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Human Metabolome Database Version 2.5

 

Showing metabocard for Ethanolamine (HMDB00149)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-29 16:20:31
Accession Number HMDB00149
Secondary Accession Numbers Not Available
Common Name Ethanolamine
Description A viscous, hygroscopic amino alcohol with an ammoniacal odor. It is widely distributed in biological tissue and is a component of lecithin. It is used as a surfactant, fluorometric reagent, and to remove CO2 and H2S from natural gas and other gases.
Synonyms
  1. 1-Amino-2-hydroxyethane
  2. 2-Amino-1-ethanol
  3. 2-Aminoethanol
  4. 2-Aminoethyl alcohol
  5. 2-Ethanolamine
  6. 2-Hydroxyethanamine
  7. 2-Hydroxyethylamine
  8. Aethanolamin
  9. Aminoethanol
  10. Colamine
  11. ETA
  12. Envision Conditioner PDD 9020
  13. Ethanolamine
  14. Ethylolamine
  15. Glycinol
  16. H-Glycinol
  17. MEA
  18. Monoaethanolamin
  19. Monoethanolamine
  20. Olamine
  21. b-Aminoethanol
  22. b-Aminoethyl alcohol
  23. b-Ethanolamine
  24. b-Hydroxyethylamine
  25. beta-Aminoethanol
  26. beta-Aminoethyl alcohol
  27. beta-Hydroxyethylamine
  28. beta-ethanolamine
Chemical IUPAC Name 2-aminoethanol
Chemical Formula C2H7NO
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Amino Alcohols
Sub Class
  • Primary amino alcohols
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • 1,2-aminoalcohol
  • primary amine
  • primary aliphatic amine (alkylamine)
Biofunction
  • Component of Glycerophospholipid metabolism
Application
Source
  • Endogenous
Average Molecular Weight 61.083
Monoisotopic Molecular Weight 61.052765
Isomeric SMILES NCCO
Canonical SMILES NCCO
KEGG Compound ID C00189 Link Image
BioCyc ID ETHANOL-AMINE Link Image
BiGG ID 34189 Link Image
Wikipedia Link Ethanolamine Link Image
NuGOwiki Link HMDB00149 Link Image
Metagene Link HMDB00149 Link Image
METLIN ID 3207 Link Image
PubChem Compound 700 Link Image
PubChem Substance 583749 Link Image
ChEBI ID 16000 Link Image
CAS Registry Number 141-43-5
InChI Identifier InChI=1/C2H7NO/c3-1-2-4/h4H,1-3H2
Synthesis Reference Soucaille, Philippe. Ethanolamine production by fermentation of genetically modified Escherichia coli. PCT Int. Appl. (2007), 23pp.
Melting Point (Experimental) 10.5 oC
Experimental Water Solubility 1000.0 mg/mL [RIDDICK,JA et al. (1986)] Source: PhysProp
Predicted Water Solubility 849.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 1
State Liquid
Experimental LogP/Hydrophobicity -1.31 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -1.53 [Predicted by ALOGPS]; -1.3 [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 1AII Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Brain
Epidermis
Most Tissues
Myelin
Nerve Cells
Pancreas
Stratum Corneum
Concentrations (Normal)
Biofluid Blood
Value 52.3 (26.2-91.7) uM
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 1.6 (0.0-11.5) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 14.1 +/- 3.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 8.43 (2.62-14.24) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. [PubMed Link Image]
Biofluid Urine
Value 21.4 (6.579-36.2) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value 29.5 +/- 7.8 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 30.9 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed Link Image]
Biofluid Urine
Value 42.75 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Shaykhutdinov RA, MacInnis GD, Dowlatabadi R, Weljie AM, Vogel HJ. Quantitative analysis of metabolite concentrations in human urine samples using 13C{1H} NMR spectroscopy. Metabolomics. 2009
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Phospholipid Biosynthesis SMP00025 Link Image map00564 Link Image
General References
  1. Denissen JF, Grabowski BA, Johnson MK, Boyd SA, Uchic JT, Stein H, Cepa S, Hill P: The orally active renin inhibitor A-74273. In vivo and in vitro morpholine ring metabolism in rats, dogs, and humans. Drug Metab Dispos. 1994 Nov-Dec;22(6):880-8. [PubMed Link Image]
  2. Vance JE: Lipoproteins secreted by cultured rat hepatocytes contain the antioxidant 1-alk-1-enyl-2-acylglycerophosphoethanolamine. Biochim Biophys Acta. 1990 Jul 16;1045(2):128-34. [PubMed Link Image]
  3. Alberghina M, Giacchetto A, Cavallaro N: Levels of ethanolamine intermediates in the human and rat visual system structures: comparison with neural tissues of a lower vertebrate (Mustelus canis) and an invertebrate (Loligo pealei). Neurochem Int. 1993 Jan;22(1):45-51. [PubMed Link Image]
  4. Hammond EJ, Uthman BM, Wilder BJ, Ben-Menachem E, Hamberger A, Hedner T, Ekman R: Neurochemical effects of vagus nerve stimulation in humans. Brain Res. 1992 Jun 26;583(1-2):300-3. [PubMed Link Image]
  5. Perschak H, Amsler U, Vischer A, Siegfried J, Cuenod M: Ventricular cerebrospinal fluid concentrations of putative amino acid transmitters in Parkinson's disease and other disorders. Hum Neurobiol. 1987;6(3):191-4. [PubMed Link Image]
  6. Renkonen O: Chromatographic separation of plasmalogenic, alkyl-acyl, and diacyl forms of ethanolamine glycerophosphatides. J Lipid Res. 1968 Jan;9(1):34-9. [PubMed Link Image]
  7. Ginsberg L, Rafique S, Xuereb JH, Rapoport SI, Gershfeld NL: Disease and anatomic specificity of ethanolamine plasmalogen deficiency in Alzheimer's disease brain. Brain Res. 1995 Nov 6;698(1-2):223-6. [PubMed Link Image]
  8. Bluml S, Seymour KJ, Ross BD: Developmental changes in choline- and ethanolamine-containing compounds measured with proton-decoupled (31)P MRS in in vivo human brain. Magn Reson Med. 1999 Oct;42(4):643-54. [PubMed Link Image]
  9. Farooqui AA, Rapoport SI, Horrocks LA: Membrane phospholipid alterations in Alzheimer's disease: deficiency of ethanolamine plasmalogens. Neurochem Res. 1997 Apr;22(4):523-7. [PubMed Link Image]
  10. Mikhaevich IS, Vlasenkova NK, Gerasimova GK: Synergistic antiproliferative effect of cis-diammine-dichloroplatinum (II) and a new anticancer agent, plasmanyl-(N-acyl)-ethanolamine, an inhibitor of protein kinase C. Biomed Sci. 1991;2(6):659-64. [PubMed Link Image]
