We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for 1-Butanol (HMDB04327)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-13 17:50:24
Update Date 2009-05-05 20:59:57
Accession Number HMDB04327
Secondary Accession Numbers Not Available
Common Name 1-Butanol
Description 1-Butanol, which is also known as n-butanol or 1-butanol or butyl alcohol (sometimes also called biobutanol when produced biologically), is an alcohol with a 4 carbon structure and the molecular formula of C4H10O. It is primarily used as a solvent, as an intermediate in chemical synthesis, and as a fuel. There are four isomeric structures for butanol. The straight chain isomer with the alcohol at an internal carbon is sec-butanol or 2-butanol. The branched isomer with the alcohol at a terminal carbon is isobutanol, and the branched isomer with the alcohol at the internal carbon is tert-butanol. 1-Butanol is produced in small amounts by gut microbial fermenetation through the butanoate metabolic pathway.
Synonyms
  1. 1-Butanol
  2. 1-Butyl alcohol
  3. Butanol
  4. Butyl alcohol
  5. Butyl hydroxide
  6. Hemostyp
  7. Methylolpropane
  8. n-Butanol
  9. n-Butyl alcohol
  10. Propylcarbinol
Chemical IUPAC Name butan-1-ol
Chemical Formula C4H10O
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Alcohols and Polyols
Sub Class
  • Simple alcohols
Family
  • Microbial Metabolite
Species
  • primary alcohol
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 74.122
Monoisotopic Molecular Weight 74.073166
Isomeric SMILES CCCCO
Canonical SMILES CCCCO
KEGG Compound ID C06142 Link Image
BioCyc ID BUTANOL Link Image
BiGG ID Not Available
Wikipedia Link 1-Butanol Link Image
NuGOwiki Link HMDB04327 Link Image
Metagene Link HMDB04327 Link Image
METLIN ID 7052 Link Image
PubChem Compound 263 Link Image
PubChem Substance 10341851 Link Image
ChEBI ID 28885 Link Image
CAS Registry Number 71-36-3
InChI Identifier InChI=1/C4H10O/c1-2-3-4-5/h5H,2-4H2,1H3
Synthesis Reference Tsuchida, Takashi; Sakuma, Shuji. Ethanol to 1-butanol on hydroxyapatite. Shokubai (2007), 49(3), 238-243.
Melting Point (Experimental) -89.8 oC
Experimental Water Solubility 63.2 mg/mL at 25 oC [TEWARI,YB et al. (1982)] Source: PhysProp
Predicted Water Solubility 158.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Liquid
Experimental LogP/Hydrophobicity 0.88 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity 0.84 [Predicted by ALOGPS]; 0.9 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
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 Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location
  • Blood
Tissue Location
Tissue References
Epidermis
Fibroblasts
Kidney
Liver
Pancreas
Spleen
Stratum Corneum
Concentrations (Normal)
Biofluid Blood
Value 0.08 (0.00 - 0.27) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Liebich HM, Buelow HJ, Kallmayer R: Quantification of endogenous aliphatic alcohols in serum and urine. J Chromatogr. 1982 Apr 30;239:343-9. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.11 (0 - 2.43) uM
Age Adult:>18 yrs old
Sex Both
Condition Diabetes mellitus type 2
Comments Not Available
References
  • Liebich HM, Buelow HJ, Kallmayer R: Quantification of endogenous aliphatic alcohols in serum and urine. J Chromatogr. 1982 Apr 30;239:343-9. [PubMed Link Image]
Associated Disorders
Condition References
Diabetes mellitus type 2
  • Liebich HM, Buelow HJ, Kallmayer R: Quantification of endogenous aliphatic alcohols in serum and urine. J Chromatogr. 1982 Apr 30;239:343-9. [PubMed Link Image]
OMIM ID
Pathways Not Available
General References
  1. Copovi A, Diez-Sales O, Herraez-Dominguez JV, Herraez-Dominguez M: Enhancing effect of alpha-hydroxyacids on "in vitro" permeation across the human skin of compounds with different lipophilicity. Int J Pharm. 2006 May 11;314(1):31-6. Epub 2006 Mar 20. [PubMed Link Image]
  2. Bailyes EM, Seabrook RN, Calvin J, Maguire GA, Price CP, Siddle K, Luzio JP: The preparation of monoclonal antibodies to human bone and liver alkaline phosphatase and their use in immunoaffinity purification and in studying these enzymes when present in serum. Biochem J. 1987 Jun 15;244(3):725-33. [PubMed Link Image]
  3. Gainer AL, Stinson RA: Evidence that alkaline phosphatase from human neutrophils is the same gene product as the liver/kidney/bone isoenzyme. Clin Chim Acta. 1982 Aug 4;123(1-2):11-7. [PubMed Link Image]
  4. Yamamoto K, Takahashi Y, Mano T, Sakata Y, Nishikawa N, Yoshida J, Oishi Y, Hori M, Miwa T, Inoue S, Masuyama T: N-methylethanolamine attenuates cardiac fibrosis and improves diastolic function: inhibition of phospholipase D as a possible mechanism. Eur Heart J. 2004 Jul;25(14):1221-9. [PubMed Link Image]
  5. Seiffert UB, Siede WH, Welsch GJ, Oremek G: Multiple forms of alkaline phosphatases in human liver tissue. Clin Chim Acta. 1984 Dec 15;144(1):17-27. [PubMed Link Image]
  6. Chen M: Amended final report of the safety assessment of t-Butyl Alcohol as used in cosmetics. Int J Toxicol. 2005;24 Suppl 2:1-20. [PubMed Link Image]
  7. Okamoto M, Kaji R, Kasetani H, Yoshida H, Moriya Y, Saito M, Sato M: Purification and characterization of interferon-gamma-inducing molecule of OK-432, a penicillin-killed streptococcal preparation, by monoclonal antibody neutralizing interferon-gamma-inducing activity of OK-432. J Immunother. 1993 May 4;13(4):232-42. [PubMed Link Image]
  8. Chang CH, Angellis D: Identification of a butanol-extractable human placenta-specific antigen with alkaline phosphatase activity. J Immunol. 1976 Jul;117(1):91-6. [PubMed Link Image]
  9. Oakley DM, Swarbrick J: Effects of ionization on the percutaneous absorption of drugs: partitioning of nicotine into organic liquids and hydrated stratum corneum. J Pharm Sci. 1987 Dec;76(12):866-71. [PubMed Link Image]
  10. Waddell WJ, Marlowe C: Inhibition by alcohols of the localization of radioactive nitrosonornicotine in sites of tumor formation. Science. 1983 Jul 1;221(4605):51-3. [PubMed Link Image]
  11. Bieler CA, Cornelius MG, Klein R, Arlt VM, Wiessler M, Phillips DH, Schmeiser HH: DNA adduct formation by the environmental contaminant 3-nitrobenzanthrone after intratracheal instillation in rats. Int J Cancer. 2005 Oct 10;116(6):833-8. [PubMed Link Image]
  12. Wulkan RW, Huijskes-Heins MI, Leijnse B: Hydrophobic properties of alkaline phosphatases. Int J Biochem. 1986;18(11):1045-51. [PubMed Link Image]
  13. Kalimanovska V, Whitaker KB, Moss DW: Effect of bromelain on alkaline phosphatases of intestinal and non-intestinal tissues and serum. Clin Chim Acta. 1987 Dec;170(2-3):219-25. [PubMed Link Image]
  14. Basu A, Glew RH: Characterization of the activation of rat liver beta-glucosidase by sialosylgangliotetraosylceramide. J Biol Chem. 1985 Oct 25;260(24):13067-73. [PubMed Link Image]
  15. Arlt VM, Sorg BL, Osborne M, Hewer A, Seidel A, Schmeiser HH, Phillips DH: DNA adduct formation by the ubiquitous environmental pollutant 3-nitrobenzanthrone and its metabolites in rats. Biochem Biophys Res Commun. 2003 Jan 3;300(1):107-14. [PubMed Link Image]
  16. Wikipedia Link Image
Metabolic Enzymes
  1. Serum paraoxonase/lactonase 3
  2. Serum paraoxonase/arylesterase 1
  3. Serum paraoxonase/arylesterase 2
  4. Intestinal alkaline phosphatase precursor
  5. Lysosomal acid phosphatase precursor
  6. Alkaline phosphatase, tissue-nonspecific isozyme precursor
  7. Tartrate-resistant acid phosphatase type 5 precursor
  8. Alkaline phosphatase, placental-like precursor
  9. Aldehyde dehydrogenase X, mitochondrial precursor
  10. Sulfotransferase family cytosolic 2B member 1
  11. Sorbitol dehydrogenase
  12. Alcohol dehydrogenase [NADP+]
  13. Alcohol dehydrogenase 4
  14. Alcohol dehydrogenase 1B
  15. Alcohol dehydrogenase 1A
  16. Alcohol dehydrogenase 6
  17. Beta-glucuronidase precursor
  18. Plasma alpha-L-fucosidase precursor
  19. Trans-2-enoyl-CoA reductase, mitochondrial precursor
  20. Lecithin retinol acyltransferase
  21. Orphan nuclear receptor NR1I3
  22. Zinc-binding alcohol dehydrogenase domain-containing protein 2
  23. Retinol dehydrogenase 13
  24. Alcohol dehydrogenase iron-containing 1
  25. Fatty acyl-CoA reductase 2
  26. Acyl-CoA wax alcohol acyltransferase 2
  27. Klotho precursor
  28. CDNA FLJ16165 fis, clone BRCOC2019841
  29. Testicular acid phosphatase
  30. Carboxylesterase 7
  31. Acid phosphatase-like protein 2
  32. Synaptic vesicle membrane protein VAT-1 homolog-like
  33. Putative quinone oxidoreductase
  34. Synaptic vesicle membrane protein VAT-1 homolog
  35. cDNA FLJ52809, highly similar to Zinc-binding alcohol dehydrogenasedomain-containing protein 2 (EC 1.-.-.-)
  36. Reticulon-4-interacting protein 1, mitochondrial
