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Human Metabolome Database Version 2.5

 

Showing metabocard for Choline (HMDB00097)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-05-21 14:54:25
Accession Number HMDB00097
Secondary Accession Numbers Not Available
Common Name Choline
Description A basic constituent of lecithin that is found in many plants and animal organs. It is important as a precursor of acetylcholine, as a methyl donor in various metabolic processes, and in lipid metabolism. Choline is now considered to be an essential vitamin. While humans can synthesize small amounts (by converting phosphatidylethanolamine to phosphatidylcholine), it must be consumed in the diet to maintain health. Required levels are between 425 mg/day (female) and 550 mg/day (male). Milk, eggs, liver and peanuts are especially rich in choline. Most choline is found in phospholipids, namely phosphatidylcholine or lecithin. Choline can be oxidized to form betaine, which is a methyl source for many reactions (i.e. conversion of homocysteine e to methionine). Lack of sufficient amounts of choline in the diet can lead to a fatty liver condition and general liver damage. This arises from the lack of VLDL, which is necessary to transport fats away from the liver. Choline deficiency also leads to elevated serum levels of alanine amino transferase and is associated with increased incidence of liver cancer.
Synonyms
  1. (2-Hydroxyethyl)trimethyl ammonium
  2. (2-Hydroxyethyl)trimethylammonium
  3. (beta-hydroxyethyl)trimethylammonium
  4. 2-hydroxy-N,N,N-trimethylethanaminium
  5. Bilineurine
  6. Biocolina
  7. Biocoline
  8. Choline
  9. Choline cation
  10. Choline ion
  11. Cholinum
  12. Hepacholine
  13. Hormocline
  14. Lipotril
  15. N,N,N-trimethylethanolammonium
  16. Neocolina
  17. Paresan
  18. 2-hydroxy-N,N,N-trimethyl-ethanaminium
  19. N,N,N-trimethylethanol-ammonium
Chemical IUPAC Name 2-hydroxyethyl-trimethyl-ammonium
Chemical Formula C5H14NO
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Quaternary Amines
Sub Class
  • Short chain quaternary ammonium salts
Family
  • Mammalian Metabolite
Species
  • cation
  • primary alcohol
  • quaternary ammonium salt
Biofunction
  • Essential vitamins
  • Component of Glycerophospholipid metabolism
  • Component of Glycine, serine and threonine metabolism
  • Component of Glycosphingolipid metabolism
Application
Source
  • Exogenous
Average Molecular Weight 104.171
Monoisotopic Molecular Weight 104.107536
Isomeric SMILES C[N+](C)(C)CCO
Canonical SMILES C[N+](C)(C)CCO
KEGG Compound ID C00114 Link Image
BioCyc ID CPD-563 Link Image
BiGG ID 33910 Link Image
Wikipedia Link Choline Link Image
NuGOwiki Link HMDB00097 Link Image
Metagene Link HMDB00097 Link Image
METLIN ID 56 Link Image
PubChem Compound 305 Link Image
PubChem Substance 608363 Link Image
ChEBI ID 15354 Link Image
CAS Registry Number 62-49-7
InChI Identifier InChI=1/C5H14NO/c1-6(2,3)4-5-7/h7H,4-5H2,1-3H3/q+1
Synthesis Reference Hasegawa, Yoichi; Hyoda, Shunji; Sawada, Hirotoshi; Baba, Masakatsu. Preparation of high-purity organic carboxylic acid choline salts and choline. Jpn. Kokai Tokkyo Koho (1999), 9 pp.
Melting Point (Experimental) 302-303 oC (Chloride salt)
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 3.61 mg/mL [Predicted by ALOGPS]; 1000 mg/mL at 25 oC [MEYLAN,WM et al. (1996)] Calculated using ALOGPS
Physiological Charge 1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -3.59 [Predicted by ALOGPS]; -5.16 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1GVM 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)
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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
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Medium Energy
Download File
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High Energy
Download File
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Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
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Cellular Location
  • Cytoplasm
  • endoplasmic reticulum
  • Extracellular
  • golgi apparatus
  • mitochondria
  • nucleus
Biofluid Location
  • Blood
  • Breast Milk
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
Basal Ganglia
Bladder
Brain
Epidermis
Fibroblasts
Hippocampus
Intestine
Kidney
Liver
Muscle
Myelin
Nerve Cells
Neuron
Placenta
Platelet
Prostate
Skeletal Muscle
Spleen
Stratum Corneum
Temporal Lobe
Testes
Thalamus
Concentrations (Normal)
Biofluid Blood
Value 6.0 +/- 0.3 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Jacob RA, Jenden DJ, Allman-Farinelli MA, Swendseid ME: Folate nutriture alters choline status of women and men fed low choline diets. J Nutr. 1999 Mar;129(3):712-7. [PubMed Link Image]
Biofluid Blood
Value 27.5 +/- 3.3 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 10.6 +/- 1.9 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 Blood
Value 6.8 +/- 0.3 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Jacob RA, Jenden DJ, Allman-Farinelli MA, Swendseid ME: Folate nutriture alters choline status of women and men fed low choline diets. J Nutr. 1999 Mar;129(3):712-7. [PubMed Link Image]
Biofluid Breast Milk
Value 116 +/- 22 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Holmes-McNary MQ, Cheng WL, Mar MH, Fussell S, Zeisel SH: Choline and choline esters in human and rat milk and in infant formulas. Am J Clin Nutr. 1996 Oct;64(4):572-6. [PubMed Link Image]
Biofluid CSF
Value 8.3 (7.0-13.0) 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 3 +/- 1 uM
Age N/A
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Lewis MJ, Morrissey JA, Flegel MD, Jeroncic K, Xiong Y, Cheng D, Eisner R, Gautam B, Tzur D, Sawhney S, Bamforth F, Greiner R, Li L: The human cerebrospinal fluid metabolome. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Aug 15;871(2):164-173. Epub 2008 May 8. [PubMed Link Image]
Biofluid Saliva
Value >10 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
Biofluid Urine
Value 6.3 (0.72-28.5) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Male
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 86 +/- 42 uM
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)
Biofluid CSF
Value 170.0 +/- 70.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Spina Bifida
Comments Not Available
References
  • Pal K, Sharma U, Gupta DK, Pratap A, Jagannathan NR: Metabolite profile of cerebrospinal fluid in patients with spina bifida: a proton magnetic resonance spectroscopy study. Spine. 2005 Feb 1;30(3):E68-72. [PubMed Link Image]
Biofluid CSF
Value 140.0 +/- 180.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Spina Bifida
Comments Not Available
References
  • Pal K, Sharma U, Gupta DK, Pratap A, Jagannathan NR: Metabolite profile of cerebrospinal fluid in patients with spina bifida: a proton magnetic resonance spectroscopy study. Spine. 2005 Feb 1;30(3):E68-72. [PubMed Link Image]
Biofluid CSF
Value 1.46 +/- 0.54 uM
Age Adult:>18 yrs old
Sex N/A
Condition Multi-infarct dementia
Comments Not Available
References
  • Walter A, Korth U, Hilgert M, Hartmann J, Weichel O, Hilgert M, Fassbender K, Schmitt A, Klein J: Glycerophosphocholine is elevated in cerebrospinal fluid of Alzheimer patients. Neurobiol Aging. 2004 Nov-Dec;25(10):1299-303. [PubMed Link Image]
Biofluid CSF
Value 2.5 +/- 1.0 uM
Age Elderly:>65 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Walter A, Korth U, Hilgert M, Hartmann J, Weichel O, Hilgert M, Fassbender K, Schmitt A, Klein J: Glycerophosphocholine is elevated in cerebrospinal fluid of Alzheimer patients. Neurobiol Aging. 2004 Nov-Dec;25(10):1299-303. [PubMed Link Image]
Biofluid Urine
Value 3.0 (0.0-8.0) umol/mmol creatinine
Age N/A
Sex Both
Condition Lung Cancer
Comments Not Available
References
  • HMP experimental
Associated Disorders
Condition References
Alzheimer's disease
  • Walter A, Korth U, Hilgert M, Hartmann J, Weichel O, Hilgert M, Fassbender K, Schmitt A, Klein J: Glycerophosphocholine is elevated in cerebrospinal fluid of Alzheimer patients. Neurobiol Aging. 2004 Nov-Dec;25(10):1299-303. [PubMed Link Image]
Lung Cancer
  • HMP experimental
Multi-infarct dementia
  • Walter A, Korth U, Hilgert M, Hartmann J, Weichel O, Hilgert M, Fassbender K, Schmitt A, Klein J: Glycerophosphocholine is elevated in cerebrospinal fluid of Alzheimer patients. Neurobiol Aging. 2004 Nov-Dec;25(10):1299-303. [PubMed Link Image]
Spina Bifida
  • Pal K, Sharma U, Gupta DK, Pratap A, Jagannathan NR: Metabolite profile of cerebrospinal fluid in patients with spina bifida: a proton magnetic resonance spectroscopy study. Spine. 2005 Feb 1;30(3):E68-72. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Betaine Metabolism SMP00123 Link Image map00260 Link Image
Methionine Metabolism SMP00033 Link Image map00270 Link Image
Phospholipid Biosynthesis SMP00025 Link Image map00564 Link Image
General References
  1. Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
  2. Kohlmeier M, da Costa KA, Fischer LM, Zeisel SH: Genetic variation of folate-mediated one-carbon transfer pathway predicts susceptibility to choline deficiency in humans. Proc Natl Acad Sci U S A. 2005 Nov 1;102(44):16025-30. Epub 2005 Oct 18. [PubMed Link Image]
  3. Babb SM, Ke Y, Lange N, Kaufman MJ, Renshaw PF, Cohen BM: Oral choline increases choline metabolites in human brain. Psychiatry Res. 2004 Jan 15;130(1):1-9. [PubMed Link Image]
  4. Pal K, Sharma U, Gupta DK, Pratap A, Jagannathan NR: Metabolite profile of cerebrospinal fluid in patients with spina bifida: a proton magnetic resonance spectroscopy study. Spine. 2005 Feb 1;30(3):E68-72. [PubMed Link Image]
  5. Farsad M, Schiavina R, Castellucci P, Nanni C, Corti B, Martorana G, Canini R, Grigioni W, Boschi S, Marengo M, Pettinato C, Salizzoni E, Monetti N, Franchi R, Fanti S: Detection and localization of prostate cancer: correlation of (11)C-choline PET/CT with histopathologic step-section analysis. J Nucl Med. 2005 Oct;46(10):1642-9. [PubMed Link Image]
  6. Yanagawa T, Watanabe H, Inoue T, Ahmed AR, Tomiyoshi K, Shinozaki T, Oriuchi N, Endo K, Takagishi K: Carbon-11 choline positron emission tomography in musculoskeletal tumors: comparison with fluorine-18 fluorodeoxyglucose positron emission tomography. J Comput Assist Tomogr. 2003 Mar-Apr;27(2):175-82. [PubMed Link Image]
  7. Zeisel SH: Nutritional importance of choline for brain development. J Am Coll Nutr. 2004 Dec;23(6 Suppl):621S-626S. [PubMed Link Image]
  8. Walter A, Korth U, Hilgert M, Hartmann J, Weichel O, Hilgert M, Fassbender K, Schmitt A, Klein J: Glycerophosphocholine is elevated in cerebrospinal fluid of Alzheimer patients. Neurobiol Aging. 2004 Nov-Dec;25(10):1299-303. [PubMed Link Image]
  9. Garner SC, Chou SC, Mar MH, Coleman RA, Zeisel SH: Characterization of choline metabolism and secretion by human placental trophoblasts in culture. Biochim Biophys Acta. 1993 Jul 1;1168(3):358-64. [PubMed Link Image]
  10. Rumpel H, Ho GL, Chan LL, Lim WE, Chong VF: Concomitant diminishing magnetization-transfer effect and increasing choline level in radiation-induced temporal-lobe changes. Australas Radiol. 2002 Sep;46(3):340-4. [PubMed Link Image]
  11. Zeisel SH: Choline: critical role during fetal development and dietary requirements in adults. Annu Rev Nutr. 2006;26:229-50. [PubMed Link Image]
  12. Ozarda Ilcol Y, Ozyurt G, Kilicturgay S, Uncu G, Ulus IH: The decline in serum choline concentration in humans during and after surgery is associated with the elevation of cortisol, adrenocorticotropic hormone, prolactin and beta-endorphin concentrations. Neurosci Lett. 2002 May 10;324(1):41-4. [PubMed Link Image]
  13. Van Hove JL, Lazeyras F, Zeisel SH, Bottiglieri T, Hyland K, Charles HC, Gray L, Jaeken J, Kahler SG: One-methyl group metabolism in non-ketotic hyperglycinaemia: mildly elevated cerebrospinal fluid homocysteine levels. J Inherit Metab Dis. 1998 Dec;21(8):799-811. [PubMed Link Image]
  14. Nicholson JK, Foxall PJ, Spraul M, Farrant RD, Lindon JC: 750 MHz 1H and 1H-13C NMR spectroscopy of human blood plasma. Anal Chem. 1995 Mar 1;67(5):793-811. [PubMed Link Image]
  15. Chen CY, Li CW, Kuo YT, Jaw TS, Wu DK, Jao JC, Hsu JS, Liu GC: Early response of hepatocellular carcinoma to transcatheter arterial chemoembolization: choline levels and MR diffusion constants--initial experience. Radiology. 2006 May;239(2):448-56. Epub 2006 Mar 28. [PubMed Link Image]
  16. Buchman AL, Ament ME, Sohel M, Dubin M, Jenden DJ, Roch M, Pownall H, Farley W, Awal M, Ahn C: Choline deficiency causes reversible hepatic abnormalities in patients receiving parenteral nutrition: proof of a human choline requirement: a placebo-controlled trial. JPEN J Parenter Enteral Nutr. 2001 Sep-Oct;25(5):260-8. [PubMed Link Image]
  17. da Costa KA, Badea M, Fischer LM, Zeisel SH: Elevated serum creatine phosphokinase in choline-deficient humans: mechanistic studies in C2C12 mouse myoblasts. Am J Clin Nutr. 2004 Jul;80(1):163-70. [PubMed Link Image]
  18. Katz-Brull R, Margalit R, Degani H: Differential routing of choline in implanted breast cancer and normal organs. Magn Reson Med. 2001 Jul;46(1):31-8. [PubMed Link Image]
  19. Ilcol YO, Donmez O, Yavuz M, Dilek K, Yurtkuran M, Ulus IH: Free choline and phospholipid-bound choline concentrations in serum and dialysate during peritoneal dialysis in children and adults. Clin Biochem. 2002 Jun;35(4):307-13. [PubMed Link Image]
  20. Jacob RA, Jenden DJ, Allman-Farinelli MA, Swendseid ME: Folate nutriture alters choline status of women and men fed low choline diets. J Nutr. 1999 Mar;129(3):712-7. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Choline O-acetyltransferase
  2. Phospholipase D2
  3. Phospholipase D1
  4. Choline dehydrogenase, mitochondrial precursor
  5. Acetylcholinesterase precursor
  6. Cholinesterase precursor
  7. Choline-phosphate cytidylyltransferase B
  8. Choline-phosphate cytidylyltransferase A
  9. Choline/ethanolamine kinase [Includes: Choline kinase beta
  10. Choline kinase alpha
  11. Alcohol dehydrogenase class 3