  11. Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. [PubMed Link Image]
  12. Wikipedia Link Image
Metabolic Enzymes
  1. Phospholipase D2
  2. Ectonucleotide pyrophosphatase/phosphodiesterase family member 2
  3. Choline/ethanolamine kinase
  4. Ethanolamine kinase 1
  5. Phosphoethanolamine/phosphocholine phosphatase
  6. Ethanolamine kinase 2
  7. Choline kinase beta
  8. Glycerophosphodiester phosphodiesterase 1
  9. Phospholipase D1 variant
  10. ETNK2 protein (Ethanolamine kinase 2, isoform CRA_b) (Ethanolamine kinase 2)
Enzyme 1 [top]
Enzyme 1 ID 5309
Enzyme 1 Name Phospholipase D2
Enzyme 1 Synonyms
  1. PLD 2
  2. hPLD2
  3. Choline phosphatase 2
  4. PLD1C
  5. Phosphatidylcholine-hydrolyzing phospholipase D2
Enzyme 1 Gene Name PLD2
Enzyme 1 Protein Sequence >Phospholipase D2
MTATPESLFPTGDELDSSQLQMESDEVDTLKEGEDPADRMHPFLAIYELQSLKVHPLVFA
PGVPVTAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVL
MSLLPLARFAVAYSPARDAGNREMPSLPRAGPEGSTRHAASKQKYLENYLNRLLTMSFYR
NYHAMTEFLEVSQLSFIPDLGRKGLEGMIRKRSGGHRVPGLTCCGRDQVCYRWSKRWLVV
KDSFLLYMCLETGAISFVQLFDPGFEVQVGKRSTEARHGVRIDTSHRSLILKCSSYRQAR
WWAQEITELAQGPGRDFLQLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIF
ITDWWLSPEVYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRAL
MLLHPNIKVMRHPDQVTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDLGDSSE
SAASQPPTPRPDSPATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPW
RDVGVVVHGLPARDLARHFIQRWNFTKTTKAKYKTPTYPYLLPKSTSTANQLPFTLPGGQ
CTTVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDE
IVDRILKAHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHR
LKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSANINDRSLL
GKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILGANTRPDLDLRDPICD
DFFQLWQDMAESNANIYEQIFRCLPSNATRSLRTLREYVAVEPLATVSPPLARSELTQVQ
GHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT
Enzyme 1 Number of Residues 933
Enzyme 1 Molecular Weight 105986.1
Enzyme 1 Theoretical pI 7.68
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • lipid binding
  • phosphoinositide binding
  • phospholipid binding
  • protein binding
Process
  • cell communication
  • cellular process
  • metabolic process
Component
Enzyme 1 General Function Involved in protein binding
Enzyme 1 Specific Function May have a role in signal-induced cytoskeletal regulation and/or endocytosis
Enzyme 1 Pathways
Enzyme 1 Reactions
  • a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2645858 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O14939 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PLD2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2802 bp
ATGACGGCGACCCCTGAGAGCCTCTTCCCCACTGGGGACGAACTGGACTCCAGCCAGCTC
CAGATGGAGTCCGATGAGGTGGACACCCTGAAGGAGGGAGAGGACCCAGCCGACCGGATG
CACCCGTTTCTGGCCATCTATGAGCTTCAGTCTCTGAAAGTGCACCCCTTGGTGTTCGCA
CCTGGGGTCCCTGTCACAGCCCAGGTGGTGGGCACCGAAAGATATACCAGCGGATCCAAG
GTGGGAACCTGCACTCTGTATTCTGTCCGCTTGACTCACGGCGACTTTTCCTGGACAACC
AAGAAGAAATACCGTCATTTTCAGGAGCTGCATCGGGACCTCCTGAGACACAAAGTCTTG
ATGAGTCTGCTCCCTCTGGCTCGATTTGCCGTTGCCTATTCTCCAGCCCGAGATGCAGGC
AACAGAGAGATGCCCTCTCTACCCCGGGCAGGTCCTGAGGGCTCCACCAGACATGCAGCC
AGCAAACAGAAATACCTGGAGAATTACCTCAACTGTCTCTTGACCATGTCTTTCTATCGC
AACTACCATGCCATGACAGAGTTCCTGGAAGTCAGTCAGCTGTCCTTTATCCCGGACTTG
GGCCGCAAAGGACTGGAGGGGATGATCCGGAAGCGCTCAGGTGGCCACCGTGTTCCTGGC
CTCACCTGCTGTGGCCGAGACCAAGTTTGTTATCGCTGGTCCAAGAGGTGGCTGGTGGTG
AAGGACTCCTTCCTGCTGTACATGTGCCTCGAGACAGGTGCCATCTCATTTGTTCAGCTC
TTTGACCCTGGCTTTGAGGTGCAAGTGGGGAAAAGGAGCACGGAGGCACGGCACGGCGTG
CGGATCGATACCTCCCACAGGTCCTTGATTCTCAAGTGCAGCAGCTACCGGCAGGCACGG
TGGTGGGCCCAAGAGATCACTGAGCTGGCACAGGGCCCAGGCAGAGACTTCCTACAGCTG
CACCGGCATGACAGCTACGCCCCACCCCGGCCTGGGACCTTGGCCCGGTGGTTTGTGAAT
GGGGCAGGTTACTTTGCTGCTGTGGCAGATGCCATCCTTCGAGCTCAAGAGGAGATTTTC
ATCACAGACTGGTGGTTGAGTCCTGAGGTTTACCTGAAGCGTCCGGCCCATTCAGATGAC
TGGAGACTGGACATTATGCTCAAGAGGAAGGCGGAGGAAGGTGTCCGTGTGTCTATTCTG
CTGTTTAAAGAAGTGGAATTGGCCTTGGGCATCAACAGTGGCTATAGCAAGAGGGCGCTG
ATGCTGCTGCACCCCAACATAAAGGTGATGCGTCACCCAGACCAAGTGACGTTGTGGGCC
CATCATGAGAAGCTCCTGGTGGTGGACCAAGTGGTAGCATTCCTGGGGGGACTGGACCTT
GCCTATGGCCGCTGGGATGACCTGCACTACCGACTGACTGACCTTGGAGACTCCTCTGAA
TCAGCTGCCTCCCAGCCTCCCACCCCGCGCCCAGACTCACCAGCCACCCCAGACCTCTCT
CACAACCAATTCTTCTGGCTGGGCAAGGACTACAGCAATCTTATCACCAAGGACTGGGTG
CAGCTGGACCGGCCTTTCGAAGATTTCATTGACAGGGAGACGACCCCTCGGATGCCATGG
CGGGACGTTGGGGTGGTCGTCCATGGCCTACCGGCCCGGGACCTTGCCCGGCACTTCATC
CAGCGCTGGAACTTCACCAAGACCACCAAGGCCAAGTACAAGACTCCCACATACCCCTAC
CTGCTTCCCAAGTCTACCAGCACGGCCAATCAGCTCCCCTTCACACTTCCAGGAGGGCAG
TGCACCACCGTACAGGTCTTGCGATCAGTGGACCGCTGGTCAGCAGGGACTCTGGAGAAC
TCCATCCTCAATGCCTACCTGCACACCATCAGGGAGAGCCAGCACTTCCTCTACATTGAG
AATCAGTTCTTCATTAGCTGCTCAGATGGGCGGACGGTTCTGAACAAGGTGGGCGATGAG
ATTGTGGACAGAATCCTGAAGGCCCACAAACAGGGGTGGTGTTACCGAGTCTACGTGCTT
TTGCCCTTACTCCCTGGCTTCGAGGGTGACATCTCCACGGGCGGTGGCAACTCCATCCAG
GCCATTCTGCACTTTACTTACAGGACCCTGTGTCGTGGGGAGTATTCAATCCTGCATCGC
CTTAAAGCAGCCATGGGGACAGCATGGCGGGACTATATTTCCATCTGCGGGCTTCGTACA
CACGGAGAGCTGGGCGGGCACCCCGTCTCGGAGCTCATCTACATCCACAGCAAGGTGCTC
ATCGCAGATGACCGGACAGTCATCATTGGTTCTGCAAACATCAATGACCGGAGCTTGCTG
GGGAAGCGGGACAGTGAGCTGGCCGTGCTGATCGAGGACACAGAGACGGAACCATCCCTC
ATGAATGGGGCAGAGTATCAGGCGGGCAGGTTTGCCTTGAGTCTGCGGAAGCACTGCTTC
GGTGTGATTCTTGGAGCAAATACCCGGCCAGACTTGGATCTCCGAGACCCCATCTGTGAT
GACTTCTTCCAGTTGTGGCAAGACATGGCTGAGAGCAACGCCAATATCTATGAGCAGATC
TTCCGCTGCCTGCCATCCAATGCCACGCGTTCCCTGCGGACTCTCCGGGAGTACGTGGCC
GTGGAGCCCTTGGCCACGGTCAGTCCCCCCTTGGCTCGGTCTGAGCTCACCCAGGTCCAG
GGCCACCTGGTCCACTTCCCCCTCAAGTTCCTAGAGGATGAGTCTTTGCTGCCCCCGCTG
GGTAGCAAGGAGGGCATGATCCCCCTAGAAGTGTGGACATAG
Enzyme 1 GenBank Gene ID AF033850 Link Image
Enzyme 1 GeneCard ID PLD2 Link Image
Enzyme 1 GenAtlas ID PLD2 Link Image
Enzyme 1 HGNC ID HGNC:9068 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 17p13.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Steed PM, Clark KL, Boyar WC, Lasala DJ: Characterization of human PLD2 and the analysis of PLD isoform splice variants. FASEB J. 1998 Oct;12(13):1309-17. [PubMed Link Image]