Enzyme 1 [top]
Enzyme 1 ID 5321
Enzyme 1 Name Serum paraoxonase/lactonase 3
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name PON3
Enzyme 1 Protein Sequence >Serum paraoxonase/lactonase 3
MGKLVALVLLGVGLSLVGEMFLAFRERVNASREVEPVEPENCHLIEELESGSEDIDILPS
GLAFISSGLKYPGMPNFAPDEPGKIFLMDLNEQNPRAQALEISGGFDKELFNPHGISIFI
DKDNTVYLYVVNHPHMKSTVEIFKFEEQQRSLVYLKTIKHELLKSVNDIVVLGPEQFYAT
RDHYFTNSLLSFFEMILDLRWTYVLFYSPREVKVVAKGFCSANGITVSADQKYVYVADVA
AKNIHIMEKHDNWDLTQLKVIQLGTLVDNLTVDPATGDILAGCHPNPMKLLNYNPEDPPG
SEVLRIQNVLSEKPRVSTVYANNGSVLQGTSVASVYHGKILIGTVFHKTLYCEL
Enzyme 1 Number of Residues 354
Enzyme 1 Molecular Weight 39608
Enzyme 1 Theoretical pI 5.10
Enzyme 1 GO Classification
Function
  • arylesterase activity
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
Component
  • extracellular region
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Has very limited arylesterase and no paraoxonase activities but rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-
Enzyme 1 Transmembrane Regions
  • 5-24
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 12751374 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q15166 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PON3_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1064 bp
ATGGGGAAGCTCGTGGCGCTGGTCCTGCTGGGGGTCGGCCTGTCCTTAGTCGGGGAGATG
TTCCTGGCGTTTAGAGAAAGGGTGAATGCCTCTCGAGAAGTGGAGCCAGTAGAACCTGAA
AACTGCCACCTTATTGAGGAACTTGAAAGTGGCTCTGAAGATATTGATATATTCCTCAGT
GGGCTGGCTTTTATCTCCAGTGGATTAAAATATCCAGGCATGCCAAACTTTGCGCCAGAT
GAACCAGGAAAAATCTTCTTGATGGATCTGAATGAACAAAACCCAAGGGCACAAGCACTA
GAAATCAGTGGTGGATTTGACAAAGAATTATTTAATCCACATGGGATCAGTATTTTCATC
GACAAAGACAATACTGTGTATCTTTATGTTGTGAATCATCCCCACATGAAGTCCACTGTG
GAGATATTTAAATTTGAGGAACAACAACGTTCTCTGGTATACCTGAAAACTATAAAACAT
GAACTTCTCAAAAGTGTGAATGACATTGTGGTTCTTGGACCAGAACAGTTCTATGCCACC
AGAGACCACTATTTTACCAACTCCCTCCTGTCATTTTTTGAGATGATCTTGGATCTTCGC
TGGACTTATGTTCTTTTCTACAGCCCAAGGGAGGTTAAAGTGGTGGCCAAAGGATTTTGT
AGTGCCAATGGGATCACAGTCTCAGCAGACCAGAAGTATGTCTATGTAGCTGATGTAGCA
GCTAAGAACATTCACATAATGGAAAAACATGATAACTGGGATTTAACTCAACTGAAGGTG
ATACAGTTGGGCACCTTAGTGGATAACCTGACTGTCGATCCTGCCACAGGAGACATTTTG
GCAGGATGCCATCCTAATCCTATGAAGCTACTGAACTATAACCCTGAGGACCCTCCAGGA
TCAGAAGTACTTCGCATCCAGAATGTTTTGTCTGAGAAGCCCAGGGTGAGCACCGTGTAT
GCCAACAATGGCTCTGTGCTTCAGGGCACCTCTGTGGCTTCTGTGTACCATGGGAAAATT
CTCATAGGCACCGTATTTCACAAAACTCTGTACTGTGAGCTCTA
Enzyme 1 GenBank Gene ID AF320003 Link Image
Enzyme 1 GeneCard ID PON3 Link Image
Enzyme 1 GenAtlas ID PON3 Link Image
Enzyme 1 HGNC ID HGNC:9206 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7q21.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. 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]
  2. Primo-Parmo SL, Sorenson RC, Teiber J, La Du BN: The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family. Genomics. 1996 May 1;33(3):498-507. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5323
Enzyme 2 Name Serum paraoxonase/arylesterase 1
Enzyme 2 Synonyms
  1. PON 1
  2. Serum aryldialkylphosphatase 1
  3. A-esterase 1
  4. Aromatic esterase 1
  5. K-45
Enzyme 2 Gene Name PON1
Enzyme 2 Protein Sequence >Serum paraoxonase/arylesterase 1
MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDMEILPN
GLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTF
TDEDNAMYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYG
TNDHYFLDPYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAEL
LAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPP
ASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCEL
Enzyme 2 Number of Residues 355
Enzyme 2 Molecular Weight 39750
Enzyme 2 Theoretical pI 4.89
Enzyme 2 GO Classification
Function
  • arylesterase activity
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
Component
  • extracellular region
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and a number of aromatic carboxylic acid esters. May mediate an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation
Enzyme 2 Pathways
  • gamma-Hexachlorocyclohexane Degradation (map00361 Link Image)
Enzyme 2 Reactions
  • An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 190192 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P27169 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PON1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1068 bp
ATGGCGAAGCTGATTGCGCTCACCCTCTTGGGGATGGGACTGGCACTCTTCAGGAACCAC
CAGTCTTCTTACCAAACACGACTTAATGCTCTCCGAGAGGTACAACCCGTAGAACTTCCT
AACTGTAATTTAGTTAAAGGAATCGAAACTGGCTCTGAAGACATGGAGATACTGCCTAAT
GGACTGGCTTTCATTAGCTCTGGATTAAAGTATCCTGGAATAAAGAGCTTCAACCCCAAC
AGTCCTGGAAAAATACTTCTGATGGACCTGAATGAAGAAGATCCAACAGTGTTGGAATTG
GGGATCACTGGAAGTAAATTTGATGTATCTTCATTTAACCCTCATGGGATTAGCACATTC
ACAGATGAAGATAATGCCATGTACCTCCTGGTGGTGAACCATCCAGATGCCAAGTCCACA
GTGGAGTTGTTTAAATTTCAAGAAGAAGAAAAATCGCTTTTGCATCTAAAAACCATCAGA
CATAAACTTCTGCCTAATTTGAATGATATTGTTGCTGTGGGACCTGAGCACTTTTATGGC
ACAAATGATCACTATTTTCTTGACCCCTACTTACAATCCTGGGAGATGTATTTGGGTTTA
GCGTGGTCGTATGTTGTCTACTATAGTCCAAGTGAAGTTCGAGTGGTGGCAGAAGGATTT
GATTTTGCTAATGGAATCAACATTTCACCCGATGGCAAGTATGTCTATATAGCTGAGTTG
CTGGCTCATAAGATTCATGTGTATGAAAAGCATGCTAATTGGACTTTAACTCCATTGAAG
TCCCTTGACTTTAATACCCTCGTGGATAACATATCTGTGGATCCTGAGACAGGAGACCTT
TGGGTTGGATGCCATCCCAATGGCATGAAAATCTTCTTCTATGACTCAGAGAATCCTCCT
GCATCAGAGGTGCTTCGAATCCAGAACATTCTAACAGAAGAACCTAAAGTGACACAGGTT
TATGCAGAAAATGGCACAGTGTTGCAAGGCAGTACAGTTGCCTCTGTGTACAAAGGGAAA
CTGCTGATTGGCACAGTGTTTCACAAAGCTCTTTACTGTGAGCTCTAA
Enzyme 2 GenBank Gene ID M63012 Link Image
Enzyme 2 GeneCard ID PON1 Link Image
Enzyme 2 GenAtlas ID PON1 Link Image
Enzyme 2 HGNC ID HGNC:9204 Link Image
Enzyme 2 Chromosome Location 7
Enzyme 2 Locus 7q21.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Hassett C, Richter RJ, Humbert R, Chapline C, Crabb JW, Omiecinski CJ, Furlong CE: Characterization of cDNA clones encoding rabbit and human serum paraoxonase: the mature protein retains its signal sequence. Biochemistry. 1991 Oct 22;30(42):10141-9. [PubMed Link Image]
  2. Adkins S, Gan KN, Mody M, La Du BN: Molecular basis for the polymorphic forms of human serum paraoxonase/arylesterase: glutamine or arginine at position 191, for the respective A or B allozymes. Am J Hum Genet. 1993 Mar;52(3):598-608. [PubMed Link Image]
  3. La Du BN, Adkins S, Kuo CL, Lipsig D: Studies on human serum paraoxonase/arylesterase. Chem Biol Interact. 1993 Jun;87(1-3):25-34. [PubMed Link Image]
  4. Furlong CE, Costa LG, Hassett C, Richter RJ, Sundstrom JA, Adler DA, Disteche CM, Omiecinski CJ, Chapline C, Crabb JW, et al.: Human and rabbit paraoxonases: purification, cloning, sequencing, mapping and role of polymorphism in organophosphate detoxification. Chem Biol Interact. 1993 Jun;87(1-3):35-48. [PubMed Link Image]
  5. Clendenning JB, Humbert R, Green ED, Wood C, Traver D, Furlong CE: Structural organization of the human PON1 gene. Genomics. 1996 Aug 1;35(3):586-9. [PubMed Link Image]
  6. 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]
  7. Blatter MC, James RW, Messmer S, Barja F, Pometta D: Identification of a distinct human high-density lipoprotein subspecies defined by a lipoprotein-associated protein, K-45. Identity of K-45 with paraoxonase. Eur J Biochem. 1993 Feb 1;211(3):871-9. [PubMed Link Image]
  8. Furlong CE, Richter RJ, Chapline C, Crabb JW: Purification of rabbit and human serum paraoxonase. Biochemistry. 1991 Oct 22;30(42):10133-40. [PubMed Link Image]
  9. Gan KN, Smolen A, Eckerson HW, La Du BN: Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities. Drug Metab Dispos. 1991 Jan-Feb;19(1):100-6. [PubMed Link Image]
  10. Sorenson RC, Primo-Parmo SL, Kuo CL, Adkins S, Lockridge O, La Du BN: Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesterase. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7187-91. [PubMed Link Image]
  11. Humbert R, Adler DA, Disteche CM, Hassett C, Omiecinski CJ, Furlong CE: The molecular basis of the human serum paraoxonase activity polymorphism. Nat Genet. 1993 Jan;3(1):73-6. [PubMed Link Image]
  12. Marchesani M, Hakkarainen A, Tuomainen TP, Kaikkonen J, Pukkala E, Uimari P, Seppala E, Matikainen M, Kallioniemi OP, Schleutker J, Lehtimaki T, Salonen JT: New paraoxonase 1 polymorphism I102V and the risk of prostate cancer in Finnish men. J Natl Cancer Inst. 2003 Jun 4;95(11):812-8. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5324
Enzyme 3 Name Serum paraoxonase/arylesterase 2
Enzyme 3 Synonyms
  1. PON 2
  2. Serum aryldialkylphosphatase 2
  3. A-esterase 2
  4. Aromatic esterase 2
Enzyme 3 Gene Name PON2
Enzyme 3 Protein Sequence >Serum paraoxonase/arylesterase 2
MGAWVGCGLAGDRAGFLGERLLALRNRLKASREVESVDLPHCHLIKGIEAGSEDIDILPN
GLAFFSVGLKFPGLHSFAPDKPGGILMMDLKEEKPRARELRISRGFDLASFNPHGISTFI
DNDDTVYLFVVNHPEFKNTVEIFKFEEAENSLLHLKTVKHELLPSVNDITAVGPAHFYAT
