCCAAGTCGCGGCGCCGGTCGCTCTCCCGTCCCCGCCGACTCCCTCCGAT
GGCGGCACCAAGAGGCCCGGGCTGCGGGCGCTGAAGAAGATGGGCCTGACGGAGGACGAG
GACGTGCGCGCCATGCTGCGGGGCTCCCGGCTCCGCAAGATCCGCTCGCGCACGTGGCAC
AAGGAGCGGCTGTACCGGCTGCAGGAGGACGGCCTGAGCGTGTGGTTCCAGCGGCGCATC
CCGCGTGCGCCATCGCAGCACATCTTCTTCGTGCAGCACATCGAGGCGGTCCGCGAGGGC
CACCAGTCCGAGGGCCTGCGGCGCTTCGGGGGTGCCTTCGCGCCAGCGCGCTGCCTCACC
ATCGCCTTCAAGGGCCGCCGCAAGAACCTGGACCTGGCGGCGCCCACGGCTGAGGAAGCG
CAGCGCTGGGTGCGCGGTCTGACCAAGCTCCGCGCGCGCCTGGACGCCATGAGCCAGCGC
GAGCGGCTAGACCACTGGATCCACTCCTATCTGCACCGGGCTGACTCCAACCAGGACAGC
AAGATGAGCTTCAAGGAGATCAAGAGCCTGCTGAGAATGGTCAACGTGGACATGAACGAC
ATGTACGCCTACCTCCTCTTCAAGGAGTGTGACCACTCCAACAACGACCGTCTAGAGGGG
GCTGAGATCGAGGAGTTCCTGCGGCGGCTGCTGAAGCGGCCGGAGCTGGAGGAGATCTTC
CATCAGTACTCGGGCGAGGACCGCGTGCTGAGTGCCCCTGAGCTGCTGGAGTTCCTGGAG
GACCAGGGCGAGGAGGGCGCCACACTGGCCCGCGCCCAGCAGCTCATTCAGACCTATGAG
CTCAACGAGACAGCCAAGCAGCATGAGCTGATGACACTGGATGGCTTCATGATGTACCTG
TTGTCGCCGGAGGGGGCTGCCTTGGACAACACCCACACGTGTGTGTTCCAGGACATGAAC
CAGCCCCTTGCCCACTACTTCATCTCTTCCTCCCACAACACCTATCTGACTGACTCCCAG
ATCGGGGGGCCCAGCAGCACCGAGGCCTATGTTAGGGCCTTTGCCCAGGGATGCCGCTGC
GTGGAGCTGGACTGCTGGGAGGGGCCAGGAGGGGAGCCCGTCATCTATCATGGCCATACC
CTCACCTCCAAGATTCTCTTCCGGGACGTGGTCCAAGCCGTGCGCGACCATGCCTTCACG
CTGTCCCCTTACCCTGTCATCCTATCCCTGGAGAACCACTGCGGGCTGGAGCAGCAGGCT
GCCATGGCCCGCCACCTCTGCACCATCCTGGGGGACATGCTGGTGACACAGGCGCTGGAC
TCCCCAAATCCCGAGGAGCTGCCATCCCCAGAGCAGCTGAAGGGCCGGGTCCTGGTGAAG
GGAAAGAAGTTGCCCGCTGCTCGGAGCGAGGATGGCCGGGCTCTGTCGGATCGGGAGGAG
GAGGAGGAGGATGACGAGGAGGAAGAAGAGGAGGTGGAGGCTGCAGCGCAGAGGCGGCTG
GCCAAGCAGATCTCCCCGGAGCTGTCGGCCCTGGCTGTGTACTGCCACGCCACCCGCCTG
CGGACCCTGCACCCTGCCCCCAACGCCCCACAACCCTGCCAGGTCAGCTCCCTCAGCGAG
CGCAAAGCCAAGAAACTCATTCGGGAGGCAGGGAACAGCTTTGTCAGGCACAATGCCCGC
CAGCTGACCCGCGTGTACCCGCTGGGGCTGCGGATGAACTCAGCCAACTACAGTCCCCAG
GAGATGTGGAACTCGGGCTGTCAGCTGGTGGCCTTGAACTTCCAGACGCCAGGCTACGAG
ATGGACCTCAATGCCGGGCGCTTCCTAGTCAATGGGCAGTGTGGCTACGTCCTAAAACCT
GCCTGCCTGCGGCAACCTGACTCGACCTTTGACCCCGAGTACCCAGGACCTCCCAGAACC
ACTCTCAGCATCCAGGTGCTGACTGCACAGCAGCTGCCCAAGCTGAATGCCGAGAAGCCA
CACTCCATTGTGGACCCCCTGGTGCGCATTGAGATCCATGGGGTGCCCGCAGACTGTGCC
CGGCAGGAGACTGACTACGTGCTCAACAATGGCTTCAACCCCCGCTGGGGGCAGACCCTG
CAGTTCCAGCTGCGGGCTCCGGAGCTGGCACTGGTCCGGTTTGTGGTGGAAGATTATGAC
GCCACCTCCCCCAATGACTTTGTGGGCCAGTTTACACTGCCTCTTAGCAGCCTAAAGCAA
GGGTACCGCCACATACACCTGCTTTCCAAGGACGGGGCCTCACTGTCACCAGCCACGCTC
TTCATCCAAATCCGCATCCAGCGCTCCTGA
Enzyme 15 GenBank Gene ID AK074240 Link Image
Enzyme 15 GeneCard ID PLCD3 Link Image
Enzyme 15 GenAtlas ID PLCD3 Link Image
Enzyme 15 HGNC ID HGNC:9061 Link Image
Enzyme 15 Chromosome Location 1
Enzyme 15 Locus 17q21.31
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. 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]
  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. 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]
  4. Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed Link Image]
  5. Pawelczyk T, Matecki A: Expression, purification and kinetic properties of human recombinant phospholipase C delta 3. Acta Biochim Pol. 1997;44(2):221-9. [PubMed Link Image]
  6. Ghosh S, Pawelczyk T, Lowenstein JM: Phospholipase C isoforms delta 1 and delta 3 from human fibroblasts. High-yield expression in Escherichia coli, simple purification, and properties. Protein Expr Purif. 1997 Mar;9(2):262-78. [PubMed Link Image]
  7. Pawelczyk T, Matecki A: Localization of phospholipase C delta3 in the cell and regulation of its activity by phospholipids and calcium. Eur J Biochem. 1998 Oct 1;257(1):169-77. [PubMed Link Image]
  8. Kim H, Suh PG, Ryu SH, Park SH: Assignment of the human PLC delta3 gene (PLCD3) to human chromosome band 17q21 by fluorescence in situ hybridization. Cytogenet Cell Genet. 1999;87(3-4):209-10. [PubMed Link Image]
  9. Pawelczyk T, Matecki A: Phospholipase C-delta3 binds with high specificity to phosphatidylinositol 4,5-bisphosphate and phosphatidic acid in bilayer membranes. Eur J Biochem. 1999 Jun;262(2):291-8. [PubMed Link Image]
  10. Lin FG, Cheng HF, Lee IF, Kao HJ, Loh SH, Lee WH: Downregulation of phospholipase C delta3 by cAMP and calcium. Biochem Biophys Res Commun. 2001 Aug 17;286(2):274-80. [PubMed Link Image]
  11. Ananthanarayanan B, Das S, Rhee SG, Murray D, Cho W: Membrane targeting of C2 domains of phospholipase C-delta isoforms. J Biol Chem. 2002 Feb 1;277(5):3568-75. Epub 2001 Nov 12. [PubMed Link Image]
  12. Landreville S, Coulombe S, Carrier P, Gelb MH, Guerin SL, Salesse C: Expression of phospholipases A2 and C in human corneal epithelial cells. Invest Ophthalmol Vis Sci. 2004 Nov;45(11):3997-4003. [PubMed Link Image]
  13. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  14. Naito Y, Okada M, Yagisawa H: Phospholipase C isoforms are localized at the cleavage furrow during cytokinesis. J Biochem. 2006 Dec;140(6):785-91. Epub 2006 Oct 14. [PubMed Link Image]
  15. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 13062
Enzyme 16 Name Multiple inositol polyphosphate phosphatase 1
Enzyme 16 Synonyms
  1. Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase
  2. Ins(1,3,4,5)P(4) 3-phosphatase
Enzyme 16 Gene Name MINPP1
Enzyme 16 Protein Sequence >Multiple inositol polyphosphate phosphatase 1
MLRAPGCLLRTSVAPAAALAAALLSSLARCSLLEPRDPVASSLSPYFGTKTRYEDVNPVL
LSGPEAPWRDPELLEGTCTPVQLVALIRHGTRYPTVKQIRKLRQLHGLLQARGSRDGGAS
STGSRDLGAALADWPLWYADWMDGQLVEKGRQDMRQLALRLASLFPALFSRENYGRLRLI
TSSKHRCMDSSAAFLQGLWQHYHPGLPPPDVADMEFGPPTVNDKLMRFFDHCEKFLTEVE
KNATALYHVEAFKTGPEMQNILKKVAATLQVPVNDLNADLIQVAFFTCSFDLAIKGVKSP
WCDVFDIDDAKVLEYLNDLKQYWKRGYGYTINSRSSCTLFQDIFQHLDKAVEQKQRSQPI
SSPVILQFGHAETLLPLLSLMGYFKDKEPLTAYNYKKQMHRKFRSGLIVPYASNLIFVLY
HCENAKTPKEQFRVQMLLNEKVLPLAYSQETVSFYEDLKNHYKDILQSCQTSEECELARA
NSTSDEL
Enzyme 16 Number of Residues 487
Enzyme 16 Molecular Weight 55050.6
Enzyme 16 Theoretical pI 7.89
Enzyme 16 GO Classification
Function
  • acid phosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
Component
Enzyme 16 General Function Involved in acid phosphatase activity
Enzyme 16 Specific Function Acts as a phosphoinositide 5- and phosphoinositide 6- phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). May play a role in bone development (endochondral ossification)
Enzyme 16 Pathways
Enzyme 16 Reactions
  • myo-inositol hexakisphosphate + H2O = myo-inositol pentakisphosphate (mixed isomers) + phosphate [RN:R07584]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-30
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 19923761 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q9UNW1 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name MINP1_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1464 bp
ATGCTACGCGCGCCCGGCTGCCTCCTCCGGACCTCCGTAGCGCCTGCCGCGGCCCTGGCT
GCGGCGCTGCTCTCGTCGCTTGCGCGCTGCTCTCTTCTAGAGCCGAGGGACCCGGTGGCC
TCGTCGCTCAGCCCCTATTTCGGCACCAAGACTCGCTACGAGGATGTCAACCCCGTGCTA
