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Human Metabolome Database Version 2.5

 

Showing metabocard for Inositol 1,3,4,5,6-pentakisphosphate (HMDB03529)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-13 00:08:41
Update Date 2010-04-26 12:44:21
Accession Number HMDB03529
Secondary Accession Numbers HMDB06232
Common Name Inositol 1,3,4,5,6-pentakisphosphate
Description myo-Inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P(5)), an inositol polyphosphate of emerging significance in cellular signalling, and its C-2 epimer scyllo-inositol pentakisphosphate (scyllo-InsP(5)) were synthesised from the same myo-inositol-based precursor. (PMID: 16755629) InsP6, Ins(1,3,4,5,6)P5 and their close metabolic relatives, which are amongst the more abundant intracellular inositol polyphosphates, in chromatin organization, DNA maintenance, gene transcription, nuclear mRNA transport, membrane trafficking and control of cell proliferation. (PMID: 14992690)
Synonyms
  1. 1D-myo-Inositol 1,3,4,5,6-pentakisphosphate
  2. Inositol 1,3,4,5,6-pentaphosphate
  3. Inositol pentaphosphate
  4. myo-Inositol 1,3,4,5,6-pentakis(phosphate)
  5. myo-Inositol 1,3,4,5,6-pentaphosphate;myo-inositol pentakisphosphate
Chemical IUPAC Name [(2R,3S,5R,6S)-4-hydroxy-2,3,5,6-tetraphosphonooxy-cyclohexyl]oxyphosphonic acid
Chemical Formula C6H17O21P5
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Alcohol Phosphates
Sub Class
  • Inositol phosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • phosphoric acid ester
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 580.055
Monoisotopic Molecular Weight 579.895020
Isomeric SMILES O[C@@H]1[C@H](OP(O)(O)=O)[C@@H](OP(O)(O)=O)[C@H](OP(O)(O)=O)[C@@H](OP(O)(O)=O)[C@@H]1OP(O)(O)=O
Canonical SMILES OC1C(OP(O)(O)=O)C(OP(O)(O)=O)C(OP(O)(O)=O)C(OP(O)(O)=O)C1OP(O)(O)=O
KEGG Compound ID C01284 Link Image
BioCyc ID Not Available
BiGG ID 37275 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB03529 Link Image
Metagene Link HMDB03529 Link Image
METLIN ID Not Available
PubChem Compound 439468 Link Image
PubChem Substance 4503 Link Image
ChEBI ID 16322 Link Image
CAS Registry Number 20298-95-7
InChI Identifier InChI=1/C6H17O21P5/c7-1-2(23-28(8,9)10)4(25-30(14,15)16)6(27-32(20,21)22)5(26-31(17,18)19)3(1)24-29(11,12)13/h1-7H,(H2,8,9,10)(H2,11,12,13)(H2,14,15,16)(H2,17,18,19)(H2,20,21,22)/t1-,2+,3-,4-,5+,6+
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 13.400001 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -10
State Solid
Experimental LogP/Hydrophobicity -7.999 Source: PhysProp
Predicted LogP/Hydrophobicity -0.14 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • nucleus