NDHYFSDPFLKYLETYLNLHWANVVYYSPNEVKVVAEGFDSANGINISPDDKYIYVADIL
AHEIHVLEKHTNMNLTQLKVLELDTLVDNLSIDPSSGDIWVGCHPNGQKLFVYDPNNPPS
SEVLRIQNILCEKPTVTTVYANNGSVLQGSSVASVYDGKLLIGTLYHRALYCEL
Enzyme 3 Number of Residues 354
Enzyme 3 Molecular Weight 39398
Enzyme 3 Theoretical pI 5.21
Enzyme 3 GO Classification
Function
  • arylesterase activity
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
Component
  • extracellular region
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and a number of aromatic carboxylic acid esters. Has antioxidant activity. Is not associated with high density lipoprotein. Prevents LDL lipid peroxidation, reverses the oxidation of mildly oxidized LDL, and inhibits the ability of MM-LDL to induce monocyte chemotaxis
Enzyme 3 Pathways
  • gamma-Hexachlorocyclohexane Degradation (map00361 Link Image)
Enzyme 3 Reactions
  • An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1333632 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q15165 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PON2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1065 bp
ATGGGGGCCTGGGTGGGCTGTGGGCTTGCTGGGGATCGCGCTGGCTTCCTGGGCGAGAGG
CTTCTGGCACTCAGAAATCGACTTAAAGCCTCCAGAGAAGTAGAATCTGTAGACCTTCCA
CACTGCCACCTGATTAAAGGAATTGAAGCTGGCTCTGAAGATATTGACATACTTCCCAAT
GGTCTGGCTTTTTTTAGTGTGGGTCTAAAATTCCCAGGACTCCACAGCTTTGCACCAGAT
AAGCCTGGAGGAATACTAATGATGGATCTAAAAGAAGAAAAACCAAGGGCACGGGAATTA
AGAATCAGTCGTGGGTTTGATTTGGCCTCATTCAATCCACATGGCATCAGCACTTTCATA
GACAACGATGACACAGTTTATCTCTTTGTTGTAAACCACCCAGAATTCAAGAATACAGTG
GAAATTTTTAAATTTGAAGAAGCAGAAAATTCTCTGTTGCATCTGAAAACAGTCAAACAT
GAGCTTCTTCCAAGTGTGAATGACATCACAGCTGTTGGACCGGCACATTTCTATGCCACA
AATGACCACTACTTCTCTGATCCTTTCTTAAAGTATTTAGGAACATACTTGAACTTACAC
TGGGCAAATGTTGTTTACTACAGTCCAAATGAAGTTAAAGTGGTAGCAGAAGGATTTGAT
TCAGCAAATGGGATCAATATTTCACCTGATGATAAGTATATCTATGTTGCTGACATATTG
GCTCATGAAATTCATGTTTTGGAAAAACACACTAATATGAATTTAACTCAGTTGAAGGTA
CTTGAGCTGGATACACTGGTGGATAATTTATCTATTGATCCTTCCTCGGGGGACATCTGG
GTAGGCTGTCATCCTAATGGCCAGAAGCTCTTCGTGTATGACCCGAACAATCCTCCCTCG
TCAGAGGTTCTCCGCATCCAGAACATTCTATGTGAGAAGCCTACAGTGACTACAGTTTAT
GCCAACAATGGGTCTGTTCTCCAAGGAAGTTCTGTAGCCTCAGTGTATGATGGGAAGCTG
CTCATAGGCACTTTATACCACAGAGCCTTGTATTGTGAACTCTAA
Enzyme 3 GenBank Gene ID L48513 Link Image
Enzyme 3 GeneCard ID PON2 Link Image
Enzyme 3 GenAtlas ID PON2 Link Image
Enzyme 3 HGNC ID HGNC:9205 Link Image
Enzyme 3 Chromosome Location 7
Enzyme 3 Locus 7q21.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Primo-Parmo SL, Sorenson RC, Teiber J, La Du BN: The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family. Genomics. 1996 May 1;33(3):498-507. [PubMed Link Image]
  2. Mochizuki H, Scherer SW, Xi T, Nickle DC, Majer M, Huizenga JJ, Tsui LC, Prochazka M: Human PON2 gene at 7q21.3: cloning, multiple mRNA forms, and missense polymorphisms in the coding sequence. Gene. 1998 Jun 15;213(1-2):149-57. [PubMed Link Image]
  3. 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]
  4. Ng CJ, Wadleigh DJ, Gangopadhyay A, Hama S, Grijalva VR, Navab M, Fogelman AM, Reddy ST: Paraoxonase-2 is a ubiquitously expressed protein with antioxidant properties and is capable of preventing cell-mediated oxidative modification of low density lipoprotein. J Biol Chem. 2001 Nov 30;276(48):44444-9. Epub 2001 Sep 28. [PubMed Link Image]
  5. Hegele RA, Connelly PW, Scherer SW, Hanley AJ, Harris SB, Tsui LC, Zinman B: Paraoxonase-2 gene (PON2) G148 variant associated with elevated fasting plasma glucose in noninsulin-dependent diabetes mellitus. J Clin Endocrinol Metab. 1997 Oct;82(10):3373-7. [PubMed Link Image]
  6. Sanghera DK, Aston CE, Saha N, Kamboh MI: DNA polymorphisms in two paraoxonase genes (PON1 and PON2) are associated with the risk of coronary heart disease. Am J Hum Genet. 1998 Jan;62(1):36-44. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5325
Enzyme 4 Name Intestinal alkaline phosphatase precursor
Enzyme 4 Synonyms
  1. IAP
Enzyme 4 Gene Name ALPI
Enzyme 4 Protein Sequence >Intestinal alkaline phosphatase precursor
MQGPWVLLLLGLRLQLSLGVIPAEEENPAFWNRQAAEALDAAKKLQPIQKVAKNLILFLG
DGLGVPTVTATRILKGQKNGKLGPETPLAMDRFPYLALSKTYNVDRQVPDSAATATAYLC
GVKANFQTIGLSAAARFNQCNTTRGNEVISVMNRAKQAGKSVGVVTTTRVQHASPAGTYA
HTVNRNWYSDADMPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPADA
SQNGIRLDGKNLVQEWLAKHQGAWYVWNRTELMQASLDQSVTHLMGLFEPGDTKYEIHRD
PTLDPSLMEMTEAALRLLSRNPRGFYLFVEGGRIDHGHHEGVAYQALTEAVMFDDAIERA
GQLTSEEDTLTLVTADHSHVFSFGGYTLRGSSIFGLAPSKAQDSKAYTSILYGNGPGYVF
NSGVRPDVNESESGSPDYQQQAAVPLSSETHGGEDVAVFARGPQAHLVHGVQEQSFVAHV
MAFAACLEPYTACDLAPPACTTDAAHPVAASLPLLAGTLLLLGASAAP
Enzyme 4 Number of Residues 528
Enzyme 4 Molecular Weight 56813
Enzyme 4 Theoretical pI 5.70
Enzyme 4 GO Classification
Function
Process
  • metabolism
  • physiological process
Component
Enzyme 4 General Function Inorganic ion transport and metabolism
Enzyme 4 Specific Function A phosphate monoester + H(2)O = an alcohol + phosphate
Enzyme 4 Pathways
  • Folate and Pterine Biosynthesis (map00790 Link Image)
  • gamma-Hexachlorocyclohexane Degradation (map00361 Link Image)
Enzyme 4 Reactions
  • A phosphate monoester + H2O = an alcohol + phosphate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-19
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 178432 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P09923 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PPBI_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1587 bp
ATGCAGGGGCCCTGGGTGCTGCTGCTGCTGGGCCTGAGGCTACAGCTCTCCCTGGGCGTC
ATCCCAGCTGAGGAGGAGAACCCGGCCTTCTGGAACCGCCAGGCAGCTGAGGCCCTGGAT
GCTGCCAAGAAGCTGCAGCCCATCCAGAAGGTCGCCAAGAACCTCATCCTCTTCCTGGGC
GATGGGTTGGGGGTGCCCACGGTGACAGCCACCAGGATCCTAAAGGGGCAGAAGAATGGC
AAACTGGGGCCTGAGACGCCCCTGGCCATGGACCGCTTCCCATACCTGGCTCTGTCCAAG
ACATACAATGTGGACAGACAGGTGCCAGACAGCGCAGCCACAGCCACGGCCTACCTGTGC
GGGGTCAAGGCCAACTTCCAGACCATCGGCTTGAGTGCAGCCGCCCGCTTTAACCAGTGC
AACACGACACGCGGCAATGAGGTCATCTCCGTGATGAACCGGGCCAAGCAAGCAGGAAAG
TCAGTAGGAGTGGTGACCACCACACGGGTGCAGCACGCCTCGCCAGCCGGCACCTACGCA
CACACAGTGAACCGCAACTGGTACTCAGATGCTGACATGCCTGCCTCAGCCCGCCAGGAG
GGGTGCCAGGACATCGCCACTCAGCTCATCTCCAACATGGACATTGACGTGATCCTTGGC
GGAGGCCGCAAGTACATGTTTCCCATGGGGACCCCAGACCCTGAGTACCCAGCTGATGCC
AGCCAGAATGGAATCAGGCTGGACGGGAAGAACCTGGTGCAGGAATGGCTGGCAAAGCAC
CAGGGTGCCTGGTATGTGTGGAACCGCACTGAGCTCATGCAGGCGTCCCTGGACCAGTCT
GTGACCCATCTCATGGGCCTCTTTGAGCCCGGAGACACGAAATATGAGATCCTCCGAGAC
CCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCGCCTGCTGAGCAGG
AACCCCCGCGGCTTCTACCTCTTTGTGGAGGGCGGCCGCATCGACCATGGTCATCATGAG
GGTGTGGCTTACCAGGCAGTCACTGAGGCGGTCATGTTCGACGACGCCATTGAGAGGGCG
GGCCAGCTCACCAGCGAGGAGGACACGCTGACCCTCGTCACCGCTGACCACTCCCATGTC
TTCTCCTTTGGTGGCTACACCTTGCGAGGGAGCTCCATCTTCGGGTTGGCCCCCAGCAAG
GCTCAGGACAGCAAAGCCTACACGTCCATCCTGTACGGCAATGGCCCGGGCTACGTGTTC
AACTCAGGCGTGCGACCAGACGTGAATGAGAGCGAGAGCGGGAGCCCCGATTACCAGCAG
CAGGCGGCGGTGCCCCTGTCGTCCGAGACCCACGGAGGCGAAGACGTGGCGGTGTTTGCG
CGCGGCCCGCAGGCGCACCTGGTGCATGGTGTGCAGGAGCAGAGCTTCGTAGCGCATGTC
ATGGCCTTCGCTGCCTGTCTGGAGCCCTACACGGCCTGCGACCTGGCGCTCCCCGCCTGC
ACCACCGACGCCGCGCACCCAGTTGCCGCGTCGCTGCCACTGCTGGCCGGGACCCTGCTG
CTGCTGGGGGCGTCCGCTGCTCCCTGA
Enzyme 4 GenBank Gene ID M15694 Link Image
Enzyme 4 GeneCard ID ALPI Link Image
Enzyme 4 GenAtlas ID ALPI Link Image
Enzyme 4 HGNC ID HGNC:437 Link Image
Enzyme 4 Chromosome Location 2
Enzyme 4 Locus 2q37.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Berger J, Garattini E, Hua JC, Udenfriend S: Cloning and sequencing of human intestinal alkaline phosphatase cDNA. Proc Natl Acad Sci U S A. 1987 Feb;84(3):695-8. [PubMed Link Image]
  2. Henthorn PS, Raducha M, Edwards YH, Weiss MJ, Slaughter C, Lafferty MA, Harris H: Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1234-8. [PubMed Link Image]
  3. Henthorn PS, Raducha M, Kadesch T, Weiss MJ, Harris H: Sequence and characterization of the human intestinal alkaline phosphatase gene. J Biol Chem. 1988 Aug 25;263(24):12011-9. [PubMed Link Image]
  4. Millan JL: Promoter structure of the human intestinal alkaline phosphatase gene. Nucleic Acids Res. 1987 Dec 23;15(24):10599. [PubMed Link Image]
  5. Knoll BJ, Rothblum KN, Longley M: Two gene duplication events in the evolution of the human heat-stable alkaline phosphatases. Gene. 1987;60(2-3):267-76. [PubMed Link Image]
  6. Hua JC, Berger J, Pan YC, Hulmes JD, Udenfriend S: Partial sequencing of human adult, human fetal, and bovine intestinal alkaline phosphatases: comparison with the human placental and liver isozymes. Proc Natl Acad Sci U S A. 1986 Apr;83(8):2368-72. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5326
Enzyme 5 Name Lysosomal acid phosphatase precursor
Enzyme 5 Synonyms
  1. LAP
Enzyme 5 Gene Name ACP2
Enzyme 5 Protein Sequence >Lysosomal acid phosphatase precursor
MAGKRSGWSRAALLQLLLGVNLVVMPPTRARSLRFVTLLYRHGDRSPVKTYPKDPYQEEE