TTGTCGGGCCCCGAGGCTCCGTGGCGGGACCCTGAGCTGCTGGAGGGGACCTGCACCCCG
GTGCAGCTGGTCGCCCTCATTCGCCACGGCACCCGCTACCCCACGGTCAAACAGATCCGC
AAGCTGAGGCAGCTGCACGGGTTGCTGCAGGCCCGCGGGTCCAGGGATGGCGGGGCTAGT
AGTACCGGCAGCCGCGACCTGGGTGCAGCGCTGGCCGACTGGCCTTTGTGGTACGCGGAC
TGGATGGACGGGCAGCTAGTAGAGAAGGGACGGCAGGATATGCGACAGCTGGCGCTGCGT
CTGGCCTCGCTCTTCCCGGCCCTTTTCAGCCGTGAGAACTACGGCCGCCTGCGGCTCATC
ACCAGTTCCAAGCACCGCTGCATGGATAGCAGCGCCGCCTTCCTGCAGGGGCTGTGGCAG
CACTACCACCCTGGCTTGCCGCCGCCGGACGTCGCAGATATGGAGTTTGGACCTCCAACA
GTTAATGATAAACTAATGAGATTTTTTGATCACTGTGAGAAGTTTTTAACTGAAGTAGAA
AAAAATGCTACAGCTCTTTATCACGTGGAAGCCTTCAAAACTGGACCAGAAATGCAGAAC
ATTTTAAAAAAAGTTGCAGCTACTTTGCAAGTGCCAGTAAATGATTTAAATGCAGATTTA
ATTCAAGTAGCCTTTTTCACCTGTTCATTTGACCTGGCAATTAAAGGTGTTAAATCTCCT
TGGTGTGATGTTTTTGACATAGATGATGCAAAGGTATTAGAATATTTAAATGATCTGAAA
CAATATTGGAAAAGAGGATATGGGTATACTATTAACAGTCGATCCAGCTGCACCTTGTTT
CAGGATATCTTTCAGCACTTGGACAAAGCAGTTGAACAGAAACAAAGGTCTCAGCCAATT
TCTTCTCCAGTCATCCTCCAGTTTGGTCATGCAGAGACTCTTCTTCCACTGCTTTCTCTC
ATGGGCTACTTCAAAGACAAGGAACCCCTAACAGCGTACAATTACAAAAAACAAATGCAT
CGGAAGTTCCGAAGTGGTCTCATTGTACCTTATGCCTCGAACCTGATATTTGTGCTTTAC
CACTGTGAAAATGCTAAGACTCCTAAAGAACAATTCCGAGTGCAGATGTTATTAAATGAA
AAGGTGTTACCTTTGGCTTACTCACAAGAAACTGTTTCATTTTATGAAGATCTGAAGAAC
CACTACAAGGACATCCTTCAGAGTTGTCAAACCAGTGAAGAATGTGAATTAGCAAGGGCT
AACAGTACATCTGATGAACTATGA
Enzyme 16 GenBank Gene ID NM_004897.4 Link Image
Enzyme 16 GeneCard ID MINPP1 Link Image
Enzyme 16 GenAtlas ID MINPP1 Link Image
Enzyme 16 HGNC ID HGNC:7102 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 10q23
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Caffrey JJ, Hidaka K, Matsuda M, Hirata M, Shears SB: The human and rat forms of multiple inositol polyphosphate phosphatase: functional homology with a histidine acid phosphatase up-regulated during endochondral ossification. FEBS Lett. 1999 Jan 8;442(1):99-104. [PubMed Link Image]
  2. Chi H, Tiller GE, Dasouki MJ, Romano PR, Wang J, O'keefe RJ, Puzas JE, Rosier RN, Reynolds PR: Multiple inositol polyphosphate phosphatase: evolution as a distinct group within the histidine phosphatase family and chromosomal localization of the human and mouse genes to chromosomes 10q23 and 19. Genomics. 1999 Mar 15;56(3):324-36. [PubMed Link Image]
  3. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  4. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  5. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  6. 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]
  7. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  8. Gimm O, Chi H, Dahia PL, Perren A, Hinze R, Komminoth P, Dralle H, Reynolds PR, Eng C: Somatic mutation and germline variants of MINPP1, a phosphatase gene located in proximity to PTEN on 10q23.3, in follicular thyroid carcinomas. J Clin Endocrinol Metab. 2001 Apr;86(4):1801-5. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 13454
Enzyme 17 Name Inositol 1,4,5-trisphosphate receptor type 2
Enzyme 17 Synonyms
  1. IP3 receptor isoform 2
  2. IP3R 2
  3. InsP3R2
  4. Type 2 inositol 1,4,5-trisphosphate receptor
  5. Type 2 InsP3 receptor
Enzyme 17 Gene Name ITPR2
Enzyme 17 Protein Sequence >Inositol 1,4,5-trisphosphate receptor type 2
MTEKMSSFLYIGDIVSLYAEGSVNGFISTLGLVDDRCVVHPEAGDLANPPKKFRDCLFKV
CPMNRYSAQKQYWKAKQAKQGNHTEAALLKKLQHAAELEQKQNESENKKLLGEIVKYSNV
IQLLHIKSNKYLTVNKRLPALLEKNAMRVSLDAAGNEGSWFYIHPFWKLRSEGDNIVVGD
KVVLMPVNAGQPLHASNIELLDNPGCKEVNAVNCNTSWKITLFMKYSSYREDVLKGGDVV
RLFHAEQEKFLTCDEYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAGQWN
SLFRFKHLATGNYLAAELNPDYRDAQNEGKNVRDGVPPTSKKKRQAGEKIMYTLVSVPHG
NDIASLFELDATTLQRADCLVPRNSYVRLRHLCTNTWVTSTSIPIDTDEERPVMLKIGTC
QTKEDKEAFAIVSVPLSEVRDLDFANDANKVLATTVKKLENGTITQNERRFVTKLLEDLI
FFVADVPNNGQEVLDVVITKPNRERQKLMREQNILAQVFGILKAPFKEKAGEGSMLRLED
LGDQRYAPYKYMLRLCYRVLRHSQQDYRKNQEYIAKNFCVMQSQIGYDILAEDTITALLH
NNRKLLEKHITAKEIETFVSLLRRNREPRFLDYLSDLCVSNTTAIPVTQELICKFMLSPG
NADILIQTKVVSMQADNPMESSILSDDIDDEEVWLYWIDSNKEPHGKAIRHLAQEAKEGT
KADLEVLTYYRYQLNLFARMCLDRQYLAINQISTQLSVDLILRCVSDESLPFDLRASFCR
LMLHMHVDRDPQESVVPVRYARLWTEIPTKITIHEYDSITDSSRNDMKRKFALTMEFVEE
YLKEVVNQPFPFGDKEKNKLTFEVVHLARNLIYFGFYSFSELLRLTRTLLAILDIVQAPM
SSYFERLSKFQDGGNNVMRTIHGVGEMMTQMVLSRGSIFPMSVPDVPPSIHPSKQGSPTE
HEDVTVMDTKLKIIEILQFILSVRLDYRISYMLSIYKKEFGEDNDNAETSASGSPDTLLP
SAIVPDIDEIAAQAETMFAGRKEKNPVQLDDEGGRTFLRVLIHLIMHDYPPLLSGALQLL
FKHFSQRAEVLQAFKQVQLLVSNQDVDNYKQIKADLDQLRLTVEKSELWVEKSSNYENGE
IGESQVKGGEEPIEESNILSPVQDGTKKPQIDSNKSNNYRIVKEILIRLSKLCVQNKKCR
NQHQRLLKNMGAHSVVLDLLQIPYEKNDEKMNEVMNLAHTFLQNFCRGNPQNQVLLHKHL
NLFLTPGLLEAETMRHIFMNNYHLCNEISERVVQHFVHCIETHGRHVEYLRFLQTIVKAD
GKYVKKCQDMVMTELINGGEDVLIFYNDRASFPILLHMMCSERDRGDESGPLAYHITLVE
LLAACTEGKNVYTEIKCNSLLPLDDIVRVVTHDDCIPEVKIAYVNFVNHCYVDTEVEMKE
IYTSNHIWKLFENFLVDMARVCNTTTDRKHADIFLEKCVTESIMNIVSGFFNSPFSDNST
SLQTHQPVFIQLLQSAFRIYNCTWPNPAQKASVESCIRTLAEVAKNRGIAIPVDLDSQVN
TLFMKSHSNMVQRAAMGWRLSARSGPRFKEALGGPAWDYRNIIEKLQDVVASLEHQFSPM
MQAEFSVLVDVLYSPELLFPEGSDARIRCGAFMSKLINHTKKLMEKEEKLCIKILQTLRE
MLEKKDSFVEEGNTLRKILLNRYFKGDYSIGVNGHLSGAYSKTAQVGGSFSGQDSDKMGI
SMSDIQCLLDKEGASELVIDVIVNTKNDRIFSEGIFLGIALLEGGNTQTQYSFYQQLHEQ
KKSEKFFKVLYDRMKAAQKEIRSTVTVNTIDLGNKKRDDDNELMTSGPRMRVRDSTLHLK
EGMKGQLTEASSATSKAYCVYRREMDPEIDIMCTGPEAGNTEEKSAEEVTMSPAIAIMQP
ILRFLQLLCENHNRELQNFLRNQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEK
NVALVNQNLESLTEYCQGPCHENQTCIATHESNGIDIIIALILNDINPLGKYRMDLVLQL
KNNASKLLLAIMESRHDSENAERILFNMRPRELVDVMKNAYNQGLECDHGDDEGGDDGVS
PKDVGHNIYILAHQLARHNKLLQQMLKPGSDPDEGDEALKYYANHTAQIEIVRHDRTMEQ
IVFPVPNICEYLTRESKCRVFNTTERDEQGSKVNDFFQQTEDLYNEMKWQKKIRNNPALF
WFSRHISLWGSISFNLAVFINLAVALFYPFGDDGDEGTLSPLFSVLLWIAVAICTSMLFF
FSKPVGIRPFLVSIMLRSIYTIGLGPTLILLGAANLCNKIVFLVSFVGNRGTFTRGYRAV
ILDMAFLYHVAYVLVCMLGLFVHEFFYSFLLFDLVYREETLLNVIKSVTRNGRSIILTAV
LALILVYLFSIIGFLFLKDDFTMEVDRLKNRTPVTGSHQVPTMTLTTMMEACAKENCSPT
IPASNTADEEYEDGIERTCDTLLMCIVTVLNQGLRNGGGVGDVLRRPSKDEPLFAARVVY
DLLFYFIVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVSFE
EHIKSEHNMWHYLYFIVLVKVKDPTEYTGPESYVAQMIVEKNLDWFPRMRAMSLVSNEGD
SEQNEIRSLQEKLESTMSLVKQLSGQLAELKEQMTEQRKNKQRLGFLGSNTPHVNHHMPP
H
Enzyme 17 Number of Residues 2701
Enzyme 17 Molecular Weight 308061.1
Enzyme 17 Theoretical pI 6.39
Enzyme 17 GO Classification
Function
  • calcium channel activity
  • cation channel activity
  • inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity
  • intracellular ligand-gated ion channel activity
  • ion channel activity
  • ion transmembrane transporter activity
  • ligand-gated ion channel activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • calcium ion transport
  • cation transport
  • di-, tri-valent inorganic cation transport
  • divalent metal ion transport
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • endoplasmic reticulum
  • intracellular membrane-bounded organelle
  • membrane
  • membrane-bounded organelle
  • organelle
Enzyme 17 General Function Involved in calcium channel activity