  12. Alcohol dehydrogenase 1B
  13. Alcohol dehydrogenase 1C
  14. Choline transporter-like protein 1
  15. High-affinity choline transporter 1
  16. Organic cation transporter
  17. Phosphoethanolamine/phosphocholine phosphatase
  18. Choline/ethanolaminephosphotransferase 1
  19. Phospholipase D3
  20. Phospholipase D4
  21. cDNA FLJ75261, highly similar to Human class I alcohol dehydrogenase
  22. Choline kinase beta
  23. Glycerophosphodiester phosphodiesterase 1
  24. Acetylcholinesterase
  25. cDNA FLJ77091, highly similar to Homo sapiens alcohol dehydrogenase 4 (class II), pi polypeptide (ADH4), mRNA
  26. Alcohol dehydrogenase 7 (Class IV), mu or sigma polypeptide
  27. Phospholipase D1 variant (Fragment)
  28. cDNA FLJ35449 fis, clone SMINT2004144, highly similar to ALCOHOL DEHYDROGENASE 6 (EC 1.1.1.1)
  29. Phospholipase D6
  30. Choline transporter-like protein 4
  31. Choline transporter-like protein 2
  32. Choline transporter-like protein 3
Enzyme 1 [top]
Enzyme 1 ID 5254
Enzyme 1 Name Choline O-acetyltransferase
Enzyme 1 Synonyms
  1. CHOACTase
  2. Choline acetylase
  3. ChAT
Enzyme 1 Gene Name CHAT
Enzyme 1 Protein Sequence >Choline O-acetyltransferase
MGLRTAKKRGLGGGGKWKREEGGGTRGRREVRPACFLQSGGRGDPGDVGGPAGNPGCSPH
PRAATRPPPLPAHTPAHTPEWCGAASAEAAEPRRAGPHLCIPAPGLTKTPILEKVPRKMA
AKTPSSEESGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGETLQ
QKLLERQEKTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFPGTDDQLRFAASLIS
GVLSYKALLDSHSIPTDCAKGQLSGQPLCMKQYYGLFSSYRLPGHTQDTLVAQNSSIMPE
PEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNEDERLPPIGLLTSDGRSE
WAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANR
WYDKSLQFVVGRDGTCGVVCEHSPFDGIVLVQCTEHLLKHMTQSSRKLIRADSVSELPAP
RRLRWKCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQKCSPDAFIQVALQ
LAFYRLHRRLVPTYESASIRRFQEGRVDNIRSATPEALAFVRAVTDHKAAVPASEKLLLL
KDAIRAQTAYTVMAITGMAIDNHLLALRELARAMCKELPEMFMDETYLMSNRFVLSTSQV
PTTTEMFCCYGPVVPNGYGACYNPQPETILFCISSFHSCKETSSSKFAKAVEESLIDMRD
LCSLLPPTESKPLATKEKATRPSQGHQP
Enzyme 1 Number of Residues 748
Enzyme 1 Molecular Weight 82569
Enzyme 1 Theoretical pI 8.69
Enzyme 1 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
Component
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses
Enzyme 1 Pathways
Enzyme 1 Reactions
  • acetyl-CoA + choline = CoA + O-acetylcholine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 301096 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P28329 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name CLAT_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2247 bp
ATGGGGCTGAGGACAGCGAAGAAGAGGGGGCTTGGGGGAGGGGGGAAATGGAAGAGAGAG
GAGGGAGGAGGTACAAGAGGAAGGAGAGAAGTGCGGCCAGCTTGCTTTCTCCAGTCGGGT
GGCCGCGGGGACCCGGGCGACGTCGGAGGCCCTGCCGGGAACCCAGGCTGCAGCCCCCAC
CCCCGCGCTGCGACACGCCCCCCACCCCTTCCGGCTCACACCCCCGCCCACACTCCTGAG
TGGTGCGGTGCAGCGTCGGCCGAGGCAGCAGAGCCGAGGAGAGCAGGTCCACACCTCTGC
ATCCCTGCACCAGGACTCACCAAGACGCCCATCCTGGAAAAGGTCCCCCGTAAGATGGCA
GCAAAAACTCCCAGCAGTGAGGAGTCTGGGCTGCCCAAACTGCCCGTGCCCCCGCTGCAG
CAGACCCTGGCCACGTACCTGCAGTGCATGCGACACTTGGTGTCTGAGGAGCAGTTCAGG
AAGAGCCAGGCCATTGTGCAGCAGTTTGGGGCCCCTGGTGGCCTCGGCGAGACCCTGCAG
CAGAAACTCCTGGAGCGGCAGGAGAAGACAGCCAACTGGGTGTCTGAGTACTGGCTGAAT
GACATGTATCTCAACAACCGCCTGGCCCTGCCTGTCAACTCCAGCCCTGCCGTGATCTTT
GCTCGGCAGCACTTCCCTGGCACCGATGACCAGCTGAGGTTTGCAGCCAGCCTCATCTCT
GGTGTACTCAGCTACAAGGCCCTGCTGGACAGCCACTCCATTCCCACTGACTGTGCCAAA
CCGGAGCTGTCAGGGCAGCCCCTTTGCATGAAGCAATACTATGGGCTCTTCTCCTCCTAC
CGGCTCCCCGGCCATACCCAGGACACGCTGGTGGCTCAGAACAGCAGCATCATGCCGGAG
CCTGAGCACGTCATCGTAGCCTGCTGCAATCAGTTCTTTGTCTTGGATGTTGTCATTAAT
TTCCGCCGTCTCAGTGAGGGGGATCTGTTCACTCAGTTGAGAAAGATAGTCAAAATGGCT
TCCAACGAGGACGAGCGTTTGCCTCCAATTGGCCTGCTGACGTCTGACGGGAGGAGCGAG
TGGGCCGAGGCCAGGACGGTCCTCGTGAAAGACTCCACCAACCGGGACTCGCTGGACATG
ATTGAGCGCTGCATCTGCCTTGTATGCCTGGACGGCCCAGGAGGCGTGGAGCTCAGCGAC
ACCCACAGGGCACTCCAGCTCCTTCACGGCGGAGGCTACAGCAAGAACGGGGCCAATCGC
TGGTACGACAAGTCCCTGCAGTTTGTGGTGGGCCGAGACGCGACCTGCGGTGTGGTGTGC
GAACACTCCCCATTCGATGGCATCGTCCTGGTGCAGTGCACTGAGCATCTGCTCAAGCAC
ATGACGCAGAGCAGCAGGAAGCTGATCCGAGCAGACTCCGTCAGCGAGCTCCCCGCCCCC
CGGAGGCTGCGGTGGAAATGCTCCCCGGAAATTCAAGGCCACTTAGCCTCCTCGGCAGAA
AAACTTCAACGAATAGTAAAGAACCTTGACTTCATTGTCTATAAGTTTGACAACTATGGG
AAAACATTCATTAAGAAGCAGAAATGCAGCCCTGATGCCTTCATCCAGGTGGCCCTCCAG
CTGGCCTTCTACAGGCTCCACCGAAGACTGGTGCCCACCTACGAGAGCGCGTCCATCCGC
CGATTCCAGGAGGGACGCGTGGACAACATCAGATCGGCCACTCCAGAGGCACTGGCTTTT
GTGAGAGCCGTGACTGACCACAAGGCTGCTGTGCCAGCTTCTGAGAAGCTTCTGCTCCTG
AAGGATGCCATCCGTGCCCAGACTGCATACACAGTCATGGCCATAACAGGGATGGCCATT
GACAACCACCTGCTGGCACTGCGGGAGCTGGCCCGGGCCATGTGCAAGGAGCTGCCCGAG
ATGTTCATGGATGAAACCTACCTGATGAGCAACCGGTTTGTCCTCTCCACTAGCCAGGTG
CCCACAACCACGGAGATGTTCTGCTGCTATGGTCCTGTGGTCCCAAATGGGTATGGTGCC
TGCTACAACCCCCAGCCAGAGACCATCCTTTTCTGCATCTCTAGCTTTCACAGCTGCAAA
GAGACTTCTTCTAGCAAGTTTGCAAAAGCTGTGGAAGAAAGCCTCATTGACATGAGAGAC
CTCTGCAGTCTGCTGCCGCCTACTGAGAGCAAGCCATTGGCAACAAAGGAAAAAGCCACG
AGGCCCAGCCAGGGACACCAACCTTGA
Enzyme 1 GenBank Gene ID S56138 Link Image
Enzyme 1 GeneCard ID CHAT Link Image
Enzyme 1 GenAtlas ID CHAT Link Image
Enzyme 1 HGNC ID HGNC:1912 Link Image
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Oda Y, Nakanishi I, Deguchi T: A complementary DNA for human choline acetyltransferase induces two forms of enzyme with different molecular weights in cultured cells. Brain Res Mol Brain Res. 1992 Dec;16(3-4):287-94. [PubMed Link Image]
  2. Ohno K, Tsujino A, Brengman JM, Harper CM, Bajzer Z, Udd B, Beyring R, Robb S, Kirkham FJ, Engel AG: Choline acetyltransferase mutations cause myasthenic syndrome associated with episodic apnea in humans. Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):2017-22. [PubMed Link Image]
  3. Lorenzi MV, Trinidad AC, Zhang R, Strauss WL: Two mRNAs are transcribed from the human gene for choline acetyltransferase. DNA Cell Biol. 1992 Oct;11(8):593-603. [PubMed Link Image]
  4. Toussaint JL, Geoffroy V, Schmitt M, Werner A, Garnier JM, Simoni P, Kempf J: Human choline acetyltransferase (CHAT): partial gene sequence and potential control regions. Genomics. 1992 Feb;12(2):412-6. [PubMed Link Image]
  5. Cervini R, Rocchi M, DiDonato S, Finocchiaro G: Isolation and sub-chromosomal localization of a DNA fragment of the human choline acetyltransferase gene. Neurosci Lett. 1991 Nov 11;132(2):191-4. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5309
Enzyme 2 Name Phospholipase D2
Enzyme 2 Synonyms
  1. PLD 2
  2. Choline phosphatase 2
  3. Phosphatidylcholine-hydrolyzing phospholipase D2
  4. PLD1C
  5. hPLD2
Enzyme 2 Gene Name PLD2
Enzyme 2 Protein Sequence >Phospholipase D2
MTATPESLFPTGDELDSSQLQMESDEVDTLKEGEDPADRMHPFLAIYELQSLKVHPLVFA
PGVPVTAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVL
MSLLPLARFAVAYSPARDAGNREMPSLPRAGPEGSTRHAASKQKYLENYLNRLLTMSFYR
NYHAMTEFLEVSQLSFIPDLGRKGLEGMIRKRSGGHRVPGLTCCGRDQVCYRWSKRWLVV
KDSFLLYMCLETGAISFVQLFDPGFEVQVGKRSTEARHGVRIDTSHRSLILKCSSYRQAR
WWAQEITELAQGPGRDFLQLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIF
ITDWWLSPEVYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRAL
MLLHPNIKVMRHPDQVTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDLGDSSE
SAASQPPTPRPDSPATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPW
RDVGVVVHGLPARDLARHFIQRWNFTKTTKAKYKTPTYPYLLPKSTSTANQLPFTLPGGQ
CTTVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDE
IVDRILKAHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHR
LKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSANINDRSLL
GKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILGANTRPDLDLRDPICD
DFFQLWQDMAESNANIYEQIFRCLPSNATRSLRTLREYVAVEPLATVSPPLARSELTQVQ
GHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT
Enzyme 2 Number of Residues 933
Enzyme 2 Molecular Weight 105988
Enzyme 2 Theoretical pI 7.68
Enzyme 2 GO Classification
Function
  • catalytic activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • metabolism
  • physiological process
  • signal transduction
Component
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function May have a role in signal-induced cytoskeletal regulation and/or endocytosis
Enzyme 2 Pathways
Enzyme 2 Reactions
  • A phosphatidylcholine + H2O = choline + a phosphatidate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 2645858 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O14939 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PLD2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID AF033850 Link Image
Enzyme 2 GeneCard ID PLD2 Link Image
Enzyme 2 GenAtlas ID PLD2 Link Image
Enzyme 2 HGNC ID HGNC:9068 Link Image
Enzyme 2 Chromosome Location 17
Enzyme 2 Locus 17p13.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5311
Enzyme 3 Name Phospholipase D1
Enzyme 3 Synonyms
  1. PLD 1
  2. Choline phosphatase 1
  3. Phosphatidylcholine-hydrolyzing phospholipase D1
  4. hPLD1
Enzyme 3 Gene Name PLD1
Enzyme 3 Protein Sequence >Phospholipase D1
MSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEGEEVDYDVSPSDPKIQEVYIPFSA
IYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRKF
KHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEPREMPSLPRSSENMIREEQFLGRR
KQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDLGPKGIEGMIMKRSGGHRIPGLNC
CGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFKIKVGKKETETKYGIRID
NLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKDHRFGSYAAIQENALAKWYVNAKG
YFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLY
KEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGI
DLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAMESMESLRLKDKNEPVQNLPIQKS
IDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSISSIDSTSSYFNHYRSHHNLIHGL
KPHFKLFHPSSESEQGLTRPHADTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQL
DKPFADFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLL
PKSQTTAHELRYQVPGSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIE
NQFFISCADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQ
AIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLL
IADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCF
RVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFI
NKPVLAKEDPIRAEEELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
Enzyme 3 Number of Residues 1074
Enzyme 3 Molecular Weight 124186
Enzyme 3 Theoretical pI 9.07
Enzyme 3 GO Classification
Function
  • catalytic activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • metabolism
  • physiological process
  • signal transduction
Component
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic
Enzyme 3 Pathways
Enzyme 3 Reactions
  • A phosphatidylcholine + H2O = choline + a phosphatidate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1185463 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q13393 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PLD1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >3225 bp
ATGTCACTGAAAAACGAGCCACGGGTAAATACCTCTGCACTGCAGAAAATTGCTGCTGAC
ATGAGTAATATCATAGAAAATCTGGACACGCGGGAACTCCACTTTGAGGGAGAGGAGGTA
GACTACGACGTGTCTCCCAGCGATCCCAAGATACAAGAAGTGTATATCCCTTTCTCTGCT
ATTTATAACACTCAAGGATTTAAGGAGCCTAATATACAGACGTATCTCTCCGGCTGTCCA
ATAAAAGCACAAGTTCTGGAAGTGGAACGCTTCACATCTACAACAAGGGTACCAAGTATT
AATCTTTACACTATTGAATTAACACATGGGGAATTTAAATGGCAAGTTAAGAGGAAATTC
AAGCATTTTCAAGAATTTCACAGAGAGCTGCTCAAGTACAAAGCCTTTATCCGCATCCCC
ATTCCCACTAGAAGACACACGTTTAGGAGGCAAAACGTCAGAGAGGAGCCTCGAGAGATG
CCCAGTTTGCCCCGTTCATCTGAAAACATGATAAGAGAAGAACAATTCCTTGGTAGAAGA
AAACAACTGGAAGATTACTTGACAAAGATACTAAAAATGCCCATGTATAGAAACTATCAT
GCCACAACAGAGTTTCTTGATATAAGCCAGCTGTCTTTCATCCATGATTTGGGACCAAAG
GGCATAGAAGGTATGATAATGAAAAGATCTGGAGGACACAGAATACCAGGCTTGAATTGC
TGTGGTCAGGGAAGAGCCTGCTACAGATGGTCAAAAAGATGGTTAATAGTGAAAGATTCC
TTTTTATTGTATATGAAACCAGACAGCGGTGCCATTGCCTTCGTCCTGCTGGTAGACAAA
GAATTCAAAATTAAGGTGGGGAAGAAGGAGACAGAAACGAAATATGGAATCCGAATTGAT
AATCTTTCAAGGACACTTATTTTAAAATGCAACAGCTATAGACATGCTCGGTGGTGGGGA
GGGGCTATAGAAGAATTCATCCAGAAACATGGCACCAACTTTCTCAAAGATCATCGATTT
GGGTCATATGCTGCTATCCAAGAGAATGCTTTAGCTAAATGGTATGTTAATGCCAAAGGA
TATTTTGAAGATGTGGCAAATGCAATGGAAGAGGCAAATGAAGAGATTTTTATCACAGAC
TGGTGGCTGAGTCCAGAAATCTTCCTGAAACGCCCAGTGGTTGAGGGAAATCGTTGGAGG
TTGGACTGCATTCTTAAACGAAAAGCACAACAAGGAGTGAGGATCTTCATAATGCTCTAC
AAAGAGGTGGAACTCGCTCTTGGCATCAATAGTGAATACACCAAGAGGACTTTGATGCGT
CTACATCCCAACATAAAGGTGATGAGACACCCGGATCATGTGTCATCCACCGTCTATTTG
TGGGCTCACCATGAGAAGCTTGTCATCATTGACCAATCGGTGGCCTTTGTGGGAGGGATT
GACCTGGCCTATGGAAGGTGGGACGACAATGAGCACAGACTCACAGACGTGGGCAGTGTG
AAGCGGGTCACTTCAGGACCGTCTCTGGGTTCCCTCCCACCTGCCGCAATGGAGTCTATG
GAATCCTTAAGACTCAAAGATAAAAATGAGCCTGTTCAAAACCTACCCATCCAGAAGAGT
ATTGATGATGTGGATTCAAAACTGAAAGGAATAGGAAAGCCAAGAAAGTTCTCCAAATTT
AGTCTCTACAAGCAGCTCCACAGGCACCACCTGCACGACGCAGATAGCATCAGCAGCATT
GACAGCACCTCCAGTTATTTTAATCACTATAGAAGTCATCACAATTTAATCCATGGTTTA
AAACCCCACTTCAAACTCTTTCACCCGTCCAGTGAGTCTGAGCAAGGACTCACTAGACCT
CATGCTGATACCGGGTCCATCCGTAGTTTACAGACAGGTGTGGGAGAGCTGCATGGGGAA
ACCAGATTCTGGCATGGAAAGGACTACTGCAATTTCGTCTTCAAAGACTGGGTTCAACTT
GATAAACCTTTTGCTGATTTCATTGACAGGTACTCCACGCCCCGGATGCCCTGGCATGAC
ATTGCCTCTGCAGTCCACGGGAAGGCGGCTCGTGATGTGGCACGTCACTTCATCCAGCGC
TGGAACTTCACAAAAATTATGAAATCAAAATATCGGTCCCTTTCTTATCCTTTTCTGCTT
CCAAAGTCTCAAACAACAGCCCATGAGTTGAGATATCAAGTGCCTGGGTCTGTCCATGCT
AACGTACAGTTGCTCCGCTCTGCTGCTGATTGGTCTGCTGGTATAAAGTACCATGAAGAG
TCCATCCACGCCGCTTACGTCCATGTGATAGAGAACAGCAGGCACTATATCTATATCGAA
AACCAGTTTTTCATAAGCTGTGCTGATGACAAAGTTGTGTTCAACAAGATAGGCGATGCC
ATTGCCCAGAGGATCCTGAAAGCTCACAGGGAAAACCAGAAATACCGGGTATATGTCGTG
ATACCACTTCTGCCAGGGTTCGAAGGAGACATTTCAACCGGCGGAGGAAATGCTCTACAG
GCAATCATGCACTTCAACTACAGAACCATGTGCAGAGGAGAAAATTCCATCCTTGGACAG
TTAAAAGCAGAGCTTGGTAATCAGTGGATAAATTACATATCATTCTGTGGTCTTAGAACA
CATGCAGAGCTCGAAGGAAACCTAGTAACTGAGCTTATCTATGTCCACAGCAAGTTGTTA
ATTGCTGATGATAACACTGTTATTATTGGCTCTGCCAACATAAATGACCGCAGCATGCTG
GGAAAGCGTGACAGTGAAATGGCTGTCATTGTGCAAGATACAGAGACTGTTCCTTCAGTA
ATGGATGGAAAAGAGTACCAAGCTGGCCGGTTTGCCCGAGGACTTCGGCTACAGTGCTTT
AGGGTTGTCCTTGGCTATCTTGATGACCCAAGTGAGGACATTCAGGATCCAGTGAGTGAC
AAATTCTTCAAGGAGGTGTGGGTTTCAACAGCAGCTCGAAATGCTACAATTTATGACAAG
GTTTTCCGGTGCCTTCCCAATGATGAAGTACACAATTTAATTCAGCTGAGAGACTTTATA
AACAAGCCCGTATTAGCTAAGGAAGATCCCATTCGAGCTGAGGAGGAACTGAAGAAGATC
CGTGGATTTTTGGTGCAATTCCCCTTTTATTTCTTGTCTGAAGAAAGCCTACTGCCTTCT
GTTGGGACCAAAGAGGCCATAGTGCCCATGGAGGTTTGGACTTAA
Enzyme 3 GenBank Gene ID U38545 Link Image
Enzyme 3 GeneCard ID PLD1 Link Image
Enzyme 3 GenAtlas ID PLD1 Link Image