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Inositol Metabolism SMP00011 Link Image map00562 Link Image
Inositol Phosphate Metabolism SMP00462 Link Image map00562 Link Image
General References Not Available
Metabolic Enzymes
  1. Inositol polyphosphate multikinase
  2. Sedoheptulokinase
  3. Inositol-tetrakisphosphate 1-kinase
  4. Inositol-pentakisphosphate 2-kinase
Enzyme 1 [top]
Enzyme 1 ID 6582
Enzyme 1 Name Inositol polyphosphate multikinase
Enzyme 1 Synonyms
  1. Inositol 1,3,4,6-tetrakisphosphate 5-kinase
Enzyme 1 Gene Name IPMK
Enzyme 1 Protein Sequence >Inositol polyphosphate multikinase 
MATEPPSPLRVEAPGPPEMRTSPAIESTPEGTPQPAGGRLRFLNGCVPLSHQVAGHMYGK
DKVGILQHPDGTVLKQLQPPPRGPRELEFYNMVYAADCFDGVLLELRKYLPKYYGIWSPP
TAPNDLYLKLEDVTHKFNKPCIMDVKIGQKSYDPFASSEKIQQQVSKYPLMEEIGFLVLG
MRVYHVHSDSYETENQHYGRSLTKETIKDGVSRFFHNGYCLRKDAVAASIQKIEKILQWF
ENQKQLNFYASSLLFVYEGSSQPTTTKLNDRTLAEKFLSKGQLSDTEVLEYNNNFHVLSS
TANGKIESSVGKSLSKMYARHRKIYTKKHHSQTSLKVENLEQDNGWKSMSQEHLNGNVLS
QLEKVFYHLPTGCQEIAEVEVRMIDFAHVFPSNTIDEGYVYGLKHLISVLRSILDN
Enzyme 1 Number of Residues 416
Enzyme 1 Molecular Weight 47221.5
Enzyme 1 Theoretical pI 7.71
Enzyme 1 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 1 General Function Involved in inositol trisphosphate 3-kinase activity
Enzyme 1 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 1 Pathways
Enzyme 1 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 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 22532105 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q8NFU5 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name IPMK_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID AF432853 Link Image
Enzyme 1 GeneCard ID IPMK Link Image
Enzyme 1 GenAtlas ID IPMK Link Image
Enzyme 1 HGNC ID HGNC:20739 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 10q21.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 12895
Enzyme 2 Name Sedoheptulokinase
Enzyme 2 Synonyms
  1. SHK
  2. Carbohydrate kinase-like protein
Enzyme 2 Gene Name SHPK
Enzyme 2 Protein Sequence >Sedoheptulokinase 
MAARPITLGIDLGTTSVKAALLRAAPDDPSGFAVLASCARAARAEAAVESAVAGPQGREQ
DVSRILQALHECLAALPRPQLRSVVGIGVSGQMHGVVFWKTGQGCEWTEGGITPVFEPRA
VSHLVTWQDGRCSSEFLASLPQPKSHLSVATGFGCATIFWLLKYRPEFLKSYDAAGTIHD
YVVAMLCGLPRPLMSDQNAASWGYFNTQSQSWNVETLRSSGFPVHLLPDIAEPGSVAGRT
SHMWFEIPKGTQVGVALGDLQASVYSCMAQRTDAVLNISTSVQLAASMPSGFQPAQTPDP
TAPVAYFPYFNRTYLGVAASLNGGNVLATFVHMLVQWMADLGLEVEESTVYSRMIQAAVQ
QRDTHLTITPTVLGERHLPDQLASVTRISSSDLSLGHVTRALCRGIVQNLHSMLPIQQLQ
DWGVERVMGSGSALSRNDVLKQEVQRAFPLPMSFGQDVDAAVGAALVMLRRHLNQKES
Enzyme 2 Number of Residues 478
Enzyme 2 Molecular Weight 51490.4
Enzyme 2 Theoretical pI 6.83
Enzyme 2 GO Classification
Function
  • catalytic activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
—