Enzyme 17 Specific Function Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • 2228-2248 2261-2281 2308-2328 2352-2372 2395-2415 2522-2542
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 95147335 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q14571 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name ITPR2_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >8106 bp
ATGACTGAGAAAATGTCCAGCTTCCTCTACATAGGGGACATCGTGTCCCTGTACGCGGAG
GGCTCGGTCAACGGCTTCATCAGCACCTTGGGGTTAGTGGATGACAGATGTGTGGTGCAC
CCAGAGGCCGGGGACCTTGCCAACCCTCCCAAGAAGTTCAGAGACTGCCTTTTCAAGGTG
TGCCCTATGAACAGATATTCTGCCCAGAAGCAATATTGGAAAGCAAAGCAAGCCAAACAA
GGGAACCACACCGAGGCAGCCTTGCTGAAGAAACTACAGCACGCTGCAGAACTGGAACAA
AAACAAAATGAATCGGAGAATAAGAAACTGTTGGGAGAAATTGTAAAATACAGTAATGTT
ATACAACTACTGCATATAAAAAGCAACAAATATCTTACTGTCAACAAGAGATTACCTGCT
TTACTGGAGAAGAATGCCATGCGTGTGTCCTTGGATGCTGCAGGAAATGAAGGGTCTTGG
TTTTATATTCATCCGTTCTGGAAACTGAGAAGCGAGGGTGACAATATTGTTGTAGGAGAT
AAAGTTGTTTTGATGCCTGTGAATGCAGGGCAGCCACTACATGCCAGCAACATAGAGCTT
CTTGATAACCCAGGGTGTAAAGAGGTGAATGCTGTCAATTGCAACACCAGCTGGAAAATC
ACTTTATTCATGAAATATAGTTCCTATCGAGAGGATGTATTAAAAGGAGGGGACGTTGTT
AGATTATTTCATGCGGAACAAGAGAAGTTTTTGACTTGTGATGAATATGAGAAAAAACAG
CACATTTTCCTTCGTACGACCTTGCGCCAATCAGCTACTTCTGCTACTAGTTCTAAAGCA
CTCTGGGAAATAGAGGTGGTTCATCATGACCCATGCCGTGGGGGTGCAGGACAGTGGAAC
AGCTTGTTCAGATTTAAGCATCTTGCAACTGGAAACTATTTAGCTGCAGAGCTTAATCCT
GATTATCGAGATGCCCAAAATGAAGGAAAAAATGTGAGAGATGGAGTCCCTCCAACTTCA
AAGAAAAAACGCCAGGCAGGGGAGAAGATCATGTATACTTTGGTTTCAGTCCCGCATGGC
AATGACATTGCATCCCTTTTTGAACTAGATGCCACAACTCTTCAGAGAGCTGACTGCCTG
GTTCCAAGGAACTCATATGTTCGGTTAAGGCATTTATGCACCAACACATGGGTAACCAGT
ACTAGTATCCCCATAGACACAGATGAAGAGAGGCCTGTTATGTTAAAGATTGGAACCTGC
CAAACCAAAGAAGATAAAGAAGCGTTCGCAATCGTGTCTGTTCCACTGTCTGAAGTTCGA
GACTTAGACTTTGCCAATGATGCCAATAAAGTACTAGCGACCACAGTTAAAAAGCTAGAA
AACGGCACAATAACTCAGAATGAAAGGAGGTTTGTAACCAAATTATTGGAAGATCTCATA
TTCTTTGTTGCTGATGTGCCTAATAATGGACAAGAAGTTCTGGATGTGGTTATCACTAAG
CCAAACCGAGAGCGTCAAAAATTGATGAGGGAACAAAACATACTGGCACAGGTATTTGGA
ATTCTTAAAGCACCCTTTAAAGAGAAAGCAGGAGAAGGCTCGATGCTGAGACTTGAAGAT
CTGGGGGATCAAAGATATGCACCCTACAAGTACATGCTGCGGCTCTGTTACCGCGTCCTG
AGACACTCGCAGCAGGATTACCGGAAAAATCAGGAATATATTGCTAAGAATTTCTGTGTC
ATGCAGTCCCAGATTGGCTATGATATTTTGGCAGAAGATACTATCACAGCTTTGTTGCAC
AACAACAGAAAACTACTAGAGAAACATATCACAGCAAAAGAAATAGAAACATTTGTCAGT
TTACTCAGGAGAAATCGGGAGCCAAGGTTTTTGGATTATTTGTCAGATCTGTGTGTGTCT
AATACCACTGCTATCCCTGTAACTCAAGAACTCATCTGTAAATTTATGTTGAGTCCAGGC
AATGCAGACATTCTCATTCAAACTAAGGTGGTCTCAATGCAAGCAGACAACCCCATGGAG
AGCTCCATCCTTTCAGATGACATTGATGATGAAGAAGTTTGGCTCTATTGGATTGACAGC
AACAAGGAACCTCATGGCAAAGCTATCAGGCACCTTGCTCAAGAGGCAAAAGAAGGCACC
AAAGCTGACTTAGAAGTTCTTACCTATTACAGGTACCAGCTAAACCTCTTTGCAAGGATG
TGCTTGGATCGCCAGTATCTGGCCATAAACCAGATTTCTACACAGCTGTCTGTAGACCTG
ATCCTGCGGTGTGTGTCGGATGAGAGCCTGCCGTTCGACCTCCGAGCGTCCTTCTGTCGC
CTCATGCTCCACATGCACGTTGACCGGGATCCCCAGGAGTCCGTGGTGCCTGTTCGCTAT
GCCAGGCTCTGGACAGAAATCCCCACAAAGATCACAATTCATGAATATGATTCTATAACA
GACTCTTCCAGAAATGATATGAAGAGGAAATTTGCCCTGACAATGGAATTTGTTGAAGAA
TATTTGAAAGAAGTTGTAAACCAGCCCTTTCCTTTTGGGGATAAAGAAAAAAATAAACTG
ACATTTGAGGTGGTCCACTTGGCTCGGAATCTTATATACTTTGGATTTTATAGTTTCAGT
GAGTTATTAAGGCTAACAAGAACACTTCTGGCTATTTTAGACATTGTACAGGCCCCCATG
TCATCATACTTTGAAAGATTAAGCAAATTTCAAGATGGAGGAAACAATGTGATGAGAACC
ATTCATGGGGTGGGAGAGATGATGACCCAGATGGTACTCAGTAGAGGCTCCATCTTCCCC
ATGAGCGTGCCGGATGTGCCACCCAGCATCCACCCGAGCAAGCAAGGGAGCCCCACCGAG
CACGAGGATGTGACTGTGATGGACACCAAGCTGAAGATCATTGAGATTTTGCAGTTTATC
CTGAGTGTCAGACTGGATTATAGGATCTCATATATGCTGTCAATATATAAGAAGGAGTTT
GGAGAGGACAATGACAATGCGGAGACATCTGCCAGTGGATCTCCAGACACTTTACTACCA
TCAGCTATTGTTCCTGATATAGATGAAATTGCAGCTCAGGCAGAAACTATGTTTGCGGGA
AGAAAAGAAAAAAATCCAGTTCAACTTGACGATGAAGGAGGCAGGACGTTTTTACGGGTC
CTCATTCATCTGATCATGCACGACTACCCGCCTTTGCTGTCTGGAGCCCTGCAGCTGTTG
TTTAAGCACTTCAGCCAGAGGGCAGAGGTTTTACAGGCATTTAAGCAGGTGCAATTACTG
GTGTCTAATCAAGACGTAGATAACTACAAGCAAATCAAGGCAGATCTAGACCAGCTTCGA
CTGACAGTAGAAAAGTCTGAGCTATGGGTGGAGAAGAGCAGCAACTATGAGAATGGAGAA
ATAGGGGAAAGTCAAGTGAAAGGTGGTGAAGAGCCAATTGAGGAATCAAACATTTTAAGT
CCAGTGCAGGATGGAACAAAGAAACCTCAGATTGACAGCAACAAGAGCAATAACTACCGG
ATTGTAAAGGAGATTTTGATCAGGCTAAGTAAACTCTGTGTGCAGAATAAAAAGTGTCGG
AATCAACATCAACGATTACTGAAAAATATGGGGGCGCATTCGGTGGTGTTGGATCTTCTG
CAGATACCCTATGAAAAGAATGATGAAAAGATGAATGAAGTAATGAATCTAGCCCATACA
TTTCTGCAGAATTTCTGTCGAGGAAATCCACAGAATCAAGTTCTTCTTCATAAACATCTG
AATTTGTTTTTAACTCCAGGTCTCCTTGAAGCAGAAACCATGCGGCACATCTTCATGAAC
AATTACCATCTGTGCAACGAAATTAGCGAGAGAGTTGTACAACACTTTGTGCACTGCATT
GAGACACATGGCCGCCACGTGGAGTACCTGAGGTTTTTGCAAACAATTGTAAAAGCAGAT
GGTAAATATGTGAAGAAATGCCAGGATATGGTAATGACAGAGTTGATAAATGGGGGTGAA
GACGTGCTGATATTTTACAATGATAGAGCATCATTTCCAATCCTTCTCCATATGATGTGT
TCAGAGAGAGACCGAGGGGATGAGAGTGGCCCCTTAGCCTACCACATCACCCTGGTGGAG
TTGCTGGCAGCATGCACAGAGGGGAAAAATGTCTACACTGAAATCAAGTGTAATTCCCTT
CTCCCGCTGGACGACATAGTGAGGGTGGTGACCCATGACGACTGCATCCCTGAGGTTAAA
ATTGCTTATGTGAACTTTGTTAATCACTGTTATGTTGACACTGAAGTGGAAATGAAAGAA
ATCTATACAAGTAACCACATTTGGAAATTATTTGAGAACTTCTTGGTGGATATGGCAAGG
GTTTGCAACACAACTACAGACAGGAAACATGCAGACATCTTTTTGGAAAAGTGTGTTACT
GAGTCAATAATGAATATTGTGAGCGGCTTCTTTAATTCTCCCTTTTCAGACAATAGTACC
AGCCTCCAGACACATCAGCCAGTTTTTATTCAGCTACTGCAATCTGCCTTCAGAATTTAC
AATTGCACCTGGCCAAACCCAGCGCAGAAAGCCTCAGTGGAATCCTGTATCAGAACTTTG
GCTGAAGTGGCAAAAAATCGTGGAATTGCCATTCCAGTGGATTTGGACAGCCAAGTTAAT
ACTCTTTTCATGAAGAGCCATTCAAATATGGTGCAGAGAGCAGCAATGGGTTGGAGACTA
TCAGCTCGCTCTGGGCCACGCTTTAAGGAAGCTCTTGGAGGGCCTGCTTGGGATTACAGA
AATATTATTGAAAAGTTACAGGATGTAGTGGCCTCCTTGGAGCACCAGTTCAGCCCAATG
ATGCAGGCTGAATTCTCAGTGTTGGTTGATGTATTGTACAGTCCAGAACTGCTGTTCCCT
GAGGGAAGCGATGCAAGAATAAGATGTGGCGCTTTCATGTCGAAGTTGATTAATCATACA
AAGAAACTAATGGAGAAAGAAGAAAAACTGTGCATTAAAATTCTTCAGACATTACGAGAA
ATGTTAGAGAAGAAAGACAGCTTTGTGGAAGAGGGTAACACATTAAGAAAGATACTTCTG
AATCGATACTTTAAAGGTGATTATAGTATTGGTGTGAATGGACACCTATCAGGAGCCTAC
TCCAAAACTGCACAGGTGGGAGGAAGCTTTTCTGGACAAGATTCAGATAAGATGGGGATA
TCAATGTCAGACATTCAGTGTCTGCTGGATAAAGAAGGTGCATCAGAACTTGTCATCGAT
GTTATAGTGAACACCAAAAATGACAGAATTTTTTCAGAAGGCATTTTCCTCGGCATTGCC
TTGCTTGAAGGAGGAAATACACAAACACAGTATTCTTTCTACCAGCAGTTGCATGAACAA
AAAAAGTCAGAAAAATTCTTTAAAGTTCTCTATGATCGAATGAAGGCTGCTCAGAAAGAA
ATAAGATCAACAGTGACAGTTAATACCATAGATTTAGGTAACAAAAAAAGGGACGATGAC
AATGAATTGATGACATCTGGTCCACGAATGAGAGTAAGAGATTCAACACTACATTTAAAA
GAGGGAATGAAAGGGCAATTAACAGAAGCTTCTTCAGCAACATCCAAAGCATATTGTGTA
TACAGAAGAGAAATGGATCCAGAAATAGACATTATGTGCACAGGACCAGAAGCGGGAAAC
ACTGAGGAAAAATCCGCAGAGGAAGTAACAATGAGTCCCGCAATTGCCATCATGCAGCCA
ATACTGAGATTTCTTCAGTTACTGTGTGAGAATCACAACCGGGAATTGCAGAACTTCTTG
AGGAATCAAAACAACAAAACAAATTACAACCTAGTCTGTGAGACCCTTCAGTTTCTGGAC
TGCATTTGTGGAAGTACAACCGGTGGCCTGGGCCTGTTGGGTCTCTACATCAATGAGAAG
AATGTAGCGCTGGTCAACCAGAACCTGGAGAGCTTGACTGAGTATTGCCAGGGCCCTTGC
CATGAAAATCAGACCTGTATCGCTACACATGAGTCTAATGGGATTGATATCATCATTGCT
TTGATTCTGAATGACATAAACCCTCTTGGTAAATACCGAATGGACCTGGTGCTCCAGCTA
AAGAACAATGCATCTAAACTTTTGCTGGCCATTATGGAAAGCAGACATGACAGTGAGAAT
GCAGAAAGAATTCTTTTTAACATGAGACCCAGAGAACTGGTGGATGTGATGAAGAATGCC
TATAACCAAGGATTGGAATGTGACCATGGGGATGATGAGGGTGGAGATGATGGTGTTTCT