  2. Lopez I, Arnold RS, Lambeth JD: Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2. J Biol Chem. 1998 May 22;273(21):12846-52. [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. Divecha N, Roefs M, Halstead JR, D'Andrea S, Fernandez-Borga M, Oomen L, Saqib KM, Wakelam MJ, D'Santos C: Interaction of the type Ialpha PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4, 5-bisphosphate in the regulation of PLD2 activity. EMBO J. 2000 Oct 16;19(20):5440-9. [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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5399
Enzyme 2 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 2
Enzyme 2 Synonyms
  1. E-NPP 2
  2. Autotaxin
  3. Extracellular lysophospholipase D
  4. LysoPLD
Enzyme 2 Gene Name ENPP2
Enzyme 2 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 2
MARRSSFQSCQIISLFTFAVGVNICLGFTAHRIKRAEGWEEGPPTVLSDSPWTNISGSCK
GRCFELQEAGPPDCRCDNLCKSYTSCCHDFDELCLKTARGWECTKDRCGEVRNEENACHC
SEDCLARGDCCTNYQVVCKGESHWVDDDCEEIKAAECPAGFVRPPLIIFSVDGFRASYMK
KGSKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDA
TFHLRGREKFNHRWWGGQPLWITATKQGVKAGTFFWSVVIPHERRILTILQWLTLPDHER
PSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDH
GMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRSKFSNNAKYDPKAIIANLTCKKPDQH
FKPYLKQHLPKRLHYANNRRIEDIHLLVERRWHVARKPLDVYKKPSGKCFFQGDHGFDNK
VNSMQTVFVGYGSTFKYKTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTF
RPTMPEEVTRPNYPGIMYLQSDFDLGCTCDDKVEPKNKLDELNKRLHTKGSTEERHLLYG
RPAVLYRTRYDILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDHLTSCVRPDVRVS
PSFSQNCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWNYFQRVL
VKKYASERNGVNVISGPIFDYDYDGLHDTEDKIKQYVEGSSIPVPTHYYSIITSCLDFTQ
PADKCDGPLSVSSFILPHRPDNEESCNSSEDESKWVEELMKMHTARVRDIEHLTSLDFFR
KTSRSYPEILTLKTYLHTYESEI
Enzyme 2 Number of Residues 863
Enzyme 2 Molecular Weight 98992.8
Enzyme 2 Theoretical pI 7.39
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • ion binding
  • metal ion binding
  • molecular transducer activity
  • nucleic acid binding
  • pattern binding
  • polysaccharide binding
  • receptor activity
  • scavenger receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • immune response
  • immune system process
  • metabolic process
Component
Enzyme 2 General Function Involved in catalytic activity
Enzyme 2 Specific Function Hydrolyzes lysophospholipids to produce lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine. Also can act on sphingosylphosphphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility- related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development. Tumor cell motility-stimulating factor
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • 1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine [RN:R04362]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-27
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 91823602 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q13822 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ENPP2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2592 bp
ATGGCAAGGAGGAGCTCGTTCCAGTCGTGTCAGATAATATCCCTGTTCACTTTTGCCGTT
GGAGTCAATATCTGCTTAGGATTCACTGCACATCGAATTAAGAGAGCAGAAGGATGGGAG
GAAGGTCCTCCTACAGTGCTATCAGACTCCCCCTGGACCAACATCTCCGGATCTTGCAAG
GGCAGGTGCTTTGAACTTCAAGAGGCTGGACCTCCTGATTGTCGCTGTGACAACTTGTGT
AAGAGCTATACCAGTTGCTGCCATGACTTTGATGAGCTGTGTTTGAAGACAGCCCGTGGC
TGGGAGTGTACTAAGGACAGATGTGGAGAAGTCAGAAATGAAGAAAATGCCTGTCACTGC
TCAGAGGACTGCTTGGCCAGGGGAGACTGCTGTACCAATTACCAAGTGGTTTGCAAAGGA
GAGTCGCATTGGGTTGATGATGACTGTGAGGAAATAAAGGCCGCAGAATGCCCTGCAGGG
TTTGTTCGCCCTCCATTAATCATCTTCTCCGTGGATGGCTTCCGTGCATCATACATGAAG
AAAGGCAGCAAAGTCATGCCTAATATTGAAAAACTAAGGTCTTGTGGCACACACTCTCCC
TACATGAGGCCGGTGTACCCAACTAAAACCTTTCCTAACTTATACACTTTGGCCACTGGG
CTATATCCAGAATCACATGGAATTGTTGGCAATTCAATGTATGATCCTGTATTTGATGCC
ACTTTTCATCTGCGAGGGCGAGAGAAATTTAATCATAGATGGTGGGGAGGTCAACCGCTA
TGGATTACAGCCACCAAGCAAGGGGTGAAAGCTGGAACATTCTTTTGGTCTGTTGTCATC
CCTCACGAGCGGAGAATATTAACCATATTGCAGTGGCTCACCCTGCCAGATCATGAGAGG
CCTTCGGTCTATGCCTTCTATTCTGAGCAACCTGATTTCTCTGGACACAAATATGGCCCT
TTCGGCCCTGAGATGACAAATCCTCTGAGGGAAATCGACAAAATTGTGGGGCAATTAATG
GATGGACTGAAACAACTAAAACTGCATCGGTGTGTCAACGTCATCTTTGTCGGAGACCAT
GGAATGGAAGATGTCACATGTGATAGAACTGAGTTCTTGAGTAATTACCTAACTAATGTG
GATGATATTACTTTAGTGCCTGGAACTCTAGGAAGAATTCGATCCAAATTTAGCAACAAT
GCTAAATATGACCCCAAAGCCATTATTGCCAATCTCACGTGTAAAAAACCAGATCAGCAC
TTTAAGCCTTACTTGAAACAGCACCTTCCCAAACGTTTGCACTATGCCAACAACAGAAGA
ATTGAGGATATCCATTTATTGGTGGAACGCAGATGGCATGTTGCAAGGAAACCTTTGGAT
GTTTATAAGAAACCATCAGGAAAATGCTTTTTCCAGGGAGACCACGGATTTGATAACAAG
GTCAACAGCATGCAGACTGTTTTTGTAGGTTATGGCTCAACATTTAAGTACAAGACTAAA
GTGCCTCCATTTGAAAACATTGAACTTTACAATGTTATGTGTGATCTCCTGGGATTGAAG
CCAGCTCCTAATAATGGGACCCATGGAAGTTTGAATCATCTCCTGCGCACTAATACCTTC
AGGCCAACCATGCCAGAGGAAGTTACCAGACCCAATTATCCAGGGATTATGTACCTTCAG
TCTGATTTTGACCTGGGCTGCACTTGTGATGATAAGGTAGAGCCAAAGAACAAGTTGGAT
GAACTCAACAAACGGCTTCATACAAAAGGGTCTACAGAAGAGAGACACCTCCTCTATGGG
CGACCTGCAGTGCTTTATCGGACTAGATATGATATCTTATATCACACTGACTTTGAAAGT
GGTTATAGTGAAATATTCCTAATGCCACTCTGGACATCATATACTGTTTCCAAACAGGCT
GAGGTTTCCAGCGTTCCTGACCATCTGACCAGTTGCGTCCGGCCTGATGTCCGTGTTTCT
CCGAGTTTCAGTCAGAACTGTTTGGCCTACAAAAATGATAAGCAGATGTCCTACGGATTC
CTCTTTCCTCCTTATCTGAGCTCTTCACCAGAGGCTAAATATGATGCATTCCTTGTAACC
AATATGGTTCCAATGTATCCTGCTTTCAAACGGGTCTGGAATTATTTCCAAAGGGTATTG
GTGAAGAAATATGCTTCGGAAAGAAATGGAGTTAACGTGATAAGTGGACCAATCTTCGAC
TATGACTATGATGGCTTACATGACACAGAAGACAAAATAAAACAGTACGTGGAAGGCAGT
TCCATTCCTGTTCCAACTCACTACTACAGCATCATCACCAGCTGTCTGGATTTCACTCAG
CCTGCCGACAAGTGTGACGGCCCTCTCTCTGTGTCCTCCTTCATCCTGCCTCACCGGCCT
GACAACGAGGAGAGCTGCAATAGCTCAGAGGACGAATCAAAATGGGTAGAAGAACTCATG
AAGATGCACACAGCTAGGGTGCGTGACATTGAACATCTCACCAGCCTGGACTTCTTCCGA
AAGACCAGCCGCAGCTACCCAGAAATCCTGACACTCAAGACATACCTGCATACATATGAG
AGCGAGATTTAA
Enzyme 2 GenBank Gene ID NM_001040092.1 Link Image
Enzyme 2 GeneCard ID ENPP2 Link Image
Enzyme 2 GenAtlas ID ENPP2 Link Image
Enzyme 2 HGNC ID HGNC:3357 Link Image
Enzyme 2 Chromosome Location 8
Enzyme 2 Locus 8q24.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Murata J, Lee HY, Clair T, Krutzsch HC, Arestad AA, Sobel ME, Liotta LA, Stracke ML: cDNA cloning of the human tumor motility-stimulating protein, autotaxin, reveals a homology with phosphodiesterases. J Biol Chem. 1994 Dec 2;269(48):30479-84. [PubMed Link Image]