Enzyme 2 General Function Involved in phosphotransferase activity, alcohol group as acceptor
Enzyme 2 Specific Function ATP + sedoheptulose = ADP + sedoheptulose 7- phosphate
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • ATP + sedoheptulose = ADP + sedoheptulose 7-phosphate [RN:R01844]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 74315356 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9UHJ6 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name SHPK_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1437 bp 
ATGGCTGCGCGGCCGATCACCCTCGGCATTGACCTGGGCACCACATCTGTGAAGGCAGCT
CTGCTGAGGGCCGCGCCCGACGACCCATCCGGGTTCGCAGTGCTGGCGAGCTGTGCCCGT
GCTGCGCGGGCAGAGGCGGCGGTCGAGAGCGCGGTGGCCGGGCCCCAGGGGCGGGAGCAG
GATGTGAGTAGAATCCTCCAAGCCCTACACGAGTGCCTTGCTGCCCTTCCCCGACCCCAG
CTCCGGAGCGTCGTGGGCATCGGGGTGTCGGGCCAGATGCATGGAGTCGTGTTTTGGAAA
ACAGGCCAAGGCTGTGAATGGACAGAGGGAGGGATTACCCCGGTGTTCGAGCCCCGAGCT
GTTAGCCACCTGGTCACGTGGCAGGATGGCCGATGTAGCAGCGAATTCCTGGCCTCTCTG
CCCCAGCCGAAGTCTCATCTCAGTGTGGCCACGGGCTTCGGCTGTGCAACCATCTTCTGG
CTTTTGAAATATCGCCCAGAGTTCCTGAAGTCCTACGACGCAGCCGGTACCATCCACGAC
TATGTGGTTGCCATGCTGTGTGGCTTGCCAAGACCTCTGATGTCCGACCAGAATGCTGCC
AGCTGGGGCTATTTCAACACGCAGAGCCAAAGCTGGAACGTAGAGACACTGAGGAGCTCG
GGTTTTCCTGTCCACCTGCTCCCAGACATCGCCGAGCCTGGCAGTGTGGCGGGCAGAACT
TCCCACATGTGGTTTGAAATCCCAAAGGGGACGCAGGTGGGAGTGGCCTTGGGTGATTTA
CAGGCCTCTGTCTATTCCTGCATGGCCCAGAGGACAGATGCAGTTCTCAACATCAGCACC
TCGGTTCAGCTGGCAGCCTCCATGCCTTCAGGATTCCAGCCTGCACAGACTCCAGACCCT
ACGGCCCCAGTCGCCTACTTCCCATACTTCAACAGGACCTACCTGGGGGTGGCCGCGTCA
CTCAACGGGGGCAATGTGCTGGCCACGTTCGTCCACATGCTGGTTCAGTGGATGGCAGAT
CTAGGCCTGGAGGTTGAAGAATCCACTGTGTATTCACGCATGATTCAGGCAGCTGTGCAG
CAGAGAGATACCCACCTGACCATCACCCCGACAGTGCTGGGGGAGAGGCACCTGCCGGAC
CAGCTGGCCTCAGTGACCAGAATCTCCTCCTCCGACCTCTCCCTGGGGCACGTGACCCGG
GCTCTGTGCCGAGGCATTGTTCAGAACCTGCACTCCATGCTTCCGATTCAGCAGCTCCAG
GAGTGGGGCGTGGAGAGGGTGATGGGCAGTGGGAGTGCGCTGTCCAGGAATGACGTGCTG
AAGCAGGAGGTGCAGAGGGCTTTCCCTTTGCCCATGTCCTTTGGGCAGGATGTGGATGCA
GCTGTCGGGGCAGCTCTGGTCATGCTCCGGAGACACCTCAACCAGAAGGAATCTTAG
Enzyme 2 GenBank Gene ID NM_013276.2 Link Image
Enzyme 2 GeneCard ID SHPK Link Image
Enzyme 2 GenAtlas ID SHPK Link Image
Enzyme 2 HGNC ID HGNC:1492 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 17p13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Touchman JW, Anikster Y, Dietrich NL, Maduro VV, McDowell G, Shotelersuk V, Bouffard GG, Beckstrom-Sternberg SM, Gahl WA, Green ED: The genomic region encompassing the nephropathic cystinosis gene (CTNS): complete sequencing of a 200-kb segment and discovery of a novel gene within the common cystinosis-causing deletion. Genome Res. 2000 Feb;10(2):165-73. [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. 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. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Wamelink MM, Struys EA, Jansen EE, Levtchenko EN, Zijlstra FS, Engelke U, Blom HJ, Jakobs C, Wevers RA: Sedoheptulokinase deficiency due to a 57-kb deletion in cystinosis patients causes urinary accumulation of sedoheptulose: elucidation of the CARKL gene. Hum Mutat. 2008 Apr;29(4):532-6. [PubMed Link Image]