WPQGFGQLTKEGMLQHWELGQALRQRYHGFLNTSYHRQEVYVRSTDFDRTLMSAEANLAG
LFPPNGMQRFNPNISWQPIPVHTVPITEDRLLKFPLGPCPRYEQLQNETRQTPEYQNESS
RNAQFLDMVANETGLTDLTLETVWNVYDTLFCEQTHGLRLPPWASPQTMQRLSRLKDFSF
RFLFGIYQQAEKARLQGGVLLAQIRKNLTLMATTSQLPKLLVYSAHDTTLVALQMALDVY
NGEQAPYASCHIFELYQEDSGNFSVEMYFRNESDKAPWPLSLPGCPHRCPLQDFLRLTEP
VVPKDWQQECQLASGPADTEVIVALAVCGSILFLLIVLLLTVLFRMQAQPPGYRHVADGE
DHA
Enzyme 5 Number of Residues 423
Enzyme 5 Molecular Weight 48345
Enzyme 5 Theoretical pI 6.73
Enzyme 5 GO Classification
Function
  • acid phosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
Component
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function A phosphate monoester + H(2)O = an alcohol + phosphate
Enzyme 5 Pathways
Enzyme 5 Reactions
  • A phosphate monoester + H2O = an alcohol + phosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-30
Enzyme 5 Transmembrane Regions
  • 382-404
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 34263 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P11117 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PPAL_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1272 bp
ATGGCGGGCAAGCGGTCCGGCTGGAGCCGGGCGGCTCTCCTCCAGCTCCTTCTCGGCGTG
AACCTGGTGGTGATGCCGCCCACCCGGGCCCGGAGTCTGCGCTTCGTTACCTTGCTGTAC
CGCCATGGAGACCGTTCACCAGTGAAGACATATCCCAAGGACCCCTATCAGGAAGAAGAA
TGGCCCCAGGGGTTTGGTCAGTTAACCAAGGAGGGGATGCTACAGCACTGGGAACTGGGC
CAGGCCCTGCGGCAGCGCTATCACGGCTTCCTAAACACCTCTTATCACCGGCAAGAGGTT
TATGTGCGAAGCACAGACTTTGACCGGACTCTCATGAGTGCTGAGGCCAACCTGGCTGGA
CTCTTCCCTCCCAACGGGATGCAGCGCTTCAACCCGAACATCTCGTGGCAGCCTATTCCT
GTGCACACTGTGCCCATCACTGAGGACAGGCTGCTGAAGTTCCCGTTGGGCCCATGTCCC
CGTTATGAGCAGCTGCAGAACGAGACCCGGCAGACACCAGAGTATCAGAATGAGAGTTCT
CGGAATGCACAATTTCTGGACATGGTGGCCAACGAGACAGGGCTTACAGACCTGACACTG
GAGACCGTCTGGAATGTCTATGACACACTCTTCTGTGAGCAAACGCACGGGCTGCGCCTG
CCGCCCTGGGCCTCACCCCAAACCATGCAGCGTCTCAGCCGGCTAAAGGACTTCAGCTTC
CGCTTCCTCTTCGGAATCTACCAGCAGGCGGAGAAGGCCCGGCTTCAGGGGGGAGTCCTG
CTGGCTCAGATAAGGAAGAACCTGACCCTAATGGCGACCACCTCCCAGCTCCCCAAGCTG
CTGGTTTACTCTGCGCACGACACTACCCTGGTTGCCCTGCAAATGGCACTGGATGTCTAC
AATGGTGAACAAGCCCCCTACGCCTCCTGCCACATATTTGAACTGTACCAGGAAGATTCT
GGGAATTTCTCAGTGGAGATGTACTTTCGGAACGAGAGTGACAAGGCCCCCTGGCCGCTC
AGCCTGCCTGGCTGCCCTCACCGCTGCCCACTGCAGGACTTCCTTCGCCTCACAGAGCCC
GTCGTGCCCAAGGATTGGCAGCAGGAGTGCCAGCTGGCAAGCGGTCCTGCAGACACAGAG
GTGATTGTGGCCTTGGCTGTATGTGGCTCCATCCTCTTCCTCCTCATAGTGCTGCTCCTC
ACCGTCCTCTTCCGGATGCAGGCCCAGCCTCCTGGCTACCGCCACGTCGCAGATGGGGAG
GACCACGCCTGA
Enzyme 5 GenBank Gene ID X12548 Link Image
Enzyme 5 GeneCard ID ACP2 Link Image
Enzyme 5 GenAtlas ID ACP2 Link Image
Enzyme 5 HGNC ID HGNC:123 Link Image
Enzyme 5 Chromosome Location 11
Enzyme 5 Locus 11p11.2-p11.11|11p12-p11
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Pohlmann R, Krentler C, Schmidt B, Schroder W, Lorkowski G, Culley J, Mersmann G, Geier C, Waheed A, Gottschalk S, et al.: Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment. EMBO J. 1988 Aug;7(8):2343-50. [PubMed Link Image]
  2. Geier C, von Figura K, Pohlmann R: Structure of the human lysosomal acid phosphatase gene. Eur J Biochem. 1989 Aug 15;183(3):611-6. [PubMed Link Image]
  3. Nadler HL, Egan TJ: Deficiency of lysosomal acid phosphatase. A new familial metabolic disorder. N Engl J Med. 1970 Feb 5;282(6):302-7. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5328
Enzyme 6 Name Alkaline phosphatase, tissue-nonspecific isozyme precursor
Enzyme 6 Synonyms
  1. AP-TNAP
  2. TNSALP
  3. Alkaline phosphatase liver/bone/kidney isozyme
Enzyme 6 Gene Name ALPL
Enzyme 6 Protein Sequence >Alkaline phosphatase, tissue-nonspecific isozyme precursor
MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGD
GMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCG
VKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAH
SADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDE
KARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELN
RNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIG
QAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPG
YKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYV
PHVMAYAACIGANLGHCAPASSAGSLAAGPLLLALALYPLSVLF
Enzyme 6 Number of Residues 524
Enzyme 6 Molecular Weight 57305
Enzyme 6 Theoretical pI 6.66
Enzyme 6 GO Classification
Function
Process
  • metabolism
  • physiological process
Component
Enzyme 6 General Function Inorganic ion transport and metabolism
Enzyme 6 Specific Function This isozyme may play a role in skeletal mineralization
Enzyme 6 Pathways
  • Folate and Pterine Biosynthesis (map00790 Link Image)
  • gamma-Hexachlorocyclohexane Degradation (map00361 Link Image)
Enzyme 6 Reactions
  • A phosphate monoester + H2O = an alcohol + phosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-17
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 28738 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P05186 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PPBT_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1575 bp
ATGATTTCACCATTCTTAGTACTGGCCATTGGCACCTGCCTTACTAACTCCTTAGTGCCA
GAGAAAGAGAAAGACCCCAAGTACTGGCGAGACCAAGCGCAAGAGACACTGAAATATGCC
CTGGAGCTTCAGAAGCTCAACACCAACGTGGCTAAGAATGTCATCATGTTCCTGGGAGAT
GGGATGGGTGTCTCCACAGTGACGGCTGCCCGCATCCTCAAGGGTCAGCTCCACCACAAC
CCTGGGGAGGAGACCAGGCTGGAGATGGACAAGTTCCCCTTCGTGGCCCTCTCCAAGACG
TACAACACCAAAGCCCAGGTCCCTGACAGCGCCGGCACCGCCACCGCCTACCTGTGTGGG
GTGAAGGCCAATGAGGGCACCGTGGGGGTAAGCGCAGCCACTGAGCGTTCCCGGTGCAAC
ACCACCCAGGGGAACGAGGTCACCTCCATCCTGCGCTGGGCCAAGGACGCTGGGAAATCT
GTGGGCATTGTGACCACCACGAGAGTGAACCATGCCACCCCCAGCGCCGCCTACGCCCAC
TCGGCTGACCGGGACTGGTACTCAGACAACGAGATGCCCCCTGAGGCCTTGAGCCAGGGC
TGTAAGGACATCGCCTACCAGCTCATGCATAACATCAGGGACATTGACGTGATCATGGGG
GGTGGCCGGAAATACATGTACCCCAAGAATAAAACTGATGTGGAGTATGAGAGTGACGAG
AAAGCCAGGGGCACGAGGCTGGACGGCCTGGACCTCGTTGACACCTGGAAGAGCTTCAAA
CCGAGACACAAGCACTCCCACTTCATCTGGAACCGCACGGAACTCCTGACCCTTGACCCC
CACAATGTGGACTACCTATTGGGTCTCTTCGAGCCGGGGGACATGCAGTACGAGCTGAAC
AGGAACAACGTGACGGACCCGTCACTCTCCGAGATGGTGGTGGTGGCCATCCAGATCCTG
CGGAAGAACCCCAAAGGCTTCTTCTTGCTGGTGGAAGGAGGCAGAATTGACCACGGGCAC
CATGAAGGAAAAGCCAAGCAGGCCCTGCATGAGGCGGTGGAGATGGACCGGGCCATCGGG
CAGGCAGGCAGCTTGACCTCCTCGGAAGACACTCTGACCGTGGTCACTGCGGACCATTCC
CACGTCTTCACATTTGGTGGATACACCCCCCGTGGCAACTCTATCTTTGGTCTGGCCCCC
ATGCTGAGTGACACAGACAAGAAGCCCTTCACTGCCATCCTGTATGGCAATGGGCCTGGC
TACAAGGTGGTGGGCGGTGAACGAGAGAATGTCTCCATGGTGGACTATGCTCACAACAAC
TACCAGGCGCAGTCTGCTGTGCCCCTGCGCCACGAGACCCACGGCGGGGAGGACGTGGCC
GTCTTCTCCAAGGGCCCCATGGCGCACCTGCTGCACGGCGTCCACGAGCAGAACTACGTC
CCCCACGTGATGGCGTATGCAGCCTGCATCGGGGCCAACCTCGGCCACTGTGCTCCTGCC
AGCTCGGCAGGCAGCCTTGCTGCAGGCCCCCTGCTGCTCGCGCTGGCCCTCTACCCCCTG
AGCGTCCTGTTCTGA
Enzyme 6 GenBank Gene ID X14174 Link Image
Enzyme 6 GeneCard ID ALPL Link Image
Enzyme 6 GenAtlas ID ALPL Link Image
Enzyme 6 HGNC ID HGNC:438 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 1p36.1-p34
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Kishi F, Matsuura S, Kajii T: Nucleotide sequence of the human liver-type alkaline phosphatase cDNA. Nucleic Acids Res. 1989 Mar 11;17(5):2129. [PubMed Link Image]
  2. Weiss MJ, Henthorn PS, Lafferty MA, Slaughter C, Raducha M, Harris H: Isolation and characterization of a cDNA encoding a human liver/bone/kidney-type alkaline phosphatase. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7182-6. [PubMed Link Image]
  3. Weiss MJ, Ray K, Henthorn PS, Lamb B, Kadesch T, Harris H: Structure of the human liver/bone/kidney alkaline phosphatase gene. J Biol Chem. 1988 Aug 25;263(24):12002-10. [PubMed Link Image]
  4. Garattini E, Hua JC, Pan YC, Udenfriend S: Human liver alkaline phosphatase, purification and partial sequencing: homology with the placental isozyme. Arch Biochem Biophys. 1986 Mar;245(2):331-7. [PubMed Link Image]
  5. Weiss MJ, Cole DE, Ray K, Whyte MP, Lafferty MA, Mulivor RA, Harris H: A missense mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia. Proc Natl Acad Sci U S A. 1988 Oct;85(20):7666-9. [PubMed Link Image]
  6. Henthorn PS, Raducha M, Fedde KN, Lafferty MA, Whyte MP: Different missense mutations at the tissue-nonspecific alkaline phosphatase gene locus in autosomal recessively inherited forms of mild and severe hypophosphatasia. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9924-8. [PubMed Link Image]
  7. Greenberg CR, Taylor CL, Haworth JC, Seargeant LE, Philipps S, Triggs-Raine B, Chodirker BN: A homoallelic Gly317-->Asp mutation in ALPL causes the perinatal (lethal) form of hypophosphatasia in Canadian mennonites. Genomics. 1993 Jul;17(1):215-7. [PubMed Link Image]
  8. Ozono K, Yamagata M, Michigami T, Nakajima S, Sakai N, Cai G, Satomura K, Yasui N, Okada S, Nakayama M: Identification of novel missense mutations (Phe310Leu and Gly439Arg) in a neonatal case of hypophosphatasia. J Clin Endocrinol Metab. 1996 Dec;81(12):4458-61. [PubMed Link Image]