CCAAAAGATGTTGGACACAATATCTATATTCTGGCCCATCAGTTGGCCCGCCACAATAAA
CTGTTGCAGCAGATGCTCAAACCAGGATCGGATCCAGATGAAGGAGATGAAGCCTTAAAG
TATTATGCCAACCACACTGCACAGATTGAGATTGTCCGGCATGATAGGACCATGGAACAA
ATAGTTTTTCCTGTCCCCAATATATGTGAATACCTCACTCGAGAATCCAAGTGCCGTGTG
TTCAATACAACTGAAAGGGATGAACAAGGAAGTAAAGTGAATGACTTTTTCCAGCAAACA
GAAGATCTCTACAATGAAATGAAGTGGCAGAAGAAAATCAGGAATAACCCTGCACTGTTC
TGGTTCTCGAGGCACATCTCTCTCTGGGGGAGCATTTCCTTCAACCTGGCTGTGTTCATC
AATTTAGCTGTTGCTCTCTTCTACCCATTTGGGGATGATGGAGATGAAGGTACACTTTCT
CCATTGTTCTCGGTTCTTCTTTGGATAGCAGTTGCGATCTGCACATCTATGCTGTTTTTC
TTCTCCAAGCCTGTGGGTATTCGGCCGTTTCTTGTATCAATAATGCTCAGATCAATATAT
ACAATAGGTCTTGGGCCTACATTAATACTTCTTGGTGCAGCTAATCTTTGTAATAAAATT
GTTTTTCTGGTGAGTTTTGTTGGAAATCGTGGCACGTTCACCCGTGGGTACCGAGCAGTC
ATCCTGGATATGGCCTTTCTCTATCACGTGGCGTATGTCCTGGTTTGCATGCTGGGCCTT
TTTGTCCATGAATTCTTCTATAGCTTCCTGCTTTTTGATTTGGTGTACAGGGAAGAGACT
TTGCTGAATGTCATAAAAAGTGTCACACGAAATGGCCGCTCTATTATTCTAACTGCAGTC
CTGGCTCTCATCCTCGTCTACCTGTTTTCCATTATTGGGTTCCTTTTTTTGAAGGATGAC
TTCACTATGGAAGTTGATAGGCTGAAAAACCGAACTCCTGTTACAGGCAGTCATCAAGTG
CCTACTATGACTTTAACTACCATGATGGAAGCATGTGCCAAGGAGAACTGTTCACCCACA
ATTCCAGCTTCAAATACAGCTGATGAAGAGTATGAAGATGGAATTGAAAGGACGTGTGAC
ACTCTCCTTATGTGCATTGTCACCGTGCTGAACCAGGGCCTCAGGAATGGCGGTGGTGTG
GGGGATGTGCTAAGAAGGCCATCGAAAGATGAGCCCTTGTTTGCTGCCCGAGTGGTTTAT
GACCTTCTTTTTTATTTCATTGTTATCATTATTGTTCTGAACTTGATTTTTGGTGTTATC
ATCGATACTTTTGCTGATCTCAGAAGCGAAAAACAGAAAAAAGAAGAAATTCTAAAGACA
ACTTGTTTCATCTGTGGACTTGAGAGAGACAAGTTTGATAATAAAACGGTTTCATTTGAG
GAGCACATTAAGTCAGAACACAATATGTGGCATTATTTGTACTTCATAGTCCTGGTGAAA
GTTAAAGACCCAACAGAATACACTGGACCTGAAAGTTATGTGGCTCAAATGATTGTGGAG
AAGAATTTGGATTGGTTTCCTCGGATGCGAGCCATGTCCCTCGTTAGCAATGAAGGCGAC
AGTGAGCAAAATGAAATTCGGAGCCTTCAGGAGAAGTTGGAATCGACCATGAGTCTGGTC
AAACAGCTGTCGGGTCAGCTGGCGGAGCTCAAGGAGCAGATGACAGAACAAAGGAAGAAT
AAGCAGAGACTGGGCTTCCTCGGATCAAACACACCCCATGTGAATCATCACATGCCACCA
CACTGA
Enzyme 17 GenBank Gene ID NM_002223.2 Link Image
Enzyme 17 GeneCard ID ITPR2 Link Image
Enzyme 17 GenAtlas ID ITPR2 Link Image
Enzyme 17 HGNC ID HGNC:6181 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 12p11
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Yamamoto-Hino M, Sugiyama T, Hikichi K, Mattei MG, Hasegawa K, Sekine S, Sakurada K, Miyawaki A, Furuichi T, Hasegawa M, et al.: Cloning and characterization of human type 2 and type 3 inositol 1,4,5-trisphosphate receptors. Receptors Channels. 1994;2(1):9-22. [PubMed Link Image]
  2. Futatsugi A, Kuwajima G, Mikoshiba K: Muscle-specific mRNA isoform encodes a protein composed mainly of the N-terminal 175 residues of type 2 Ins(1,4,5)P3 receptor. Biochem J. 1998 Sep 15;334 ( Pt 3):559-63. [PubMed Link Image]
  3. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  4. Yang J, McBride S, Mak DO, Vardi N, Palczewski K, Haeseleer F, Foskett JK: Identification of a family of calcium sensors as protein ligands of inositol trisphosphate receptor Ca(2+) release channels. Proc Natl Acad Sci U S A. 2002 May 28;99(11):7711-6. [PubMed Link Image]
  5. 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]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 13455
Enzyme 18 Name Inositol 1,4,5-trisphosphate receptor type 3
Enzyme 18 Synonyms
  1. IP3 receptor isoform 3
  2. IP3R 3
  3. InsP3R3
  4. Type 3 inositol 1,4,5-trisphosphate receptor
  5. Type 3 InsP3 receptor
Enzyme 18 Gene Name ITPR3
Enzyme 18 Protein Sequence >Inositol 1,4,5-trisphosphate receptor type 3
MSEMSSFLHIGDIVSLYAEGSVNGFISTLGLVDDRCVVEPAAGDLDNPPKKFRDCLFKVC
PMNRYSAQKQYWKAKQTKQDKEKIADVVLLQKLQHAAQMEQKQNDTENKKVHGDVVKYGS
VIQLLHMKSNKYLTVNKRLPALLEKNAMRVTLDATGNEGSWLFIQPFWKLRSNGDNVVVG
DKVILNPVNAGQPLHASNYELSDNAGCKEVNSVNCNTSWKINLFMQFRDHLEEVLKGGDV
VRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHW
NGLYRFKHLATGNYLAAEENPSYKGDASDPKAAGMGAQGRTGRRNAGEKIKYCLVAVPHG
NDIASLFELDPTTLQKTDSFVPRNSYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTC
PTKEDKEAFAIVSVPVSEIRDLDFANDASSMLASAVEKLNEGFISQNDRRFVIQLLEDLV
FFVSDVPNNGQNVLDIMVTKPNRERQKLMREQNILKQVFGILKAPFREKGGEGPLVRLEE
LSDQKNAPYQHMFRLCYRVLRHSQEDYRKNQEHIAKQFGMMQSQIGYDILAEDTITALLH
NNRKLLEKHITKTEVETFVSLVRKNREPRFLDYLSDLCVSNHIAIPVTQELICKCVLDPK
NSDILIRTELRPVKEMAQSHEYLSIEYSEEEVWLTWTDKNNEHHEKSVRQLAQEARAGNA
HDENVLSYYRYQLKLFARMCLDRQYLAIDEISQQLGVDLIFLCMADEMLPFDLRASFCHL
MLHVHVDRDPQELVTPVKFARLWTEIPTAITIKDYDSNLNASRDDKKNKFANTMEFVEDY
LNNVVSEAVPFANEEKNKLTFEVVSLAHNLIYFGFYSFSELLRLTRTLLGIIDCVQGPPA
MLQAYEDPGGKNVRRSIQGVGHMMSTMVLSRKQSVFSAPSLSAGASAAEPLDRSKFEENE
DIVVMETKLKILEILQFILNVRLDYRISYLLSVFKKEFVEVFPMQDSGADGTAPAFDSTT
ANMNLDRIGEQAEAMFGVGKTSSMLEVDDEGGRMFLRVLIHLTMHDYAPLVSGALQLLFK
HFSQRQEAMHTFKQVQLLISAQDVENYKVIKSELDRLRTMVEKSELWVDKKGSGKGEEVE
AGAAKDKKERPTDEEGFLHPPGEKSSENYQIVKGILERLNKMCGVGEQMRKKQQRLLKNM
DAHKVMLDLLQIPYDKGDAKMMEILRYTHQFLQKFCAGNPGNQALLHKHLHLFLTPGLLE
AETMQHIFLNNYQLCSEISEPVLQHFVHLLATHGRHVQYLDFLHTVIKAEGKYVKKCQDM
IMTELTNAGDDVVVFYNDKASLAHLLDMMKAARDGVEDHSPLMYHISLVDLLAACAEGKN
VYTEIKCTSLLPLEDVVSVVTHEDCITEVKMAYVNFVNHCYVDTEVEMKEIYTSNHIWTL
FENFTLDMARVCSKREKRVADPTLEKYVLSVVLDTINAFFSSPFSENSTSLQTHQTIVVQ
LLQSTTRLLECPWLQQQHKGSVEACIRTLAMVAKGRAILLPMDLDAHISSMLSSGASCAA
AAQRNASSYKATTRAFPRVTPTANQWDYKNIIEKLQDIITALEERLKPLVQAELSVLVDV
LHWPELLFLEGSEAYQRCESGGFLSKLIQHTKDLMESEEKLCIKVLRTLQQMLLKKTKYG
DRGNQLRKMLLQNYLQNRKSTSRGDLPDPIGTGLDPDWSAIAATQCRLDKEGATKLVCDL
ITSTKNEKIFQESIGLAIHLLDGGNTEIQKSFHNLMMSDKKSERFFKVLHDRMKRAQQET
KSTVAVNMNDLGSQPHEDREPVDPTTKGRVASFSIPGSSSRYSLGPSLRRGHEVSERVQS
SEMGTSVLIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDIMCGSTTG
GLGLLGLYINEDNVGLVIQTLETLTEYCQGPCHENQTCIVTHESNGIDIITALILNDISP
LCKYRMDLVLQLKDNASKLLLALMESRHDSENAERILISLRPQELVDVIKKAYLQEEERE
NSEVSPREVGHNIYILALQLSRHNKQLQHLLKPVKRIQEEEAEGISSMLSLNNKQLSQML
KSSAPAQEEEEDPLAYYENHTSQIEIVRQDRSMEQIVFPVPGICQFLTEETKHRLFTTTE
QDEQGSKVSDFFDQSSFLHNEMEWQRKLRSMPLIYWFSRRMTLWGSISFNLAVFINIIIA
FFYPYMEGASTGVLDSPLISLLFWILICFSIAALFTKRYSIRPLIVALILRSIYYLGIGP
TLNILGALNLTNKIVFVVSFVGNRGTFIRGYKAMVMDMEFLYHVGYILTSVLGLFAHELF
YSILLFDLIYREETLFNVIKSVTRNGRSILLTALLALILVYLFSIVGFLFLKDDFILEVD
RLPNNHSTASPLGMPHGAAAFVDTCSGDKMDCVSGLSVPEVLEEDRELDSTERACDTLLM
CIVTVMNHGLRNGGGVGDILRKPSKDESLFPARVVYDLLFFFIVIIIVLNLIFGVIIDTF
ADLRSEKQKKEEILKTTCFICGLERDKFDNKTVSFEEHIKLEHNMWNYLYFIVLVRVKNK
TDYTGPESYVAQMIKNKNLDWFPRMRAMSLVSNEGEGEQNEIRILQDKLNSTMKLVSHLT
AQLNELKEQMTEQRKRRQRLGFVDVQNCISR
Enzyme 18 Number of Residues 2671
Enzyme 18 Molecular Weight 304104.0
Enzyme 18 Theoretical pI 6.45
Enzyme 18 GO Classification
Function
  • calcium channel activity
  • cation channel activity
  • inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity
  • intracellular ligand-gated ion channel activity
  • ion channel activity
  • ion transmembrane transporter activity
  • ligand-gated ion channel activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • calcium ion transport
  • cation transport
  • di-, tri-valent inorganic cation transport
  • divalent metal ion transport
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • endoplasmic reticulum