  2. Kawagoe H, Soma O, Goji J, Nishimura N, Narita M, Inazawa J, Nakamura H, Sano K: Molecular cloning and chromosomal assignment of the human brain-type phosphodiesterase I/nucleotide pyrophosphatase gene (PDNP2). Genomics. 1995 Nov 20;30(2):380-4. [PubMed Link Image]
  3. Lee HY, Murata J, Clair T, Polymeropoulos MH, Torres R, Manrow RE, Liotta LA, Stracke ML: Cloning, chromosomal localization, and tissue expression of autotaxin from human teratocarcinoma cells. Biochem Biophys Res Commun. 1996 Jan 26;218(3):714-9. [PubMed Link Image]
  4. van Meeteren LA, Ruurs P, Christodoulou E, Goding JW, Takakusa H, Kikuchi K, Perrakis A, Nagano T, Moolenaar WH: Inhibition of autotaxin by lysophosphatidic acid and sphingosine 1-phosphate. J Biol Chem. 2005 Jun 3;280(22):21155-61. Epub 2005 Mar 15. [PubMed Link Image]
  5. Giganti A, Rodriguez M, Fould B, Moulharat N, Coge F, Chomarat P, Galizzi JP, Valet P, Saulnier-Blache JS, Boutin JA, Ferry G: Murine and human autotaxin alpha, beta, and gamma isoforms: gene organization, tissue distribution, and biochemical characterization. J Biol Chem. 2008 Mar 21;283(12):7776-89. Epub 2008 Jan 6. [PubMed Link Image]
  6. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  7. 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]
  8. Tokumura A, Majima E, Kariya Y, Tominaga K, Kogure K, Yasuda K, Fukuzawa K: Identification of human plasma lysophospholipase D, a lysophosphatidic acid-producing enzyme, as autotaxin, a multifunctional phosphodiesterase. J Biol Chem. 2002 Oct 18;277(42):39436-42. Epub 2002 Aug 9. [PubMed Link Image]
  9. Stracke ML, Krutzsch HC, Unsworth EJ, Arestad A, Cioce V, Schiffmann E, Liotta LA: Identification, purification, and partial sequence analysis of autotaxin, a novel motility-stimulating protein. J Biol Chem. 1992 Feb 5;267(4):2524-9. [PubMed Link Image]
  10. Nam SW, Clair T, Kim YS, McMarlin A, Schiffmann E, Liotta LA, Stracke ML: Autotaxin (NPP-2), a metastasis-enhancing motogen, is an angiogenic factor. Cancer Res. 2001 Sep 15;61(18):6938-44. [PubMed Link Image]
  11. Boucher J, Quilliot D, Praderes JP, Simon MF, Gres S, Guigne C, Prevot D, Ferry G, Boutin JA, Carpene C, Valet P, Saulnier-Blache JS: Potential involvement of adipocyte insulin resistance in obesity-associated up-regulation of adipocyte lysophospholipase D/autotaxin expression. Diabetologia. 2005 Mar;48(3):569-77. Epub 2005 Feb 8. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6056
Enzyme 3 Name Choline/ethanolamine kinase
Enzyme 3 Synonyms
  1. Choline kinase beta
  2. CK
  3. CKB
  4. Choline kinase-like protein
  5. Ethanolamine kinase
  6. EK
  7. Ethanolamine kinase beta
  8. EKB
  9. choline/ethanolamine kinase beta
  10. CKEKB
Enzyme 3 Gene Name CHKB
Enzyme 3 Protein Sequence >Choline/ethanolamine kinase
MAAEATAVAGSGAVGGCLAKDGLQQSKCPDTTPKRRRASSLSRDAERRAYQWCREYLGGA
WRRVQPEELRVYPVSGGLSNLLFRCSLPDHLPSVGEEPREVLLRLYGAILQGVDSLVLES
VMFAILAERSLGPQLYGVFPEGRLEQYIPSRPLKTQELREPVLSAAIATKMAQFHGMEMP
FTKEPHWLFGTMERYLKQIQDLPPTGLPEMNLLEMYSLKDEMGNLRKLLESTPSPVVFCH
NDIQEGNILLLSEPENADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTHEEWPFYKARP
TDYPTQEQQLHFIRHYLAEAKKGETLSQEEQRKLEEDLLVEVSRYALASHFFWGLWSILQ
ASMSTIEFGYLDYAQSRFQFYFQQKGQLTSVHSSS
Enzyme 3 Number of Residues 395
Enzyme 3 Molecular Weight 45271.0
Enzyme 3 Theoretical pI 5.20
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Cell wall/membrane/envelope biogenesis
Enzyme 3 Specific Function Has a key role in phospholipid biosynthesis. Catalyzes the first step in phosphatidylethanolamine biosynthesis. Phosphorylates ethanolamine, and can also act on choline (in vitro). Has higher activity with ethanolamine. May not significantly contribute to in vivo phosphatidylcholine biosynthesis
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + ethanolamine = ADP + O-phosphoethanolamine [RN:R01468]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID Q9Y259 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name CHKB_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1188 bp
ATGGCGGCCGAGGCGACAGCTGTGGCCGGAAGCGGGGCTGTTGGCGGCTGCCTGGCCAAA
GACGGCTTGCAGCAGTCTAAGTGCCCGGACACTACCCCAAAACGGCGGCGCGCCTCGTCG
CTGTCGCGTGACGCCGAGCGCCGAGCCTACCAATGGTGCCGGGAGTACTTGGGCGGGGCC
TGGCGCCGAGTGCAGCCCGAGGAGCTGAGGGTTTACCCCGTGAGCGGAGGCCTCAGCAAC
CTGCTCTTCCGCTGCTCGCTCCCGGACCACCTGCCCAGCGTTGGCGAGGAGCCCCGGGAG
GTGCTTCTGCGGCTGTACGGAGCCATCTTGCAGGGCGTGGACTCCCTGGTGCTAGAAAGC
GTGATGTTCGCCATACTTGCGGAGCGGTCGCTGGGGCCCCAGCTGTACGGAGTCTTCCCA
GAGGGCCGGCTGGAACAGTACATCCCAAGTCGGCCATTGAAAACTCAAGAGCTTCGAGAG
CCAGTGTTGTCAGCAGCCATTGCCACGAAGATGGCGCAATTTCATGGCATGGAGATGCCT
TTCACCAAGGAGCCCCACTGGCTGTTTGGGACCATGGAGCGGTACCTAAAACAGATCCAG
GACCTGCCCCCAACTGGCCTCCCTGAGATGAACCTGCTGGAGATGTACAGCCTGAAGGAT
GAGATGGGCAACCTCAGGAAGTTACTAGAGTCTACCCCATCGCCAGTCGTCTTCTGCCAC
AATGACATCCAGGAAGGGAACATCTTGCTGCTCTCAGAGCCAGAAAATGCTGACAGCCTC
ATGCTGGTGGACTTCGAGTACAGCAGTTATAACTATAGGGGCTTTGACATTGGGAACCAT
TTTTGTGAGTGGGTTTATGATTATACTCACGAGGAATGGCCTTTCTACAAAGCAAGGCCC
ACAGACTACCCCACTCAAGAACAGCAGTTGCATTTTATTCGTCATTACCTGGCAGAGGCA
AAGAAAGGTGAGACCCTCTCCCAAGAGGAGCAGAGAAAACTGGAAGAAGATTTGCTGGTA
GAAGTCAGTCGGTATGCTCTGGCATCCCATTTCTTCTGGGGTCTGTGGTCCATCCTCCAG
GCATCCATGTCCACCATAGAATTTGGTTACTTGGACTATGCCCAGTCTCGGTTCCAGTTC
TACTTCCAGCAGAAGGGGCAGCTGACCAGTGTCCACTCCTCATCCTGA
Enzyme 3 GenBank Gene ID AB029886 Link Image
Enzyme 3 GeneCard ID CHKB Link Image
Enzyme 3 GenAtlas ID CHKB Link Image
Enzyme 3 HGNC ID HGNC:1938 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 22q13.33
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Yamazaki N, Shinohara Y, Kajimoto K, Shindo M, Terada H: Novel expression of equivocal messages containing both regions of choline/ethanolamine kinase and muscle type carnitine palmitoyltransferase I. J Biol Chem. 2000 Oct 13;275(41):31739-46. [PubMed Link Image]
  2. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  3. 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]
  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. 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]
  6. Gallego-Ortega D, Ramirez de Molina A, Ramos MA, Valdes-Mora F, Barderas MG, Sarmentero-Estrada J, Lacal JC: Differential role of human choline kinase alpha and beta enzymes in lipid metabolism: implications in cancer onset and treatment. PLoS One. 2009 Nov 12;4(11):e7819. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6137