  7. 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 13063
Enzyme 3 Name Inositol-tetrakisphosphate 1-kinase
Enzyme 3 Synonyms
  1. Inositol 1,3,4-trisphosphate 5/6-kinase
  2. Inositol-triphosphate 5/6-kinase
  3. Ins(1,3,4)P(3) 5/6-kinase
Enzyme 3 Gene Name ITPK1
Enzyme 3 Protein Sequence >Inositol-tetrakisphosphate 1-kinase 
MQTFLKGKRVGYWLSEKKIKKLNFQAFAELCRKRGMEVVQLNLSRPIEEQGPLDVIIHKL
TDVILEADQNDSQSLELVHRFQEYIDAHPETIVLDPLPAIRTLLDRSKSYELIRKIEAYM
EDDRICSPPFMELTSLCGDDTMRLLEKNGLTFPFICKTRVAHGTNSHEMAIVFNQEGLNA
IQPPCVVQNFINHNAVLYKVFVVGESYTVVQRPSLKNFSAGTSDRESIFFNSHNVSKPES
SSVLTELDKIEGVFERPSDEVIRELSRALRQALGVSLFGIDIIINNQTGQHAVIDINAFP
GYEGVSEFFTDLLNHIATVLQGQSTAMAATGDVALLRHSKLLAEPAGGLVGERTCSASPG
CCGSMMGQDAPWKAEADAGGTAKLPHQRLGCNAGVSPSFQQHCVASLATKASSQ
Enzyme 3 Number of Residues 414
Enzyme 3 Molecular Weight 45620.6
Enzyme 3 Theoretical pI 6.09
Enzyme 3 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • inositol or phosphatidylinositol kinase activity
  • inositol tetrakisphosphate 1-kinase activity
  • inositol tetrakisphosphate kinase activity
  • inositol trisphosphate kinase activity
  • inositol-1,3,4-trisphosphate 5/6-kinase activity
  • ion binding
  • kinase activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolic process
  • inositol metabolic process
  • inositol phosphate metabolic process
  • inositol trisphosphate metabolic process
  • metabolic process
  • polyol metabolic process
  • small molecule metabolic process
Component
  • cell part
  • intracellular
Enzyme 3 General Function Involved in catalytic activity
Enzyme 3 Specific Function Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. Phosphorylates Ins(3,4,5,6)P4 at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5 is not. Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate (InsP6) pathway. Also acts as an inositol polyphosphate phosphatase that dephosphorylate Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 to Ins(1,3,4)P3, and Ins(1,3,4,5,6)P5 to Ins(3,4,5,6)P4. May also act as an isomerase that interconverts the inositol tetraphosphate isomers Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the presence of ADP and magnesium. Probably acts as the rate-limiting enzyme of the InsP6 pathway. Modifies TNF-alpha-induced apoptosis by interfering with the activation of TNFRSF1A-associated death domain
Enzyme 3 Pathways