  • intracellular membrane-bounded organelle
  • membrane
  • membrane-bounded organelle
  • organelle
Enzyme 18 General Function Involved in calcium channel activity
Enzyme 18 Specific Function Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • 2203-2223 2236-2256 2265-2285 2326-2346 2369-2389 2497-2517
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 55957567 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q14573 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name ITPR3_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >8016 bp
ATGAGTGAAATGTCCAGCTTTCTTCACATCGGGGACATCGTCTCCCTGTACGCCGAGGGC
TCCGTCAATGGCTTCATCAGCACTTTGGGGCTGGTGGATGACCGCTGTGTGGTGGAGCCC
GCGGCCGGGGACCTGGACAACCCCCCTAAGAAGTTCCGTGACTGCCTCTTCAAGGTGTGC
CCCATGAACCGCTACTCGGCCCAGAAGCAGTACTGGAAGGCCAAGCAGACTAAGCAGGAC
AAGGAGAAGATCGCTGATGTGGTGTTGCTGCAGAAGCTGCAGCATGCGGCGCAGATGGAG
CAGAAGCAAAATGACACGGAGAACAAGAAGGTGCATGGGGATGTCGTGAAGTATGGCAGT
GTGATCCAGCTCCTGCACATGAAGAGCAACAAGTACCTGACAGTGAACAAGCGGCTTCCG
GCCTTGCTGGAGAAGAACGCCATGCGGGTGACTCTGGATGCCACAGGCAACGAGGGTTCC
TGGCTCTTCATCCAGCCCTTCTGGAAGCTGCGGAGCAACGGGGACAACGTGGTCGTGGGG
GACAAGGTGATCCTGAATCCTGTCAATGCCGGGCAGCCTCTGCATGCCAGCAATTACGAG
CTCAGCGACAACGCCGGCTGCAAGGAGGTCAATTCTGTGAACTGCAACACCAGCTGGAAG
ATCAACCTGTTTATGCAGTTTCGGGACCACCTGGAGGAGGTGTTGAAAGGGGGAGACGTG
GTGCGGCTGTTCCATGCGGAGCAGGAGAAGTTCCTGACGTGTGACGAGTACAAGGGCAAG
CTGCAGGTGTTCCTGCGAACTACACTGCGCCAGTCTGCCACCTCGGCCACCAGCTCCAAT
GCTCTCTGGGAGGTGGAGGTGGTCCACCACGACCCCTGCCGTGGAGGAGCTGGGCACTGG
AATGGCTTGTACCGCTTCAAGCACCTGGCTACAGGCAACTACCTGGCTGCTGAGGAGAAC
CCCAGTTACAAAGGTGATGCCTCAGATCCCAAGGCAGCAGGAATGGGGGCACAGGGCCGC
ACAGGCCGCAGGAATGCTGGGGAGAAGATCAAGTACTGCCTGGTGGCTGTGCCTCATGGC
AATGACATCGCCTCTCTCTTTGAGCTGGACCCCACCACCTTGCAGAAAACCGACTCTTTC
GTGCCCCGGAACTCGTACGTCCGGCTGCGGCACCTCTGCACCAACACGTGGATTCAGAGC
ACCAATGTGCCCATTGACATCGAGGAGGAGCGGCCCATCCGGCTCATGCTGGGCACCTGC
CCCACCAAGGAGGACAAGGAGGCCTTTGCCATCGTGTCAGTGCCCGTGTCTGAGATCCGA
GACCTGGACTTTGCCAATGACGCCAGCTCCATGCTGGCCAGTGCCGTGGAGAAACTCAAC
GAGGGCTTCATCAGCCAGAATGACCGCAGGTTTGTCATCCAGCTGCTGGAAGACCTGGTG
TTCTTTGTCAGCGATGTCCCCAACAATGGGCAGAATGTCCTGGACATCATGGTCACTAAG
CCCAACCGGGAACGGCAGAAGCTGATGAGGGAGCAGAACATCCTCAAACAGGTCTTTGGC
ATTCTGAAGGCCCCGTTCCGTGAGAAGGGGGGTGAAGGTCCCCTGGTGCGGCTGGAGGAG
CTGTCAGACCAGAAGAACGCCCCCTACCAGCACATGTTCCGCCTGTGCTACCGCGTGTTG
CGGCATTCCCAGGAGGACTACCGCAAGAACCAGGAGCACATTGCCAAGCAGTTTGGGATG
ATGCAGTCCCAGATTGGCTACGACATCCTGGCCGAGGACACCATCACTGCCCTGCTGCAC
AACAACCGCAAGCTCCTGGAAAAGCACATCACCAAGACCGAGGTGGAGACCTTCGTCAGC
CTTGTGCGCAAGAACCGGGAGCCCAGGTTCCTGGACTACCTCTCTGACCTGTGTGTGTCC
AACCACATCGCCATCCCCGTCACCCAAGAGCTCATCTGCAAGTGTGTGCTGGACCCCAAG
AACAGTGACATTCTCATCCGGACCGAGCTTCGGCCCGTGAAGGAGATGGCCCAATCCCAC
GAGTACCTGAGCATCGAGTACTCAGAAGAGGAAGTGTGGCTCACGTGGACTGACAAGAAT
AACGAGCATCATGAGAAGAGTGTGAGGCAGCTGGCCCAGGAGGCGCGGGCCGGCAACGCC
CACGACGAGAATGTGCTCAGCTACTACAGGTACCAGCTGAAGCTCTTTGCCCGCATGTGC
TTGGACCGCCAGTACTTGGCCATCGACGAGATCTCCCAGCAGCTGGGCGTGGACCTGATT
TTCCTGTGCATGGCAGACGAGATGCTGCCCTTTGACCTGCGCGCCTCCTTCTGCCACCTG
ATGCTGCACGTGCACGTGGACCGTGACCCCCAGGAGCTGGTCACGCCGGTCAAGTTTGCC
CGTCTCTGGACTGAGATCCCCACAGCCATCACCATCAAGGACTATGATTCCAACCTCAAC
GCGTCCCGAGATGACAAGAAGAACAAGTTTGCCAACACCATGGAGTTCGTGGAGGACTAC
CTCAACAATGTAGTCAGCGAGGCCGTGCCCTTTGCCAACGAGGAGAAGAACAAGCTCACT
TTTGAGGTGGTCAGCCTGGCGCACAATCTCATCTACTTCGGCTTCTACAGCTTCAGCGAG
CTGCTGCGGCTCACTCGCACACTGCTGGGCATCATCGACTGTGTGCAGGGGCCCCCGGCC
ATGCTGCAGGCCTATGAGGACCCCGGTGGCAAGAATGTGCGGCGGTCCATCCAGGGCGTG
GGGCACATGATGTCCACCATGGTGCTGAGCCGCAAGCAGTCCGTCTTCAGTGCCCCCAGC
CTGTCTGCTGGGGCCAGTGCTGCTGAGCCGCTGGACAGAAGCAAGTTTGAGGAGAATGAG
GACATTGTGGTGATGGAGACCAAGCTGAAGATCCTGGAAATCCTTCAGTTCATCCTCAAT
GTCCGCCTGGATTACCGCATATCCTACCTGCTGTCTGTCTTCAAGAAGGAGTTTGTGGAG
GTGTTTCCCATGCAGGACAGTGGGGCTGATGGCACAGCCCCTGCCTTCGACTCTACCACT
GCCAACATGAACCTGGATCGCATCGGGGAGCAGGCGGAGGCCATGTTTGGAGTGGGGAAG
ACAAGCAGCATGCTGGAGGTGGATGACGAGGGCGGCCGCATGTTCCTGCGCGTGCTCATC
CACCTCACCATGCACGACTATGCGCCGCTGGTCTCGGGTGCCCTGCAGCTGCTCTTCAAG
CACTTCAGCCAGCGCCAGGAGGCCATGCACACCTTCAAGCAGGTTCAGCTGCTGATCTCA
GCGCAGGACGTGGAGAACTACAAGGTGATCAAGTCGGAGCTGGACCGGCTGCGGACCATG
GTGGAGAAGTCAGAGCTGTGGGTGGACAAGAAGGGCAGTGGCAAGGGTGAGGAGGTGGAG
GCAGGCGCCGCCAAGGACAAGAAAGAGCGTCCCACGGACGAGGAGGGCTTTCTGCACCCA
CCAGGGGAGAAAAGCAGTGAGAACTACCAGATCGTCAAGGGCATCCTGGAAAGGCTGAAC
AAGATGTGCGGGGTTGGGGAGCAAATGAGGAAGAAGCAGCAACGGCTGCTGAAGAACATG
GATGCCCACAAGGTCATGCTGGACCTGCTGCAGATCCCCTATGACAAGGGTGATGCCAAG
ATGATGGAGATCCTGCGCTACACGCACCAGTTCCTGCAGAAGTTCTGTGCAGGGAACCCC
GGCAACCAGGCCCTGCTGCACAAACACCTGCACCTCTTCCTCACGCCAGGGCTCCTGGAG
GCAGAGACCATGCAGCACATCTTCCTGAACAACTATCAGCTCTGCTCCGAGATCAGCGAG
CCTGTGTTGCAGCACTTCGTGCACCTGCTGGCCACGCACGGGCGCCATGTGCAGTACCTG
GACTTCCTGCACACCGTCATTAAGGCCGAGGGCAAGTACGTCAAGAAGTGCCAGGACATG
ATCATGACTGAGCTGACCAATGCAGGTGACGATGTGGTCGTGTTCTACAATGATAAGGCA
TCGCTGGCCCACCTGCTGGACATGATGAAGGCCGCCCGCGACGGCGTGGAGGACCACAGC
CCCCTCATGTACCACATTTCCCTGGTGGACCTGCTGGCCGCCTGTGCCGAGGGCAAAAAC
GTCTACACTGAGATCAAGTGCACCTCCCTGCTGCCGCTGGAGGACGTGGTGTCTGTGGTG
ACGCATGAGGACTGCATCACTGAGGTGAAAATGGCCTATGTGAACTTCGTGAACCACTGC
TACGTGGACACGGAGGTGGAGATGAAGGAGATCTACACCAGCAACCACATCTGGACGCTC
TTTGAGAACTTCACCCTGGACATGGCCCGGGTCTGCAGCAAGCGTGAGAAGCGCGTGGCT
GACCCCACCTTGGAGAAGTACGTGCTGAGCGTTGTGCTGGACACCATCAACGCCTTCTTC
AGCTCCCCATTCTCTGAGAACAGCACTTCCCTGCAGACACACCAGACGATTGTGGTGCAG
CTGCTGCAGTCTACCACACGCCTCCTCGAGTGTCCGTGGCTACAGCAGCAGCACAAGGGC
TCCGTGGAGGCCTGCATCCGGACCCTCGCCATGGTGGCCAAGGGCCGGGCCATCTTGCTG
CCCATGGACCTGGATGCCCACATCAGCTCGATGCTCAGCAGTGGAGCCAGCTGTGCAGCT
GCCGCCCAGCGGAACGCCTCCAGCTACAAGGCAACCACGCGGGCCTTCCCCCGCGTCACC
CCCACCGCCAACCAGTGGGACTACAAGAACATCATTGAGAAGCTGCAGGACATCATCACA
GCCCTGGAGGAGCGGCTGAAGCCCCTGGTACAGGCTGAGCTGTCCGTGCTGGTGGATGTC
CTGCACTGGCCTGAGCTGCTCTTCCTGGAGGGCAGTGAGGCCTACCAGCGCTGCGAGAGT
GGGGGCTTCCTGTCCAAGCTGATCCAGCACACCAAGGACCTCATGGAGTCGGAGGAGAAG
CTGTGCATCAAGGTGCTGCGGACCCTGCAGCAGATGCTGCTCAAGAAGACCAAGTACGGG
GACCGGGGCAACCAGCTGCGCAAGATGCTGCTGCAAAACTACCTCCAGAACCGGAAGTCC
ACCTCGCGGGGGGACCTTCCCGACCCCATAGGCACTGGCCTGGACCCAGACTGGTCGGCA
ATCGCAGCCACCCAGTGCCGGCTGGACAAGGAGGGGGCCACCAAGTTGGTATGCGACCTC
ATCACCAGCACCAAGAACGAGAAGATCTTCCAGGAGAGCATCGGCCTGGCCATCCACCTG
CTGGATGGTGGCAACACAGAGATCCAGAAATCCTTCCACAACCTGATGATGAGTGACAAG
AAGTCAGAGCGCTTCTTCAAGGTGCTGCACGACCGCATGAAGCGGGCCCAGCAGGAGACC
AAGTCCACGGTGGCAGTCAACATGAATGACCTGGGCAGCCAGCCACATGAGGACCGCGAG
CCAGTCGACCCCACCACCAAAGGCCGCGTGGCCTCCTTCTCGATACCTGGCTCCTCATCC
CGCTACTCGCTGGGCCCCAGCCTGCGCCGGGGGCACGAGGTGAGCGAACGTGTGCAGAGC
AGTGAGATGGGCACATCCGTGCTCATCATGCAGCCCATCCTGCGCTTTCTGCAGCTGCTG
TGTGAGAACCACAACCGGGACCTGCAGAACTTCCTGCGCTGTCAGAACAACAAAACCAAC
TACAACTTGGTATGCGAGACGCTGCAGTTCCTGGACATCATGTGCGGCAGCACCACGGGC
GGCCTGGGGCTGCTGGGGCTCTACATCAATGAGGACAACGTGGGCCTCGTCATCCAGACC
TTGGAGACCCTCACTGAGTACTGCCAGGGCCCCTGCCATGAGAACCAGACTTGCATTGTG
ACTCACGAGTCCAATGGCATAGACATCATCACCGCACTGATCCTCAATGACATCAGCCCC
CTGTGCAAGTACCGCATGGATCTGGTGCTGCAGCTCAAGGACAATGCCTCCAAGCTGCTC
CTGGCTCTGATGGAGAGCCGGCATGACAGTGAAAATGCTGAGCGAATCCTCATCAGCCTG
CGGCCCCAGGAGCTGGTGGACGTCATCAAGAAGGCCTACCTGCAGGAGGAAGAGCGTGAG