Enzyme 4 Name Ethanolamine kinase 1
Enzyme 4 Synonyms
  1. EKI 1
Enzyme 4 Gene Name ETNK1
Enzyme 4 Protein Sequence >Ethanolamine kinase 1
MLCGRPRSSSDNRNFLRERAGLSSAAVQTRIGNSAASRRSPAARPPVPAPPALPRGRPGT
EGSTSLSAPAVLVVAVAVVVVVVSAVAWAMANYIHVPPGSPEVPKLNVTVQDQEEHRCRE
GALSLLQHLRPHWDPQEVTLQLFTDGITNKLIGCYVGNTMEDVVLVRIYGNKTELLVDRD
EEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEALDPKHVCNPAIFRLIARQLAKIHAI
HAHNGWIPKSNLWLKMGKYFSLIPTGFADEDINKRFLSDIPSSQILQEEMTWMKEILSNL
GSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVSDVDYSLY
PDRELQSQWLRAYLEAYKEFKGFGTEVTEKEVEILFIQVNQFALASHFFWGLWALIQAKY
STIEFDFLGYAIVRFNQYFKMKPEVTALKVPE
Enzyme 4 Number of Residues 452
Enzyme 4 Molecular Weight 50967.9
Enzyme 4 Theoretical pI 6.51
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Cell wall/membrane/envelope biogenesis
Enzyme 4 Specific Function Highly specific for ethanolamine phosphorylation. May be a rate-controlling step in phosphatidylethanolamine biosynthesis
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + ethanolamine = ADP + O-phosphoethanolamine [RN:R01468]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 9998952 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9HBU6 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name EKI1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1359 bp
ATGCTCTGCGGCCGCCCGCGGTCCAGCTCCGACAACAGGAATTTTCTCCGAGAGCGGGCC
GGGCTCAGTTCAGCTGCTGTCCAGACCCGGATCGGCAACAGTGCCGCCTCCAGACGTTCT
CCTGCCGCTCGCCCGCCCGTCCCAGCGCCCCCAGCCCTCCCGCGAGGGCGCCCCGGGACG
GAAGGATCCACCAGTCTGTCGGCGCCCGCCGTTCTCGTGGTCGCCGTCGCCGTCGTCGTG
GTGGTAGTCTCCGCCGTCGCCTGGGCCATGGCCAATTACATCCACGTCCCTCCCGGCTCC
CCGGAGGTGCCCAAGCTGAACGTCACCGTTCAGGATCAGGAGGAGCATCGCTGCCGGGAG
GGGGCCCTGAGCCTCCTGCAACACCTGCGGCCTCACTGGGACCCCCAGGAGGTGACCCTG
CAGCTCTTCACAGATGGAATCACAAATAAACTTATTGGCTGTTACGTGGGAAACACCATG
GAGGATGTAGTCCTGGTGAGAATTTATGGCAATAAGACTGAGTTATTAGTCGATCGAGAT
GAGGAAGTAAAGAGTTTTCGAGTGTTGCAGGCTCATGGGTGTGCACCACAACTCTACTGT
ACCTTCAATAATGGACTATGCTATGAATTTATACAAGGAGAAGCACTGGATCCAAAGCAT
GTCTGCAACCCAGCCATTTTCAGGCTAATAGCTCGTCAGCTTGCTAAAATCCATGCTATT
CATGCACACAATGGCTGGATCCCCAAATCTAATCTTTGGCTAAAGATGGGAAAGTATTTC
TCTCTCATTCCCACAGGATTTGCAGATGAAGACATTAATAAAAGGTTCCTAAGTGATATC
CCAAGCTCTCAGATTCTCCAGGAAGAGATGACTTGGATGAAGGAGATTCTTTCCAACCTG
GGCTCACCTGTTGTGCTTTGCCATAATGACCTATTGTGTAAGAATATAATCTACAATGAG
AAACAAGGTGATGTACAGTTCATTGATTATGAATATTCTGGATACAACTACCTGGCATAT
GATATTGGAAATCATTTCAATGAATTTGCAGGTGTGAGTGATGTAGACTATAGTCTGTAT
CCAGATAGAGAACTACAGAGTCAGTGGCTGCGTGCTTACCTTGAAGCCTACAAAGAATTT
AAGGGCTTTGGGACTGAAGTTACTGAAAAGGAGGTAGAAATACTCTTCATTCAAGTCAAT
CAGTTTGCATTGGCTTCTCATTTCTTTTGGGGATTGTGGGCTTTGATTCAAGCCAAATAC
TCCACTATTGAGTTTGATTTCCTTGGGTATGCAATTGTTCGTTTTAACCAGTACTTTAAA
ATGAAGCCTGAGGTTACTGCATTAAAAGTGCCTGAGTAA
Enzyme 4 GenBank Gene ID AF207600 Link Image
Enzyme 4 GeneCard ID ETNK1 Link Image
Enzyme 4 GenAtlas ID ETNK1 Link Image
Enzyme 4 HGNC ID HGNC:24649 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 12p12.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Lykidis A, Wang J, Karim MA, Jackowski S: Overexpression of a mammalian ethanolamine-specific kinase accelerates the CDP-ethanolamine pathway. J Biol Chem. 2001 Jan 19;276(3):2174-9. Epub 2000 Oct 23. [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. 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 8634
Enzyme 5 Name Phosphoethanolamine/phosphocholine phosphatase
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name PHOSPHO1
Enzyme 5 Protein Sequence >Phosphoethanolamine/phosphocholine phosphatase
MSGCFPVSGLRCLSRDGRMAAQGAPRFLLTFDFDETIVDENSDDSIVRAAPGQRLPESLR
ATYREGFYNEYMQRVFKYLGEQGVRPRDLSAIYEAIPLSPGMSDLLQFVAKQGACFEVIL
ISDANTFGVESSLRAAGHHSLFRRILSNPSGPDARGLLALRPFHTHSCARCPANMCKHKV
LSDYLRERAHDGVHFERLFYVGDGANDFCPMGLLAGGDVAFPRRGYPMHRLIQEAQKAEP
SSFRASVVPWETAADVRLHLQQVLKSC
Enzyme 5 Number of Residues 267
Enzyme 5 Molecular Weight 29712.5
Enzyme 5 Theoretical pI 7.78
Enzyme 5 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
  • metabolic process
Component
Enzyme 5 General Function Involved in phosphatase activity
Enzyme 5 Specific Function Phosphatase that has a high activity toward phosphoethanolamine (PEA) and phosphocholine (PCho). May be involved in the generation of inorganic phosphate for bone mineralization
Enzyme 5 Pathways
Enzyme 5 Reactions
  • (1) O-phosphoethanolamine + H2O = ethanolamine + phosphate [RN:R06870]
  • (2) phosphocholine + H2O = choline + phosphate [RN:R06871]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 20196839 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q8TCT1 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PHOP1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >804 bp
ATGAGTGGCTGTTTTCCAGTTTCTGGCCTCCGCTGCCTATCTAGGGACGGCAGGATGGCC
GCGCAGGGCGCGCCGCGCTTCCTCCTGACCTTCGACTTCGACGAGACTATCGTGGACGAA
AACAGCGACGATTCGATCGTGCGCGCCGCGCCGGGCCAGCGGCTCCCGGAGAGCCTGCGA
GCCACCTACCGCGAGGGCTTCTACAACGAGTACATGCAGCGCGTCTTCAAGTACCTGGGC
GAGCAGGGCGTGCGGCCGCGGGACCTGAGCGCCATCTACGAAGCCATCCCTTTGTCGCCA
GGCATGAGCGACCTGCTGCAGTTTGTGGCAAAACAGGGCGCCTGCTTCGAGGTGATTCTC
ATCTCCGATGCCAACACCTTTGGCGTGGAGAGCTCGCTGCGCGCCGCCGGCCACCACAGC
CTGTTCCGCCGCATCCTCAGCAACCCGTCGGGGCCGGATGCGCGGGGACTGCTGGCTCTG
CGGCCGTTCCACACACACAGCTGCGCGCGCTGCCCCGCCAACATGTGCAAGCACAAGGTG
CTCAGCGACTACCTGCGCGAGCGGGCCCACGACGGCGTGCACTTCGAGCGCCTCTTCTAC
GTGGGCGACGGCGCCAACGACTTCTGCCCCATGGGGCTGCTGGCGGGCGGCGACGTGGCC
TTCCCGCGCCGCGGCTACCCCATGCACCGCCTCATTCAGGAGGCCCAGAAGGCCGAGCCC
AGCTCGTTCCGCGCCAGCGTGGTGCCCTGGGAAACGGCTGCAGATGTGCGCCTCCACCTG
CAACAGGTGCTGAAGTCGTGCTGA
Enzyme 5 GenBank Gene ID AJ457189 Link Image
Enzyme 5 GeneCard ID PHOSPHO1 Link Image
Enzyme 5 GenAtlas ID PHOSPHO1 Link Image
Enzyme 5 HGNC ID HGNC:16815 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 17q21.32
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Houston B, Paton IR, Burt DW, Farquharson C: Chromosomal localization of the chicken and mammalian orthologues of the orphan phosphatase PHOSPHO1 gene. Anim Genet. 2002 Dec;33(6):451-4. [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. Roberts SJ, Stewart AJ, Sadler PJ, Farquharson C: Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities. Biochem J. 2004 Aug 15;382(Pt 1):59-65. [PubMed Link Image]