  9. Goseki-Sone M, Orimo H, Iimura T, Takagi Y, Watanabe H, Taketa K, Sato S, Mayanagi H, Shimada T, Oida S: Hypophosphatasia: identification of five novel missense mutations (G507A, G705A, A748G, T1155C, G1320A) in the tissue-nonspecific alkaline phosphatase gene among Japanese patients. Hum Mutat. 1998;Suppl 1:S263-7. [PubMed Link Image]
  10. Sugimoto N, Iwamoto S, Hoshino Y, Kajii E: A novel missense mutation of the tissue-nonspecific alkaline phosphatase gene detected in a patient with hypophosphatasia. J Hum Genet. 1998;43(3):160-4. [PubMed Link Image]
  11. Zurutuza L, Muller F, Gibrat JF, Taillandier A, Simon-Bouy B, Serre JL, Mornet E: Correlations of genotype and phenotype in hypophosphatasia. Hum Mol Genet. 1999 Jun;8(6):1039-46. [PubMed Link Image]
  12. Taillandier A, Zurutuza L, Muller F, Simon-Bouy B, Serre JL, Bird L, Brenner R, Boute O, Cousin J, Gaillard D, Heidemann PH, Steinmann B, Wallot M, Mornet E: Characterization of eleven novel mutations (M45L, R119H, 544delG, G145V, H154Y, C184Y, D289V, 862+5A, 1172delC, R411X, E459K) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with severe hypophosphatasia. Mutations in brief no. 217. Online. Hum Mutat. 1999;13(2):171-2. [PubMed Link Image]
  13. Mochizuki H, Saito M, Michigami T, Ohashi H, Koda N, Yamaguchi S, Ozono K: Severe hypercalcaemia and respiratory insufficiency associated with infantile hypophosphatasia caused by two novel mutations of the tissue-nonspecific alkaline phosphatase gene. Eur J Pediatr. 2000 May;159(5):375-9. [PubMed Link Image]
  14. Taillandier A, Cozien E, Muller F, Merrien Y, Bonnin E, Fribourg C, Simon-Bouy B, Serre JL, Bieth E, Brenner R, Cordier MP, De Bie S, Fellmann F, Freisinger P, Hesse V, Hennekam RC, Josifova D, Kerzin-Storrar L, Leporrier N, Zabot MT, Mornet E: Fifteen new mutations (-195C>T, L-12X, 298-2A>G, T117N, A159T, R229S, 997+2T>A, E274X, A331T, H364R, D389G, 1256delC, R433H, N461I, C472S) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with hypophosphatasia. Hum Mutat. 2000 Mar;15(3):293. [PubMed Link Image]
  15. Muller HL, Yamazaki M, Michigami T, Kageyama T, Schonau E, Schneider P, Ozono K: Asp361Val Mutant of alkaline phosphatase found in patients with dominantly inherited hypophosphatasia inhibits the activity of the wild-type enzyme. J Clin Endocrinol Metab. 2000 Feb;85(2):743-7. [PubMed Link Image]
  16. Lia-Baldini AS, Muller F, Taillandier A, Gibrat JF, Mouchard M, Robin B, Simon-Bouy B, Serre JL, Aylsworth AS, Bieth E, Delanote S, Freisinger P, Hu JC, Krohn HP, Nunes ME, Mornet E: A molecular approach to dominance in hypophosphatasia. Hum Genet. 2001 Jul;109(1):99-108. [PubMed Link Image]
  17. Taillandier A, Lia-Baldini AS, Mouchard M, Robin B, Muller F, Simon-Bouy B, Serre JL, Bera-Louville A, Bonduelle M, Eckhardt J, Gaillard D, Myhre AG, Kortge-Jung S, Larget-Piet L, Malou E, Sillence D, Temple IK, Viot G, Mornet E: Twelve novel mutations in the tissue-nonspecific alkaline phosphatase gene (ALPL) in patients with various forms of hypophosphatasia. Hum Mutat. 2001;18(1):83-4. [PubMed Link Image]
  18. Watanabe H, Hashimoto-Uoshima M, Goseki-Sone M, Orimo H, Ishikawa I: A novel point mutation (C571T) in the tissue-non-specific alkaline phosphatase gene in a case of adult-type hypophosphatasia. Oral Dis. 2001 Nov;7(6):331-5. [PubMed Link Image]
  19. Litmanovitz, Reish O, Dolfin T, Arnon S, Regev R, Grinshpan G, Yamazaki M, Ozono K: Glu274Lys/Gly309Arg mutation of the tissue-nonspecific alkaline phosphatase gene in neonatal hypophosphatasia associated with convulsions. J Inherit Metab Dis. 2002 Feb;25(1):35-40. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5329
Enzyme 7 Name Tartrate-resistant acid phosphatase type 5 precursor
Enzyme 7 Synonyms
  1. TR- AP
  2. Tartrate-resistant acid ATPase
  3. TrATPase
  4. Acid phosphatase 5, tartrate resistant
Enzyme 7 Gene Name ACP5
Enzyme 7 Protein Sequence >Tartrate-resistant acid phosphatase type 5 precursor
MDMWTALLILQALLLPSLADGATPALRFVAVGDWGGVPNAPFHTAREMANAKEIARTVQI
LGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRKVPWYVLAGNHDHLGNVSAQ
IAYSKISKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKL
ARTQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGH
DHNLQYLQDENGVGYVLSGAGNFMDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSK
EMTVTYIEASGKSLFKTRLPRRARP
Enzyme 7 Number of Residues 325
Enzyme 7 Molecular Weight 36599
Enzyme 7 Theoretical pI 8.95
Enzyme 7 GO Classification
Function
  • acid phosphatase activity
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • iron ion binding
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
  • transition metal ion binding
Process
Component
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function A phosphate monoester + H(2)O = an alcohol + phosphate
Enzyme 7 Pathways
Enzyme 7 Reactions
  • A phosphate monoester + H2O = an alcohol + phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-21
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 178006 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P13686 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PPA5_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >972 bp
ATGGACATGTGGACGGCGCTGCTCATCCTGCAAGCCTTGTTGCTACCCTCCCTGGCTGAT
GGTGCCACCCCTGCCCTGCGCTTTGTAGCCGTGGGTGACTGGGGAGGGGTCCCCAATGCC
CCATTCCACACGGGCCCGGAAATGGCCAATGCCAAGGAGATCGCTCGGACTGTGCAGATC
CTGGGTGCAGACTTCATCCTGTCTCTAGGGGACAATTTTTACTTCACTGGTGTGCAAGAC
ATCAATGACAAGAGGTTCCAGGAGACCTTTGAGGACGTATTCTCTGACCGCTCCCTTCGC
AAAGTGCCCTGGTACGTGCTAGCCGGAAACCATGACCACCTTGGCAATGTCTCTGCCCAG
ATTGCATACTCTAAGATCTCCAAGCGCTGGAACTTCCCCAGCCCTTTCTACCGCCTGCAC
TTCAAGATCCCACAGACCAATGTGTCTGTGGCCATTTTTATGCTGGACACAGTGACACTA
TGTGGCAACTCAGATGACTTCCTCAGCCAGCAGCCTGAGAGGCCCCGACTAACTGCCCGC
ACACAGCTGTCCTGGCTCAAGAAACAGCTGGCGGCGGCCAGGGAGGACTACGTGCTGGTG
GCTGGCCACTACCCCGTGTGGTCCATAGCCGAGCACGGGCCTACCCACTGCCTGGTCAAG
CAGCTACGGCCACTGCTGGCCACATACGGGGTCACTGCCTACCTGTGCGGCCACGATCAC
AATCTGCAGTACCTGCAAGATGAGAATGGCGTGGGCTACGTGCTGAGTGGGGCTGGGAAT
TTCATGGACCCCTCAAAGCGGCACCAGCGCAAGGTCCCCAACGGCTATCTGCGCTTCCAC
TATGGGACTGAAGACTCACTGGGTGGCTTTGCCTATGTGGAGATCAGCTCCAAAGAGATG
ACTGTCACTTACATCGAGGCCTCGGGCAAGTCCCTCTTTAAGACCAGGCTGCCGAGGCGA
GCCAGGCCCTGA
Enzyme 7 GenBank Gene ID J04430 Link Image
Enzyme 7 GeneCard ID ACP5 Link Image
Enzyme 7 GenAtlas ID ACP5 Link Image
Enzyme 7 HGNC ID HGNC:124 Link Image
Enzyme 7 Chromosome Location 19
Enzyme 7 Locus 19p13.3-p13.2
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Ketcham CM, Roberts RM, Simmen RC, Nick HS: Molecular cloning of the type 5, iron-containing, tartrate-resistant acid phosphatase from human placenta. J Biol Chem. 1989 Jan 5;264(1):557-63. [PubMed Link Image]
  2. Lord DK, Cross NC, Bevilacqua MA, Rider SH, Gorman PA, Groves AV, Moss DW, Sheer D, Cox TM: Type 5 acid phosphatase. Sequence, expression and chromosomal localization of a differentiation-associated protein of the human macrophage. Eur J Biochem. 1990 Apr 30;189(2):287-93. [PubMed Link Image]
  3. Cassady AI, King AG, Cross NC, Hume DA: Isolation and characterization of the genes encoding mouse and human type-5 acid phosphatase. Gene. 1993 Aug 25;130(2):201-7. [PubMed Link Image]
  4. Stepan JJ, Lau KH, Mohan S, Kraenzlin M, Baylink DJ: Purification and N-terminal sequence of two tartrate-resistant acid phosphatases type-5 from the hairy cell leukemia spleen. Biochem Biophys Res Commun. 1989 Dec 29;165(3):1027-34. [PubMed Link Image]
  5. Stepan JJ, Lau KH, Mohan S, Singer FR, Baylink DJ: Purification and N-terminal amino acid sequence of the tartrate-resistant acid phosphatase from human osteoclastoma: evidence for a single structure. Biochem Biophys Res Commun. 1990 Apr 30;168(2):792-800. [PubMed Link Image]
  6. Hayman AR, Warburton MJ, Pringle JA, Coles B, Chambers TJ: Purification and characterization of a tartrate-resistant acid phosphatase from human osteoclastomas. Biochem J. 1989 Jul 15;261(2):601-9. [PubMed Link Image]
  7. Hayman AR, Dryden AJ, Chambers TJ, Warburton MJ: Tartrate-resistant acid phosphatase from human osteoclastomas is translated as a single polypeptide. Biochem J. 1991 Aug 1;277 ( Pt 3):631-4. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5331
Enzyme 8 Name Alkaline phosphatase, placental-like precursor
Enzyme 8 Synonyms
  1. Alkaline phosphatase Nagao isozyme
  2. Germ-cell alkaline phosphatase
  3. GCAP
  4. PLAP-like
  5. ALP-1
Enzyme 8 Gene Name ALPPL2
Enzyme 8 Protein Sequence >Alkaline phosphatase, placental-like precursor
MQGPWVLLLLGLRLQLSLGIIPVEEENPDFWNRQAAEALGAAKKLQPAQTAAKNLIIFLG
DGMGVSTVTAARILKGQKKDKLGPETFLAMDRFPYVALSKTYSVDKHVPDSGATATAYLC
GVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGAYA
HTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPDDY
SQGGTRLDGKNLVQEWLAKHQGARYVWNRTELLQASLDPSVTHLMGLFEPGDMKYEIHRD
STLDPSLMEMTEAALLLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAIERA
GQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYVL
KDGARPDVTESESGSPEYRQQSAVPLDGETHAGEDVAVFARGPQAHLVHGVQEQTFIAHV
MAFAACLEPYTACDLAPRAGTTDAAHPGPSVVPALLPLLAGTLLLLGTATAP
Enzyme 8 Number of Residues 532
Enzyme 8 Molecular Weight 57378
Enzyme 8 Theoretical pI 6.31
Enzyme 8 GO Classification
Function
Process
  • metabolism
  • physiological process
Component
Enzyme 8 General Function Inorganic ion transport and metabolism
Enzyme 8 Specific Function A phosphate monoester + H(2)O = an alcohol + phosphate
Enzyme 8 Pathways
  • Folate and Pterine Biosynthesis (map00790 Link Image)
  • gamma-Hexachlorocyclohexane Degradation (map00361 Link Image)
Enzyme 8 Reactions
  • A phosphate monoester + H2O = an alcohol + phosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-19
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 178428 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P10696 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PPBN_HUMAN Link Image
Enzyme 8 PDB ID 1EW2 Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1599 bp
ATGCAGGGGCCCTGGGTGCTGCTCCTGCTGGGCCTGAGGCTACAGCTCTCCCTGGGCATC
ATCCCAGTTGAGGAGGAGAACCCGGACTTCTGGAACCGCCAGGCAGCCGAGGCCCTGGGT
GCCGCCAAGAAGCTGCAGCCTGCACAGACAGCCGCCAAGAACCTCATCATGTTCCTGGGT
GACGGGATGGGGGTGTCTACGGTGACAGCTGCCAGGATCCTAAAAGGGCAGAAGAAGGAC
AAACTGGGGCCTGAGACCTTCCTGGCCATGGACCGCTTCCCGTACGTGGCTCTGTCCAAG
ACATACAGTGTAGACAAGCATGTGCCAGACAGTGGAGCCACAGCCACGGCCTACCTGTGC
GGGGTCAAGGGCAACTTCCAGACCATTGGCTTGAGTGCAGCCGCCCGCTTTAACCAGTGC
AACACGACACGCGGCAACGAGGTCATCTCCGTGGTGAATCGGGCCAAGAAAGCAGGAAAG
TCAGTGGGAGTGGTAACCACCACACGGGTGCAGCATGCCTCGCCAGCCGGCACCTACGCC
CACACGGTGAACCGCAACTGGTACTCGGATGCCGACGTGCCTGCCTCGGCCCGCCAGGAG
GGGTGCCAGGACATCGCCACGCAGCTCATCTCCAACATGGACATTGATGTGATCCTAGGT
GGAGGCCGAAAGTACATGTTTCCCATGGGGACCCCAGACCCTGAGTACCCAGATGACTAC
AGCCAAGGTGGGACCAGGCTGGACGGGAAGAATCTGGTGCAGGAATGGCTGGCGAAGCAC
CAGGGTGCCCGGTACGTGTGGAACCGCACTGAGCTCCTGCAGGCTTCCCTGGACCCGTCT
GTGACCCATCTCATGGGTCTCTTTGAGCCTGGAGACATGAAATACGAGATCCACCGAGAC
TCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCTCCTGCTGAGCAGG
AACCCCCGCGGCTTCTTCCTCTTCGTGGAGGGTGGTCGCATCGACCATGGTCATCATGAA
AGCAGGGCTTACCGGGCACTGACTGAGACGATCATGTTCGACGACGCCATTGAGAGGGCG
GGCCAGCTCACCAGCGAGGAGGACACGCTGAGCCTCGTCACTGCCGACCACTCCCACGTC
TTCTCCTTCGGAGGCTACCCCCTGCGAGGGAGCTCCATCTTCGGGCTGGCCCCTGGCAAG
GCCCGGGACAGGAAGGCCTACACGGTCCTCCTATACGGAAACGGTCCAGGCTATGTGCTC
AAGGACGGCGCCCGGCCGGATGTTACGGAGAGCGAGAGCGGGAGCCCCGAGTATCGGCAG
CAGTCAGCAGTGCCCCTGGACGGAGAGACCCACGCAGGCGAGGACGTGGCGGTGTTCGCG
CGCGGCCCGCAGGCGCACCTGGTTCACGGCGTGCAGGAGCAGACCTTCATAGCGCACGTC
ATGGCCTTCGCCGCCTGCCTGGAGCCCTACACCGCCTGCGACCTGGCGCCCCCCGCCGGC
ACCACCGACGCCGCGCACCCGGGGCCGTCCGTGGTCCCCGCGTTGCTTCCTCTGCTGGCA
GGGACCTTGCTGCTGCTGGGGACGGCCACTGCTCCCTGA
Enzyme 8 GenBank Gene ID J03252 Link Image
Enzyme 8 GeneCard ID ALPPL2 Link Image
Enzyme 8 GenAtlas ID ALPPL2 Link Image
Enzyme 8 HGNC ID HGNC:441 Link Image
Enzyme 8 Chromosome Location 2
Enzyme 8 Locus 2q37
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Millan JL, Manes T: Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline phosphatase gene. Proc Natl Acad Sci U S A. 1988 May;85(9):3024-8. [PubMed Link Image]
  2. Watanabe S, Watanabe T, Li WB, Soong BW, Chou JY: Expression of the germ cell alkaline phosphatase gene in human choriocarcinoma cells. J Biol Chem. 1989 Jul 25;264(21):12611-9. [PubMed Link Image]
  3. Gum JR, Hicks JW, Sack TL, Kim YS: Molecular cloning of complementary DNAs encoding alkaline phosphatase in human colon cancer cells. Cancer Res. 1990 Feb 15;50(4):1085-91. [PubMed Link Image]
  4. Lowe ME, Strauss AW: Expression of a Nagao-type, phosphatidylinositol-glycan anchored alkaline phosphatase in human choriocarcinomas. Cancer Res. 1990 Jul 1;50(13):3956-62. [PubMed Link Image]
  5. Shen LP, Liu H, Kan YW, Kam W: 5' nucleotide sequence of a putative human placental alkaline phosphatase-like gene. Nucleic Acids Res. 1988 Jun 24;16(12):5694. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5532
Enzyme 9 Name Aldehyde dehydrogenase X, mitochondrial precursor
Enzyme 9 Synonyms
  1. Aldehyde dehydrogenase family 1 member B1
  2. ALDH class 2
Enzyme 9 Gene Name ALDH1B1
Enzyme 9 Protein Sequence >Aldehyde dehydrogenase X, mitochondrial precursor
MLRFLAPRLLSLQGRTARYSSAAALPSPILNPDIPYNQLFINNEWQDAVSKKTFPTVNPT
TGEVIGHVAEGDRADVDRAVKAAREAFRLGSPWRRMDASERGRLLNLLADLVERDRVYLA
SLETLDNGKPFQESYALDLDEVIKVYRYFAGWADKWHGKTIPMDGQHFCFTRHEPVGVCG
QIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITG
YGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGDSNLKRVTLELGGKSPSIVLADADM
EHAVEQCHEALFFNMGQCCCAGSRTFVEESIYNEFLERTVEKAKQRKVGNPFELDTQQGP
QVDKEQFERVLGYIQLGQKEGAKLLCGGERFGERGFFIKPTVFGGVQDDMRIAKEEIFGP
VQPLFKFKKIEEVVERANNTRYGLAAAVFTRDLDKAMYFTQALQAGTVWVNTYNIVTCHT
PFGGFKESGNGRELGEDGLKAYTEVKTVTIKVPQKNS
Enzyme 9 Number of Residues 517
Enzyme 9 Molecular Weight 57239
Enzyme 9 Theoretical pI 6.79
Enzyme 9 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 9 General Function Energy production and conversion
Enzyme 9 Specific Function ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation
Enzyme 9 Pathways
Enzyme 9 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-22
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 1263008 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P30837 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name AL1B1_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1554 bp
ATGCTGCGCTTCCTGGCACCCCGGCTGCTTAGCCTCCAGGGCAGGACCGCCCTCTACTCC
TCGGCAGCAGCCCTCCCAAGCCCCATTCTGAACCCAGACATCCCCTACAACCAGCTGTTC
ATCAACAATGAATGGCAAGATGCAGTCAGCAAGAAGACCTTCCCGACGGTCAACCCTACC
ACCGGGGAGGTCATCGGGCACGTGGCTGAAGGTGACCGGGCTGATGTGGATCGGGCCGTG
AAAGCAGCCCGGGAAGCCTTCCGCCTGGGGTCCCCATGGCGCCGGATGGATGCCTCTGAG
CGGGGCCGGCTGCTGAACCTCCTGGCAGACCTAGTGGAGCGGGATCGAGTCTACTTGGCC
TCACTCGAGACCTTGGACAATGGGAAGCCTTTCCAAGAGTCTTACGCCTTGGACTTGGAT
GAGGTCATCAAGGTGTATCGGTACTTTGCTGGCTGGGCTGACAAGTGGCATGGCAAGACC
ATCCCCATGCATGGCCAGCATTTCTGCTTCACCCGGCATGAGCCCGTTGGTGTCTGTGGC
CAGATCATCCCGTGGAACTTCCCCTTGGTCATGCAGGGTTGGAAACTTGCCCCGGCACTC
GCCACAGGCAACACTGTGGTTATGAAGGTGGCAGAGCAGACCCCCCTCTCTGCCCTGTAT
TTGGCCTCCCTCATCAAGGAGGCAGGCTTTCCCCCTGGGGTGGTGAACATCATCACGGGG
TATGGCCCAACAGCAGGTGCGGCCATCGCCCAGCACATGGATGTTGACAAAGTTGCCTTC
ACCGGTTCCACCGAGGTGGGCCACCTGATCCAGAAAGCAGCTGGCGATTCCAACCTCAAG
AGAGTCACCCTGGAGCTGGGTGGTAAGAGCCCCAGCATCGTGCTGGCCGATGCTGACATG
GAGCATGCCGTGGAGCAGTGCCACGAAGCCCTGTTCTTCAACATGGGCCAGTGCTGCTGT
GCTGGCTCCCGGACCTTCGTGGAAGAATCCATCTACAATGAGTTTCTCGAGAGAACCGTG
GAGAAAGCAAAGCAGAGGAAAGTGGGGAACCCCTTTGAGCTGGACACCCAGCAGGGGCCT
CAGGTGGACAAGGAGCAGTTTGAACGAGTCCTAGGCTACATCCAGCTTGGCCAGAAGGAG
GGCGCAAAACTCCTCTGTGGCGGAGAGCGTTTCGGGGAGCGTGGTTTCTTCATCAAGCCT
ACTGTCTTTGGTGGCGTGCAGGATGACATGAGAATTGCCAAAGAGGAGATCTTTGGGCCT
GTGCAGCCCCTGTTCAAGTTCAAGAAGATTGAGGAGGTGGTTGAGAGGGCCAACAACACC
AGGTATGGCCTGGCTGCGGCTGTGTTCACCCGGGATCTGGACAAGGCCATGTACTTCACC
CAGGCACTCCAGGCCGGGACCGTGTGGGTAAACACCTACAACATCGTCACCTGCCACACG
CCATTTGGAGGGTTTAAGGAATCTGGAAACGGGAGGGAGCTGGGTGAGGATGGGCTTAAG
GCCTACACAGAGGTAAAGACGGTCACCATCAAGGTTCCTCAGAAGAACTCGTAA
Enzyme 9 GenBank Gene ID M63967 Link Image
Enzyme 9 GeneCard ID ALDH1B1 Link Image
Enzyme 9 GenAtlas ID ALDH1B1 Link Image
Enzyme 9 HGNC ID HGNC:407 Link Image
Enzyme 9 Chromosome Location 9
Enzyme 9 Locus 9p11.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Hsu LC, Chang WC: Cloning and characterization of a new functional human aldehyde dehydrogenase gene. J Biol Chem. 1991 Jul 5;266(19):12257-65. [PubMed Link Image]
  2. Sherman D, Dave V, Hsu LC, Peters TJ, Yoshida A: Diverse polymorphism within a short coding region of the human aldehyde dehydrogenase-5 (ALDH5) gene. Hum Genet. 1993 Nov;92(5):477-80. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5591
Enzyme 10 Name Sulfotransferase family cytosolic 2B member 1
Enzyme 10 Synonyms
  1. Sulfotransferase 2B1
  2. Alcohol sulfotransferase
  3. Hydroxysteroid sulfotransferase 2
Enzyme 10 Gene Name SULT2B1
Enzyme 10 Protein Sequence >Sulfotransferase family cytosolic 2B member 1
MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRD
DDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPR
LMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFL
KGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSV
VAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQ
MRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETP
HPRPS
Enzyme 10 Number of Residues 365
Enzyme 10 Molecular Weight 41308
Enzyme 10 Theoretical pI 5.05
Enzyme 10 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Catalyzes the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Sulfates hydroxysteroids like DHEA. Isoform 1 preferentially sulfonates cholesterol, and isoform 2 avidly sulfonates pregnenolone but not cholesterol