Enzyme 3 HGNC ID HGNC:9067 Link Image
Enzyme 3 Chromosome Location 3
Enzyme 3 Locus 3q26
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Hammond SM, Altshuller YM, Sung TC, Rudge SA, Rose K, Engebrecht J, Morris AJ, Frohman MA: Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. J Biol Chem. 1995 Dec 15;270(50):29640-3. [PubMed Link Image]
  2. Hammond SM, Jenco JM, Nakashima S, Cadwallader K, Gu Q, Cook S, Nozawa Y, Prestwich GD, Frohman MA, Morris AJ: Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-alpha. J Biol Chem. 1997 Feb 7;272(6):3860-8. [PubMed Link Image]
  3. 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]
  4. 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]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5433
Enzyme 4 Name Choline dehydrogenase, mitochondrial precursor
Enzyme 4 Synonyms
  1. CHD
  2. CDH
Enzyme 4 Gene Name CHDH
Enzyme 4 Protein Sequence >Choline dehydrogenase, mitochondrial precursor
MWCLLRGLGRPGALARGALGQQQSLGARALASAGSESRDEYSYVVVGAGSAGCVLAGRLT
EDPAERVLLLEAGPKDVRAGSKRLSWKIHMPAALVANLCDDRYNWCYHTEVQRGLDGRVL
YWPRGRVWGGSSSLNAMVYVRGHAEDYERWQRQGARGWDYAHCLPYFRKAQGHELGASRY
RGADGPLRVSRGKTNHPLHCAFLEATQQAGYPLTEDMNGFQQEGFGWMDMTIHEGKRWSA
ACAYLHPALSRTNLKAEAETLVSRVLFEGTRAVGVEYVKNGQSHRAYASKEVILSGGAIN
SPQLLMLSGIGNADDLKKLGIPVVCHLPGVGQNLQDHLEIYIQQACTRPITLHSAQKPLR
KVCIGLEWLWKFTGEGATAHLETGGFIRSQPGVPHPDIQFHFLPSQVIDHGRVPTQQEAY
QVHVGPMRGTSVGWLKLRSANPQDHPVIQPNYLSTETDIEDFRLCVKLTREIFAQEALAP
FRGKELQPGSHIQSDKEIDAFVRAKADSAYHPSCTCKMGQPSDPTAVVDPQTRVLGVENL
RVVDASIMPSMVSGNLNAPTIMIAEKAADIIKGQPALWDKDVPVYKPRTLATQR
Enzyme 4 Number of Residues 594
Enzyme 4 Molecular Weight 65402
Enzyme 4 Theoretical pI 8.47
Enzyme 4 GO Classification
Function
  • FAD binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • purine nucleotide binding
Process
  • alcohol metabolism
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 4 General Function Amino acid transport and metabolism
Enzyme 4 Specific Function Choline + acceptor = betaine aldehyde + reduced acceptor
Enzyme 4 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 4 Reactions
  • choline + acceptor = betaine aldehyde + reduced acceptor
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-15
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 21759795 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q8NE62 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name CHDH_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1785 bp
ATGTGGTGTCTCCTACGAGGCCTGGGCCGGCCTGGAGCCCTGGCACGGGGAGCCCTGGGG
CAGCAGCAATCCCTGGGTGCCCGGGCCCTGGCCAGCGCAGGCTCTGAGAGCCGGGACGAG
TACAGCTATGTGGTGGTGGGCGCGGGCTCGGCGGGCTGCGTGCTGGCTGGGAGGCTCACG
GAGGACCCCGCCGAGCGCGTGCTGCTGCTGGAGGCCGGGCCCAAGGACGTGCGCGCGGGG
AGCAAGCGGCTCTCGTGGAAGATCCACATGCCCGCGGCCCTGGTGGCCAACCTGTGCGAC
GACAGGTACAACTGGTGCTACCACACAGAGGTGCAGCGGGGCCTGGACGGCCGCGTGCTG
TACTGGCCACGCGGCCGCGTCTGGGGTGGCTCCTCATCCCTCAATGCCATGGTCTACGTC
CGTGGGCACGCCGAGGACTACGAGCGCTGGCAGCGCCAGGGCGCCCGCGGCTGGGACTAC
GCGCACTGCCTGCCCTACTTCCGCAAGGCGCAGGGCCACGAGCTGGGCGCCAGCCGGTAC
CGGGGCGCCGATGGCCCGCTGCGGGTGTCCCGGGGCAAGACCAACCACCCGCTGCACTGC
GCATTCCTGGAGGCCACGCAGCAGGCCGGCTACCCGCTCACCGAGGACATGAATGGCTTC
CAGCAGGAGGGCTTCGGCTGGATGGACATGACCATCCATGAAGGCAAACGGTGGAGCGCA
GCCTGTGCCTACCTGCACCCAGCACTGAGCCGCACCAACCTCAAGGCCGAGGCCGAGACG
CTTGTGAGCAGGGTGCTATTTGAGGGCACCCGTGCAGTGGGCGTGGAGTATGTCAAGAAT
GGCCAGAGCCACAGGGCTTATGCCAGCAAGGAGGTGATTCTGAGTGGAGGTGCCATCAAC
TCTCCACAGCTGCTCATGCTCTCTGGCATCGGGAATGCTGATGACCTCAAGAAACTGGGC
ATCCCTGTGGTGTGCCACCTACCTGGGGTTGGCCAGAACCTGCAAGACCACCTGGAGATC
TACATTCAGCAGGCATGCACCCGCCCTATCACCCTCCATTCAGCACAGAAGCCCCTGCGG
AAGGTCTGCATTGGTCTGGAGTGGCTCTGGAAATTCACAGGGGAGGGAGCCACTGCCCAT
CTGGAAACAGGTGGGTTCATCCGCAGCCAGCCTGGGGTCCCCCACCCGGACATCCAGTTC
CATTTCCTGCCATCCCAAGTGATTGACCACGGGCGGGTCCCCACCCAGCAGGAGGCTTAC
CAGGTACATGTGGGGCCCATGCGGGGCACGAGTGTGGGCTGGCTCAAACTGAGAAGTGCC
AATCCCCAAGACCACCCTGTGATCCAGCCCAACTACTTGTCAACAGAAACTGATATTGAG
GATTTCCGTCTGTGTGTGAAGCTCACCAGAGAAATTTTTGCACAGGAAGCCCTGGCTCCG
TTCCGAGGGAAAGAGCTCCAGCCAGGAAGCCACATTCAGTCAGATAAAGAGATAGATGCC
TTTGTGCGGGCAAAAGCCGACAGCGCCTACCACCCCTCGTGCACCTGTAAGATGGGCCAG
CCCTCCGATCCCACTGCCGTGGTGGATCCGCAGACAAGGGTCCTCGGGGTGGAAAACCTC
AGGGTCGTCGATGCCTCCATCATGCCTAGCATGGTCAGCGGCAACCTGAACGCCCCCACA
ATCATGATCGCAGAGAAGGCAGCTGACATTATCAAGGGGCAGCCTGCACTCTGGGACAAA
GATGTCCCTGTCTACAAGCCCAGGACGCTGGCCACCCAGCGCTAA
Enzyme 4 GenBank Gene ID BC034502 Link Image
Enzyme 4 GeneCard ID CHDH Link Image
Enzyme 4 GenAtlas ID CHDH Link Image
Enzyme 4 HGNC ID HGNC:24288 Link Image
Enzyme 4 Chromosome Location 3
Enzyme 4 Locus 3p21.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5772
Enzyme 5 Name Acetylcholinesterase precursor
Enzyme 5 Synonyms
  1. AChE
Enzyme 5 Gene Name ACHE
Enzyme 5 Protein Sequence >Acetylcholinesterase precursor
MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPV
SAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPN
RELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSM
NYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASV
GMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTEL
VACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVG
VVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPE
DPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGY
EIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQ
YVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN
QFDHYSKQDRCSDL
Enzyme 5 Number of Residues 614
Enzyme 5 Molecular Weight 67797
Enzyme 5 Theoretical pI 6.24
Enzyme 5 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cholinesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
Component
Enzyme 5 General Function Lipid transport and metabolism
Enzyme 5 Specific Function Rapidly hydrolyzes choline released into the synapse
Enzyme 5 Pathways
Enzyme 5 Reactions
  • acetylcholine + H2O = choline + acetate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-31
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 177975 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P22303 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name ACES_HUMAN Link Image
Enzyme 5 PDB ID 1F8U Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1845 bp
ATGAGGCCCCCGCAGTGTCTGCTGCACACGCCTTCCCTGGCTTCCCCACTCCTTCTCCTC
CTCCTCTGGCTCCTGGGTGGAGGAGTGGGGGCTGAGGGCCGGGAGGATGCAGAGCTGCTG
GTGACGGTGCGTGGGGGCCGGCTGCGGGGCATTCGCCTGAAGACCCCCGGGGGCCCTGTC
TCTGCTTTCCTGGGCATCCCCTTTGCGGAGCCACCCATGGGACCCCGTCGCTTTCTGCCA
CCGGAGCCCAAGCAGCCTTGGTCAGGGGTGGTAGACGCTACAACCTTCCAGAGTGTCTGC
TACCAATATGTGGACACCCTATACCCAGGTTTTGAGGGCACCGAGATGTGGAACCCCAAC
CGTGAGCTGAGCGAGGACTGCCTGTACCTCAACGTGTGGACACCATACCCCCGGCCTACA
TCCCCCACCCCTGTCCTCGTCTGGATCTATGGGGGTGGCTTCTACAGTGGGGCCTCCTCC
TTGGACGTGTACGATGGCCGCTTCTTGGTACAGGCCGAGAGGACTGTGCTGGTGTCCATG
AACTACCGGGTGGGAGCCTTTGGCTTCCTGGCCCTGCCGGGGAGCCGAGAGGCCCCGGGC
AATGTGGGTCTCCTGGATCAGAGGCTGGCCCTGCAGTGGGTGCAGGAGAACGTGGCAGCC
TTCGGGGGTGACCCGACATCAGTGACGCTGTTTGGGGAGAGCGCGGGAGCCGCCTCGGTG
GGCATGCACCTGCTGTCCCCGCCCAGCCGGGGCCTGTTCCACAGGGCCGTGCTGCAGAGC
GGTGCCCCCAATGGACCCTGGGCCACGGTGGGCATGGGAGAGGCCCGTCGCAGGGCCACG
CAGCTGGCCCACCTTGTGGGCTGTCCTCCAGGCGGCACTGGTGGGAATGACACAGAGCTG
GTAGCCTGCCTTCGGACACGACCAGCGCAGGTCCTGGTGAACCACGAATGGCACGTGCTG
CCTCAAGAAAGCGTCTTCCGGTTCTCCTTCGTGCCTGTGGTAGATGGAGACTTCCTCAGT
GACACCCCAGAGGCCCTCATCAACGCGGGAGACTTCCACGGCCTGCAGGTGCTGGTGGGT
GTGGTGAAGGATGAGGGCTCGTATTTTCTGGTTTACGGGGCCCCAGGCTTCAGCAAAGAC
AACGAGTCTCTCATCAGCCGGGCCGAGTTCCTGGCCGGGGTGCGGGTCGGGGTTCCCCAG
GTAAGTGACCTGGCAGCCGAGGCTGTGGTCCTGCATTACACAGACTGGCTGCATCCCGAG
GACCCGGCACGCCTGAGGGAGGCCCTGAGCGATGTGGTGGGCGACCACAATGTCGTGTGC
CCCGTGGCCCAGCTGGCTGGGCGACTGGCTGCCCAGGGTGCCCGGGTCTACGCCTACGTC
TTTGAACACCGTGCTTCCACGCTCTCCTGGCCCCTGTGGATGGGGGTGCCCCACGGCTAC
GAGATCGAGTTCATCTTTGGGATCCCCCTGGACCCCTCTCGAAACTACACGGCAGAGGAG
AAAATCTTCGCCCAGCGACTGATGCGATACTGGGCCAACTTTGCCCGCACAGGGGATCCC
AATGAGCCCCGAGACCCCAAGGCCCCACAATGGCCCCCGTACACGGCGGGGGCTCAGCAG
TACGTTAGTCTGGACCTGCGGCCGCTGGAGGTGCGGCGGGGGCTGCGCGCCCAGGCCTGC
GCCTTCTGGAACCGCTTCCTCCCCAAATTGCTCAGCGCCACCGACACGCTCGACGAGGCG
GAGCGCCAGTGGAAGGCCGAGTTCCACCGCTGGAGCTCCTACATGGTGCACTGGAAGAAC
CAGTTCGACCACTACAGCAAGCAGGATCGCTGCTCAGACCTGTGA
Enzyme 5 GenBank Gene ID M55040 Link Image
Enzyme 5 GeneCard ID ACHE Link Image
Enzyme 5 GenAtlas ID ACHE Link Image
Enzyme 5 HGNC ID HGNC:108 Link Image
Enzyme 5 Chromosome Location 7
Enzyme 5 Locus 7q22
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Soreq H, Ben-Aziz R, Prody CA, Seidman S, Gnatt A, Neville L, Lieman-Hurwitz J, Lev-Lehman E, Ginzberg D, Lipidot-Lifson Y, et al.: Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure. Proc Natl Acad Sci U S A. 1990 Dec;87(24):9688-92. [PubMed Link Image]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  3. Wilson MD, Riemer C, Martindale DW, Schnupf P, Boright AP, Cheung TL, Hardy DM, Schwartz S, Scherer SW, Tsui LC, Miller W, Koop BF: Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5. Nucleic Acids Res. 2001 Mar 15;29(6):1352-65. [PubMed Link Image]
  4. Karpel R, Ben Aziz-Aloya R, Sternfeld M, Ehrlich G, Ginzberg D, Tarroni P, Clementi F, Zakut H, Soreq H: Expression of three alternative acetylcholinesterase messenger RNAs in human tumor cell lines of different tissue origins. Exp Cell Res. 1994 Feb;210(2):268-77. [PubMed Link Image]
  5. Chhajlani V, Derr D, Earles B, Schmell E, August T: Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase. FEBS Lett. 1989 Apr 24;247(2):279-82. [PubMed Link Image]
  6. Velan B, Grosfeld H, Kronman C, Leitner M, Gozes Y, Lazar A, Flashner Y, Marcus D, Cohen S, Shafferman A: The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580----Ala mutant. J Biol Chem. 1991 Dec 15;266(35):23977-84. [PubMed Link Image]
  7. Shafferman A, Kronman C, Flashner Y, Leitner M, Grosfeld H, Ordentlich A, Gozes Y, Cohen S, Ariel N, Barak D, et al.: Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding. J Biol Chem. 1992 Sep 5;267(25):17640-8. [PubMed Link Image]
  8. Felder CE, Botti SA, Lifson S, Silman I, Sussman JL: External and internal electrostatic potentials of cholinesterase models. J Mol Graph Model. 1997 Oct;15(5):318-27, 335-7. [PubMed Link Image]
  9. Kryger G, Harel M, Giles K, Toker L, Velan B, Lazar A, Kronman C, Barak D, Ariel N, Shafferman A, Silman I, Sussman JL: Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II. Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1385-94. [PubMed Link Image]
  10. Bartels CF, Zelinski T, Lockridge O: Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene accounts for YT blood group polymorphism. Am J Hum Genet. 1993 May;52(5):928-36. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5774
Enzyme 6 Name Cholinesterase precursor
Enzyme 6 Synonyms
  1. Acylcholine acylhydrolase
  2. Choline esterase II
  3. Butyrylcholine esterase
  4. Pseudocholinesterase
Enzyme 6 Gene Name BCHE
Enzyme 6 Protein Sequence >Cholinesterase precursor
MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIP
YAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDC
LYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG
FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPG
SHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEI
LLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVY
GAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDV
VGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER
RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMT
KLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCV
GL
Enzyme 6 Number of Residues 602
Enzyme 6 Molecular Weight 68419
Enzyme 6 Theoretical pI 7.47
Enzyme 6 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cholinesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
Component
Enzyme 6 General Function Lipid transport and metabolism
Enzyme 6 Specific Function An acylcholine + H(2)O = choline + a carboxylate
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • An acylcholine + H2O = choline + a carboxylate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-28
Enzyme 6 Transmembrane Regions
  • 45-67
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 1311630 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P06276 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name CHLE_HUMAN Link Image
Enzyme 6 PDB ID 1P0Q Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1809 bp
ATGCATAGCAAAGTCACAATCATATGCATCAGATTTCTCTTTTGGTTTCTTTTGCTCTGC
ATGCTTATTGGGAAGTCACATACTGAAGATGACATCATAATTGCAACAAAGAATGGAAAA
GTCAGAGGGATGAACTTGACAGTTTTTGGTGGCACGGTAACAGCCTTTCTTGGAATTCCC
TATGCACAGCCACCTCTTGGTAGACTTCGATTCAAAAAGCCACAGTCTCTGACCAAGTGG
TCTGATATTTGGAATGCCACAAAATATGCAAATTCTTGCTGTCAGAACATAGATCAAAGT
TTTCCAGGCTTCCATGGATCAGAGATGTGGAACCCAAACACTGACCTCAGTGAAGACTGT
TTATATCTAAATGTATGGATTCCAGCACCTAAACCAAAAAATGCCACTGTATTGATATGG
ATTTATGGTGGTGGTTTTCAAACTGGAACATCATCTTTACATGTTTATGATGGCAAGTTT
CTGGCTCGGGTTGAAAGAGTTATTGTAGTGTCAATGAACTATAGGGTGGGTGCCCTAGGA
TTCTTAGCTTTGCCAGGAAATCCTGAGGCTCCAGGGAACATGGGTTTATTTGATCAACAG
TTGGCTCTTCAGTGGGTTCAAAAAAATATAGCAGCCTTTGGTGGAAATCCTAAAAGTGTA
ACTCTCTTTGGAGAAAGTGCAGGAGCAGCTTCAGTTAGCCTGCATTTGCTTTCTCCTGGA
AGCCATTCATTGTTCACCAGAGCCATTCTGCAAAGTGGATCCTTTAATGCTCCTTGGGCG
GTAACATCTCTTTATGAAGCTAGGAACAGAACGTTGAACTTAGCTAAATTGACTGGTTGC
TCTAGAGAGAATGAGACTGAAATAATCAAGTGTCTTAGAAATAAAGATCCCCAAGAAATT
CTTCTGAATGAAGCATTTGTTGTCCCCTATGGGACTCCTTTGTCAGTAAACTTTGGTCCG
ACCGTGGATGGTGATTTTCTCACTGACATGCCAGACATATTACTTGAACTTGGACAATTT
AAAAAAACCCAGATTTTGGTGGGTGTTAATAAAGATGAAGGGACAGCTTTTTTAGTCTAT
GGTGCTCCTGGCTTCAGCAAAGATAACAATAGTATCATAACTAGAAAAGAATTTCAGGAA
GGTTTAAAAATATTTTTTCCAGGAGTGAGTGAGTTTGGAAAGGAATCCATCCTTTTTCAT
TACACAGACTGGGTAGATGATCAGAGACCTGAAAACTACCGTGAGGCCTTGGGTGATGTT
GTTGGGGATTATAATTTCATATGCCCTGCCTTGGAGTTCACCAAGAAGTTCTCAGAATGG
GGAAATAATGCCTTTTTCTACTATTTTGAACACCGATCCTCCAAACTTCCGTGGCCAGAA
TGGATGGGAGTGATGCATGGCTATGAAATTGAATTTGTCTTTGGTTTACCTCTGGAAAGA
AGAGATAATTACACAAAAGCCGAGGAAATTTTGAGTAGATCCATAGTGAAACGTTGGGCA
AATTTTGCAAAATATGGGAATCCAAATGAGACTCAGAACAATAGCACAAGCTGGCCTGTC
TTCAAAAGCACTGAACAAAAATATCTAACCTTGAATACAGAGTCAACAAGAATAATGACG
AAACTACGTGCTCAACAATGTCGATTCTGGACATCATTTTTTCCAAAAGTCTTGGAAATG
ACAGGAAATATTGATGAAGCAGAATGGGAGTGGAAAGCAGGATTCCATCGCTGGAACAAT
TACATGATGGACTGGAAAAATCAATTTAACGATTACACTAGCAAGAAAGAAAGTTGTGTG
GGTCTCTAA
Enzyme 6 GenBank Gene ID M32391 Link Image
Enzyme 6 GeneCard ID BCHE Link Image
Enzyme 6 GenAtlas ID BCHE Link Image
Enzyme 6 HGNC ID HGNC:983 Link Image