  4. Houston B, Stewart AJ, Farquharson C: PHOSPHO1-A novel phosphatase specifically expressed at sites of mineralisation in bone and cartilage. Bone. 2004 Apr;34(4):629-37. [PubMed Link Image]
  5. Stewart AJ, Schmid R, Blindauer CA, Paisey SJ, Farquharson C: Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily. Protein Eng. 2003 Dec;16(12):889-95. [PubMed Link Image]
  6. Roberts SJ, Stewart AJ, Schmid R, Blindauer CA, Bond SR, Sadler PJ, Farquharson C: Probing the substrate specificities of human PHOSPHO1 and PHOSPHO2. Biochim Biophys Acta. 2005 Aug 31;1752(1):73-82. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 9700
Enzyme 6 Name Ethanolamine kinase 2
Enzyme 6 Synonyms
  1. EKI 2
  2. Ethanolamine kinase-like protein
Enzyme 6 Gene Name ETNK2
Enzyme 6 Protein Sequence >Ethanolamine kinase 2
MAVPPSAPQPRASFHLRRHTPCPQCSWGMEEKAAASASCREPPGPPRAAAVAYFGISVDP
DDILPGALRLIQELRPHWKPEQVRTKRFTDGITNKLVACYVEEDMQDCVLVRVYGERTEL
LVDRENEVRNFQLLRAHSCAPKLYCTFQNGLCYEYMQGVALEPEHIREPRLFRLIALEMA
KIHTIHANGSLPKPILWHKMHNYFTLVKNEINPSLSADVPKVEVLERELAWLKEHLSQLE
SPVVFCHNDLLCKNIIYDSIKGHVRFIDYEYAGYNYQAFDIGNHFNEFAGVNEVDYCLYP
ARETQLQWLHYYLQAQKGMAVTPREVQRLYVQVNKFALASHFFWALWALIQNQYSTIDFD
FLRYAVIRFNQYFKVKPQASALEMPK
Enzyme 6 Number of Residues 386
Enzyme 6 Molecular Weight 44781.1
Enzyme 6 Theoretical pI 7.36
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Cell wall/membrane/envelope biogenesis
Enzyme 6 Specific Function Highly specific for ethanolamine phosphorylation. Does not have choline kinase activity
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + ethanolamine = ADP + O-phosphoethanolamine [RN:R01468]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 186659525 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9NVF9 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name EKI2_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1161 bp
ATGGCTGTGCCCCCTTCGGCCCCTCAGCCGCGCGCGTCCTTTCACCTGAGGAGGCACACG
CCTTGCCCGCAGTGCTCATGGGGCATGGAGGAGAAGGCGGCGGCCAGCGCCAGCTGCCGG
GAGCCGCCGGGCCCCCCGAGGGCCGCCGCCGTCGCGTACTTCGGCATTTCCGTGGACCCG
GACGACATCCTTCCCGGGGCCCTGCGCCTCATCCAGGAGCTGCGGCCGCATTGGAAACCC
GAGCAAGTTCGGACCAAGCGCTTCACGGATGGCATCACCAACAAGCTGGTGGCCTGCTAT
GTGGAGGAGGACATGCAGGACTGCGTGCTGGTCCGGGTGTATGGGGAGCGGACGGAGCTG
CTGGTGGACCGGGAGAATGAGGTCAGAAACTTCCAGCTGCTGCGAGCACACAGCTGTGCC
CCCAAACTCTACTGCACCTTCCAGAATGGGCTGTGCTATGAGTACATGCAGGGTGTGGCC
CTGGAGCCTGAGCACATCCGTGAGCCCCGGCTTTTCAGGTTAATCGCCTTAGAAATGGCA
AAGATTCATACTATCCACGCCAACGGCAGCCTGCCCAAGCCCATCCTCTGGCACAAGATG
CACAATTATTTCACGCTTGTGAAGAACGAGATCAACCCCAGCCTTTCTGCAGATGTCCCT
AAGGTAGAGGTGTTGGAACGGGAGCTGGCCTGGCTGAAGGAGCATCTGTCCCAGCTGGAG
TCCCCTGTGGTGTTTTGTCACAATGACCTGCTCTGCAAGAATATCATCTATGACAGCATC
AAAGGTCACGTGCGGTTCATTGACTATGAATATGCTGGCTACAACTACCAAGCTTTTGAC
ATTGGCAACCATTTCAATGAGTTTGCAGGCGTGAATGAGGTGGATTACTGCCTGTACCCG
GCGCGGGAGACCCAGCTGCAGTGGCTGCACTACTACCTGCAGGCACAAAAGGGGATGGCC
GTGACCCCCAGGGAGGTGCAAAGGCTCTACGTGCAAGTCAACAAGTTTGCCCTGGCGTCT
CACTTCTTCTGGGCTCTCTGGGCCCTCATCCAGAACCAGTACTCCACCATCGACTTTGAT
TTCCTCAGGTACGCAGTGATCCGATTCAACCAGTACTTCAAGGTGAAGCCTCAAGCGTCA
GCCTTGGAGATGCCAAAGTGA
Enzyme 6 GenBank Gene ID NM_018208.2 Link Image
Enzyme 6 GeneCard ID ETNK2 Link Image
Enzyme 6 GenAtlas ID ETNK2 Link Image
Enzyme 6 HGNC ID HGNC:25575 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 1q32.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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. 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. Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed Link Image]
  5. Lykidis A, Wang J, Karim MA, Jackowski S: Overexpression of a mammalian ethanolamine-specific kinase accelerates the CDP-ethanolamine pathway. J Biol Chem. 2001 Jan 19;276(3):2174-9. Epub 2000 Oct 23. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 13049
Enzyme 7 Name Choline kinase beta
Enzyme 7 Synonyms
  1. SubName: HCG16873, isoform CRA_a
  2. SubName: cDNA, FLJ95084, Homo sapiens choline kinase-like (CHKL), transcript variant 1,mRNA
Enzyme 7 Gene Name CHKB
Enzyme 7 Protein Sequence >Choline kinase beta
MAAEATAVAGSGAVGGCLAKDGLQQSKCPDTTPKRRRASSLSRDAERRAYQWCREYLGGA
WRRVQPEELRVYPVSGGLSNLLFRCSLPDHLPSVGEEPREVLLRLYGAILQGVDSLVLES
VMFAILAERSLGPQLYGVFPEGRLEQYIPSRPLKTQELREPVLSAAIATKMAQFHGMEMP
FTKEPHWLFGTMERYLKQIQDLPPTGLPEMNLLEMYSLKDEMGNLRKLLESTPSPVVFCH
NDIQEGNILLLSEPENADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTHEEWPFYKARP
TDYPTQEQQLHFIRHYLAEAKKGETLSQEEQRKLEEDLLVEVSRYALASHFFWGLWSILQ
ASMSTIEFGYLDYAQSRFQFYFQQKGQLTSVHSSS
Enzyme 7 Number of Residues 395
Enzyme 7 Molecular Weight 45271.0
Enzyme 7 Theoretical pI 5.20
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Cell wall/membrane/envelope biogenesis
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 189067262 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID A0PJM6 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name A0PJM6_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1188 bp
ATGGCGGCCGAGGCGACAGCTGTGGCCGGAAGCGGGGCTGTTGGCGGCTGCCTGGCCAAA
GACGGCTTGCAGCAGTCTAAGTGCCCGGACACTACCCCAAAACGGCGGCGCGCCTCGTCG
CTGTCGCGTGACGCCGAGCGCCGAGCCTACCAATGGTGCCGGGAGTACTTGGGCGGGGCC
TGGCGCCGAGTGCAGCCCGAGGAGCTGAGGGTTTACCCCGTGAGCGGAGGCCTCAGCAAC
CTGCTCTTCCGCTGCTCGCTCCCGGACCACCTGCCCAGCGTTGGCGAGGAGCCCCGGGAG
GTGCTTCTGCGGCTGTACGGAGCCATCTTGCAGGGCGTGGACTCCCTGGTGCTAGAAAGC
GTGATGTTCGCCATACTTGCGGAGCGGTCGCTGGGGCCCCAGCTGTACGGAGTCTTCCCA
GAGGGCCGGCTGGAACAGTACATCCCAAGTCGGCCATTGAAAACTCAAGAGCTTCGAGAG
CCAGTGTTGTCAGCAGCCATTGCCACGAAGATGGCGCAATTTCATGGCATGGAGATGCCT
TTCACCAAGGAGCCCCACTGGCTGTTTGGGACCATGGAGCGGTACCTAAAACAGATCCAG
GACCTGCCCCCAACTGGCCTCCCTGAGATGAACCTGCTGGAGATGTACAGCCTGAAGGAT
GAGATGGGCAACCTCAGGAAGTTACTAGAGTCTACCCCATCGCCAGTCGTCTTCTGCCAC
AATGACATCCAGGAAGGGAACATCTTGCTGCTCTCAGAGCCAGAAAATGCTGACAGCCTC
ATGCTGGTGGACTTCGAGTACAGCAGTTATAACTATAGGGGCTTTGACATTGGGAACCAT
TTTTGTGAGTGGGTTTATGATTATACTCACGAGGAATGGCCTTTCTACAAAGCAAGGCCC
ACAGACTACCCCACTCAAGAACAGCAGTTGCATTTTATTCGTCATTACCTGGCAGAGGCA
AAGAAAGGTGAGACCCTCTCCCAAGAGGAGCAGAGAAAACTGGAAGAAGATTTGCTGGTA
GAAGTCAGTCGGTATGCTCTGGCATCCCATTTCTTCTGGGGTCTGTGGTCCATCCTCCAG