Enzyme 10 Pathways
Enzyme 10 Reactions
  • 3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 1923291 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID O00204 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name ST2B1_HUMAN Link Image
Enzyme 10 PDB ID 1Q1Q Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1053 bp
ATGGCGTCTCCCCCACCTTTCCACAGCCAGAAGTTGCCAGGTGAATACTTCCGGTACAAG
GGCGTCCCCTTCCCCGTCGGCCTGTACTCGCTCGAGAGCATCAGCTTGGCGGAGAACACC
CAAGATGTGCGGGACGACGACATCTTTATCATCACCTACCCCAAGTCAGGCACGACCTGG
ATGATCGAGATCATCTGCTTAATCCTGAAGGAAGGGGATCCATCCTGGATCCGCTCCGTG
CCCATCTGGGAGCGGGCACCCTGGTGTGAGACCATTGTGGGTGCTTTCAGCCTCCCGGAC
CAGTACAGCCCCCGCCTCATGAGCTCCCATCTTCCCATCCAGATCTTCACCAAGGCCTTC
TTCAGCTCCAAGGCCAAGGTGATCTACATGGGCCGCAACCCCCGGGACGTTGTGGTCTCC
CTCTATCATTACTCCAAGATCGCCGGGCAGTTAAAGGACCCGGGCACACCCGACCAGTTC
CTGAGGGACTTCCTCAAAGGCGAAGTGCAGTTTGGCTCCTGGTTCGACCACATTAAGGGC
TGGCTTCGGATGAAGGGCAAAGACAACTTCCTATTTATCACCTACGAGGAGCTGCAGCAG
GACTTACAGGGCTCCGTGGAGCGCATCTGTGGGTTCCTGGGCCGTCCGCTGGGCAAGGAG
GCACTGGGCTCCGTCGTGGCACACTCAACCTTCAGCGCCATGAAGGCCAACACCATGTCC
AACTACACGCTGCTGCCTCCCAGCCTGCTGGACCACCGTCGCGGGGCCTTCCTCCGGAAA
GGGGTCTGCGGCGACTGGAAGAACCACTTCACGGTGGCCCAGAGCGAAGCCTTCGATCGT
GCCTACCGCAAGCAGATGCGGGGGATGCCGACCTTCCCCTGGGATGAAGACCCGGAGGAG
GATGGCAGCCCAGATCCTGAGCCCAGCCCTGAGCCTGAGCCCAAGCCCAGCCTTGAGCCC
AACACCAGCCTGGAGCGTGAGCCCAGACCCAACTCCAGCCCCAACCCCAGCCCCGGCCAG
GCCTCTGAGACCCCGCACCCACGACCCTCATAA
Enzyme 10 GenBank Gene ID U92314 Link Image
Enzyme 10 GeneCard ID SULT2B1 Link Image
Enzyme 10 GenAtlas ID SULT2B1 Link Image
Enzyme 10 HGNC ID HGNC:11459 Link Image
Enzyme 10 Chromosome Location 19
Enzyme 10 Locus 19q13.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Her C, Wood TC, Eichler EE, Mohrenweiser HW, Ramagli LS, Siciliano MJ, Weinshilboum RM: Human hydroxysteroid sulfotransferase SULT2B1: two enzymes encoded by a single chromosome 19 gene. Genomics. 1998 Nov 1;53(3):284-95. [PubMed Link Image]
  2. Fuda H, Lee YC, Shimizu C, Javitt NB, Strott CA: Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase. J Biol Chem. 2002 Sep 27;277(39):36161-6. Epub 2002 Jul 26. [PubMed Link Image]
  3. Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC: Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. J Biol Chem. 2003 Nov 7;278(45):44593-9. Epub 2003 Aug 14. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5753
Enzyme 11 Name Sorbitol dehydrogenase
Enzyme 11 Synonyms
  1. L-iditol 2-dehydrogenase
Enzyme 11 Gene Name SORD
Enzyme 11 Protein Sequence >Sorbitol dehydrogenase
MAAAAKPNNLSLVVHGPGDLRLENYPIPEPGPNEVLLRMHSVGICGSDVHYWEYGRIGNF
IVKKPMVLGHEASGTVEKVGSSVKHLKPGDRVAIEPGAPRENDEFCKMGRYNLSPSIFFC
ATPPDDGNLCRFYKHNAAFCYKLPDNVTFEEGALIEPLSVGIHACRRGGVTLGHKVLVCG
AGPIGMVTLLVAKAMGAAQVVVTDLSATRLSKAKEIGADLVLQISKESPQEIARKVEGLL
GCKPEVTIECTGAEASIQAGIYATRSGGTLVLVGLGSEMTTVPLLHAAIREVDIKGVFRY
CNTWPVAISMLASKSVNVKPLVTHRFPLEKALEAFETFKKGLGLKIMLKCDPSDQNP
Enzyme 11 Number of Residues 357
Enzyme 11 Molecular Weight 38297
Enzyme 11 Theoretical pI 8.06
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 Amino acid transport and metabolism
Enzyme 11 Specific Function L-iditol + NAD(+) = L-sorbose + NADH
Enzyme 11 Pathways
Enzyme 11 Reactions
  • L-iditol + NAD+ = L-sorbose + 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 520450 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q00796 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name DHSO_HUMAN Link Image
Enzyme 11 PDB ID 1PL8 Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1074 bp
ATGGCGGCGGCGGCCAAGCCCAACAACCTTTCCCTGGTGGTGCACGGACCGGGGGACTTG
CGCCTGGAGAACTATCCTATCCCTGAACCAGGCCCAAATGAGGTCTTGCTGAGGATGCAT
TCTGTTGGAATCTGTGGCTCAGATGTCCACTACTGGGAGTATGGTCGAATTGGGAATTTT
ATTGTGAAAAAGCCCATGGTGCTGGGACATGAAGCTTCGGGAACAGTCGAAAAAGTGGGA
TCATCGGTAAAGCACCTAAAACCAGGTGATCGTGTTGCCATCGAGCCTGGTGCTCCCCGA
GAAAATGATGAATTCTGCAAGATGGGCCGATACAATCTGTCACCTTCCATCTTCTTCTGT
GCCACGCCCCCCGATGACGGGAACCTCTGCCGGTTCTATAAGCACAATGCAGCCTTTTGT
TACAAGCTTCCTGACAATGTCACCTTTGAGGAAGGCGCCCTGATCGAGCCACTTTCTGTG
GGGATCCATGCCTGCAGGAGAGGCGGAGTTACCCTGGGACACAAGGTCCTTGTGTGTGGA
GCTGGGCCAATCGGGATGGTCACTTTGCTCGTGGCCAAAGCAATGGGAGCAGCTCAAGTA
GTGGTGACTGATCTGTCTGCTACCCGATTGTCCAAAGCCAAGGAGATTGGGGCTGATTTA
GTCCTCCAGATCTCCAAGGAGAGCCCTCAGGAAATCGCCAGGAAAGTAGAAGGTCAGCTG
GGGTGCAAGCCGGAAGTCACCATCGAGTGCACGGGGGCAGAGGCCTCCATCCAGGCGGGC
ATCTACGCCACTCGCTCTGGTGGGACCCTCGTGCTTGTGGGGCTGGGCTCTGAGATGACC
ACCGTACCCCTACTGCATGCAGCCATCCGGGAGGTGGATATCAAGGGCGTGTTTCGATAC
TGCAACACGTGGCCAGTGGCGATTTCGATGCTTGCGTCCAAGTCTGTGAATGTAAAACCC
CTCGTCACCCATAGGTTTCCTCTGGAGAAAGCTCTGGAGGCCTTTGAAACATTTAAAAAG
GGATTGGGGTTGAAAATCATGCTCAAGTGTGACCCCAGTGACCAGAATCCCTGA
Enzyme 11 GenBank Gene ID U07361 Link Image
Enzyme 11 GeneCard ID SORD Link Image
Enzyme 11 GenAtlas ID SORD Link Image
Enzyme 11 HGNC ID HGNC:11184 Link Image
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Lee FK, Cheung MC, Chung S: The human sorbitol dehydrogenase gene: cDNA cloning, sequence determination, and mapping by fluorescence in situ hybridization. Genomics. 1994 May 15;21(2):354-8. [PubMed Link Image]
  2. Iwata T, Popescu NC, Zimonjic DB, Karlsson C, Hoog JO, Vaca G, Rodriguez IR, Carper D: Structural organization of the human sorbitol dehydrogenase gene (SORD). Genomics. 1995 Mar 1;26(1):55-62. [PubMed Link Image]
  3. Carr IM, Markham AF, Coletta PL: Identification and characterisation of a sequence related to human sorbitol dehydrogenase. Eur J Biochem. 1997 May 1;245(3):760-7. [PubMed Link Image]
  4. Karlsson C, Maret W, Auld DS, Hoog JO, Jornvall H: Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzyme. Eur J Biochem. 1989 Dec 22;186(3):543-50. [PubMed Link Image]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5754
Enzyme 12 Name Alcohol dehydrogenase [NADP+]
Enzyme 12 Synonyms
  1. Aldehyde reductase
  2. Aldo- keto reductase family 1 member A1
Enzyme 12 Gene Name AKR1A1
Enzyme 12 Protein Sequence >Alcohol dehydrogenase [NADP+]
MAASCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEAL
KEDVGPGKAVPREELFVTSKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFER
GDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDILSVASVRP
AVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPDEPVLLEEPVVLALAEK
YGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIV
PMLTVDGKRVPRDAGHPLYPFNDPY
Enzyme 12 Number of Residues 325
Enzyme 12 Molecular Weight 36573
Enzyme 12 Theoretical pI 6.79
Enzyme 12 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
Component
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Catalyzes the NADPH-dependent reduction of a variety of aldehydes to their corresponding alcohols
Enzyme 12 Pathways
Enzyme 12 Reactions
  • an alcohol + NADP+ = an aldehyde + NADPH + 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 178481 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P14550 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name AK1A1_HUMAN Link Image
Enzyme 12 PDB ID 2ALR Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >978 bp
ATGGCGGCTTCCTGTGTTCTACTGCACACTGGGCAGAAGATGCCTCTGATTGGTCTGGGT
ACCTGGAAGAGTGAGCCTGGTCAGGTAAAAGCAGCTGTTAAGTATGCCCTTAGCGTAGGC
TACCGCCACATTGATTGTGCTGCTATCTACGGCAATGAGCCTGAGATTGGGGAGGCCCTG
AAGGAGGACGTGGGACCAGGCAAGGCGGTGCCTCGGGAGGAGCTGTTTGTGACATCCAAG
CTGTGGAACACCAAGCACCACCCCGAGGATGTGGAGCCTGCCCTCCGGAAGACTCTGGCT
GACCTCCAGCTGGAGTATCTGGACCTGTACCTGATGCACTGGCCTTATGCCTTTGAGCGG
GGAGACAACCCCTTCCCCAAGAATGCTGATGGGACTATATGCTACGACTCCACCCACTAC
AAGGAGACTTGGAAGGCTCTGGAGGCACTGGTGGCTAAGGGGCTGGTGCAGGCGCTGGGC
CTGTCCAACTTCAACAGTCGGCAGATTGATGACATACTCAGTGTGGCCTCCGTGCGTCCA
GCTGTCTTGCAGGTGGAATGCCACCCATACTTGGCTCAAAATGAGCTAATTGCCCACTGC
CAAGCACGTGGCTTGGAGGTAACTGCTTATAGCCCTTTGGGCTCCTCTGATCGTGCATGG
CGTGATCCTGATGAGCCTGTCCTGCTGGAGGAACCAGTAGTCCTGGCATTGGCTGAAAAG
TATGGCCGATCTCCAGCTCAGATCTTGCTCAGGTGGCAGGTCCAGCGGAAAGTGATCTGC
ATCCCCAAAAGTATCACTCCTTCTCGAATCCTTCAGAACATCAAGGTGTTTGACTTCACC
TTTAGCCCAGAAGAGATGAAGCAGCTAAATGCCCTGAACAAAAATTGGAGATATATTGTG
CCTATGCTTACGGTGGATGGGAAGAGAGTCCCAAGGGATGCAGGGCATCCTCTGTACCCC
TTTAATGACCCGTACTGA
Enzyme 12 GenBank Gene ID J04794 Link Image
Enzyme 12 GeneCard ID AKR1A1 Link Image
Enzyme 12 GenAtlas ID AKR1A1 Link Image
Enzyme 12 HGNC ID HGNC:380 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Bohren KM, Bullock B, Wermuth B, Gabbay KH: The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem. 1989 Jun 5;264(16):9547-51. [PubMed Link Image]
  2. Barski OA, Gabbay KH, Bohren KM: Characterization of the human aldehyde reductase gene and promoter. Genomics. 1999 Sep 1;60(2):188-98. [PubMed Link Image]
  3. Wermuth B, Omar A, Forster A, di Francesco C, Wolf M, von Wartburg JP, Bullock B, Gabbay KH: Primary structure of aldehyde reductase from human liver. Prog Clin Biol Res. 1987;232:297-307. [PubMed Link Image]