Enzyme 6 Chromosome Location 3
Enzyme 6 Locus 3q26.1-q26.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Arpagaus M, Kott M, Vatsis KP, Bartels CF, La Du BN, Lockridge O: Structure of the gene for human butyrylcholinesterase. Evidence for a single copy. Biochemistry. 1990 Jan 9;29(1):124-31. [PubMed Link Image]
  2. Prody CA, Zevin-Sonkin D, Gnatt A, Goldberg O, Soreq H: Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3555-9. [PubMed Link Image]
  3. McTiernan C, Adkins S, Chatonnet A, Vaughan TA, Bartels CF, Kott M, Rosenberry TL, La Du BN, Lockridge O: Brain cDNA clone for human cholinesterase. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6682-6. [PubMed Link Image]
  4. Lockridge O, Bartels CF, Vaughan TA, Wong CK, Norton SE, Johnson LL: Complete amino acid sequence of human serum cholinesterase. J Biol Chem. 1987 Jan 15;262(2):549-57. [PubMed Link Image]
  5. Lockridge O, Adkins S, La Du BN: Location of disulfide bonds within the sequence of human serum cholinesterase. J Biol Chem. 1987 Sep 25;262(27):12945-52. [PubMed Link Image]
  6. Lockridge O: Structure of human serum cholinesterase. Bioessays. 1988 Oct;9(4):125-8. [PubMed Link Image]
  7. McGuire MC, Nogueira CP, Bartels CF, Lightstone H, Hajra A, Van der Spek AF, Lockridge O, La Du BN: Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase. Proc Natl Acad Sci U S A. 1989 Feb;86(3):953-7. [PubMed Link Image]
  8. Iida S, Kinoshita M, Fujii H, Moriyama Y, Nakamura Y, Yura N, Moriwaki K: Mutations of human butyrylcholinesterase gene in a family with hypocholinesterasemia. Hum Mutat. 1995;6(4):349-51. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6007
Enzyme 7 Name Choline-phosphate cytidylyltransferase B
Enzyme 7 Synonyms
  1. Phosphorylcholine transferase B
  2. CTP:phosphocholine cytidylyltransferase B
  3. CT B
  4. CCT B
  5. CCT-beta
Enzyme 7 Gene Name PCYT1B
Enzyme 7 Protein Sequence >Choline-phosphate cytidylyltransferase B
MPVVTTDAESETGIPKSLSNEPPSETMEEIEHTCPQPRLTLTAPAPFADETNCQCQAPHE
KLTIAQARLGTPADRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHK
FKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLEKHKIDFVAHDDIPYSSAGSDD
VYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKRY
RFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLELFGPDGAWK
QMFQERSSRMLQALSPKQSPVSSPTRSRSPSRSPSPTFSWLPLKTSPPSSPKAASASISS
MSEGDEDEK
Enzyme 7 Number of Residues 369
Enzyme 7 Molecular Weight 41940
Enzyme 7 Theoretical pI 6.36
Enzyme 7 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 7 General Function Cell wall/membrane/envelope biogenesis
Enzyme 7 Specific Function Controls phosphatidylcholine synthesis
Enzyme 7 Pathways
Enzyme 7 Reactions
  • CTP + choline phosphate = diphosphate + CDP-choline
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 3153239 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9Y5K3 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PCY1B_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >993 bp
ATGCCAGTAGTTACCACTGATGCTGAGTCAGAAACAGGTATCCCAAAATCCCTTTCCAAT
GAGCCTCCCTCAGAAACCATGGAGGAAATAGAGCACACATGCCCACAGCCTCGACTGACC
CTGACTGCACCTGCCCCATTTGCTGATGAAACCAACTGCCAGTGTCAAGCACCCCATGAA
AAACTGACCATTGCTCAGGCCCGCTTAGGAACACCAGCTGACAGGCCTGTCAGAGTATAC
GCCGATGGAATATTTGACCTCTTCCACTCAGGTCATGCAAGAGCCCTTATGCAAGCAAAA
ACACTGTTTCCCAACAGCTACTTGTTGGTAGGAGTTTGCAGTGATGATCTCACCCACAAA
TTCAAAGGTTTCACCGTGATGAATGAAGCCGAGAGATACGAAGCTCTCAGACACTGTCGC
TACGTAGACGAAGTTATCAGAGATGCTCCCTGGACACTCACGCCAGAGTTTCTGGAAAAA
CACAAGATTGACTTTGTGGCTCATGATGACATTCCGTATTCCTCTGCTGGCTCTGATGAT
GTTTACAAGCACATAAAGGAAGCAGGGATGTTCGTTCCAACGCAGAGAACAGAAGGCATC
TCAACATCGGACATCATTACCAGAATTGTTCGTGACTATGATGTTTATGCCCGACGTAAC
CTCCAGAGAGGGTATACAGCCAAGGAACTGAATGTCAGCTTTATAAATGAGAAGAGGTAC
CGTTTCCAGAACCAAGTGGACAAAATGAAGGAAAAAGTCAAGAATGTGGAGGAAAGATCA
AAGGAATTTGTGAACAGAGTGGAAGAAAAGAGCCATGATCTAATTCAAAAGTGGGAAGAG
AAGTCAAGGGAATTCATTGGCAACTTCCTAGAACTGTTTGGACCTGATGGAGCATGGAAG
CAGATGTTCCAGGAGAGGAGCAGCCGGATGCTGCAGGCCTTATCCCCGAAGCAGAGCCCT
CTGAAGAGTTGGGCGAGGTGCAGAGACTTCTAG
Enzyme 7 GenBank Gene ID AF052510 Link Image
Enzyme 7 GeneCard ID PCYT1B Link Image
Enzyme 7 GenAtlas ID PCYT1B Link Image
Enzyme 7 HGNC ID HGNC:8755 Link Image
Enzyme 7 Chromosome Location X
Enzyme 7 Locus Xp22.11
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Lykidis A, Murti KG, Jackowski S: Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase. J Biol Chem. 1998 May 29;273(22):14022-9. [PubMed Link Image]
  2. Lykidis A, Baburina I, Jackowski S: Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant. J Biol Chem. 1999 Sep 17;274(38):26992-7001. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6030
Enzyme 8 Name Choline-phosphate cytidylyltransferase A
Enzyme 8 Synonyms
  1. Phosphorylcholine transferase A
  2. CTP:phosphocholine cytidylyltransferase A
  3. CT A
  4. CCT A
  5. CCT-alpha
Enzyme 8 Gene Name PCYT1A
Enzyme 8 Protein Sequence >Choline-phosphate cytidylyltransferase A
MDAQCSAKVNARKRRKEAPGPNGATEEDGVPSKVQRCAVGLRQPAPFSDEIEVDFSKPYV
RVTMEEASRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHN
FKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDD
VYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKY
HLQERVDKVKEKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALK
HMLKEGKGRMLQAISPKQSPSSSPTRERSPSPSFRWPFSGKTSPPCSPANLSRHKAAAYD
ISEDEED
Enzyme 8 Number of Residues 367
Enzyme 8 Molecular Weight 41732
Enzyme 8 Theoretical pI 6.85
Enzyme 8 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 8 General Function Cell wall/membrane/envelope biogenesis
Enzyme 8 Specific Function Controls phosphatidylcholine synthesis
Enzyme 8 Pathways
Enzyme 8 Reactions
  • CTP + choline phosphate = diphosphate + CDP-choline
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 575486 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P49585 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PCY1A_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1104 bp
ATGGATGCACAGTGTTCAGCCAAGGTCAATGCAAGGAAGAGGAGAAAAGAGGCGCCCGGA
CCCAACGGGGCAACAGAAGAAGATGGGGTTCCTTCCAAAGTGCAGCGCTGTGCAGTGGGC
TTACGGCAACCAGCTCCTTTTTCTGATGAAATTGAAGTTGACTTTAGTAAGCCCTATGTC
AGGGTAACTATGGAAGAAGCCAGCAGAGGAACTCCTTGTGAGCGACCTGTGAGAGTTTAT
GCCGATGGAATATTTGACTTATTTCACTCTGGTCACGCCCGAGCTCTGATGCAAGCGAAG
AACCTTTTCCCTAATACGTACCTCATTGTGGGAGTTTGCAGTGATGAGCTCACACACAAC
TTCAAAGGCTTCACGGTGATGAACGAGAATGAGCGCTATGACGCAGTCCAGCACTGCCGC
TACGTGGATGAGGTGGTGAGGAATGCGCCCTGGACGCTGACACCCGAGTTCCTGGCCGAA
CACCGGATTGATTTTGTAGCCCATGATGATATTCCTTATTCATCTGCTGGCAGTGATGAT
GTTTATAAGCACATCAAGGAGGCAGGCATGTTTGCTCCAACACAGAGGACAGAAGGTATC
TCCACATCAGACATCATCACCCGAATTGTGCGGGATTATGATGTGTATGCGAGGCGGAAC
CTGCAGAGGGGCTACACAGCAAAGGAGCTCAATGTCAGCTTTATCAACGAGAAGAAATAC
CACTTGCAGGAGAGGGTTGACAAAGTAAAGGAGAAAGTGAAAGATGTGGAGGAAAAGTCA
AAAGAATTTGTTCAGAAGGTGGAGGAAAAAAGCATTGACCTCATTCAGAAGTGGGAGGAG
AAGTCCCGAGAATTCATTGGAAGTTTTCTGGAAATGTTTGGTCCGGAAGGAGCACTGAAA
CATATGCTGAAAGAGGGGAAGGGCCGGATGCTGCAGGCCATCAGCCCGAAGCAGAGCCCC
AGCAGCAGCCCTACTCGCGAGCGCTCCCCCTCCCCCTCTTTCCGATGGCCCTTCTCCGGC
AAGACTTCCCCACCTTGCTCCCCAGCAAATCTCTCCAGGCACAAGGCTGCAGCCTATGAT
ATCAGTGAGGATGAAGAAGACTAA
Enzyme 8 GenBank Gene ID L28957 Link Image
Enzyme 8 GeneCard ID PCYT1A Link Image
Enzyme 8 GenAtlas ID PCYT1A Link Image
Enzyme 8 HGNC ID HGNC:8754 Link Image
Enzyme 8 Chromosome Location 3
Enzyme 8 Locus 3q29
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Kalmar GB, Kay RJ, LaChance AC, Cornell RB: Primary structure and expression of a human CTP:phosphocholine cytidylyltransferase. Biochim Biophys Acta. 1994 Oct 18;1219(2):328-34. [PubMed Link Image]
  2. Dunne SJ, Cornell RB, Johnson JE, Glover NR, Tracey AS: Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase. Biochemistry. 1996 Sep 17;35(37):11975-84. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6056
Enzyme 9 Name Choline/ethanolamine kinase [Includes: Choline kinase beta
Enzyme 9 Synonyms
  1. CK
  2. Ethanolamine kinase
  3. EK]
Enzyme 9 Gene Name CHKB
Enzyme 9 Protein Sequence >Choline/ethanolamine kinase [Includes: Choline kinase beta
MAAEATAVAGSGAVGGCLAKDGLQQSKCPDTTPKRRRASSLSRDAERRAYQWCREYLGGA
WRRVQPEELRVYPVSGGLSNLLFRCSLPDHLPSVGEEPREVLLRLYGAILQGVDSLVLES
VMFAILAERSLGPQLYGVFPEGRLEQYIPSRPLKTQELREPVLSAAIATKMAQFHGMEMP
FTKEPHWLFGTMERYLKQIQDLPPTGLPEMNLLEMYSLKDEMGNLRKLLESTPSPVVFCH
NDIQEGNILLLSEPENADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTHEEWPFYKARP
TDYPTQEQQLHFIRHYLAEAKKGETLSQEEQRKLEEDLLVEVSRYALASHFFWGLWSILQ
ASMSTIEFGYLDYAQSRFQFYFQQKGQLTSVHSSS
Enzyme 9 Number of Residues 395
Enzyme 9 Molecular Weight 45272
Enzyme 9 Theoretical pI 5.20
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Cell wall/membrane/envelope biogenesis
Enzyme 9 Specific Function ATP + choline = ADP + O-phosphocholine
Enzyme 9 Pathways
Enzyme 9 Reactions
  • ATP + ethanolamine = ADP + O-phosphoethanolamine
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 5509940 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9Y259 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name CHKB_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 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 9 GenBank Gene ID AB029885 Link Image
Enzyme 9 GeneCard ID CHKB Link Image
Enzyme 9 GenAtlas ID CHKB Link Image
Enzyme 9 HGNC ID HGNC:1938 Link Image
Enzyme 9 Chromosome Location 22
Enzyme 9 Locus 22q13.33
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6057
Enzyme 10 Name Choline kinase alpha
Enzyme 10 Synonyms
  1. CK
  2. CHETK-alpha
Enzyme 10 Gene Name CHKA
Enzyme 10 Protein Sequence >Choline kinase alpha
MKTKFCTGGEAEPSPLGLLLSCGSGSAAPAPGVGQQRDAASDLESKQLGGQQPPLALPPP
PPLPLPLPLPQPPPPQPPADEQPEPRTRRRAYLWCKEFLPGAWRGLREDEFHISVIRGGL
SNMLFQCSLPDTTATLGDEPRKVLLRLYGAILQVRSCNKEGSEQAQKENEFQGAEAMVLE
SVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELGLPDISAEIAEKMATFHGMKM
PFNKEPKWLFGTMEKYLKEVLRIKFTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPV
VFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYP
FFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLW
GQWSIVQAKISSIEFGYMDYAQARFDAYFHQKRKLGV
Enzyme 10 Number of Residues 457
Enzyme 10 Molecular Weight 52202
Enzyme 10 Theoretical pI 6.52
Enzyme 10 GO Classification
Function
  • nutrient reservoir activity
Process
Component
Enzyme 10 General Function Cell wall/membrane/envelope biogenesis
Enzyme 10 Specific Function May have a regulatory role in phosphatidylcholine synthesis
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + choline = ADP + O-phosphocholine
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 219541 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P35790 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name CHKA_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1371 bp
ATGAAAACCAAATTCTGCACCGGGGGCGAGGCGGAGCCCTCGCCGCTCGGGCTGCTGCTG
AGCTGCGGTAGCGGCAGCGCGGCCCCGGCGCCCGGCGTGGGGCAGCAGCGCGACGCCGCC
AGCGACCTCGAGTCCAAGCAGCTGGCGCCAACAGCCGCGCTCGCGCTGCCCCCTCCGCCG
CCGCTGCCGCTGCCGCTGCCGCTGCCCCAGCCCCCGCCGCCGCAGCCGCCCGCAGACGAG
CAGCCGGAGCCCCGGGCGCGGCGCAGGGCCTATCTGTGGTGCAAGGAGTTCCTGCCCGGC
GCCTGGCGGGGCCTCCGCGAGGACGAGTTCCACATCAGTGTCATCAGAGGCGGCCTTAGC
AACATGCTGTTCCAGTGCTCCCTACCTGACACCACAGCCACCCTTGGTGATGAGCCTCGG
AAAGTGCTCCTGCGGCTGTATGGAGCGATTTTGCAGATGAGGTCCTGTAATAAAGAGGGA
TCCGAACAAGCTCAGAAAGAAAATGAATTTCAAGGGGCTGAGGCCATGGTTCTGGAGAGC
GTTATGTTTGCCATTCTCGCAGAGAGGTCACTTGGGCCAAAACTCTATGGCATCTTTCCC
CAAGGCCGACTGGAGCAGTTCATCCCGAGCCGGCGATTAGATACTGAAGAATTAAGTTTG
CCAGATATTTCTGCAGAAATCGCCGAGAAAATGGCTACATTTCATGGTATGAAAATGCCA
TTCAATAAGGAACCAAAATGGCTTTTTGGCACAATGGAAAAGTATCTAAAGGAAGTGCTG
AGAATTAAATTTACTGAGGAATCCAGAATTAAAAAGCTCCACAAATTGCTCAGTTACAAT
CTGCCCTTGGAACTGGAAAACCTGAGATCATTGCTTGAATCTACTCCATCTCCAGTTGTA
TTTTGTCATAATGACTGTCAAGAAGGTAATATCTTGTTGCTGGAAGGCCGAGAGAATTCT
GAAAAACAGAAACTGATGCTCATTGATTTCGAATACAGCAGTTACAATTACAGGGGATTC
GACATTGGAAATCACTTCTGTGAGTGGATGTATGATTATAGCTATGAAAAATACCCTTTT
TTCAGAGCAAACATCCGGAAGTATCCCACCAAGAAACAACAGCTCCATTTTATTTCCAGT
TACTTGCCTGCATTCCAAAATGACTTTGAAAACCTCAGTACTGAAGAAAAATCCATTATA
AAAGAAGAAATGTTGCTTGAAGTTAATAGGTTTGCCCTTGCATCTCATTTCCTCTGGGGA
CTGTGGTCCATTGTACAAGCCAAGATTTCATCTATTGAATTTGGGTACATGGACTACGCC
CAAGCAAGGTTTGATGCCTATTTCCACCAGAAGAGGAAGCTTGGGGTGTGA
Enzyme 10 GenBank Gene ID D10704 Link Image
Enzyme 10 GeneCard ID CHKA Link Image
Enzyme 10 GenAtlas ID CHKA Link Image
Enzyme 10 HGNC ID HGNC:1937 Link Image
Enzyme 10 Chromosome Location 11
Enzyme 10 Locus 11q13.2
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Hosaka K, Tanaka S, Nikawa J, Yamashita S: Cloning of a human choline kinase cDNA by complementation of the yeast cki mutation. FEBS Lett. 1992 Jun 15;304(2-3):229-32. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6060
Enzyme 11 Name Alcohol dehydrogenase class 3
Enzyme 11 Synonyms
  1. Alcohol dehydrogenase class III
  2. Alcohol dehydrogenase class chi chain
  3. S-
  4. hydroxymethylglutathione dehydrogenase
  5. Glutathione- dependent formaldehyde dehydrogenase
  6. FDH
Enzyme 11 Gene Name ADH5
Enzyme 11 Protein Sequence >Alcohol dehydrogenase class 3
MANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGC
FPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGK
GLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLGCGISTGY
GAAVNTAKLEPGSVCAVFGLGGVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATEC
INPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEE
IATRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTHNLSFDEINKAFE
LMHSGKSIRTVVKI
Enzyme 11 Number of Residues 374
Enzyme 11 Molecular Weight 39725
Enzyme 11 Theoretical pI 7.54
Enzyme 11 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 11 General Function Energy production and conversion
Enzyme 11 Specific Function Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione
Enzyme 11 Pathways
Enzyme 11 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + H+
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 178134 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P11766 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name ADHX_HUMAN Link Image
Enzyme 11 PDB ID 1MC5 Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1125 bp
ATGGCGAACGAGGTTATCAAGTGCAAGGCTGCAGTTGCTTGGGAGGCTGGAAAGCCTCTC
TCCATAGAGGAGATAGAGGTGGCACCCCCAAAGGCTCATGAAGTTCGAATCAAGATCATT
GCCACTGCGGTTTGCCACACCGATGCCTATACCCTGAGTGGAGCTGATCCTGAGGGTTGT