Enzyme 3 Reactions
  • (1) ATP + 1D-myo-inositol 1,3,4-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate [RN:R03428]
  • (2) ATP + 1D-myo-inositol 1,3,4-trisphosphate = ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate [RN:R03429]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 12006346 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q13572 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ITPK1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1245 bp 
ATGCAGACCTTTCTGAAAGGGAAGAGAGTTGGCTACTGGCTGAGCGAGAAGAAAATCAAG
AAGCTGAATTTCCAGGCCTTCGCCGAGCTGTGCAGGAAGCGAGGGATGGAGGTTGTGCAG
CTGAACCTTAGCCGGCCGATCGAGGAGCAGGGCCCCCTGGACGTCATCATCCACAAGCTG
ACTGACGTCATCCTTGAAGCCGACCAGAATGATAGCCAGTCCCTGGAGCTGGTGCACAGG
TTCCAGGAGTACATCGATGCCCACCCTGAGACCATCGTCCTGGACCCGCTCCCTGCCATC
AGAACCCTGCTTGACCGCTCCAAGTCCTATGAGCTCATCCGGAAGATTGAGGCCTACATG
GAAGACGACAGGATCTGCTCGCCACCCTTCATGGAGCTCACGAGCCTGTGCGGGGATGAC
ACCATGCGGCTGCTGGAGAAGAACGGCTTGACTTTCCCATTCATTTGCAAAACCAGAGTG
GCTCATGGCACCAACTCTCACGAGATGGCTATCGTGTTCAACCAGGAGGGCCTGAACGCC
ATCCAGCCACCCTGCGTGGTCCAGAATTTCATCAACCACAACGCCGTCCTGTACAAGGTG
TTCGTGGTTGGCGAGTCCTACACCGTGGTCCAGAGGCCCTCACTCAAGAACTTCTCCGCA
GGCACATCAGACCGTGAGTCCATCTTCTTCAACAGCCACAACGTGTCAAAGCCGGAGTCG
TCATCGGTCCTGACGGAGCTGGACAAGATCGAGGGCGTGTTCGAGCGGCCGAGCGACGAG
GTCATCCGGGAGCTCTCCCGGGCCCTGCGGCAGGCACTGGGCGTGTCACTCTTTGGCATC
GACATCATCATCAACAACCAGACAGGGCAGCACGCCGTCATTGACATCAATGCCTTCCCA
GGCTACGAGGGCGTGAGCGAGTTCTTCACAGACCTCCTGAACCACATCGCCACTGTCCTG
CAGGGCCAGAGCACAGCCATGGCAGCCACAGGGGACGTGGCCCTGCTGAGGCACAGCAAG
CTTCTGGCCGAGCCGGCGGGCGGCCTGGTGGGCGAGCGGACATGCAGCGCCAGCCCCGGC
TGCTGCGGCAGCATGATGGGCCAGGACGCGCCCTGGAAGGCTGAGGCCGACGCGGGCGGC
ACCGCCAAGCTGCCGCACCAGAGACTCGGCTGCAACGCCGGCGTGTCGCCCAGCTTCCAG
CAGCATTGTGTGGCCTCCCTGGCCACCAAGGCCTCCTCCCAGTAG
Enzyme 3 GenBank Gene ID AF279372 Link Image
Enzyme 3 GeneCard ID ITPK1 Link Image
Enzyme 3 GenAtlas ID ITPK1 Link Image
Enzyme 3 HGNC ID HGNC:6177 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 14q31
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Wilson MP, Majerus PW: Isolation of inositol 1,3,4-trisphosphate 5/6-kinase, cDNA cloning and expression of the recombinant enzyme. J Biol Chem. 1996 May 17;271(20):11904-10. [PubMed Link Image]
  2. Yang X, Shears SB: Multitasking in signal transduction by a promiscuous human Ins(3,4,5,6)P(4) 1-kinase/Ins(1,3,4)P(3) 5/6-kinase. Biochem J. 2000 Nov 1;351 Pt 3:551-5. [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. Wilson MP, Sun Y, Cao L, Majerus PW: Inositol 1,3,4-trisphosphate 5/6-kinase is a protein kinase that phosphorylates the transcription factors c-Jun and ATF-2. J Biol Chem. 2001 Nov 2;276(44):40998-1004. Epub 2001 Aug 31. [PubMed Link Image]