AACTCGGAGGTGAGCCCACGTGAAGTGGGCCATAACATCTATATCCTGGCGCTGCAGCTC
TCCAGGCACAATAAACAGCTGCAGCACCTGCTGAAGCCGGTGAAGCGCATTCAAGAGGAG
GAGGCCGAGGGTATCTCTTCCATGCTCAGCCTCAACAACAAGCAGCTGTCACAGATGCTC
AAGTCCTCAGCGCCAGCACAGGAGGAGGAGGAAGACCCCCTGGCCTACTATGAGAACCAC
ACGTCCCAGATCGAGATTGTGCGGCAGGACCGCAGCATGGAGCAGATCGTGTTCCCAGTG
CCCGGCATCTGCCAGTTCCTGACGGAGGAAACCAAGCACCGGCTCTTCACCACTACTGAG
CAGGACGAGCAGGGCAGCAAAGTGAGCGACTTCTTCGACCAGTCCTCCTTCCTGCACAAC
GAGATGGAGTGGCAGCGCAAGCTCCGCAGCATGCCGCTGATCTACTGGTTCTCCCGCCGC
ATGACCCTGTGGGGCAGCATCTCCTTCAACCTGGCCGTGTTTATCAACATCATCATTGCC
TTCTTCTACCCTTACATGGAGGGCGCGTCCACAGGCGTGCTGGACTCCCCTCTCATCTCA
TTGCTCTTCTGGATCCTCATCTGCTTCTCCATCGCGGCCCTGTTCACCAAGCGCTACAGC
ATCCGCCCCCTCATCGTGGCGCTCATCCTGCGCTCCATCTACTATCTGGGCATCGGGCCC
ACACTCAACATCCTGGGTGCCCTCAATCTGACCAACAAGATCGTGTTTGTGGTGAGCTTC
GTGGGCAACCGTGGCACCTTCATCCGGGGCTATAAGGCCATGGTCATGGACATGGAATTC
CTCTACCACGTGGGCTACATCCTGACCAGTGTCCTGGGCCTCTTTGCTCATGAGCTGTTC
TACAGCATCCTGCTCTTTGACCTCATCTACCGCGAGGAGACGCTGTTCAACGTCATCAAG
AGTGTGACCCGCAATGGCCGCTCCATCCTGCTGACAGCCCTGCTGGCCCTCATCCTGGTC
TACCTCTTCTCCATCGTCGGCTTCCTCTTCCTCAAGGATGACTTCATTCTCGAGGTCGAC
CGGCTGCCCAACAACCACTCCACAGCCAGCCCCCTGGGGATGCCACATGGAGCTGCTGCA
TTTGTGGACACCTGCAGTGGGGACAAGATGGACTGTGTCTCAGGGCTCTCGGTGCCTGAG
GTCCTGGAAGAGGACAGGGAGCTGGACAGCACAGAGCGGGCCTGTGACACTCTGTTGATG
TGCATCGTCACTGTCATGAACCATGGGCTACGCAACGGTGGTGGCGTGGGCGACATTCTC
CGCAAGCCCTCCAAAGATGAGTCTCTCTTCCCAGCCCGAGTGGTCTATGACCTCCTGTTC
TTCTTCATCGTCATCATCATTGTGCTGAACCTCATCTTTGGGGTAATCATCGACACCTTC
GCTGACCTGCGTAGTGAGAAGCAGAAGAAGGAGGAGATTCTTAAGACGACATGCTTCATC
TGTGGTCTGGAGAGGGACAAGTTTGATAACAAGACAGTGTCATTTGAGGAACACATCAAG
CTGGAGCACAACATGTGGAACTACTTGTACTTCATTGTGCTGGTCCGCGTGAAGAACAAG
ACCGACTACACGGGCCCTGAGAGCTACGTGGCCCAGATGATCAAGAACAAGAACCTGGAC
TGGTTCCCCCGGATGCGGGCCATGTCCCTTGTCAGCAATGAGGGCGAGGGGGAGCAGAAT
GAGATTCGGATTCTCCAGGACAAGCTCAACTCCACCATGAAGCTGGTGTCCCACCTCACT
GCCCAGCTCAACGAGCTCAAGGAGCAGATGACGGAGCAGCGGAAACGCAGGCAACGCCTA
GGCTTTGTGGATGTCCAGAACTGCATTAGCCGCTGA
Enzyme 18 GenBank Gene ID AL139044 Link Image
Enzyme 18 GeneCard ID ITPR3 Link Image
Enzyme 18 GenAtlas ID ITPR3 Link Image
Enzyme 18 HGNC ID HGNC:6182 Link Image
Enzyme 18 Chromosome Location 6
Enzyme 18 Locus 6p21
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Yamamoto-Hino M, Sugiyama T, Hikichi K, Mattei MG, Hasegawa K, Sekine S, Sakurada K, Miyawaki A, Furuichi T, Hasegawa M, et al.: Cloning and characterization of human type 2 and type 3 inositol 1,4,5-trisphosphate receptors. Receptors Channels. 1994;2(1):9-22. [PubMed Link Image]
  2. Maranto AR: Primary structure, ligand binding, and localization of the human type 3 inositol 1,4,5-trisphosphate receptor expressed in intestinal epithelium. J Biol Chem. 1994 Jan 14;269(2):1222-30. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Yang J, McBride S, Mak DO, Vardi N, Palczewski K, Haeseleer F, Foskett JK: Identification of a family of calcium sensors as protein ligands of inositol trisphosphate receptor Ca(2+) release channels. Proc Natl Acad Sci U S A. 2002 May 28;99(11):7711-6. [PubMed Link Image]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. 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 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 16047
Enzyme 19 Name Phospholipase C, beta 3 (Phosphatidylinositol-specific) (Phospholipase C, beta 3 (Phosphatidylinositol-specific), isoform CRA_a)
Enzyme 19 Synonyms Not Available
Enzyme 19 Gene Name PLCB3
Enzyme 19 Protein Sequence >Phospholipase C, beta 3 (Phosphatidylinositol-specific) (Phospholipase C, beta 3 (Phosphatidylinositol-specific), isoform CRA_a)
MAGAQPGVHALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNME
VDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNF
MAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFS
ADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPY
LTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYL
GGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRC
VELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAK
QQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDS
AGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGD
EGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPV
KFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYM
PQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIV
DGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEP
FDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLI
YTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQL
GSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGH
KALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVED
TKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQF
KRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLE
EAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLG
DGPLVACASNGHAPGSSGHLSGADSESQEENTQL
Enzyme 19 Number of Residues 1234
Enzyme 19 Molecular Weight 138801
Enzyme 19 Theoretical pI 5.66
Enzyme 19 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Not Available
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein Not Available
Enzyme 19 UniProtKB/Swiss-Prot ID A5PKZ6 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name A5PKZ6_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID BC142681 Link Image
Enzyme 19 GeneCard ID A5PKZ6 Link Image
Enzyme 19 GenAtlas ID Not Available
Enzyme 19 HGNC ID Not Available
Enzyme 19 Chromosome Location 11
Enzyme 19 Locus 11q13
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 16048
Enzyme 20 Name Phospholipase C, gamma 1
Enzyme 20 Synonyms
  1. SubName: Phospholipase C, gamma 1, isoform CRA_b
Enzyme 20 Gene Name PLCG1
Enzyme 20 Protein Sequence >Phospholipase C, gamma 1
MAGAASPCANGCGPGAPSDAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQI
TWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTL
SLQATSEDEVNMWIKGLTWLMEDTLQAPTPLQIERWLRKQFYSVDRNREDRISAKDLKNM
LSQVNYRVPNMRFLRERLTDLEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLEASTLRA
GERPELCRVSLPEFQQFLLDYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDEFVT
FLFSKENSVWNSQLDAVCPDTMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMG
CRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIA
QQRNMAQYFKKVLGDTLLTKPVEISADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSMM
YSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEVSS
STELHSNEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFW
RNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQT
NAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQE
GQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNP
GFYVEANPMPTFKCAVKALFDYKAQREDELTFIKSAIIQNVEKQEGGWWRGDYGGKKQLW
FPSNYVEEMVNPVALEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSIS
MASVAHWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKIMERRKKIALELSELVVYC
RPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDS
SNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMTGRHCGYVLQPSTMRDEAFDPFDKS
SLRGLEPCAISIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVW
PAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDL
ELASLLIKIDIFPAKQENGDLSPFSGTSLRERGSDASGQLFHGRAREGSFESRYQQPFED
FRISQEHLADHFDSRERRAPRRTRVNGDNRL
Enzyme 20 Number of Residues 1291
Enzyme 20 Molecular Weight 148658.9
Enzyme 20 Theoretical pI 5.91
Enzyme 20 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • molecular transducer activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • protein binding
  • signal transducer activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid catabolic process
  • phospholipid metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 20 General Function Involved in calcium ion binding
Enzyme 20 Specific Function Not Available
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 123228952 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID A2A284 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name A2A284_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >3876 bp
ATGGCGGGCGCCGCGTCCCCTTGCGCCAACGGCTGCGGGCCCGGCGCGCCCTCGGACGCC
GAGGTGCTGCACCTCTGCCGCAGCCTCGAGGTGGGCACCGTCATGACTTTGTTCTACTCC
AAGAAGTCGCAGCGACCCGAGCGGAAGACCTTCCAGGTCAAGCTGGAGACGCGCCAGATC
ACGTGGAGCCGGGGCGCCGACAAGATCGAGGGGGCCATTGACATTCGTGAAATTAAGGAG
ATCCGCCCAGGGAAGACCTCACGGGACTTTGATCGCTATCAAGAGGACCCAGCTTTCCGG
CCGGACCAGTCACATTGCTTTGTCATTCTCTATGGAATGGAATTTCGCCTGAAAACGCTG
AGCCTGCAAGCCACATCTGAGGATGAAGTGAACATGTGGATCAAGGGCTTAACTTGGCTG
ATGGAGGATACATTGCAGGCACCCACACCCCTGCAGATTGAGAGGTGGCTCCGGAAGCAG
TTTTACTCAGTGGATCGGAATCGTGAGGATCGTATATCAGCCAAGGACCTGAAGAACATG
CTGTCCCAGGTCAACTACCGGGTCCCCAACATGCGCTTCCTCCGAGAGCGGCTGACGGAC
CTGGAGCAGCGCAGCGGGGACATCACCTACGGGCAGTTTGCTCAGCTGTACCGCAGCCTC
ATGTACAGCGCCCAGAAGACGATGGACCTCCCCTTCTTGGAAGCCAGTACTCTGAGGGCT
GGGGAGCGGCCGGAGCTTTGCCGAGTGTCCCTTCCTGAGTTCCAGCAGTTCCTTCTTGAC
TACCAGGGGGAGCTGTGGGCTGTTGATCGCCTCCAGGTGCAGGAGTTCATGCTCAGCTTC
CTCCGAGACCCCTTACGAGAGATCGAGGAGCCATACTTCTTCCTGGATGAGTTTGTCACC
TTCCTGTTCTCCAAAGAGAACAGTGTGTGGAACTCGCAGCTGGATGCAGTATGCCCGGAC
ACCATGAACAACCCTCTTTCCCACTACTGGATCTCCTCCTCGCACAACACGTACCTGACC
GGGGACCAGTTCTCCAGTGAGTCCTCCTTGGAAGCCTATGCTCGCTGCCTGCGGATGGGC
TGTCGCTGCATTGAGTTGGACTGCTGGGACGGCCCGGATGGGATGCCAGTTATTTACCAT
GGGCACACCCTTACCACCAAGATCAAGTTCTCAGATGTCCTGCACACCATCAAGGAGCAT
GCCTTTGTGGCCTCAGAGTACCCAGTCATCCTGTCCATTGAGGACCACTGCAGCATTGCC
CAGCAGAGAAACATGGCCCAATACTTCAAGAAGGTGCTGGGGGACACACTCCTCACCAAG
CCCGTGGAGATCTCTGCCGACGGGCTCCCCTCACCCAACCAGCTTAAGAGGAAGATCCTC
ATCAAGCACAAGAAGCTGGCTGAGGGCAGTGCCTACGAGGAGGTGCCTACATCCATGATG
TACTCTGAGAACGACATCAGCAACTCTATCAAGAATGGCATCCTCTACCTGGAGGACCCT
GTGAACCACGAATGGTATCCCCACTACTTTGTTCTGACCAGCAGCAAGATCTACTACTCT
GAGGAGACCAGCAGTGACCAGGGCAACGAGGATGAGGAGGAGCCCAAGGAGGTCAGCAGC
AGCACAGAGCTGCACTCCAATGAGAAGTGGTTCCATGGGAAGCTAGGGGCAGGGCGTGAC
GGGCGTCACATCGCTGAGCGCCTGCTTACTGAGTACTGCATCGAGACCGGAGCCCCTGAC
GGCTCCTTCCTCGTGCGAGAGAGTGAGACCTTCGTGGGCGACTACACGCTCTCTTTCTGG
CGGAACGGGAAAGTCCAGCACTGCCGTATCCACTCCCGGCAAGATGCTGGGACCCCCAAG
TTCTTCTTGACAGACAACCTCGTCTTTGACTCCCTCTATGACCTCATCACGCACTACCAG
CAGGTGCCCCTGCGCTGTAATGAGTTTGAGATGCGACTTTCAGAGCCTGTCCCACAGACC
AACGCCCACGAGAGCAAAGAGTGGTACCACGCGAGCCTGACCAGAGCACAGGCTGAGCAC
ATGCTAATGCGCGTCCCTCGTGATGGGGCCTTCCTGGTGCGGAAGCGGAATGAACCCAAC
TCATATGCCATCTCTTTCCGGGCTGAGGGCAAGATCAAGCATTGCCGTGTCCAGCAAGAG
GGCCAGACAGTGATGCTAGGGAACTCGGAGTTCGACAGCCTTGTTGACCTCATCAGCTAC
TATGAGAAACACCCGCTATACCGCAAGATGAAGCTGCGCTATCCCATCAACGAGGAGGCA
CTGGAGAAGATTGGCACAGCTGAGCCTGACTACGGGGCCCTGTATGAGGGACGCAACCCT
GGCTTCTATGTAGAGGCAAACCCTATGCCAACTTTCAAGTGTGCAGTCAAAGCCCTCTTT
GACTACAAGGCCCAGAGGGAGGACGAGCTGACCTTCATCAAGAGCGCCATCATCCAGAAT
GTGGAGAAGCAAGAGGGAGGCTGGTGGCGAGGGGACTACGGAGGGAAGAAGCAGCTGTGG
TTCCCATCAAACTACGTGGAAGAGATGGTCAACCCCGTGGCCCTGGAGCCGGAGAGGGAG
CACTTGGACGAGAACAGCCCCCTAGGGGACTTGCTGCGGGGGGTCTTGGATGTGCCGGCT
TGTCAGATTGCCATCCGTCCTGAGGGCAAGAACAACCGGCTCTTCGTCTTCTCCATCAGC
ATGGCGTCGGTGGCCCACTGGTCCCTGGATGTTGCTGCCGACTCACAGGAGGAGCTGCAG
GACTGGGTGAAAAAGATCCGTGAAGTGGCCCAGACAGCAGACGCCAGGCTCACTGAAGGG
AAGATAATGGAACGGAGGAAGAAGATTGCCCTGGAGCTCTCTGAACTTGTCGTCTACTGC
CGGCCTGTTCCCTTTGATGAAGAGAAGATTGGCACAGAACGTGCTTGCTACCGGGACATG
TCATCCTTCCCGGAAACCAAGGCTGAGAAATACGTGAACAAGGCCAAAGGCAAGAAGTTC
CTTCAGTACAATCGACTGCAGCTCTCCCGCATCTACCCCAAGGGCCAGCGACTGGATTCC
TCCAACTACGATCCTTTGCCCATGTGGATCTGTGGCAGTCAGCTTGTGGCCCTCAACTTC
CAGACCCCTGACAAGCCTATGCAGATGAACCAGGCCCTCTTCATGACGGGCAGGCACTGT
GGCTACGTGCTGCAGCCAAGCACCATGCGGGATGAGGCCTTCGACCCCTTTGACAAGAGC
AGCCTCCGCGGGCTGGAGCCATGTGCCATCTCTATTGAGGTGCTGGGGGCCCGACATCTG
CCAAAGAATGGCCGAGGCATTGTGTGTCCTTTTGTGGAGATTGAGGTGGCTGGAGCTGAG
TATGACAGCACCAAGCAGAAGACAGAGTTTGTGGTGGACAATGGACTCAACCCTGTATGG
CCAGCCAAGCCCTTCCACTTCCAGATCAGTAACCCTGAATTTGCCTTTCTGCGCTTCGTG
GTGTATGAGGAAGACATGTTTAGTGACCAGAATTTCCTGGCTCAGGCTACTTTCCCAGTA
AAAGGCCTGAAGACAGGATACAGAGCAGTGCCTTTGAAGAACAACTACAGTGAGGACCTG
GAGTTGGCCTCCCTGCTGATCAAGATTGACATTTTCCCTGCCAAGCAGGAGAATGGTGAC
CTCAGTCCCTTCAGTGGTACGTCCCTGCGGGAGCGGGGCTCAGATGCCTCAGGCCAGCTG
TTTCATGGCCGAGCCCGGGAAGGCTCCTTTGAATCCCGCTACCAGCAGCCGTTTGAGGAC
TTCCGCATCTCCCAGGAGCATCTCGCAGACCATTTTGACAGTCGAGAACGAAGGGCCCCA
AGAAGGACTCGGGTCAATGGAGACAACCGCCTCTAG
Enzyme 20 GenBank Gene ID AL022394 Link Image
Enzyme 20 GeneCard ID PLCG1 Link Image
Enzyme 20 GenAtlas ID PLCG1 Link Image
Enzyme 20 HGNC ID HGNC:9065 Link Image
Enzyme 20 Chromosome Location 2
Enzyme 20 Locus 20q12-q13.1
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References Not Available
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 16706
Enzyme 21 Name cDNA FLJ35540 fis, clone SPLEN2002493, highly similar to Phosphatidylinositol 4,5-bisphosphate5-phosphatase A (EC 3.1.3.56)
Enzyme 21 Synonyms
  1. SubName: Phosphatidylinositol (4,5) bisphosphate 5-phosphatase, A, isoform CRA_a
Enzyme 21 Gene Name PIB5PA
Enzyme 21 Protein Sequence >cDNA FLJ35540 fis, clone SPLEN2002493, highly similar to Phosphatidylinositol 4,5-bisphosphate5-phosphatase A (EC 3.1.3.56)
MALPRLGTQSTGPGRCLSPNLQAQEAPAPVTTSSSTSTLSSSPWSAQPTWKSDPGFRITV
VTWNVGTAMPPDDVTSLLHLGGGDDSDGADMIAIGLQEVNSMLNKRLKDALFTDQWSELF
MDALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRL
AAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFQGPGAQGILDHDLVFWFGDLNFR
IESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKY
DTSAKKRKPAWTDRILWKVKAPGGGPSPSGRKSHRLQVTQHSYRSHMEYTVSDHKPVAAQ
FLLQFAFRDDMPLVRLEVADEWVRPEQAVVRYRMETVFARSSWDWIGLYRVGFRHCKDYV
AYVWAKHEDVDGNTYQVTFSEESLPKGHGDFILGYYSHNHSILIGITEPFQISLPSSELA
SSSTDSSGTSSEGEDDSTLELLAPKSRSPSPGKSKRHRSRSPGLARFPGLALRPSSRERR
GASRSPSPQSRRLSRVAPDRSSNGSSRGSSEEGPSGLPGPWAFPPAVPRSLGLLPALRLE
TVDPGGGGSWGPDREALAPNSLSPSPQGHRGLEEGGLGP
Enzyme 21 Number of Residues 639
Enzyme 21 Molecular Weight 70465
Enzyme 21 Theoretical pI 8.24
Enzyme 21 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 21 General Function Not Available
Enzyme 21 Specific Function Not Available
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions
  • (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate [RN:R03394]