TTTCCAGTGATCTTGGGACATGAAGGTGCTGGAATTGTGGAAAGTGTTGGTGAGGGAGTT
ACTAAGCTGAAGGCGGGTGACACTGTCATCCCACTTTACATCCCACAGTGTGGAGAATGC
AAATTTTGTCTAAATCCTAAAACTAACCTTTGCCAGAAGATAAGAGTCACTCAAGGGAAA
GGATTAATGCCAGATGGTACCAGCAGATTTACTTGCAAAGGAAAGACAATTTTGCATTAC
ATGGGAACCAGCACATTTTCTGAATACACAGTTGTGGCTGATATCTCTGTTGCTAAAATA
GATCCTTTAGCACCTTTGGATAAAGTCTGCCTTCTAGGTTGTGGCATTTCAACCGGTTAT
GGTGCTGCTGTGAACACTGCCAAGTTGGAGCCTGGCTCTGTTTGTGCCGTCTTTGGTCTG
GGAGGAGTCGGATTGGCAGTTATCATGGGCTGTAAAGTGGCTGGTGCTTCCCGGATCATT
GGTGTGGACATCAATAAAGATAAATTTGCAAGGGCCAAAGAGTTTGGAGCCACTGAATGT
ATTAACCCTCAGGATTTTAGTAAACCCATCCAGGAAGTGCTCATTGAGATGACCGATGGA
GGAGTGGACTATTCCTTTGAATGTATTGGTAATGTGAAGGTCATGAGAGCAGCACTTGAG
GCATGTCACAAGGGCTGGGGCGTCAGCGTCGTGGTTGGAGTAGCTGCTTCAGGTGAAGAA
ATTGCCACTCGTCCATTCCAGCTGGTAACAGGTCGCACATGGAAAGGCACTGCCTTTGGA
GGATGGAAGAGTGTAGAAAGTGTCCCAAAGTTGGTGTCTGAATATATGTCCAAAAAGATA
AAAGTTGATGAATTTGTGACTCACAATCTGTCTTTTGATGAAATCAACAAAGCCTTTGAA
CTGATGCATTCTGGAAAGAGCATTCGAACTGTTGTAAAGATTTAA
Enzyme 11 GenBank Gene ID M30471 Link Image
Enzyme 11 GeneCard ID ADH5 Link Image
Enzyme 11 GenAtlas ID ADH5 Link Image
Enzyme 11 HGNC ID HGNC:253 Link Image
Enzyme 11 Chromosome Location 4
Enzyme 11 Locus 4q21-q25
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Sharma CP, Fox EA, Holmquist B, Jornvall H, Vallee BL: cDNA sequence of human class III alcohol dehydrogenase. Biochem Biophys Res Commun. 1989 Oct 31;164(2):631-7. [PubMed Link Image]
  2. Giri PR, Krug JF, Kozak C, Moretti T, O'Brien SJ, Seuanez HN, Goldman D: Cloning and comparative mapping of a human class III (chi) alcohol dehydrogenase cDNA. Biochem Biophys Res Commun. 1989 Oct 16;164(1):453-60. [PubMed Link Image]
  3. Hur MW, Edenberg HJ: Cloning and characterization of the ADH5 gene encoding human alcohol dehydrogenase 5, formaldehyde dehydrogenase. Gene. 1992 Nov 16;121(2):305-11. [PubMed Link Image]
  4. Kaiser R, Holmquist B, Hempel J, Vallee BL, Jornvall H: Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes. Biochemistry. 1988 Feb 23;27(4):1132-40. [PubMed Link Image]
  5. Holmquist B, Moulis JM, Engeland K, Vallee BL: Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase. Biochemistry. 1993 May 18;32(19):5139-44. [PubMed Link Image]
  6. Engeland K, Hoog JO, Holmquist B, Estonius M, Jornvall H, Vallee BL: Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation. Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2491-4. [PubMed Link Image]
  7. Yang ZN, Bosron WF, Hurley TD: Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase. J Mol Biol. 1997 Jan 24;265(3):330-43. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6062
Enzyme 12 Name Alcohol dehydrogenase 1B
Enzyme 12 Synonyms
  1. Alcohol dehydrogenase beta subunit
Enzyme 12 Gene Name ADH1B
Enzyme 12 Protein Sequence >Alcohol dehydrogenase 1B
MSTAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIKMVAVGICRTDDHVVSGNLVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLGNP
RGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVNVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQ
NLSINPMLLLTGRTWKGAVYGGFKSKEGIPKLVADFMAKKFSLDALITHVLPFEKINEGF
DLLHSGKSIRTVLTF
Enzyme 12 Number of Residues 375
Enzyme 12 Molecular Weight 39855
Enzyme 12 Theoretical pI 8.38
Enzyme 12 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 12 General Function Energy production and conversion
Enzyme 12 Specific Function An alcohol + NAD(+) = an aldehyde or ketone + NADH
Enzyme 12 Pathways
Enzyme 12 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + H+
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 178098 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P00325 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name ADH1B_HUMAN Link Image
Enzyme 12 PDB ID 1HSZ Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1128 bp
ATGAGCACAGCAGGAAAAGTAATCAAATGCAAAGCAGCTGTGCTATGGGAGGTAAAGAAA
CCCTTTTCCATTGAGGATGTGGAGGTTGCACCTCCTAAGGCTTATGAAGTTCGCATTAAG
ATGGTGGCTGTAGGAATCTGTCGCACAGATGACCACGTGGTTAGTGGCAACCTGGTGACC
CCCCTTCCTGTGATTTTAGGCCATGAGGCAGCCGGCATCGTGGAGAGTGTTGGAGAAGGG
GTGACTACAGTCAAACCAGGTGATAAAGTCATCCCGCTCTTTACTCCTCAGTGTGGAAAA
TGCAGAGTTTGTAAAAACCCGGAGAGCAACTACTGCTTGAAAAATGATCTAGGCAATCCT
CGGGGGACCCTGCAGGATGGCACCAGGAGGTTCACCTGCAGGGGGAAGCCCATTCACCAC
TTCCTTGGCACCAGCACCTTCTCCCAGTACACGGTGGTGGATGAGAATGCAGTGGCCAAA
ATTGATGCAGCCTCGCCCCTGGAGAAAGTCTGCCTCATTGGCTGTGGATTCTCGACTGGT
TATGGGTCTGCAGTTAACGTTGCCAAGGTCACCCCAGGCTCTACCTGTGCTGTGTTTGGC
CTGGGAGGGGTCGGCCTATCTGCTGTTATGGGCTGTAAAGCAGCTGGAGCAGCCAGAATC
ATTGCGGTGGACATCAACAAGGACAAAAAAGCAAAGGCCAAAGAGTTGGGTGCCACTGAA
TGCATCAACCCTCAAGACTACAAGAAACCCATCCAGGAAGTGCTAAAGGAAATGACTGAT
GGAGGTGTGGATTTTTCGTTTGAAGTCATCGGTCGGCTTGACACCATGATGGCTTCCCTG
TTATGTTGTCATGAGGCATGTGGCACAAGCGTCATCGTAGGGGTACCTCCTGCTTCCCAG
AACCTCTCAATAAACCCTATGCTGCTACTGACTGGACGCACCTGGAAGGGGGCTGTTTAT
GGTGGCTTTAAGAGTAAAGAAGGTATCCCAAAACTTGTGGCTGATTTTATGGCTAAGAAG
TTTTCACTGGATGCGTTAATAACCCATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCACTCTGGGAAAAGTATCCGTACCGTCCTGACGTTTTGA
Enzyme 12 GenBank Gene ID M24317 Link Image
Enzyme 12 GeneCard ID ADH1B Link Image
Enzyme 12 GenAtlas ID ADH1B Link Image
Enzyme 12 HGNC ID HGNC:250 Link Image
Enzyme 12 Chromosome Location 4
Enzyme 12 Locus 4q21-q23
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Heden LO, Hoog JO, Larsson K, Lake M, Lagerholm E, Holmgren A, Vallee BL, Jornvall H, von Bahr-Lindstrom H: cDNA clones coding for the beta-subunit of human liver alcohol dehydrogenase have differently sized 3'-non-coding regions. FEBS Lett. 1986 Jan 6;194(2):327-32. [PubMed Link Image]
  2. Duester G, Smith M, Bilanchone V, Hatfield GW: Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit. J Biol Chem. 1986 Feb 15;261(5):2027-33. [PubMed Link Image]
  3. Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. Proc Natl Acad Sci U S A. 1986 Feb;83(3):634-8. [PubMed Link Image]
  4. Carr LG, Xu Y, Ho WH, Edenberg HJ: Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit. Alcohol Clin Exp Res. 1989 Aug;13(4):594-6. [PubMed Link Image]
  5. Matsuo Y, Yokoyama R, Yokoyama S: The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide. Eur J Biochem. 1989 Aug 1;183(2):317-20. [PubMed Link Image]
  6. Hempel J, Buhler R, Kaiser R, Holmquist B, de Zalenski C, von Wartburg JP, Vallee B, Jornvall H: Human liver alcohol dehydrogenase. 1. The primary structure of the beta 1 beta 1 isoenzyme. Eur J Biochem. 1984 Dec 17;145(3):437-45. [PubMed Link Image]
  7. Xu YL, Carr LG, Bosron WF, Li TK, Edenberg HJ: Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification. Genomics. 1988 Apr;2(3):209-14. [PubMed Link Image]
  8. Jornvall H, Hempel J, Vallee BL, Bosron WF, Li TK: Human liver alcohol dehydrogenase: amino acid substitution in the beta 2 beta 2 Oriental isozyme explains functional properties, establishes an active site structure, and parallels mutational exchanges in the yeast enzyme. Proc Natl Acad Sci U S A. 1984 May;81(10):3024-8. [PubMed Link Image]
  9. Burnell JC, Carr LG, Dwulet FE, Edenberg HJ, Li TK, Bosron WF: The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding. Biochem Biophys Res Commun. 1987 Aug 14;146(3):1127-33. [PubMed Link Image]
  10. Hurley TD, Bosron WF, Hamilton JA, Amzel LM: Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8149-53. [PubMed Link Image]
  11. Hurley TD, Bosron WF, Stone CL, Amzel LM: Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences. J Mol Biol. 1994 Jun 10;239(3):415-29. [PubMed Link Image]
  12. Davis GJ, Bosron WF, Stone CL, Owusu-Dekyi K, Hurley TD: X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding. J Biol Chem. 1996 Jul 19;271(29):17057-61. [PubMed Link Image]
  13. Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD: Three-dimensional structures of the three human class I alcohol dehydrogenases. Protein Sci. 2001 Apr;10(4):697-706. [PubMed Link Image]
  14. Borras E, Coutelle C, Rosell A, Fernandez-Muixi F, Broch M, Crosas B, Hjelmqvist L, Lorenzo A, Gutierrez C, Santos M, Szczepanek M, Heilig M, Quattrocchi P, Farres J, Vidal F, Richart C, Mach T, Bogdal J, Jornvall H, Seitz HK, Couzigou P, Pares X: Genetic polymorphism of alcohol dehydrogenase in europeans: the ADH2*2 allele decreases the risk for alcoholism and is associated with ADH3*1. Hepatology. 2000 Apr;31(4):984-9. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6066
Enzyme 13 Name Alcohol dehydrogenase 1C
Enzyme 13 Synonyms
  1. Alcohol dehydrogenase gamma subunit
Enzyme 13 Gene Name ADH1C
Enzyme 13 Protein Sequence >Alcohol dehydrogenase 1C
MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAAGICRSDEHVVSGNLVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRICKNPESNYCLKNDLGNP
RGTLQDGTRRFTCSGKPIHHFVGVSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVKVAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQ
NLSINPMLLLTGRTWKGAIFGGFKSKESVPKLVADFMAKKFSLDALITNILPFEKINEGF
DLLRSGKSIRTVLTF
Enzyme 13 Number of Residues 375
Enzyme 13 Molecular Weight 39868
Enzyme 13 Theoretical pI 8.38
Enzyme 13 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 13 General Function Energy production and conversion
Enzyme 13 Specific Function An alcohol + NAD(+) = an aldehyde or ketone + NADH
Enzyme 13 Pathways
Enzyme 13 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + H+
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 28404 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P00326 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name ADH1G_HUMAN Link Image
Enzyme 13 PDB ID 1HT0 Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1128 bp
ATGAGCACAGCAGGAAAAGTAATCAAATGCAAAGCAGCTGTGCTATGGGAGTTAAAGAAA
CCCTTTTCCATTGAGGAGGTAGAGGTTGCACCTCCTAAGGCTCATGAAGTTCGCATTAAG
ATGGTGGCTGCAGGAATCTGTCGTTCAGATGAGCATGTGGTTAGTGGCAACCTGGTGACC
CCCCTTCCTGTGATTTTAGGCCATGAGGCAGCCGGCATCGTGGAAAGTGTTGGAGAAGGG
GTGACTACAGTCAAACCAGGTGATAAAGTCATCCCGCTCTTTACTCCTCAGTGTGGAAAA
TGCAGAATTTGCAAAAACCCAGAAAGCAACTACTGCTTGAAAAATGATCTAGGCAATCCT
CGGGGGACCCTGCAGGATGGCACCAGGAGGTTCACCTGCAGCGGGAAGCCCATCCACCAC
TTCGTCGGCGTCAGCACCTTCTCCCAGTACACAGTGGTGGATGAGAATGCAGTAGCCAAA
ATTGATGCAGCCTCGCCCCTGGAGAAAGTCTGCCTCATTGGCTGTGGATTTTCGACTGGT
TATGGGTCTGCAGTCAAAGTTGCCAAGGTCACCCCAGGGTCTACCTGTGCTGTGTTTGGC
CTGGGAGGGGTCGGCCTATCTGTTGTTATGGGCTGTAAAGCAGCTGGAGCAGCCAGAATC
ATTGCTGTGGACATCAACAAGGACAAATTTGCAAAGGCTAAAGAGTTGGGTGCCACTGAA
TGCATCAACCCTCAAGACTACAAGAAACCCATTCAGGAAGTGCTAAAGGAAATGACTGAT
GGAGGTGTGGATTTTTCGTTTGAAGTCATCGGTCAGCTTGACACCATGATGGCTTCCCTG
TTATGTTGTCATGAGGCATGTGGCACAAGTGTCATTGTAGGGGTACCTCCTGATTCCCAG
AACCTCTCAATAAACCCTATGCTGCTACTGACTGGACGCACGTGGAAAGGAGCTATTTTT
GGAGGCTTTAAGAGTAAAGAATCTGTCCCCAAACTTGTGGCTGACTTTATGGCTAAGAAG
TTTTCACTGGATGCATTAATAACAAATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCGCTCTGGAAAGAGTATCCGTACCGTCCTGACGTTTTGA
Enzyme 13 GenBank Gene ID X04299 Link Image
Enzyme 13 GeneCard ID ADH1C Link Image
Enzyme 13 GenAtlas ID ADH1C Link Image
Enzyme 13 HGNC ID HGNC:251 Link Image
Enzyme 13 Chromosome Location 4
Enzyme 13 Locus 4q21-q23
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Hoog JO, Heden LO, Larsson K, Jornvall H, von Bahr-Lindstrom H: The gamma 1 and gamma 2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties. Eur J Biochem. 1986 Sep 1;159(2):215-8. [PubMed Link Image]
  2. Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. Proc Natl Acad Sci U S A. 1986 Feb;83(3):634-8. [PubMed Link Image]
  3. Yokoyama S, Matsuo Y, Rajasekharan S, Yokoyama R: Molecular structure of the human alcohol dehydrogenase 3 gene. Jpn J Genet. 1992 Apr;67(2):167-71. [PubMed Link Image]
  4. Buhler R, Hempel J, Kaiser R, de Zalenski C, von Wartburg JP, Jornvall H: Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain. Eur J Biochem. 1984 Dec 17;145(3):447-53. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 7827
Enzyme 14 Name Choline transporter-like protein 1
Enzyme 14 Synonyms
  1. Solute carrier family 44 member 1
  2. CD92 antigen
  3. CDw92
Enzyme 14 Gene Name SLC44A1
Enzyme 14 Protein Sequence >Choline transporter-like protein 1
MGCCSSASSAAQSSKREWKPLEDRSCTDIPWLLLFILFCIGMGFICGFSIATGAAARLVS
GYDSYGNICGQKNTKLEAIPNSGMDHTQRKYVFFLDPCNLDLINRKIKSVALCVAACPRQ
ELKTLSDVQKFAEINGSALCSYNLKPSEYTTSPKSSVLCPKLPVPASAPIPFFHRCAPVN
ISCYAKFAEALITFVSDNSVLHRLISGVMTSKEIILGLCLLSLVLSMILMVIIRYISRVL
VWILTILVILGSLGGTGVLWWLYAKQRRSPKETVTPEQLQIAEDNLRALLIYAISATVFT
VILFLIMLVMRKRVALTIALFHVAGKVFIHLPLLVFQPFWTFFALVLFWVYWIMTLLFLG
TTGSPVQNEQGFVEFKISGPLQYMWWYHVVGLIWISEFILACQQMTVAGAVVTYYFTRDK
RNLPFTPILASVNRLIRYHLGTVAKGSFIITLVKIPRMILMYIHSQLKGKENACARCVLK
SCICCLWCLEKCLNYLNQNAYTATAINSTNFCTSAKDAFVILVENALRVATINTVGDFML
FLGKVLIVCSTGLAGIMLLNYQQDYTVWVLPLIIVCLFAFLVAHCFLSIYEMVVDVLFLC
FAIDTKYNDGSPGREFYMDKVLMEFVENSRKAMKEAGKGGVADSRELKPMASGASSA
Enzyme 14 Number of Residues 657
Enzyme 14 Molecular Weight 73303
Enzyme 14 Theoretical pI 8.69
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Probable choline transporter. May be involved in membrane synthesis and myelin production
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • 31-51 213-233 239-259 289-309 316-336 339-359 381-401 443-463 538-558 567-587
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 19571182 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q8WWI5 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name CTL1_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1965 bp
ATGGGCTGCTGCAGCTCCGCTTCCTCCGCCGCGCAGAGCTCCAAACGAGAATGGAAGCCG
CTGGAGGACCGTAGCTGCACAGACATACCATGGCTGCTGCTCTTCATCCTCTTCTGCATT
GGGATGGGATTTATTTGTGGCTTTTCAATAGCAACAGGTGCAGCAGCAAGACTAGTGTCA
GGATACGACAGCTATGGAAATATCTGTGGGCAGAAAAATACAAAGTTGGAAGCAATACCA
AACAGTGGCATGGACCACACCCAGCGGAAGTATGTATTCTTTTTGGATCCATGCAACCTG
GACTTGATAAACCGGAAGATTAAGTCTGTAGCACTGTGTGTAGCAGCGTGTCCAAGGCAA
GAACTGAAAACTCTGAGTGATGTTCAGAAGTTTGCAGAGATAAATGGTTCAGCCCTATGT
AGCTACAACCTAAAGCCTTCTGAATACACTACATCTCCAAAATCTTCTGTTCTCTGCCCC
AAACTACCAGTTCCAGCGAGTGCACCTATTCCATTCTTCCATCGCTGTGCTCCTGTGAAC
ATTTCCTGCTATGCCAAGTTTGCAGAGGCCCTGATCACCTTTGTCAGTGACAATAGTGTC
TTACACAGGCTGATTAGTGGAGTAATGACCAGCAAAGAAATTATATTGGGACTTTGCTTG
TTATCACTAGTTCTATCCATGATTTTGATGGTGATAATCAGGTATATATCAAGAGTACTT
GTGTGGATCTTAACGATTCTGGTCATACTCGGTTCACTTGGAGGCACAGGTGTACTATGG
TGGCTGTATGCAAAGCAAAGAAGGTCTCCCAAAGAAACTGTTACTCCTGAGCAGCTTCAG
ATAGCTGAAGACAATCTTCGGGCCCTCCTCATTTATGCCATTTCAGCTACAGTGTTCACA