GCATCCATGTCCACCATAGAATTTGGTTACTTGGACTATGCCCAGTCTCGGTTCCAGTTC
TACTTCCAGCAGAAGGGGCAGCTGACCAGTGTCCACTCCTCATCCTGA
Enzyme 7 GenBank Gene ID AK314324 Link Image
Enzyme 7 GeneCard ID CHKB Link Image
Enzyme 7 GenAtlas ID CHKB Link Image
Enzyme 7 HGNC ID HGNC:1938 Link Image
Enzyme 7 Chromosome Location 2
Enzyme 7 Locus 22q13.33
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 13050
Enzyme 8 Name Glycerophosphodiester phosphodiesterase 1
Enzyme 8 Synonyms
  1. Membrane-interacting protein of RGS16
  2. RGS16-interacting membrane protein
Enzyme 8 Gene Name GDE1
Enzyme 8 Protein Sequence >Glycerophosphodiester phosphodiesterase 1
MWLWEDQGGLLGPFSFLLLVLLLVTRSPVNACLLTGSLFVLLRVFSFEPVPSCRALQVLK
PRDRISAIAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGIPVLMHDNTVDRTT
DGTGRLCDLTFEQIRKLNPAANHRLRNDFPDEKIPTLREAVAECLNHNLTIFFDVKGHAH
KATEALKKMYMEFPQLYNNSVVCSFLPEVIYKMRQTDRDVITALTHRPWSLSHTGDGKPR
YDTFWKHFIFVMMDILLDWSMHNILWYLCGISAFLMQKDFVSPAYLKKWSAKGIQVVGWT
VNTFDEKSYYESHLGSSYITDSMVEDCEPHF
Enzyme 8 Number of Residues 331
Enzyme 8 Molecular Weight 37718.0
Enzyme 8 Theoretical pI 6.70
Enzyme 8 GO Classification
Function
  • catalytic activity
  • glycerophosphodiester phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • alcohol metabolic process
  • alditol metabolic process
  • glycerol metabolic process
  • lipid metabolic process
  • metabolic process
  • polyol metabolic process
  • primary metabolic process
  • small molecule metabolic process
Component
Enzyme 8 General Function Involved in glycerophosphodiester phosphodiesterase activity
Enzyme 8 Specific Function Has glycerophosphoinositol phosphodiesterase activity. Has little or no activity towards glycerophosphocholine. GDE1 activity can be modulated by G-protein signaling pathways
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • 1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O = myo-inositol + sn-glycerol 3-phosphate [RN:R01193]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 4-24 248-268
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 7637877 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9NZC3 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name GDE1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >996 bp
ATGTGGCTGTGGGAGGACCAGGGCGGCCTCCTGGGCCCTTTCTCCTTCCTGCTGCTAGTG
CTGCTGCTGGTGACGCGGAGCCCGGTCAATGCCTGCCTCCTCACCGGCAGCCTCTTCGTT
CTACTGCGCGTCTTCAGCTTTGAGCCGGTGCCCTCTTGCAGGGCCCTGCAGGTGCTCAAG
CCCCGGGACCGCATTTCTGCCATCGCCCACCGTGGCGGCAGCCACGACGCGCCCGAGAAC
ACGCTGGCGGCCATTCGGCAGGCAGCTAAGAATGGAGCAACAGGCGTGGAGTTGGACATT
GAGTTTACTTCTGACGGGATTCCTGTCTTAATGCACGATAACACAGTAGATAGGACGACT
GATGGGACTGGGCGATTGTGTGATTTGACATTTGAACAAATTAGGAAGCTGAATCCTGCA
GCAAACCACAGACTCAGGAATGATTTCCCTGATGAAAAGATCCCTACCCTAAGGGAAGCT
GTTGCAGAGTGCCTAAACCATAACCTCACAATCTTCTTTGATGTCAAAGGCCATGCACAC
AAGGCTACTGAGGCTCTAAAGAAAATGTATATGGAATTTCCTCAACTGTATAATAATAGT
GTGGTCTGTTCTTTCTTGCCAGAAGTTATCTACAAGATGAGACAAACAGATCGGGATGTA
ATAACAGCATTAACTCACAGACCTTGGAGCCTAAGCCATACAGGAGATGGGAAACCACGC
TATGATACTTTCTGGAAACATTTTATATTTGTTATGATGGACATTTTGCTCGATTGGAGC
ATGCATAATATCTTGTGGTACCTGTGTGGAATTTCAGCTTTCCTCATGCAAAAGGATTTT
GTATCCCCGGCCTACTTGAAGAAGTGGTCAGCTAAAGGAATCCAGGTTGTTGGTTGGACT
GTTAATACCTTTGATGAAAAGAGTTACTACGAATCCCATCTTGGTTCCAGCTATATCACT
GACAGCATGGTAGAAGACTGCGAACCTCACTTCTAG
Enzyme 8 GenBank Gene ID AF212862 Link Image
Enzyme 8 GeneCard ID GDE1 Link Image
Enzyme 8 GenAtlas ID GDE1 Link Image
Enzyme 8 HGNC ID HGNC:29644 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 16p12-p11.2
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Zheng B, Chen D, Farquhar MG: MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16. Proc Natl Acad Sci U S A. 2000 Apr 11;97(8):3999-4004. [PubMed Link Image]
  2. Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD: Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics. 1999 Sep 15;60(3):295-308. [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. Bachmann AS, Duennebier FF, Mocz G: Genomic organization, characterization, and molecular 3D model of GDE1, a novel mammalian glycerophosphoinositol phosphodiesterase. Gene. 2006 Apr 12;371(1):144-53. Epub 2006 Feb 9. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 15207
Enzyme 9 Name Phospholipase D1 variant
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name Not Available
Enzyme 9 Protein Sequence >Phospholipase D1 variant
ANAQVLAAPSPCSPFAFTLSKVNMSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEG
EEVDYDVSPSDPKIQEVYIPFSAIYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRV
PSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEP
REMPSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDL
GPKGIEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLL
VDKEFKIKVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKD
HRFGSYAAIQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGN
RWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSST
VYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAM
ESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSI
SSIDSTSNTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPR
MPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLLPKSQTTAHELRYQVP
GSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFN
KIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGEN
SILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANIN
DRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQ
DPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPVLAKEDPIRAEE
ELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
Enzyme 9 Number of Residues 1059
Enzyme 9 Molecular Weight 122007.8
Enzyme 9 Theoretical pI 9.03
Enzyme 9 GO Classification
Function
  • binding
  • catalytic activity
  • lipid binding
  • phosphoinositide binding
  • phospholipid binding
  • protein binding
Process
  • cell communication
  • cellular process
  • metabolic process
Component
Enzyme 9 General Function Involved in protein binding
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 62089400 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q59EA4 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name Q59EA4_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >3182 bp