  • (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate [RN:R03430] ALL_REAC R03394 R03430
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein Not Available
Enzyme 21 UniProtKB/Swiss-Prot ID B3KS54 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name B3KS54_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence Not Available
Enzyme 21 GenBank Gene ID AK092859 Link Image
Enzyme 21 GeneCard ID B3KS54 Link Image
Enzyme 21 GenAtlas ID Not Available
Enzyme 21 HGNC ID Not Available
Enzyme 21 Chromosome Location 22
Enzyme 21 Locus 22q11.2-q13.2
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References Not Available
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 16707
Enzyme 22 Name cDNA, FLJ92960, Homo sapiens skeletal muscle and kidney enriched inositolphosphatase (SKIP), transcript variant 2, mRNA (Skeletal muscle and kidney enriched inositol phosphatase, isoform CRA_a)
Enzyme 22 Synonyms Not Available
Enzyme 22 Gene Name SKIP
Enzyme 22 Protein Sequence >cDNA, FLJ92960, Homo sapiens skeletal muscle and kidney enriched inositolphosphatase (SKIP), transcript variant 2, mRNA (Skeletal muscle and kidney enriched inositol phosphatase, isoform CRA_a)
MDVLSPLSFIKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICL
KLYGYYVSIINCHLPPHISNNYQRLEHFDRILEMQNCEGRDIPNILDHDLIIWFGDMNFR
IEDFGLHFVRESIKNRCYGGLWEKDQLSIAKKHDPLLREFQEGRLLFPPTYKFDRNSNDY
DTSEKKRKPAWTDRILWRLKRQPCAGPDTPIPPASHFSLSLRGYSSHMTYGISDHKPVSG
TFDLELKPLVSAPLIVLMPEDLWTVENDMMVSYSSTSDFPSSPWDWIGLYKVGLRDVNDY
VSYAWVGDSKVSCSDNLNQVYIDISNIPTTEDEFLLCYYSNSLRSVVGISRPFQIPPGSL
REDPLGEAQPQI
Enzyme 22 Number of Residues 372
Enzyme 22 Molecular Weight 42784
Enzyme 22 Theoretical pI 6.43
Enzyme 22 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 22 General Function Not Available
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID B2R6I2 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name B2R6I2_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence Not Available
Enzyme 22 GenBank Gene ID AK312585 Link Image
Enzyme 22 GeneCard ID B2R6I2 Link Image
Enzyme 22 GenAtlas ID Not Available
Enzyme 22 HGNC ID Not Available
Enzyme 22 Chromosome Location 17
Enzyme 22 Locus 17p13.3
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References Not Available
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 16778
Enzyme 23 Name cDNA FLJ33455 fis, clone BRAMY2000354, highly similar to 1-phosphatidylinositol-4,5-bisphosphatephosphodiesterase delta 1 (EC 3.1.4.11)
Enzyme 23 Synonyms Not Available
Enzyme 23 Gene Name Not Available
Enzyme 23 Protein Sequence >cDNA FLJ33455 fis, clone BRAMY2000354, highly similar to 1-phosphatidylinositol-4,5-bisphosphatephosphodiesterase delta 1 (EC 3.1.4.11)
MQCLGIRSRSRSRELYLQERSLKVAALNGRRLGLQDDEDLQALLKGSQLLKVKSSSWRRE
RFYKLQEDCKTIWQESRKVMRTPESQLFSIEDIQEVRMGHRTEGLEKFARDVPEDRCFSI
VFKDQRNTLDLIAPSPADAQHWVLGLHKIIHHSGSMDQRQKLQHWIHSCLRKADKNKDNK
MSFKELQNFLKELNIQVDDSYARKIFRECDHSQTDSLEDEEIEAFYKMLTQRVEIDRTFA
EAAGSGETLSVDQLVTFLQHQQREEAAGPALALSLIERYEPSETAKAQRQMTKDGFLMYL
LSADGSAFSLAHRRVYQDMGQPLSHYLVSSSHNTYLLEDQLAGPSSTEAYIRALCKGCRC
LELDCWDGPNQEPIIYHGYTFTSKILFCDVLRAIRDYAFKASPYPVILSLENHCTLEQQR
VMARHLHAILGPMLLNRPLDGVTNSLPSPEQLKGKILLKGKKLGGLLPPGGEGGPEATVV
SDEDEAAEMEDEAVRSRVQHKPKEDKLRLAQELSDMVIYCKSVHFGGFSSPGTPGQAFYE
MASFSENRALRLLQESGNGFVRHNVGHLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNF
QTPGPEMDVYQGRFQDNGACGYVLKPAFLRDPNGTFNPRALAQGPWWARKRLNIRVISGQ
QLPKVNKNKNSIVDPKVTVEIHGVSRDVASRQTAVITNNGFNPWWDTEFAFEVVVPDLAL
IRFLVEDYDASSKNDFIGQSTIPLNSLKQGYRHVHLMSKNGDQHPSATLFVKISLQD
Enzyme 23 Number of Residues 777
Enzyme 23 Molecular Weight 88134.2
Enzyme 23 Theoretical pI 7.23
Enzyme 23 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 23 General Function Involved in calcium ion binding
Enzyme 23 Specific Function Not Available
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 193786903 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID B3KR14 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name B3KR14_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >2334 bp
ATGCAGTGCCTGGGGATCCGGAGCCGGAGCCGCTCCAGGGAGCTCTACCTGCAGGAGCGG
AGCCTTAAGGTGGCGGCGCTCAATGGACGGAGGCTGGGCCTACAGGATGATGAGGATCTA
CAGGCGCTGCTGAAGGGCAGCCAGCTCCTGAAGGTGAAGTCCAGCTCATGGAGGAGAGAG
CGCTTCTACAAGTTGCAGGAGGACTGCAAGACCATCTGGCAGGAGTCCCGCAAGGTCATG
CGGACCCCGGAGTCCCAGCTGTTCTCCATCGAGGACATTCAGGAGGTGCGAATGGGGCAC
CGCACGGAGGGTCTGGAGAAGTTCGCCCGTGATGTGCCCGAGGACCGCTGCTTCTCCATT
GTCTTCAAGGACCAGCGCAATACACTAGACCTCATCGCCCCATCGCCAGCTGATGCCCAG
CACTGGGTGCTGGGGCTGCACAAGATCATCCACCACTCAGGCTCCATGGACCAGCGTCAG
AAGCTACAGCACTGGATTCACTCCTGCTTGCGAAAAGCTGACAAAAACAAGGACAACAAG
ATGAGCTTCAAGGAGCTGCAGAACTTCCTGAAGGAGCTCAACATCCAGGTGGACGACAGC
TATGCCCGGAAGATCTTCAGGGAGTGTGACCACTCCCAGACAGACTCCCTGGAGGACGAG
GAGATTGAGGCCTTCTACAAGATGCTGACCCAGCGGGTGGAGATCGACCGCACCTTCGCC
GAGGCCGCGGGCTCAGGGGAGACTCTGTCGGTGGATCAGTTAGTGACGTTCCTGCAGCAC
CAGCAGCGGGAGGAGGCGGCAGGGCCTGCGCTGGCCCTCTCCCTCATTGAGCGCTACGAG
CCCAGCGAGACTGCCAAGGCGCAGCGGCAGATGACCAAGGACGGCTTCCTCATGTACTTA
CTGTCGGCTGACGGCAGCGCCTTCAGCCTGGCACACCGCCGTGTCTACCAGGACATGGGC
CAGCCACTTAGCCACTACCTGGTGTCCTCTTCACACAACACCTACCTGCTGGAGGACCAG
CTAGCCGGGCCCAGCAGCACTGAAGCCTACATCCGGGCACTGTGCAAAGGCTGCCGATGC
CTGGAGCTTGACTGCTGGGACGGGCCCAACCAGGAACCAATCATCTACCACGGCTATACT
TTCACTTCCAAGATCCTCTTCTGCGATGTGCTCAGGGCCATCCGGGACTATGCCTTCAAG
GCGTCCCCCTACCCTGTCATCCTATCCCTGGAGAACCACTGCACACTGGAGCAGCAGCGC
GTGATGGCGCGGCACCTGCATGCCATCCTGGGCCCCATGCTGTTGAACCGACCACTGGAT
GGGGTCACCAACAGCCTGCCCTCCCCTGAGCAACTGAAGGGGAAGATCCTGCTGAAGGGG
AAGAAGCTCGGGGGGCTCCTGCCCCCTGGAGGGGAGGGTGGCCCTGAGGCCACTGTGGTG
TCAGACGAAGACGAGGCTGCTGAGATGGAGGATGAGGCAGTGAGGAGCCGTGTGCAGCAC
AAGCCCAAGGAGGACAAGCTCAGGCTAGCACAGGAGCTCTCTGACATGGTCATTTACTGC
AAGAGTGTCCACTTTGGGGGCTTCTCCAGTCCTGGCACCCCTGGACAGGCCTTCTACGAG
ATGGCGTCCTTCTCTGAGAACCGTGCCCTTCGACTGCTCCAAGAATCAGGAAACGGCTTT
GTCCGCCACAACGTGGGGCACCTGAGCAGAATCTACCCGGCTGGATGGAGAACAGACTCC
TCCAACTACAGCCCCGTGGAGATGTGGAATGGGGGCTGCCAGATCGTGGCCCTGAATTTC
CAGACACCTGGGCCAGAGATGGACGTGTACCAGGGCCGCTTCCAGGACAACGGGGCCTGT
GGGTACGTGCTGAAGCCCGCCTTCCTGCGAGACCCCAACGGCACCTTTAACCCCCGCGCC
CTGGCTCAGGGGCCCTGGTGGGCACGGAAGCGGCTCAACATCAGGGTCATTTCGGGGCAG
CAGCTGCCAAAAGTCAACAAGAATAAGAATTCAATTGTGGACCCCAAAGTGACAGTGGAG
ATCCATGGCGTGAGCCGGGACGTGGCCAGCCGCCAGACTGCTGTCATCACCAACAATGGT
TTCAACCCATGGTGGGACACGGAGTTTGCGTTTGAGGTAGTTGTGCCTGACCTTGCCCTC
ATCCGCTTCTTGGTGGAAGATTATGATGCCTCCTCCAAGAATGACTTCATTGGCCAGAGT
ACCATCCCCTTGAACAGCCTCAAGCAAGGATACCGCCATGTCCACCTCATGTCTAAGAAC
GGGGACCAGCATCCATCAGCCACCCTCTTTGTGAAGATCTCCCTCCAGGACTAG
Enzyme 23 GenBank Gene ID AK090774 Link Image
Enzyme 23 GeneCard ID Not Available
Enzyme 23 GenAtlas ID Not Available
Enzyme 23 HGNC ID Not Available
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs Not Available
Enzyme 23 General References
  1. 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]
Enzyme 23 Metabolite References Not Available