GTGATCTTATTCCTGATAATGTTGGTTATGCGCAAACGTGTTGCTCTTACCATCGCCTTG
TTCCACGTAGCTGGCAAGGTCTTCATTCACTTGCCACTGCTAGTCTTCCAACCCTTCTGG
ACTTTCTTTGCTCTTGTCTTGTTTTGGGTGTACTGGATCATGACACTTCTTTTTCTTGGC
ACTACCGGCAGTCCTGTTCAGAATGAGCAAGGCTTTGTGGAGTTCAAAATTTCTGGGCCT
CTGCAGTACATGTGGTGGTACCATGTGGTGGGCCTGATTTGGATCAGTGAATTTATTCTA
GCATGTCAGCAGATGACAGTGGCAGGAGCTGTGGTAACATACTATTTTACTAGGGATAAA
AGGAATTTGCCATTTACACCTATTTTGGCATCAGTAAATCGCCTTATTCGTTACCACCTA
GGTACGGTGGCAAAAGGATCTTTCATTATCACATTAGTCAAAATTCCGCGAATGATCCTT
ATGTATATTCACAGTCAGCTCAAAGGAAAGGAAAATGCTTGTGCACGATGTGTGCTGAAA
TCTTGCATTTGTTGCCTTTGGTGTCTTGAAAAGTGCCTAAATTATTTAAATCAGAATGCA
TACACAGCCACAGCTATCAACAGCACCAACTTCTGCACCTCAGCAAAGGATGCCTTTGTC
ATTCTGGTGGAGAATGCTTTGCGAGTGGCTACCATCAACACAGTAGGAGATTTTATGTTA
TTCCTTGGCAAGGTGCTGATAGTCTGCAGCACAGGTTTAGCTGGGATTATGCTGCTCAAC
TACCAGCAGGACTACACAGTATGGGTGCTGCCTCTGATCATCGTCTGCCTCTTTGCTTTC
CTAGTCGCTCATTGCTTCCTGTCTATTTATGAAATGGTAGTGGATGTATTATTCTTGTGT
TTTGCCATTGATACAAAATACAATGATGGGAGCCCTGGCAGAGAATTCTATATGGATAAA
GTGCTGATGGAGTTTGTGGAAAACAGTAGGAAAGCAATGAAAGAAGCTGGTAAGGGAGGC
GTCGCTGATTCCAGAGAGCTAAAGCCGATGCTGAAGAAAAGGTGA
Enzyme 14 GenBank Gene ID AJ245620 Link Image
Enzyme 14 GeneCard ID SLC44A1 Link Image
Enzyme 14 GenAtlas ID SLC44A1 Link Image
Enzyme 14 HGNC ID HGNC:18798 Link Image
Enzyme 14 Chromosome Location 9
Enzyme 14 Locus 9q31.2
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. O'Regan S, Traiffort E, Ruat M, Cha N, Compaore D, Meunier FM: An electric lobe suppressor for a yeast choline transport mutation belongs to a new family of transporter-like proteins. Proc Natl Acad Sci U S A. 2000 Feb 15;97(4):1835-40. [PubMed Link Image]
  2. Wille S, Szekeres A, Majdic O, Prager E, Staffler G, Stockl J, Kunthalert D, Prieschl EE, Baumruker T, Burtscher H, Zlabinger GJ, Knapp W, Stockinger H: Characterization of CDw92 as a member of the choline transporter-like protein family regulated specifically on dendritic cells. J Immunol. 2001 Nov 15;167(10):5795-804. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 7869
Enzyme 15 Name High-affinity choline transporter 1
Enzyme 15 Synonyms
  1. Solute carrier family 5 member 7
  2. Hemicholinium-3-sensitive choline transporter
  3. CHT
Enzyme 15 Gene Name SLC5A7
Enzyme 15 Protein Sequence >High-affinity choline transporter 1
MAFHVEGLIAIIVFYLLILLVGIWAAWRTKNSGSAEERSEAIIVGGRDIGLLVGGFTMTA
TWVGGGYINGTAEAVYVPGYGLAWAQAPIGYSLSLILGGLFFAKPMRSKGYVTMLDPFQQ
IYGKRMGGLLFIPALMGEMFWAAAIFSALGATISVIIDVDMHISVIISALIATLYTLVGG
LYSVAYTDVVQLFCIFVGLWISVPFALSHPAVADIGFTAVHAKYQKPWLGTVDSSEVYSW
LDSFLLLMLGGIPWQAYFQRVLSSSSATYAQVLSFLAAFGCLVMAIPAILIGAIGASTDW
NQTAYGLPDPKTTEEADMILPIVLQYLCPVYISFFGLGAVSAAVMSSADSSILSASSMFA
RNIYQLSFRQNASDKEIVWVMRITVFVFGASATAMALLTKTVYGLWYLSSDLVYIVIFPQ
LLCVLFVKGTNTYGAVAGYVSGLFLRITGGEPYLYLQPLIFYPGYYPDDNGIYNQKFPFK
TLAMVTSFLTNICISYLAKYLFESGTLPPKLDVFDAVVARHSEENMDKTILVKNENIKLD
ELALVKPRQSMTLSSTFTNKEAFLDVDSSPEGSGTEDNLQ
Enzyme 15 Number of Residues 580
Enzyme 15 Molecular Weight 63204
Enzyme 15 Theoretical pI 4.77
Enzyme 15 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • membrane
Enzyme 15 General Function Amino acid transport and metabolism
Enzyme 15 Specific Function Imports choline from the extracellular space to the neuron with high affinity. Choline uptake is the rate-limiting step in acetylcholine synthesis. Sodium ion- and chloride ion- dependent
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-25
Enzyme 15 Transmembrane Regions Not Available
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 10998442 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q9GZV3 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name SC5A7_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1743 bp
ATGGCTTTCCATGTGGAAGGACTGATAGCTATCATCGTGTTCTACCTTCTAATTTTGCTG
GTTGGAATATGGGCTGCCTGGAGAACCAAAAACAGTGGCAGCGCAGAAGAGCGCAGCGAA
GCCATCATAGTTGGTGGCCGAGATATTGGTTTATTGGTTGGTGGATTTACCATGACAGCT
ACCTGGGTCGGAGGAGGGTATATCAATGGCACAGCTGAAGCAGTTTATGTACCAGGTTAT
GGCCTAGCTTGGGCTCAGGCACCAATTGGATATTCTCTTAGTCTGATTTTAGGTGGCCTG
TTCTTTGCAAAACCTATGCGTTCAAAGGGGTATGTGACCATGTTAGACCCGTTTCAGCAA
ATCTATGGAAAACGCATGGGCGGACTCCTGTTTATTCCTGCACTGATGGGAGAAATGTTC
TGGGCTGCAGCAATTTTCTCTGCTTTGGGAGCCACCATCAGCGTGATCATCGATGTGGAT
ATGCACATTTCTGTCATCATCTCTGCACTCATTGCCACTCTGTACACACTGGTGGGAGGG
CTCTATTCTGTGGCCTACACTGATGTCGTTCAGCTCTTTTGCATTTTTGTAGGGCTGTGG
ATCAGCGTCCCCTTTGCATTGTCACATCCTGCAGTCGCAGACATCGGGTTCACTGCTGTG
CATGCCAAATACCAAAAGCCGTGGCTGGGAACTGTTGACTCATCTGAAGTCTACTCTTGG
CTTGATAGTTTTCTGTTGTTGATGCTGGGTGGAATCCCATGGCAAGCATACTTTCAGAGG
GTTCTCTCTTCTTCCTCAGCCACCTATGCTCAAGTGCTGTCCTTCCTGGCAGCTTTCGGG
TGCCTGGTGATGGCCATCCCAGCCATACTCATTGGGGCCATTGGAGCATCAACAGACTGG
AACCAGACTGCATATGGGCTTCCAGATCCCAAGACTACAGAAGAGGCAGACATGATTTTA
CCAATTGTTCTGCAGTATCTCTGCCCTGTGTATATTTCTTTCTTTGGTCTTGGTGCAGTT
TCTGCTGCTGTTATGTCATCAGCAGATTCTTCCATCTTGTCAGCAAGTTCCATGTTTGCA
CGGAACATCTACCAGCTTTCCTTCAGACAAAATGCTTCGGACAAAGAAATCGTTTGGGTT
ATGCGAATCACAGTGTTTGTGTTTGGAGCATCTGCAACAGCCATGGCCTTGCTGACGAAA
ACTGTGTATGGGCTCTGGTACCTCAGTTCTGACCTTGTTTACATCGTTATCTTCCCCCAG
CTGCTTTGTGTACTCTTTGTTAAGGGAACCAACACCTATGGGGCCGTGGCAGGTTATGTT
TCTGGCCTCTTCCTGAGAATAACTGGAGGGGAGCCATATCTGTATCTTCAGCCCTTGATC
TTCTACCCTGGCTATTACCCTGATGATAATGGTATATATAATCAGAAATTTCCATTTAAA
ACACTTGCCATGGTTACATCATTCTTAACCAACATTTGCATCTCCTATCTAGCCAAGTAT
CTATTTGAAAGTGGAACCTTGCCACCTAAATTAGATGTATTTGATGCTGTTGTTGCAAGA
CACAGTGAAGAAAACATGGATAAGACAATTCTTGTCAAAAATGAAAATATTAAATTAGAT
GAACTTGCACTTGTGAAGCCACGACAGAGCATGACCCTCAGCTCAACTTTCACCAATAAA
GAGGCCTTCCTTGATGTTGATTCCAGTCCAGAAGGGTCTGGGACTGAAGATAATTTACAG
TGA
Enzyme 15 GenBank Gene ID AF276871 Link Image
Enzyme 15 GeneCard ID SLC5A7 Link Image
Enzyme 15 GenAtlas ID SLC5A7 Link Image
Enzyme 15 HGNC ID HGNC:14025 Link Image
Enzyme 15 Chromosome Location 2
Enzyme 15 Locus 2q12
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Apparsundaram S, Ferguson SM, George AL Jr, Blakely RD: Molecular cloning of a human, hemicholinium-3-sensitive choline transporter. Biochem Biophys Res Commun. 2000 Oct 5;276(3):862-7. [PubMed Link Image]
  2. Okuda T, Haga T: Functional characterization of the human high-affinity choline transporter. FEBS Lett. 2000 Nov 3;484(2):92-7. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 8073
Enzyme 16 Name Organic cation transporter
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name SLC22A1
Enzyme 16 Protein Sequence >Organic cation transporter
MPTVDDILEQVGESGWFQKQAFLILCLLSAAFAPICVGIVFLGFTPDHHCQSPGVAELSQ
RCGWSPAEELNYTVPGLGPAGEAFLGQCRRYEVDWNQSALSCVDPLASLATNRSHLPLGP
CQDGWVYDTPGSSIVTEFNLVCADSWKLDLFQSCLNAGFFFGSLGVGYFADRFGRKLCLL
GTVLVNAVSGVLMAFSPNYMSMLLFRLLQGLVSKGNWMAGYTLITEFVGSGSRRTVAIMY
QMAFTVGLVALTGLAYALPHWRWLQLAVSLPTFLFLLYYWCVPESPRWLLSQKRNTEAIK
IMDHIAQKNGKLPPADLKMLSLEEDVTEKLSPSFADLFRTPRLRKRTFILMYLWFTDSVL
YQGLILHMGATSGNLYLDFLYSALVEIPGAFIALITIDRVGRIYPMAMSNLLAGAACLVM
IFISPDLHWLNIIIMCVGRMGITIAIQMICLVNAELYPTFVRNLGVMVCSSLCDIGGIIT
PFIVFRLREVWQALPLILFAVLGLLAAGVTLLLPETKGVALPETMKDAENLGRKAKPKEN
TIYLKVQTSEPSGT
Enzyme 16 Number of Residues 554
Enzyme 16 Molecular Weight 61189
Enzyme 16 Theoretical pI 6.81
Enzyme 16 GO Classification
Function
  • ion transporter activity
  • transporter activity
Process
  • cellular physiological process
  • ion transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 16 General Function Carbohydrate transport and metabolism
Enzyme 16 Specific Function Not Available
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-38
Enzyme 16 Transmembrane Regions
  • 148-170
  • 177-197
  • 207-229
  • 236-258
  • 263-282
  • 348-370
  • 375-397
  • 402-424
  • 429-451
  • 463-485
  • 490-512
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 2511670 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID O15245 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name O15245_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1665 bp
ATGCCCACCGTGGATGACATTCTGGAGCAGGTTGGGGAGTCTGGCTGGTTCCAGAAGCAA
GCCTTCCTCATCTTATGCCTGCTGTCGGCTGCCTTTGCGCCCATCTGTGTGGGCATCGTC
TTCCTGGGTTTCACACCTGACCACCACTGCCAGAGCCCTGGGGTGGCTGAGCTGAGCCAG
CGCTGTGGCTGGAGCCCTGCGGAGGAGCTGAACTATACAGTGCCAGGCCTGGGGCCCGCG
GGCGAGGCCTTCCTTGGCCAGTGCAGGCGCTATGAAGTGGACTGGAACCAGAGCGCCCTC
AGCTGTGTAGACCCCCTGGCTAGCCTGGCCACCAACAGGAGCCACCTGCCGCTGGGTCCC
TGCCAGGATGGCTGGGTGTATGACACGCCCGGCTCTTCCATCGTCACTGAGTTCAACCTG
GTGTGTGCTGACTCCTGGAAGCTGGACCTCTTTCAGTCCTGTTTGAATGCGGGCTTCTTC
TTTGGCTCTCTCGGTGTTGGCTACTTTGCAGACAGGTTTGGCCGTAAGCTGTGTCTCCTG
GGAACTGTGCTGGTCAACGCGGTGTCGGGCGTGCTCATGGCCTTCTCGCCCAACTACATG
TCCATGCTGCTCTTCCGCCTGCTGCAGGGCCTGGTCAGCAAGGGCAACTGGATGGCTGGC
TACACCCTAATCACAGAATTTGTTGGCTCGGGCTCCAGAAGAACGGTGGCGATCATGTAC
CAGATGGCCTTCACGGTGGGGCTGGTGGCGCTTACCGGGCTGGCCTACGCCCTGCCTCAC
TGGCGCTGGCTGCAGCTGGCAGTCTCCCTGCCCACCTTCCTCTTCCTGCTCTACTACTGG
TGTGTGCCGGAGTCCCCTCGGTGGCTGTTATCACAAAAAAGAAACACTGAAGCAATAAAG
ATAATGGACCACATCGCTCAAAAGAATGGGAAGTTGCCTCCTGCTGATTTAAAGATGCTT
TCCCTCGAAGAGGATGTCACCGAAAAGCTGAGCCCTTCATTTGCAGACCTGTTCCGCACG
CCGCGCCTGAGGAAGCGCACCTTCATCCTGATGTACCTGTGGTTCACGGACTCTGTGCTC
TATCAGGGGCTCATCCTGCACATGGGCGCCACCAGCGGGAACCTCTACCTGGATTTCCTT
TACTCCGCTCTGGTCGAAATCCCGGGGGCCTTCATAGCCCTCATCACCATTGACCGCGTG
GGCCGCATCTACCCCATGGCCATGTCAAATTTGTTGGCGGGGGCAGCCTGCCTCGTCATG
ATTTTTATCTCACCTGACCTGCACTGGTTAAACATCATAATCATGTGTGTTGGCCGAATG
GGAATCACCATTGCAATACAAATGATCTGCCTGGTGAATGCTGAGCTGTACCCCACATTC
GTCAGGAACCTCGGAGTGATGGTGTGTTCCTCCCTGTGTGACATAGGTGGGATAATCACC
CCCTTCATAGTCTTCAGGCTGAGGGAGGTCTGGCAAGCCTTGCCCCTCATTTTGTTTGCG
GTGTTGGGCCTGCTTGCCGCGGGAGTGACGCTACTTCTTCCAGAGACCAAGGGGGTCGCT
TTGCCAGAGACCATGAAGGACGCCGAGAACCTTGGGAGAAAAGCAAAGCCCAAAGAAAAC
ACGATTTACCTTAAGGTCCAAACCTCAGAACCCTCGGGCACCTGA
Enzyme 16 GenBank Gene ID X98332 Link Image
Enzyme 16 GeneCard ID SLC22A1 Link Image
Enzyme 16 GenAtlas ID SLC22A1 Link Image
Enzyme 16 HGNC ID HGNC:10963 Link Image
Enzyme 16 Chromosome Location 6
Enzyme 16 Locus 6q26
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Gorboulev V, Ulzheimer JC, Akhoundova A, Ulzheimer-Teuber I, Karbach U, Quester S, Baumann C, Lang F, Busch AE, Koepsell H: Cloning and characterization of two human polyspecific organic cation transporters. DNA Cell Biol. 1997 Jul;16(7):871-81. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 8634
Enzyme 17 Name Phosphoethanolamine/phosphocholine phosphatase
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name PHOSPHO1
Enzyme 17 Protein Sequence >Phosphoethanolamine/phosphocholine phosphatase
MSGCFPVSGLRCLSRDGRMAAQGAPRFLLTFDFDETIVDENSDDSIVRAAPGQRLPESLR
ATYREGFYNEYMQRVFKYLGEQGVRPRDLSAIYEAIPLSPGMSDLLQFVAKQGACFEVIL
ISDANTFGVESSLRAAGHHSLFRRILSNPSGPDARGLLALRPFHTHSCARCPANMCKHKV
LSDYLRERAHDGVHFERLFYVGDGANDFCPMGLLAGGDVAFPRRGYPMHRLIQEAQKAEP
SSFRASVVPWETAADVRLHLQQVLKSC
Enzyme 17 Number of Residues 267
Enzyme 17 Molecular Weight 29713
Enzyme 17 Theoretical pI 7.78
Enzyme 17 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 17 General Function Not Available
Enzyme 17 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 17 Pathways
Enzyme 17 Reactions
  • (1) O-phosphoethanolamine + H2O = ethanolamine + phosphate
  • (2) phosphocholine + H2O = choline + phosphate
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals Not Available
Enzyme 17 Transmembrane Regions Not Available
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 20196839 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q8TCT1 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name PHOP1_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >804 bp
ATGAGTGGCTGTTTTCCAGTTTCTGGCCTCCGCTGCCTATCTAGGGACGGCAGGATGGCC
GCGCAGGGCGCGCCGCGCTTCCTCCTGACCTTCGACTTCGACGAGACTATCGTGGACGAA
AACAGCGACGATTCGATCGTGCGCGCCGCGCCGGGCCAGCGGCTCCCGGAGAGCCTGCGA
GCCACCTACCGCGAGGGCTTCTACAACGAGTACATGCAGCGCGTCTTCAAGTACCTGGGC
GAGCAGGGCGTGCGGCCGCGGGACCTGAGCGCCATCTACGAAGCCATCCCTTTGTCGCCA
GGCATGAGCGACCTGCTGCAGTTTGTGGCAAAACAGGGCGCCTGCTTCGAGGTGATTCTC
ATCTCCGATGCCAACACCTTTGGCGTGGAGAGCTCGCTGCGCGCCGCCGGCCACCACAGC
CTGTTCCGCCGCATCCTCAGCAACCCGTCGGGGCCGGATGCGCGGGGACTGCTGGCTCTG
CGGCCGTTCCACACACACAGCTGCGCGCGCTGCCCCGCCAACATGTGCAAGCACAAGGTG
CTCAGCGACTACCTGCGCGAGCGGGCCCACGACGGCGTGCACTTCGAGCGCCTCTTCTAC
GTGGGCGACGGCGCCAACGACTTCTGCCCCATGGGGCTGCTGGCGGGCGGCGACGTGGCC
TTCCCGCGCCGCGGCTACCCCATGCACCGCCTCATTCAGGAGGCCCAGAAGGCCGAGCCC
AGCTCGTTCCGCGCCAGCGTGGTGCCCTGGGAAACGGCTGCAGATGTGCGCCTCCACCTG
CAACAGGTGCTGAAGTCGTGCTGA
Enzyme 17 GenBank Gene ID AJ457189 Link Image
Enzyme 17 GeneCard ID PHOSPHO1 Link Image
Enzyme 17 GenAtlas ID PHOSPHO1 Link Image
Enzyme 17 HGNC ID HGNC:16815 Link Image
Enzyme 17 Chromosome Location 17
Enzyme 17 Locus 17q21.32
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 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]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 8937
Enzyme 18 Name Choline/ethanolaminephosphotransferase 1
Enzyme 18 Synonyms
  1. hCEPT1
Enzyme 18 Gene Name CEPT1
Enzyme 18 Protein Sequence >Choline/ethanolaminephosphotransferase 1
MSGHRSTRKRCGDSHPESPVGFGHMSTTGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAG
RSLLEPLMQGYWEWLVRRVPSWIAPNLITIIGLSINICTTILLVFYCPTATEQAPLWAYI
ACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPD
WMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSMIP
VLNIQMKIFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLA
AMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLD
QYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLHIHVFRIKVSTAHSNHH
Enzyme 18 Number of Residues 416
Enzyme 18 Molecular Weight 46554
Enzyme 18 Theoretical pI Not Available
Enzyme 18 GO Classification
Function
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity
Enzyme 18 Pathways
Enzyme 18 Reactions
  • CDPcholine + diacylglycerol (homo sapiens) --> CMP + H+ + Phosphatidylcholine (homo sapiens)
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • 87-107 115-135 186-206 209-229 239-259 283-303 317-337 365-385
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 4584877 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9Y6K0 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name CEPT1_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence Not Available
Enzyme 18 GenBank Gene ID AF068302 Link Image
Enzyme 18 GeneCard ID Not Available
Enzyme 18 GenAtlas ID CEPT1 Link Image
Enzyme 18 HGNC ID HGNC:24289 Link Image
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Henneberry AL, McMaster CR: Cloning and expression of a human choline/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidylethanolamine. Biochem J. 1999 Apr 15;339 ( Pt 2):291-8. [PubMed Link Image]