CCGCCAACGCGCAGGTGCTAGCGGCCCCTTCGCCCTGCAGCCCCTTTGCTTTTACTCTGT
CCAAAGTTAACATGTCACTGAAAAACGAGCCACGGGTAAATACCTCTGCACTGCAGAAAA
TTGCTGCTGACATGAGTAATATCATAGAAAATCTGGACACGCGGGAACTCCACTTTGAGG
GAGAGGAGGTAGACTACGACGTGTCTCCCAGCGATCCCAAGATACAAGAAGTGTATATCC
CTTTCTCTGCTATTTATAACACTCAAGGATTTAAGGAGCCTAATATACAGACGTATCTCT
CCGGCTGTCCAATAAAAGCACAAGTTCTGGAAGTGGAACGCTTCACATCTACAACAAGGG
TACCAAGTATTAATCTTTACACTATTGAATTAACACATGGGGAATTTAAATGGCAAGTTA
AGAGGAAATTCAAGCATTTTCAAGAATTTCACAGAGAGCTGCTCAAGTACAAAGCCTTTA
TCCGCATCCCCATTCCCACTAGAAGACACACGTTTAGGAGGCAAAACGTCAGAGAGGAGC
CTCGAGAGATGCCCAGTTTGCCCCGTTCATCTGAAAACATGATAAGAGAAGAACAATTCC
TTGGTAGAAGAAAACAACTGGAAGATTACTTGACAAAGATACTAAAAATGCCCATGTATA
GAAACTATCATGCCACAACAGAGTTTCTTGATATAAGCCAGCTGTCTTTCATCCATGATT
TGGGACCAAAGGGCATAGAAGGTATGATAATGAAAAGATCTGGAGGACACAGAATACCAG
GCTTGAATTGCTGTGGTCAGGGAAGAGCCTGCTACAGATGGTCAAAAAGATGGTTAATAG
TGAAAGATTCCTTTTTATTGTATATGAAACCAGACAGCGGTGCCATTGCCTTCGTCCTGC
TGGTAGACAAAGAATTCAAAATTAAGGTGGGGAAGAAGGAGACAGAAACGAAATATGGAA
TCCGAATTGATAATCTTTCAAGGACACTTATTTTAAAATGCAACAGCTATAGACATGCTC
GGTGGTGGGGAGGGGCTATAGAAGAATTCATCCAGAAACATGGCACCAACTTTCTCAAAG
ATCATCGATTTGGGTCATATGCTGCTATCCAAGAGAATGCTTTAGCTAAATGGTATGTTA
ATGCCAAAGGATATTTTGAAGATGTGGCAAATGCAATGGAAGAGGCAAATGAAGAGATTT
TTATCACAGACTGGTGGCTGAGTCCAGAAATCTTCCTGAAACGCCCAGTGGTTGAGGGAA
ATCGTTGGAGGTTGGACTGCATTCTTAAACGAAAAGCACAACAAGGAGTGAGGATCTTCA
TAATGCTCTACAAAGAGGTGGAACTCGCTCTTGGCATCAATAGTGAATACACCAAGAGGA
CTTTGATGCGTCTACATCCCAACATAAAGGTGATGAGACACCCGGATCATGTGTCATCCA
CCGTCTATTTGTGGGCTCACCATGAGAAGCTTGTCATCATTGACCAATCGGTGGCCTTTG
TGGGAGGGATTGACCTGGCCTATGGAAGGTGGGACGACAATGAGCACAGACTCACAGACG
TGGGCAGTGTGAAGCGGGTCACTTCAGGACCGTCTCTGGGTTCCCTCCCACCTGCCGCAA
TGGAGTCTATGGAATCCTTAAGACTCAAAGATAAAAATGAGCCTGTTCAAAACCTACCCA
TCCAGAAGAGTATTGATGATGTGGATTCAAAACTGAAAGGAATAGGAAAGCCAAGAAAGT
TCTCCAAATTTAGTCTCTACAAGCAGCTCCACAGGCACCACCTGCACGACGCAGATAGCA
TCAGCAGCATTGACAGCACCTCCAATACCGGGTCCATCCGTAGTTTACAGACAGGTGTGG
GAGAGCTGCATGGGGAAACCAGATTCTGGCATGGAAAGGACTACTGCAATTTCGTCTTCA
AAGACTGGGTTCAACTTGATAAACCTTTTGCTGATTTCATTGACAGGTACTCCACGCCCC
GGATGCCCTGGCATGACATTGCCTCTGCAGTCCACGGGAAGGCGGCTCGTGATGTGGCAC
GTCACTTCATCCAGCGCTGGAACTTCACAAAAATTATGAAATCAAAATATCGGTCCCTTT
CTTATCCTTTTCTGCTTCCAAAGTCTCAAACAACAGCCCATGAGTTGAGATATCAAGTGC
CTGGGTCTGTCCATGCTAACGTACAGTTGCTCCGCTCTGCTGCTGATTGGTCTGCTGGTA
TAAAGTACCATGAAGAGTCCATCCACGCCGCTTACGTCCATGTGATAGAGAACAGCAGGC
ACTATATCTATATCGAAAACCAGTTTTTCATAAGCTGTGCTGATGACAAAGTTGTGTTCA
ACAAGATAGGCGATGCCATTGCCCAGAGGATCCTGAAAGCTCACAGGGAAAACCAGAAAT
ACCGGGTATATGTCGTGATACCACTTCTGCCAGGGTTCGAAGGAGACATTTCAACCGGCG
GAGGAAATGCTCTACAGGCAATCATGCACTTCAACTACAGAACCATGTGCAGAGGAGAAA
ATTCCATCCTTGGACAGTTAAAAGCAGAGCTTGGTAATCAGTGGATAAATTACATATCAT
TCTGTGGTCTTAGAACACATGCAGAGCTCGAAGGAAACCTAGTAACTGAGCTTATCTATG
TCCACAGCAAGTTGTTAATTGCTGATGATAACACTGTTATTATTGGCTCTGCCAACATAA
ATGACCGCAGCATGCTGGGAAAGCGTGACAGTGAAATGGCTGTCATTGTGCAAGATACAG
AGACTGTTCCTTCAGTAATGGATGGAAAAGAGTACCAAGCTGGCCGGTTTGCCCGAGGAC
TTCGGCTACAGTGCTTTAGGGTTGTCCTTGGCTATCTTGATGACCCAAGTGAGGACATTC
AGGATCCAGTGAGTGACAAATTCTTCAAGGAGGTGTGGGTTTCAACAGCAGCTCGAAATG
CTACAATTTATGACAAGGTTTTCCGGTGCCTTCCCAATGATGAAGTACACAATTTAATTC
AGCTGAGAGACTTTATAAACAAGCCCGTATTAGCTAAGGAAGATCCCATTCGAGCTGAGG
AGGAACTGAAGAAGATCCGTGGATTTTTGGTGCAATTCCCCTTTTATTTCTTGTCTGAAG
AAAGCCTACTGCCTTCTGTTGGGACCAAAGAGGCCATAGTGCCCATGGAGGTTTGGACTT
AA
Enzyme 9 GenBank Gene ID AB209907 Link Image
Enzyme 9 GeneCard ID Not Available
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID HGNC:9067 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs Not Available
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 15224
Enzyme 10 Name ETNK2 protein (Ethanolamine kinase 2, isoform CRA_b) (Ethanolamine kinase 2)
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name ETNK2
Enzyme 10 Protein Sequence >ETNK2 protein (Ethanolamine kinase 2, isoform CRA_b) (Ethanolamine kinase 2)
MAVPPSAPQPRASFHLRRHTPCPQCSWGMEEKAAASASCREPPGPPRAAAVAYFGISVDP
DDILPGALRLIQELRPHWKPEQVRTKRFTDGITNKLVACYVEEDMQDCVLVRVYGERTEL
LVDRENEVRNFQLLRAHSCAPKLYCTFQNGLCYEYMQGVALEPEHIREPRLFRLIALEMA
KIHTIHANGSLPKPILWHKMHNYFTLVKNEINPSLSADVPKVEVLERELAWLKEHLSQLE
SPVVFCHNDLLCKNIIYDSIKGHVRFIDYEYAGYNYQAFDIGNHFNEFAGVNEVDYCLYP
ARETQLQWLHYYLQAQKGMAVTPREVQRLYVQVNKFALASHFFWALWALIQNQYSTIDFD
FLRYAVIRFNQYFKVKPQASALEMPK
Enzyme 10 Number of Residues 386
Enzyme 10 Molecular Weight 44782
Enzyme 10 Theoretical pI 7.36
Enzyme 10 GO Classification Not Available
Enzyme 10 General Function Cell wall/membrane/envelope biogenesis
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 14603244 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q96G05 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name Q96G05_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1161 bp
ATGGCTGTGCCCCCTTCGGCCCCTCAGCCGCGCGCGTCCTTTCACCTGAGGAGGCACACG
CCTTGCCCGCAGTGCTCATGGGGCATGGAGGAGAAGGCGGCGGCCAGCGCCAGCTGCCGG
GAGCCGCCGGGCCCCCCGAGGGCCGCCGCCGTCGCGTACTTCGGCATTTCCGTGGACCCG
GACGACATCCTTCCCGGGGCCCTGCGCCTCATCCAGGAGCTGCGGCCGCATTGGAAACCC
GAGCAAGTTCGGACCAAGCGCTTCACGGATGGCATCACCAACAAGCTGGTGGCCTGCTAT
GTGGAGGAGGACATGCAGGACTGCGTGCTGGTCCGGGTGTATGGGGAGCGGACGGAGCTG
CTGGTGGACCGGGAGAATGAGGTCAGAAACTTCCAGCTGCTGCGAGCACACAGCTGTGCC
CCCAAACTCTACTGCACCTTCCAGAATGGGCTGTGCTATGAGTACATGCAGGGTGTGGCC
CTGGAGCCTGAGCACATCCGTGAGCCCCGGCTTTTCAGGTTAATCGCCTTAGAAATGGCA
AAGATTCATACTATCCACGCCAACGGCAGCCTGCCCAAGCCCATCCTCTGGCACAAGATG
CACAATTATTTCACGCTTGTGAAGAACGAGATCAACCCCAGCCTTTCTGCAGATGTCCCT
AAGGTAGAGGTGTTGGAACGGGAGCTGGCCTGGCTGAAGGAGCATCTGTCCCAGCTGGAG
TCCCCTGTGGTGTTTTGTCACAATGACCTGCTCTGCAAGAATATCATCTATGACAGCATC
AAAGGTCACGTGCGGTTCATTGACTATGAATATGCTGGCTACAACTACCAAGCTTTTGAC
ATTGGCAACCATTTCAATGAGTTTGCAGGCGTGAATGAGGTGGATTACTGCCTGTACCCG
GCGCGGGAGACCCAGCTGCAGTGGCTGCACTACTACCTGCAGGCACAAAAGGGGATGGCC
GTGACCCCCAGGGAGGTGCAAAGGCTCTACGTGCAAGTCAACAAGTTTGCCCTGGCGTCT
CACTTCTTCTGGGCTCTCTGGGCCCTCATCCAGAACCAGTACTCCACCATCGACTTTGAT
TTCCTCAGGTACGCAGTGATCCGATTCAACCAGTACTTCAAGGTGAAGCCTCAAGCGTCA
GCCTTGGAGATGCCAAAGTGA
Enzyme 10 GenBank Gene ID BC010082 Link Image
Enzyme 10 GeneCard ID Q96G05 Link Image
Enzyme 10 GenAtlas ID ETNK2 Link Image
Enzyme 10 HGNC ID HGNC:25575 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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 10 Metabolite References Not Available