  5. Ho MW, Yang X, Carew MA, Zhang T, Hua L, Kwon YU, Chung SK, Adelt S, Vogel G, Riley AM, Potter BV, Shears SB: Regulation of Ins(3,4,5,6)P(4) signaling by a reversible kinase/phosphatase. Curr Biol. 2002 Mar 19;12(6):477-82. [PubMed Link Image]
  6. Sun Y, Wilson MP, Majerus PW: Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1. J Biol Chem. 2002 Nov 29;277(48):45759-64. Epub 2002 Sep 24. [PubMed Link Image]
  7. Sun Y, Mochizuki Y, Majerus PW: Inositol 1,3,4-trisphosphate 5/6-kinase inhibits tumor necrosis factor-induced apoptosis. J Biol Chem. 2003 Oct 31;278(44):43645-53. Epub 2003 Aug 18. [PubMed Link Image]
  8. Qian X, Mitchell J, Wei SJ, Williams J, Petrovich RM, Shears SB: The Ins(1,3,4)P3 5/6-kinase/Ins(3,4,5,6)P4 1-kinase is not a protein kinase. Biochem J. 2005 Jul 15;389(Pt 2):389-95. [PubMed Link Image]
  9. Miller GJ, Wilson MP, Majerus PW, Hurley JH: Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase. Mol Cell. 2005 Apr 15;18(2):201-12. [PubMed Link Image]
  10. Chamberlain PP, Qian X, Stiles AR, Cho J, Jones DH, Lesley SA, Grabau EA, Shears SB, Spraggon G: Integration of inositol phosphate signaling pathways via human ITPK1. J Biol Chem. 2007 Sep 21;282(38):28117-25. Epub 2007 Jul 6. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 15322
Enzyme 4 Name Inositol-pentakisphosphate 2-kinase
Enzyme 4 Synonyms
  1. IPK1 homolog
  2. Inositol-1,3,4,5,6-pentakisphosphate 2-kinase
  3. Ins(1,3,4,5,6)P5 2-kinase
  4. InsP5 2-kinase
Enzyme 4 Gene Name IPPK
Enzyme 4 Protein Sequence >Inositol-pentakisphosphate 2-kinase 
MEEGKMDENEWGYHGEGNKSLVVAHAQRCVVLRFLKFPPNRKKTSEEIFQHLQNIVDFGK
NVMKEFLGENYVHYGEVVQLPLEFVKQLCLKIQSERPESRCDKDLDTLSGYAMCLPNLTR
LQTYRFAEHRPILCVEIKPKCGFIPFSSDVTHEMKHKVCRYCMHQHLKVATGKWKQISKY
CPLDLYSGNKQRMHFALKSLLQEAQNNLKIFKNGELIYGCKDARSPVADWSELAHHLKPF
FFPSNGLASGPHCTRAVIRELVHVITRVLLSGSDKGRAGTLSPGLGPQGPRVCEASPFSR
SLRCQGKNTPERSGLPKGCLLYKTLQVQMLDLLDIEGLYPLYNRVERYLEEFPEERKTLQ
IDGPYDEAFYQKLLDLSTEDDGTVAFALTKVQQYRVAMTAKDCSIMIALSPCLQDASSDQ
RPVVPSSRSRFAFSVSVLDLDLKPYESIPHQYKLDGKIVNYYSKTVRAKDNAVMSTRFKE
SEDCTLVLHKV
Enzyme 4 Number of Residues 491
Enzyme 4 Molecular Weight 56016.1
Enzyme 4 Theoretical pI 8.46
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • inositol pentakisphosphate 2-kinase activity
  • kinase activity
  • nucleoside binding
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
—
Enzyme 4 General Function Involved in ATP binding
Enzyme 4 Specific Function Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). InsP6 is involved in many processes such as mRNA export, non-homologous end-joining, endocytosis, ion channel regulation. It also protects cells from TNF-alpha-induced apoptosis