  2. Henneberry AL, Wistow G, McMaster CR: Cloning, genomic organization, and characterization of a human cholinephosphotransferase. J Biol Chem. 2000 Sep 22;275(38):29808-15. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 12911
Enzyme 19 Name Phospholipase D3
Enzyme 19 Synonyms
  1. PLD 3
  2. Choline phosphatase 3
  3. Phosphatidylcholine-hydrolyzing phospholipase D3
  4. HindIII K4L homolog
  5. Hu-K4
Enzyme 19 Gene Name PLD3
Enzyme 19 Protein Sequence >Phospholipase D3
MKPKLMYQELKVPAEEPANELPMNEIEAWKAAEKKARWVLLVLILAVVGFGALMTQLFLW
EYGDLHLFGPNQRPAPCYDPCEAVLVESIPEGLDFPNASTGNPSTSQAWLGLLAGAHSSL
DIASFYWTLTNNDTHTQEPSAQQGEEVLRQLQTLAPKGVNVRIAVSKPSGPQPQADLQAL
LQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCL
ARDLTKIFEAYWFLGQAGSSIPSTWPRFYDTRYNQETPMEICLNGTPALAYLASAPPPLC
PSGRTPDLKALLNVVDNARSFIYVAVMNYLPTLEFSHPHRFWPAIDDGLRRATYERGVKV
RLLISCWGHSEPSMRAFLLSLAALRDNHTHSDIQVKLFVVPADEAQARIPYARVNHNKYM
VTERATYIGTSNWSGNYFTETAGTSLLVTQNGRGGLRSQLEAIFLRDWDSPYSHDLDTSA
DSVGNACRLL
Enzyme 19 Number of Residues 490
Enzyme 19 Molecular Weight 54706
Enzyme 19 Theoretical pI 6.45
Enzyme 19 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function A phosphatidylcholine + H(2)O = choline + a phosphatidate
Enzyme 19 Pathways
Enzyme 19 Reactions
  • a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310] ALL_REAC R01310
  • (other) R02051 R07385
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • 39-59
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 1575347 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q8IV08 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name PLD3_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID U60644 Link Image
Enzyme 19 GeneCard ID Q8IV08 Link Image
Enzyme 19 GenAtlas ID PLD3 Link Image
Enzyme 19 HGNC ID HGNC:17158 Link Image
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References Not Available
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 12912
Enzyme 20 Name Phospholipase D4
Enzyme 20 Synonyms
  1. PLD 4
  2. Choline phosphatase 4
  3. Phosphatidylcholine-hydrolyzing phospholipase D4
Enzyme 20 Gene Name PLD4
Enzyme 20 Protein Sequence >Phospholipase D4
MLKPLWKAAVAPTWPCSMPPRRPWDREAGTLQVLGALAVLWLGSVALICLLWQVPRPPTW
GQVQPKDVPRSWEHGSSPAWEPLEAEARQQRDSCQLVLVESIPQDLPSAAGSPSAQPLGQ
AWLQLLDTAQESVHVASYYWSLTGPDIGVNDSSSQLGEALLQKLQQLLGRNISLAVATSS
PTLARTSTDLQVLAARGAHVRQVPMGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQV
KELGAVIYNCSHLAQDLEKTFQTYWVLGVPKAVLPKTWPQNFSSHFNRFQPFHGLFDGVP
TTAYFSASPPALCPQGRTRDLEALLAVMGSAQEFIYASVMEYFPTTRFSHPPRYWPVLDN
ALRAAAFGKGVRVRLLVGCGLNTDPTMFPYLRSLQALSNPAANVSVDVKVFIVPVGNHSN
IPFSRVNHSKFMVTEKAAYIGTSNWSEDYFSSTAGVGLVVTQSPGAQPAGATVQEQLRQL
FERDWSSRYAVGLDGQAPGQDCVWQG
Enzyme 20 Number of Residues 506
Enzyme 20 Molecular Weight 55627
Enzyme 20 Theoretical pI 8.46
Enzyme 20 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function A phosphatidylcholine + H(2)O = choline + a phosphatidate
Enzyme 20 Pathways
Enzyme 20 Reactions
  • a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310] ALL_REAC R01310
  • (other) R02051 R07385
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 31-51
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 37182804 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q96BZ4 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name PLD4_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence Not Available
Enzyme 20 GenBank Gene ID AY358843 Link Image
Enzyme 20 GeneCard ID Q96BZ4 Link Image
Enzyme 20 GenAtlas ID PLD4 Link Image
Enzyme 20 HGNC ID HGNC:23792 Link Image
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 13004
Enzyme 21 Name cDNA FLJ75261, highly similar to Human class I alcohol dehydrogenase
Enzyme 21 Synonyms
  1. ADH1alpha subunit mRNA
  2. Alcohol dehydrogenase 1A
  3. Class I, alpha polypeptide, isoform CRA_b
Enzyme 21 Gene Name ADH1A
Enzyme 21 Protein Sequence >cDNA FLJ75261, highly similar to Human class I alcohol dehydrogenase
MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAVGICGTDDHVVSGTMVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNP
QGTLQDGTSRFTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQ
NLSMNPMLLLTGRTWKGAILGGFKSKECVPKLVADFMAKKFSLDALITHVLPFEKINEGF
DLLHSGKSIRTILMF
Enzyme 21 Number of Residues 375
Enzyme 21 Molecular Weight 39859
Enzyme 21 Theoretical pI 8.02
Enzyme 21 GO Classification Not Available
Enzyme 21 General Function Energy production and conversion
Enzyme 21 Specific Function Not Available
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function Not Available
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 158254548 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID A8K3E3 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name A8K3E3_HUMAN Link Image
Enzyme 21 PDB ID 1HSO Link Image
Enzyme 21 PDB File Show
Enzyme 21 3D Structure
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence Not Available
Enzyme 21 GenBank Gene ID AK290558 Link Image
Enzyme 21 GeneCard ID A8K3E3 Link Image
Enzyme 21 GenAtlas ID Not Available
Enzyme 21 HGNC ID Not Available
Enzyme 21 Chromosome Location Not Available
Enzyme 21 Locus Not Available
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References Not Available
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 13049
Enzyme 22 Name Choline kinase beta
Enzyme 22 Synonyms
  1. HCG16873, isoform CRA_a
Enzyme 22 Gene Name CHKB
Enzyme 22 Protein Sequence >Choline kinase beta
MAAEATAVAGSGAVGGCLAKDGLQQSKCPDTTPKRRRASSLSRDAERRAYQWCREYLGGA
WRRVQPEELRVYPVSGGLSNLLFRCSLPDHLPSVGEEPREVLLRLYGAILQGVDSLVLES
VMFAILAERSLGPQLYGVFPEGRLEQYIPSRPLKTQELREPVLSAAIATKMAQFHGMEMP
FTKEPHWLFGTMERYLKQIQDLPPTGLPEMNLLEMYSLKDEMGNLRKLLESTPSPVVFCH
NDIQEGNILLLSEPENADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTHEEWPFYKARP
TDYPTQEQQLHFIRHYLAEAKKGETLSQEEQRKLEEDLLVEVSRYALASHFFWGLWSILQ
ASMSTIEFGYLDYAQSRFQFYFQQKGQLTSVHSSS
Enzyme 22 Number of Residues 395
Enzyme 22 Molecular Weight 45272
Enzyme 22 Theoretical pI 5.20
Enzyme 22 GO Classification Not Available
Enzyme 22 General Function Cell wall/membrane/envelope biogenesis
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 133777770 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID A0PJM6 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name A0PJM6_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence Not Available
Enzyme 22 GenBank Gene ID BC101488 Link Image
Enzyme 22 GeneCard ID A0PJM6 Link Image
Enzyme 22 GenAtlas ID Not Available
Enzyme 22 HGNC ID Not Available
Enzyme 22 Chromosome Location Not Available
Enzyme 22 Locus Not Available
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 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 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 13050
Enzyme 23 Name Glycerophosphodiester phosphodiesterase 1
Enzyme 23 Synonyms
  1. Membrane interacting protein of RGS16
  2. RGS16-interacting membrane protein
Enzyme 23 Gene Name GDE1
Enzyme 23 Protein Sequence >Glycerophosphodiester phosphodiesterase 1
MWLWEDQGGLLGPFSFLLLVLLLVTRSPVNACLLTGSLFVLLRVFSFEPVPSCRALQVLK
PRDRISAIAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGIPVLMHDNTVDRTT
DGTGRLCDLTFEQIRKLNPAANHRLRNDFPDEKIPTLREAVAECLNHNLTIFFDVKGHAH
KATEALKKMYMEFPQLYNNSVVCSFLPEVIYKMRQTDRDVITALTHRPWSLSHTGDGKPR
YDTFWKHFIFVMMDILLDWSMHNILWYLCGISAFLMQKDFVSPAYLKKWSAKGIQVVGWT
VNTFDEKSYYESHLGSSYITDSMVEDCEPHF
Enzyme 23 Number of Residues 331
Enzyme 23 Molecular Weight 37719
Enzyme 23 Theoretical pI 6.70
Enzyme 23 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 metabolism
  • cellular metabolism
  • glycerol metabolism
  • metabolism
  • physiological process
  • polyol metabolism
Component
Enzyme 23 General Function Energy production and conversion
Enzyme 23 Specific Function Has glycerophosphoinositol phosphodiesterase activity. Has little or no activity towards glycerophosphocholine. GDE1 activity can be modulated by G-protein signaling pathways
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions
  • 1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O = myo-inositol + sn-glycerol 3-phosphate [RN:R01193] ALL_REAC R01193
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 4-24 248-268
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 7637877 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q9NZC3 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name GDE1_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence Not Available
Enzyme 23 GenBank Gene ID AF212862 Link Image
Enzyme 23 GeneCard ID Q9NZC3 Link Image
Enzyme 23 GenAtlas ID GDE1 Link Image
Enzyme 23 HGNC ID HGNC:29644 Link Image
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 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]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 13052
Enzyme 24 Name Acetylcholinesterase
Enzyme 24 Synonyms
  1. YT blood group
  2. Acetylcholinesterase
  3. Yt blood group, isoform CRA_b
  4. cDNA FLJ77135, highly similar to Homo sapiens acetylcholinesterase
  5. YT blood group
  6. ACHE, transcript variant E4- E6, mRNA
Enzyme 24 Gene Name ACHE
Enzyme 24 Protein Sequence >Acetylcholinesterase
MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPV
SAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPN
RELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSM
NYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASV
GMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTEL
VACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVG
VVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPE
DPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGY
EIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQ
YVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN
QFDHYSKQDRCSDL
Enzyme 24 Number of Residues 614
Enzyme 24 Molecular Weight 67797
Enzyme 24 Theoretical pI 6.24
Enzyme 24 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cholinesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
Component
Enzyme 24 General Function Lipid transport and metabolism
Enzyme 24 Specific Function Not Available
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 158256078 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID A4D2E2 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name A4D2E2_HUMAN Link Image
Enzyme 24 PDB ID 1F8U Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence Not Available
Enzyme 24 GenBank Gene ID AK291321 Link Image
Enzyme 24 GeneCard ID A4D2E2 Link Image
Enzyme 24 GenAtlas ID ACHE Link Image
Enzyme 24 HGNC ID HGNC:108 Link Image
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 15205
Enzyme 25 Name cDNA FLJ77091, highly similar to Homo sapiens alcohol dehydrogenase 4 (class II), pi polypeptide (ADH4), mRNA
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name Not Available
Enzyme 25 Protein Sequence >cDNA FLJ77091, highly similar to Homo sapiens alcohol dehydrogenase 4 (class II), pi polypeptide (ADH4), mRNA
MGTKGKVIKCKAAIAWEAGKPLCIEEVEVAPPKAHEVRIQIIATSLCHTDATVIDSKFEG
LAFPVIVGHEAAGIVESIGPGVTNVKPGDKVIPLYAPLCRKCKFCLSPLTNLCGKISNLK
SPASDQQLMEDKTSRFTCKGKPVYHFFGTSTFSQYTVVSDINLAKIDDDANLERVCLLGC
GFSTGYGAAINNAKVTPGSTCAVFGLGGVGLSAVMGCKAAGASRIIGIDINSEKFVKAKA
LGATDCLNPRDLHKPIQEVIIELTKGGVDFALDCAGGSETMKAALDCTTAGWGSCTFIGV
AAGSKGLTIFPEELIIGRTINGTFFGGWKSVDSIPKLVTDYKNKKFNLDALVTHTLPFDK
ISEAFDLMNQGKSVRTILIF
Enzyme 25 Number of Residues 380
Enzyme 25 Molecular Weight 40222
Enzyme 25 Theoretical pI 8.01
Enzyme 25 GO Classification Not Available
Enzyme 25 General Function Energy production and conversion
Enzyme 25 Specific Function Not Available
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function Not Available
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 158255106 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID A8K470 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name A8K470_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1143 bp
ATGGGCACCAAGGGCAAAGTTATTAAATGCAAAGCAGCCATCGCCTGGGAAGCAGGCAAG
CCCCTTTGCATTGAAGAGGTTGAAGTAGCTCCCCCCAAGGCTCATGAAGTTCGCATTCAG
ATCATTGCTACCTCCCTGTGCCATACTGATGCCACTGTTATCGATTCTAAATTTGAGGGC
CTAGCTTTCCCAGTGATCGTTGGCCATGAGGCTGCAGGTATTGTGGAAAGTATTGGGCCA
GGAGTGACCAACGTCAAACCAGGTGACAAAGTAATTCCACTTTATGCACCTCTATGTAGA
AAATGCAAGTTTTGTCTGAGTCCACTCACAAATTTGTGTGGGAAAATCAGTAATCTCAAA
AGTCCTGCTAGTGATCAACAACTAATGGAAGACAAAACCAGCAGGTTTACCTGCAAAGGA
AAACCAGTTTACCATTTCTTTGGAACCAGTACATTCTCTCAGTACACTGTGGTGTCAGAT
ATCAATCTTGCCAAAATAGATGATGATGCAAATTTAGAGAGAGTTTGTCTGCTTGGATGT
GGGTTTTCAACTGGCTATGGGGCTGCAATCAACAATGCCAAGGTCACCCCTGGTTCGACT
TGTGCTGTCTTTGGCCTAGGAGGTGTGGGTCTTTCTGCTGTAATGGGTTGTAAAGCAGCA
GGAGCTTCCAGAATCATAGGTATTGACATCAACAGTGAGAAGTTTGTGAAGGCTAAAGCC
CTGGGAGCCACTGACTGCCTCAATCCTAGAGACTTACATAAACCAATCCAGGAAGTTATC
ATTGAATTGACCAAGGGAGGTGTGGATTTTGCCCTTGACTGTGCAGGTGGATCTGAAACC
ATGAAAGCAGCCCTGGACTGTACAACCGCAGGCTGGGGATCATGTACTTTCATTGGAGTA
GCTGCTGGTAGCAAAGGATTGACTATTTTTCCAGAGGAGCTAATAATCGGCCGTACTATA
AATGGAACATTCTTTGGTGGTTGGAAAAGTGTAGATTCTATCCCAAAGCTGGTCACTGAC
TATAAGAATAAGAAATTCAATCTGGATGCATTGGTGACCCATACCCTGCCTTTTGACAAA
ATCAGTGAGGCATTTGACCTAATGAACCAAGGAAAAAGCGTCCGAACAATCCTCATCTTT
TGA
Enzyme 25 GenBank Gene ID AK290835 Link Image
Enzyme 25 GeneCard ID A8K470 Link Image
Enzyme 25 GenAtlas ID Not Available
Enzyme 25 HGNC ID Not Available
Enzyme 25 Chromosome Location Not Available
Enzyme 25 Locus Not Available
Enzyme 25 SNPs Not Available
Enzyme 25 General References Not Available
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 15206
Enzyme 26 Name Alcohol dehydrogenase 7 (Class IV), mu or sigma polypeptide
Enzyme 26 Synonyms Not Available
Enzyme 26 Gene Name ADH7
Enzyme 26 Protein Sequence >Alcohol dehydrogenase 7 (Class IV), mu or sigma polypeptide
MFAEIQIQDKDRMGTAGKVIKCKAAVLWEQKQPFSIEEIEVAPPKTKEVRIKILATGICR
TDDHVIKGTMVSKFPVIVGHEATGIVESIGEGVTTVKPGDKVIPLFLPQCRECNACRNPD
GNLCIRSDITGRGVLADGTTRFTCKGKPVHHFMNTSTFTEYTVVDESSVAKIDDAAPPEK
VCLIGCGFSTGYGAAVKTGKVKPGSTCVVFGLGGVGLSVIMGCKSAGASRIIGIDLNKDK
FEKAMAVGATECISPKDSTKPISEVLSEMTGNNVGYTFEVIGHLETMIDALASCHMNYGT
SVVVGVPPSAKMLTYDPMLLFTGRTWKGCVFGGLKSRDDVPKLVTEFLAKKFDLDQLITH
VLPFKKISEGFELLNSGQSIRTVLTF
Enzyme 26 Number of Residues 386
Enzyme 26 Molecular Weight 41482
Enzyme 26 Theoretical pI 7.94
Enzyme 26 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 26 General Function Energy production and conversion
Enzyme 26 Specific Function Not Available
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 124297943 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID A2RRB6 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name A2RRB6_HUMAN Link Image
Enzyme 26 PDB ID 1D1S Link Image
Enzyme 26 PDB File Show
Enzyme 26 3D Structure
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1161 bp
ATGTTTGCAGAAATACAGATCCAAGACAAAGACAGGATGGGCACTGCTGGAAAAGTTATT
AAATGCAAAGCAGCTGTGCTTTGGGAGCAGAAGCAACCCTTCTCCATTGAGGAAATAGAA
GTTGCCCCACCAAAGACTAAAGAAGTTCGCATTAAGATTTTGGCCACAGGAATCTGTCGC
ACAGATGACCATGTGATAAAAGGAACAATGGTGTCCAAGTTTCCAGTGATTGTGGGACAT
GAGGCAACTGGGATTGTAGAGAGCATTGGAGAAGGAGTGACTACAGTGAAACCAGGTGAC
AAAGTCATCCCTCTCTTTCTGCCACAATGTAGAGAATGCAATGCTTGTCGCAACCCAGAT
GGCAACCTTTGCATTAGGAGCGATATTACTGGTCGTGGAGTACTGGCTGATGGCACCACC
AGATTTACATGCAAGGGCAAACCAGTCCACCACTTCATGAACACCAGTACATTTACCGAG
TACACAGTGGTGGATGAATCTTCTGTTGCTAAGATTGATGATGCAGCTCCTCCTGAGAAA
GTCTGTTTAATTGGCTGTGGGTTTTCCACTGGATATGGCGCTGCTGTTAAAACTGGCAAG
GTCAAACCTGGTTCCACTTGCGTCGTCTTTGGCCTGGGAGGAGTTGGCCTGTCAGTCATC
ATGGGCTGTAAGTCAGCTGGTGCATCTAGGATCATTGGGATTGACCTCAACAAAGACAAA
TTTGAGAAGGCCATGGCTGTAGGTGCCACTGAGTGTATCAGTCCCAAGGACTCTACCAAA
CCCATCAGTGAGGTGCTGTCAGAAATGACAGGCAACAACGTGGGATACACCTTTGAAGTT
ATTGGGCATCTTGAAACCATGATTGATGCCCTGGCATCCTGCCACATGAACTATGGGACC
AGCGTGGTTGTAGGAGTTCCTCCATCAGCCAAGATGCTCACCTATGACCCGATGTTGCTC
TTCACTGGACGCACATGGAAGGGATGTGTCTTTGGAGGTTTGAAAAGCAGAGATGATGTC
CCAAAACTAGTGACTGAGTTCCTGGCAAAGAAATTTGACCTGGACCAGTTGATAACTCAT
GTTTTACCATTTAAAAAAATCAGTGAAGGATTTGAGCTGCTCAATTCAGGACAAAGCATT
CGAACGGTCCTGACGTTTTGA
Enzyme 26 GenBank Gene ID BC131512 Link Image
Enzyme 26 GeneCard ID A2RRB6 Link Image
Enzyme 26 GenAtlas ID Not Available
Enzyme 26 HGNC ID Not Available
Enzyme 26 Chromosome Location Not Available
Enzyme 26 Locus Not Available
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 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 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 15207
Enzyme 27 Name Phospholipase D1 variant (Fragment)
Enzyme 27 Synonyms Not Available
Enzyme 27 Gene Name Not Available
Enzyme 27 Protein Sequence >Phospholipase D1 variant (Fragment)
ANAQVLAAPSPCSPFAFTLSKVNMSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEG
EEVDYDVSPSDPKIQEVYIPFSAIYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRV
PSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEP
REMPSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDL
GPKGIEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLL
VDKEFKIKVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKD
HRFGSYAAIQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGN
RWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSST
VYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAM
ESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSI
SSIDSTSNTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPR
MPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLLPKSQTTAHELRYQVP
GSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFN
KIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGEN
SILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANIN
DRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQ
DPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPVLAKEDPIRAEE
ELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
Enzyme 27 Number of Residues 1059
Enzyme 27 Molecular Weight 122010
Enzyme 27 Theoretical pI 9.03
Enzyme 27 GO Classification
Function
  • catalytic activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • metabolism
  • physiological process
  • signal transduction
Component
Enzyme 27 General Function Lipid transport and metabolism
Enzyme 27 Specific Function Not Available
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 62089400 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q59EA4 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name Q59EA4_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 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 27 GenBank Gene ID AB209907 Link Image
Enzyme 27 GeneCard ID Q59EA4 Link Image
Enzyme 27 GenAtlas ID Not Available
Enzyme 27 HGNC ID HGNC:9067 Link Image
Enzyme 27 Chromosome Location Not Available
Enzyme 27 Locus Not Available
Enzyme 27 SNPs Not Available
Enzyme 27 General References Not Available
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 16485
Enzyme 28 Name cDNA FLJ35449 fis, clone SMINT2004144, highly similar to ALCOHOL DEHYDROGENASE 6 (EC 1.1.1.1)
Enzyme 28 Synonyms Not Available
Enzyme 28 Gene Name Not Available
Enzyme 28 Protein Sequence >cDNA FLJ35449 fis, clone SMINT2004144, highly similar to ALCOHOL DEHYDROGENASE 6 (EC 1.1.1.1)
MSTTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLD
LLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSK
TQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCGFSTG
FGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATE
CLNPQDLKKPIQEVLFDMTDAGIDFRFEAIGNLDVLAAALASCNESYGVCVVVGVLPASV
QLKISGQLFFSGRSLKGSVFGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAV
ELMKTGKCIRCILLL
Enzyme 28 Number of Residues 375
Enzyme 28 Molecular Weight 39868
Enzyme 28 Theoretical pI 8.09
Enzyme 28 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 28 General Function Energy production and conversion
Enzyme 28 Specific Function Not Available
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + H+ [RN:R07326 R07327] ALL_REAC R07326 > R00623 R00754 R01036 R04805 R04880 R06917 R06927
  • R07327 > R00624
  • (other) R01041 R05233 R05234 R07105
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein Not Available
Enzyme 28 UniProtKB/Swiss-Prot ID B3KS45 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name B3KS45_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence Not Available
Enzyme 28 GenBank Gene ID AK092768 Link Image
Enzyme 28 GeneCard ID B3KS45 Link Image
Enzyme 28 GenAtlas ID Not Available
Enzyme 28 HGNC ID Not Available
Enzyme 28 Chromosome Location Not Available
Enzyme 28 Locus Not Available
Enzyme 28 SNPs Not Available
Enzyme 28 General References Not Available
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 16875
Enzyme 29 Name Phospholipase D6
Enzyme 29 Synonyms
  1. PLD 6
  2. Choline phosphatase 6
  3. Phosphatidylcholine-hydrolyzing phospholipase D6
Enzyme 29 Gene Name PLD6
Enzyme 29 Protein Sequence >Phospholipase D6
MGRLSWQVAAAAAVGLALTLEALPWVLRWLRSRRRRPRREALFFPSQVTCTEALLRAPGA
ELAELPEGCPCGLPHGESALSRLLRALLAARASLDLCLFAFSSPQLGRAVQLLHQRGVRV
RVVTDCDYMALNGSQIGLLRKAGIQVRHDQDPGYMHHKFAIVDKRVLITGSLNWTTQAIQ
NNRENVLITEDDEYVRLFLEEFERIWEQFNPTKYTFFPPKKSHGSCAPPVSRAGGRLLSW
HRTCGTSSESQT
Enzyme 29 Number of Residues 252
Enzyme 29 Molecular Weight 28273
Enzyme 29 Theoretical pI 9.67
Enzyme 29 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 29 General Function Lipid transport and metabolism
Enzyme 29 Specific Function A phosphatidylcholine + H(2)O = choline + a phosphatidate
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • 5-27
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein Not Available
Enzyme 29 UniProtKB/Swiss-Prot ID Q8N2A8 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name PLD6_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence Not Available
Enzyme 29 GenBank Gene ID AK090899 Link Image
Enzyme 29 GeneCard ID Q8N2A8 Link Image
Enzyme 29 GenAtlas ID PLD6 Link Image
Enzyme 29 HGNC ID HGNC:30447 Link Image
Enzyme 29 Chromosome Location 17
Enzyme 29 Locus 17p11.2
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References Not Available
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 17068
Enzyme 30 Name Choline transporter-like protein 4
Enzyme 30 Synonyms
  1. Solute carrier family 44 member 4
Enzyme 30 Gene Name SLC44A4
Enzyme 30 Protein Sequence >Choline transporter-like protein 4
MGGKQRDEDDEAYGKPVKYDPSFRGPIKNRSCTDVICCVLFLLFILGYIVVGIVAWLYGD
PRQVLYPRNSTGAYCGMGENKDKPYLLYFNIFSCILSSNIISVAENGLQCPTPQVCVSSC
PEDPWTVGKNEFSQTVGEVFYTKNRNFCLPGVPWNMTVITSLQQELCPSFLLPSAPALGR
CFPWTNITPPALPGITNDTTIQQGISGLIDSLNARDISVKIFEDFAQSWYWILVALGVAL
VLSLLFILLLRLVAGPLVLVLILGVLGVLAYGIYYCWEEYRVLRDKGASISQLGFTTNLS
AYQSVQETWLAALIVLAVLEAILLLVLIFLRQRIRIAIALLKEASKAVGQMMSTMFYPLV
TFVLLLICIAYWAMTALYLATSGQPQYVLWASNISSPGCEKVPINTSCNPTAHLVNSSCP
GLMCVFQGYSSKGLIQRSVFNLQIYGVLGLFWTLNWVLALGQCVLAGAFASFYWAFHKPQ
DIPTFPLISAFIRTLRYHTGSLAFGALILTLVQIARVILEYIDHKLRGVQNPVARCIMCC
FKCCLWCLEKFIKFLNRNAYIMIAIYGKNFCVSAKNAFMLLMRNIVRVVVLDKVTDLLLF
FGKLLVVGGVGVLSFFFFSGRIPGLGKDFKSPHLNYYWLPIMTSILGAYVIASGFFSVFG
MCVDTLFLCFLEDLERNNGSLDRPYYMSKSLLKILGKKNEAPPDNKKRKK
Enzyme 30 Number of Residues 710
Enzyme 30 Molecular Weight 79237
Enzyme 30 Theoretical pI 8.67
Enzyme 30 GO Classification Not Available
Enzyme 30 General Function Not Available
Enzyme 30 Specific Function Not Available
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • 35-55 230-250 253-273 310-330 359-379 456-476 502-522 561-581 598-618 639-659
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein Not Available
Enzyme 30 UniProtKB/Swiss-Prot ID Q53GD3 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name CTL4_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence Not Available
Enzyme 30 GenBank Gene ID AK027397 Link Image
Enzyme 30 GeneCard ID Q53GD3 Link Image
Enzyme 30 GenAtlas ID SLC44A4 Link Image
Enzyme 30 HGNC ID HGNC:13941 Link Image
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  3. Uhl J, Penzel R, Sergi C, Kopitz J, Otto HF, Cantz M: Identification of a CTL4/Neu1 fusion transcript in a sialidosis patient. FEBS Lett. 2002 Jun 19;521(1-3):19-23. [PubMed Link Image]
  4. O'Regan S, Traiffort E, Ruat M, Cha N, Compaore D, Meunier FM: An electric lobe suppressor for a yeast choline transport mutation belongs to a new family of transporter-like proteins. Proc Natl Acad Sci U S A. 2000 Feb 15;97(4):1835-40. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 17069
Enzyme 31 Name Choline transporter-like protein 2
Enzyme 31 Synonyms
  1. Solute carrier family 44 member 2
Enzyme 31 Gene Name SLC44A2
Enzyme 31 Protein Sequence >Choline transporter-like protein 2
MGDERPHYYGKHGTPQKYDPTFKGPIYNRGCTDIICCVFLLLAIVGYVAVGIIAWTHGDP
RKVIYPTDSRGEFCGQKGTKNENKPYLFYFNIVKCASPLVLLEFQCPTPQICVEKCPDRY
LTYLNARSSRDFEYYKQFCVPGFKNNKGVAEVLRDGDCPAVLIPSKPLARRCFPAIHAYK
GVLMVGNETTYEDGHGSRKNITDLVEGAKKANGVLEARQLAMRIFEDYTVSWYWIIIGLV
IAMAMSLLFIILLRFLAGIMVWVMIIMVILVLGYGIFHCYMEYSRLRGEAGSDVSLVDLG
FQTDFRVYLHLRQTWLAFMIILSILEVIIILLLIFLRKRILIAIALIKEASRAVGYVMCS
LLYPLVTFFLLCLCIAYWASTAVFLSTSNEAVYKIFDDSPCPFTAKTCNPETFPSSNESR
QCPNARCQFAFYGGESGYHRALLGLQIFNAFMFFWLANFVLALGQVTLAGAFASYYWALR
KPDDLPAFPLFSAFGRALRYHTGSLAFGALILAIVQIIRVILEYLDQRLKAAENKFAKCL
MTCLKCCFWCLEKFIKFLNRNAYIMIAIYGTNFCTSARNAFFLLMRNIIRVAVLDKVTDF
LFLLGKLLIVGSVGILAFFFFTHRIRIVQDTAPPLNYYWVPILTVIVGSYLIAHGFFSVY
GMCVDTLFLCFLEDLERNDGSAERPYFMSSTLKKLLNKTNKKAAES
Enzyme 31 Number of Residues 706
Enzyme 31 Molecular Weight 80153
Enzyme 31 Theoretical pI 8.71
Enzyme 31 GO Classification Not Available
Enzyme 31 General Function Not Available
Enzyme 31 Specific Function Putative choline transporter
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • 34-54 233-253 257-277 316-336 365-385 458-480 505-525 564-584 600-620 639-659
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein Not Available
Enzyme 31 UniProtKB/Swiss-Prot ID Q8IWA5 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name CTL2_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence Not Available
Enzyme 31 GenBank Gene ID AJ245621 Link Image
Enzyme 31 GeneCard ID Q8IWA5 Link Image
Enzyme 31 GenAtlas ID SLC44A2 Link Image
Enzyme 31 HGNC ID HGNC:17292 Link Image
Enzyme 31 Chromosome Location 19
Enzyme 31 Locus 19p13.1
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. O'Regan S, Traiffort E, Ruat M, Cha N, Compaore D, Meunier FM: An electric lobe suppressor for a yeast choline transport mutation belongs to a new family of transporter-like proteins. Proc Natl Acad Sci U S A. 2000 Feb 15;97(4):1835-40. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 17070
Enzyme 32 Name Choline transporter-like protein 3
Enzyme 32 Synonyms
  1. Solute carrier family 44 member 3
Enzyme 32 Gene Name SLC44A3
Enzyme 32 Protein Sequence >Choline transporter-like protein 3
MHCLGAEYLVSAEGAPRQREWRPQIYRKCTDTAWLFLFFLFWTGLVFIMGYSVVAGAAGR
LLFGYDSFGNMCGKKNSPVEGAPLSGQDMTLKKHVFFMNSCNLEVKGTQLNRMALCVSNC
PEEQLDSLEEVQFFANTSGSFLCVYSLNSFNYTHSPKADSLCPRLPVPPSKSFPLFNRCV
PQTPECYSLFASVLINDVDTLHRILSGIMSGRDTILGLCILALALSLAMMFTFRFITTLL
VHIFISLVILGLLFVCGVLWWLYYDYTNDLSIELDTERENMKCVLGFAIVSTGITAVLLV
LIFVLRKRIKLTVELFQITNKAISSAPFLLFQPLWTFAILIFFWVLWVAVLLSLGTAGAA
QVMEGGQVEYKPLSGIRYMWSYHLIGLIWTSEFILACQQMTIAGAVVTCYFNRSKNDPPD
HPILSSLSILFFYHQGTIVKGSFLISVVRIPRIIVMYMQNALKEQQHGALSRYLFRCCYC
CFWCLDKYLLHLNQNAYTTTAINGTDFCTSAKDAFKILSKNSSHFTSINCFGDFIIFLGK
VLVVCFTVFGGLMAFNYNRAFQVWAVPLLLVAFFAYLVAHSFLSVFETVLDALFLCFAVD
LETNDGSSEKPYFMDQEFLSFVKRSNKLNNARAQQDKHSLRNEEGTELQAIVR
Enzyme 32 Number of Residues 653
Enzyme 32 Molecular Weight 73798
Enzyme 32 Theoretical pI 7.73
Enzyme 32 GO Classification Not Available
Enzyme 32 General Function Not Available
Enzyme 32 Specific Function Not Available
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • 34-54 213-233 243-263 284-304 334-354 384-404 428-448 534-554 563-583
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein Not Available
Enzyme 32 UniProtKB/Swiss-Prot ID Q8N4M1 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name CTL3_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence Not Available
Enzyme 32 GenBank Gene ID AC093429 Link Image
Enzyme 32 GeneCard ID Q8N4M1 Link Image
Enzyme 32 GenAtlas ID SLC44A3 Link Image
Enzyme 32 HGNC ID HGNC:28689 Link Image
Enzyme 32 Chromosome Location Not Available
Enzyme 32 Locus Not Available
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. O'Regan S, Traiffort E, Ruat M, Cha N, Compaore D, Meunier FM: An electric lobe suppressor for a yeast choline transport mutation belongs to a new family of transporter-like proteins. Proc Natl Acad Sci U S A. 2000 Feb 15;97(4):1835-40. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available