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol hexakisphosphate [RN:R05202]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 14582858 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9H8X2 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name IPPK_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1476 bp 
ATGGAAGAGGGGAAGATGGACGAGAATGAATGGGGGTACCACGGAGAGGGCAATAAGAGC
CTGGTGGTGGCCCACGCGCAGCGCTGCGTCGTGCTGCGGTTTCTGAAGTTTCCTCCAAAT
AGGAAGAAGACCTCGGAAGAGATATTTCAACACCTGCAGAACATAGTGGACTTTGGGAAA
AATGTCATGAAGGAGTTTTTGGGGGAGAACTATGTTCATTATGGGGAGGTCGTTCAGCTA
CCTTTAGAGTTTGTGAAACAGCTTTGTTTAAAGATACAATCTGAAAGACCAGAGTCTCGC
TGTGACAAGGACCTGGATACTCTCAGTGGTTACGCTATGTGCCTTCCTAATTTAACCAGA
CTCCAAACCTACCGCTTTGCAGAGCACCGGCCGATTCTGTGTGTAGAGATTAAGCCAAAA
TGTGGGTTTATTCCTTTCTCGAGTGATGTCACGCATGAGATGAAGCATAAGGTCTGTCGA
TACTGCATGCACCAGCACCTCAAGGTAGCAACTGGGAAGTGGAAGCAGATCAGCAAATAC
TGTCCCCTTGATCTCTACTCAGGAAACAAACAGAGAATGCACTTTGCCTTGAAGAGTTTG
CTGCAGGAGGCACAGAACAACTTGAAGATATTTAAGAATGGTGAGCTGATTTACGGCTGC
AAAGATGCCCGGAGCCCCGTGGCTGACTGGAGCGAGCTTGCACACCACCTGAAGCCGTTC
TTCTTCCCTTCCAACGGCCTGGCCAGTGGGCCCCACTGCACAAGGGCTGTGATCAGGGAG
CTGGTGCACGTGATCACACGGGTGCTGCTGAGTGGCTCGGACAAGGGCCGGGCAGGCACC
CTGAGTCCGGGGCTCGGGCCTCAGGGCCCGCGAGTCTGCGAAGCCAGCCCTTTCAGTAGG
AGCCTTCGCTGCCAAGGAAAAAACACCCCAGAGCGCTCGGGGTTACCGAAGGGCTGTCTT
CTGTACAAAACCCTCCAGGTGCAGATGTTGGACCTGCTGGACATCGAAGGCCTCTACCCT
CTGTACAACCGGGTTGAGCGATACCTGGAAGAGTTTCCCGAGGAGAGAAAAACCTTACAA
ATAGATGGGCCTTATGATGAAGCATTTTACCAGAAGCTGCTTGACCTTTCCACTGAGGAT
GACGGGACAGTGGCCTTCGCGCTAACGAAGGTGCAGCAGTACCGCGTCGCCATGACTGCC
AAGGACTGCTCCATCATGATTGCACTGTCTCCCTGTCTGCAGGATGCCAGCTCTGATCAA
AGGCCTGTCGTCCCTTCATCGAGGTCCAGGTTTGCCTTTTCCGTGTCTGTGCTGGACCTT
GACCTCAAGCCCTACGAGAGCATTCCCCATCAGTATAAACTGGACGGCAAGATCGTCAAC
TATTATTCAAAGACTGTACGTGCCAAAGACAACGCCGTGATGTCGACTCGGTTCAAGGAA
AGCGAAGATTGCACATTAGTTCTCCACAAGGTCTAA
Enzyme 4 GenBank Gene ID AF351202 Link Image
Enzyme 4 GeneCard ID IPPK Link Image
Enzyme 4 GenAtlas ID IPPK Link Image
Enzyme 4 HGNC ID HGNC:14645 Link Image
Enzyme 4 Chromosome Location 9
Enzyme 4 Locus 9q22.31
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Verbsky JW, Wilson MP, Kisseleva MV, Majerus PW, Wente SR: The synthesis of inositol hexakisphosphate. Characterization of human inositol 1,3,4,5,6-pentakisphosphate 2-kinase. J Biol Chem. 2002 Aug 30;277(35):31857-62. Epub 2002 Jun 25. [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. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [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. Verbsky J, Majerus PW: Increased levels of inositol hexakisphosphate (InsP6) protect HEK293 cells from tumor necrosis factor (alpha)- and Fas-induced apoptosis. J Biol Chem. 2005 Aug 12;280(32):29263-8. Epub 2005 Jun 20. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available