  4. Barski OA, Gabbay KH, Grimshaw CE, Bohren KM: Mechanism of human aldehyde reductase: characterization of the active site pocket. Biochemistry. 1995 Sep 5;34(35):11264-75. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5758
Enzyme 13 Name Alcohol dehydrogenase 4
Enzyme 13 Synonyms
  1. Alcohol dehydrogenase class II pi chain
Enzyme 13 Gene Name ADH4
Enzyme 13 Protein Sequence >Alcohol dehydrogenase 4
MGTKGKVIKCKAAIAWEAGKPLCIEEVEVAPPKAHEVRIQIIATSLCHTDATVIDSKFEG
LAFPVIVGHEAAGIVESIGPGVTNVKPGDKVIPLYAPLCRKCKFCLSPLTNLCGKISNLK
SPASDQQLMEDKTSRFTCKGKPVYHFFGTSTFSQYTVVSDINLAKIDDDANLERVCLLGC
GFSTGYGAAINNAKVTPGSTCAVFGLGGVGLSAVMGCKAAGASRIIGIDINSEKFVKAKA
LGATDCLNPRDLHKPIQEVIIELTKGGVDFALDCAGGSETMKAALDCTTAGWGSCTFIGV
AAGSKGLTVFPEELIIGRTINGTFFGGWKSVDSIPKLVTDYKNKKFNLDALVTHTLPFDK
ISEAFDLMNQGKSIRTILIF
Enzyme 13 Number of Residues 380
Enzyme 13 Molecular Weight 40222
Enzyme 13 Theoretical pI 8.01
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 178121 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P08319 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name ADH4_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1179 bp
ATGGGCACCAAGGGCAAAGTTATTAAATGCAAAGCAGCCATCGCCTGGGAAGCAGGCAAG
CCCCTTTGCATTGAAGAGGTTGAAGTAGCTCCCCCCAAGGCTCATGAAGTTCGCATTCAG
ATCATTGCTACCTCCCTGTGCCATACTGATGCCAGTGTTATCGATTCTAAATTTGAGGGC
CTAGCTTTCCCAGTGATCGTTGGCCATGAGGCTGCAGGTATTGTGGAAAGTATTGGGCCA
GGAGTGACCAACGTCAAACCAGGTGACAAAGTAATTCCACTTTATGCACCTCTATGTAGA
AAATGCAAGTTTTGTCTGAGTCCACTCACAAATTTGTGTGGGAAAATCAGTAATCTCAAA
AGTCCTGCTAGTGATCAACAACTAATGGAAGACAAAACCAGCAGGTTTACCTGCAAAGGA
AAACCAGTTTACCATTTCTTTGGAACCAGTACATTCTCTCAGTACACTGTGGTGTCAGAT
ATCAATCTTGCCAAAATAGATGATGATGCAAATTTAGAGAGAGTTTGTCTGCTTGGATGT
GGGTTTTCAACTGGCTATGGGGCTGCAATCAACAATGCCAAGGTCACCCCTGGTTCGACT
TGTGCTGTCTTTGGCCTAGGAGGTGTGGGTCTTTCTGCTGTAATGGGTTGTAAAGCAGCA
GGAGCTTCCAGAATCATAGGTATTGACATCAACAGTGAGAAGTTTGTGAAGGCTAAAGCC
CTGGGAGCCACTGACTGCCTCAATCCTAGAGACTTACATAAACCGATCCAGGAAGTTATC
ATTGAATTGACCAAGGGAGGTGTGGATTTTGCCCTTGACTGTGCAGGTGGATCTGAAACC
ATGAAAGCAGCCCTGGACTGTACAACCGCAGGCTGGGGATCATGTACTTTCATTGGAGTA
GCTGCTGGTAGCAAAGGATTGACTATTTTTCCAGAGGAGCTAATAATCGGCCGTACTATA
AATGGAACATTCTTTGGTGGTTGGAAAAGTGTAGATTCTATCCCAAAGCTGGTCACTGAC
TATAAGAATAAGAAATTCAATCTGGATGCATTGGTGACCCATACCCTGCCTTTTGACAAA
ATCAGTGAGGCATTTGACCTAATGAACCAAGGAAAAAGCGTCCGAACAATCCTCATCTTT
GGAAGATGCCAGGAGCAATTCAGAATACTATCTGATTGA
Enzyme 13 GenBank Gene ID M15943 Link Image
Enzyme 13 GeneCard ID ADH4 Link Image
Enzyme 13 GenAtlas ID ADH4 Link Image
Enzyme 13 HGNC ID HGNC:252 Link Image
Enzyme 13 Chromosome Location 4
Enzyme 13 Locus 4q21-q24|4q22
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Hoog JO, von Bahr-Lindstrom H, Heden LO, Holmquist B, Larsson K, Hempel J, Vallee BL, Jornvall H: Structure of the class II enzyme of human liver alcohol dehydrogenase: combined cDNA and protein sequence determination of the pi subunit. Biochemistry. 1987 Apr 7;26(7):1926-32. [PubMed Link Image]
  2. von Bahr-Lindstrom H, Jornvall H, Hoog JO: Cloning and characterization of the human ADH4 gene. Gene. 1991 Jul 22;103(2):269-74. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6062
Enzyme 14 Name Alcohol dehydrogenase 1B
Enzyme 14 Synonyms
  1. Alcohol dehydrogenase beta subunit
Enzyme 14 Gene Name ADH1B
Enzyme 14 Protein Sequence >Alcohol dehydrogenase 1B
MSTAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIKMVAVGICRTDDHVVSGNLVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLGNP
RGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVNVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQ
NLSINPMLLLTGRTWKGAVYGGFKSKEGIPKLVADFMAKKFSLDALITHVLPFEKINEGF
DLLHSGKSIRTVLTF
Enzyme 14 Number of Residues 375
Enzyme 14 Molecular Weight 39855
Enzyme 14 Theoretical pI 8.38
Enzyme 14 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 14 General Function Energy production and conversion
Enzyme 14 Specific Function An alcohol + NAD(+) = an aldehyde or ketone + NADH
Enzyme 14 Pathways
Enzyme 14 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + H+
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 178098 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P00325 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name ADH1B_HUMAN Link Image
Enzyme 14 PDB ID 1HSZ Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1128 bp
ATGAGCACAGCAGGAAAAGTAATCAAATGCAAAGCAGCTGTGCTATGGGAGGTAAAGAAA
CCCTTTTCCATTGAGGATGTGGAGGTTGCACCTCCTAAGGCTTATGAAGTTCGCATTAAG
ATGGTGGCTGTAGGAATCTGTCGCACAGATGACCACGTGGTTAGTGGCAACCTGGTGACC
CCCCTTCCTGTGATTTTAGGCCATGAGGCAGCCGGCATCGTGGAGAGTGTTGGAGAAGGG
GTGACTACAGTCAAACCAGGTGATAAAGTCATCCCGCTCTTTACTCCTCAGTGTGGAAAA
TGCAGAGTTTGTAAAAACCCGGAGAGCAACTACTGCTTGAAAAATGATCTAGGCAATCCT
CGGGGGACCCTGCAGGATGGCACCAGGAGGTTCACCTGCAGGGGGAAGCCCATTCACCAC
TTCCTTGGCACCAGCACCTTCTCCCAGTACACGGTGGTGGATGAGAATGCAGTGGCCAAA
ATTGATGCAGCCTCGCCCCTGGAGAAAGTCTGCCTCATTGGCTGTGGATTCTCGACTGGT
TATGGGTCTGCAGTTAACGTTGCCAAGGTCACCCCAGGCTCTACCTGTGCTGTGTTTGGC
CTGGGAGGGGTCGGCCTATCTGCTGTTATGGGCTGTAAAGCAGCTGGAGCAGCCAGAATC
ATTGCGGTGGACATCAACAAGGACAAAAAAGCAAAGGCCAAAGAGTTGGGTGCCACTGAA
TGCATCAACCCTCAAGACTACAAGAAACCCATCCAGGAAGTGCTAAAGGAAATGACTGAT
GGAGGTGTGGATTTTTCGTTTGAAGTCATCGGTCGGCTTGACACCATGATGGCTTCCCTG
TTATGTTGTCATGAGGCATGTGGCACAAGCGTCATCGTAGGGGTACCTCCTGCTTCCCAG
AACCTCTCAATAAACCCTATGCTGCTACTGACTGGACGCACCTGGAAGGGGGCTGTTTAT
GGTGGCTTTAAGAGTAAAGAAGGTATCCCAAAACTTGTGGCTGATTTTATGGCTAAGAAG
TTTTCACTGGATGCGTTAATAACCCATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCACTCTGGGAAAAGTATCCGTACCGTCCTGACGTTTTGA
Enzyme 14 GenBank Gene ID M24317 Link Image
Enzyme 14 GeneCard ID ADH1B Link Image
Enzyme 14 GenAtlas ID ADH1B Link Image
Enzyme 14 HGNC ID HGNC:250 Link Image
Enzyme 14 Chromosome Location 4
Enzyme 14 Locus 4q21-q23
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 6064
Enzyme 15 Name Alcohol dehydrogenase 1A
Enzyme 15 Synonyms
  1. Alcohol dehydrogenase alpha subunit
Enzyme 15 Gene Name ADH1A
Enzyme 15 Protein Sequence >Alcohol dehydrogenase 1A
MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAVGICGTDDHVVSGTMVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNP
QGTLQDGTSRFTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQ
NLSMNPMLLLTGRTWKGAILGGFKSKECVPKLVADFMAKKFSLDALITHVLPFEKINEGF
DLLHSGKSIRTILMF
Enzyme 15 Number of Residues 375
Enzyme 15 Molecular Weight 39859
Enzyme 15 Theoretical pI 8.02
Enzyme 15 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 15 General Function Energy production and conversion
Enzyme 15 Specific Function An alcohol + NAD(+) = an aldehyde or ketone + NADH
Enzyme 15 Pathways
Enzyme 15 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + H+
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 178092 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P07327 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name ADH1A_HUMAN Link Image
Enzyme 15 PDB ID 1HSO Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1128 bp
ATGAGCACAGCAGGAAAAGTAATCAAATGCAAAGCAGCTGTGCTATGGGAGTTAAAGAAA
CCCTTTTCCATTGAGGAGGTGGAGGTTGCACCTCCTAAGGCCCATGAAGTTCGTATTAAG
ATGGTGGCTGTAGGAATCTGTGGCACAGATGACCACGTGGTTAGTGGTACCATGGTGACC
CCACTTCCTGTGATTTTAGGCCATGAGGCAGCCGGCATCGTGGAGAGTGTTGGAGAAGGG
GTGACTACAGTCAAACCAGGTGATAAAGTCATCCCACTCGCTATTCCTCAGTGTGGAAAA
TGCAGAATTTGTAAAAACCCGGAGAGCAACTACTGCTTGAAAAACGATGTAAGCAATCCT
CAGGGGACCCTGCAGGATGGCACCAGCAGGTTCACCTGCAGGAGGAAGCCCATCCACCAC
TTCCTTGGCATCAGCACCTTCTCACAGTACACAGTGGTGGATGAAAATGCAGTAGCCAAA
ATTGATGCAGCCTCGCCTCTAGAGAAAGTCTGTCTCATTGGCTGTGGATTTTCAACTGGT
TATGGGTCTGCAGTCAATGTTGCCAAGGTCACCCCAGGCTCTACCTGTGCTGTGTTTGGC
CTGGGAGGGGTCGGCCTATCTGCTATTATGGGCTGTAAAGCAGCTGGGGCAGCCAGAATC
ATTGCGGTGGACATCAACAAGGACAAATTTGCAAAGGCCAAAGAGTTGGGGGCCACTGAA
TGCATCAACCCTCAAGACTACAAGAAACCCATCCAGGAGGTGCTAAAGGAAATGACTGAT
GGAGGTGTGGATTTTTCATTTGAAGTCATCGGTCGGCTTGACACCATGATGGCTTCCCTG
TTATGTTGTCATGAGGCATGTGGCACAAGTGTCATCGTAGGGGTACCTCCTGATTCCCAA
AACCTCTCAATGAACCCTATGCTGCTACTGACTGGACGTACCTGGAAGGGAGCTATTCTT
GGTGGCTTTAAAAGTAAAGAATGTGTCCCAAAACTTGTGGCTGATTTTATGGCTAAGAAG
TTTTCATTGGATGCATTAATAACCCATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCACTCTGGGAAAAGTATCCGTACCATTCTGATGTTTTGA
Enzyme 15 GenBank Gene ID M12271 Link Image
Enzyme 15 GeneCard ID ADH1A Link Image
Enzyme 15 GenAtlas ID ADH1A Link Image
Enzyme 15 HGNC ID HGNC:249 Link Image
Enzyme 15 Chromosome Location 4
Enzyme 15 Locus 4q21-q23
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. von Bahr-Lindstrom H, Hoog JO, Heden LO, Kaiser R, Fleetwood L, Larsson K, Lake M, Holmquist B, Holmgren A, Hempel J, et al.: cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase. Biochemistry. 1986 May 6;25(9):2465-70. [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. Matsuo Y, Yokoyama S: Molecular structure of the human alcohol dehydrogenase 1 gene. FEBS Lett. 1989 Jan 16;243(1):57-60. [PubMed Link Image]
  4. Yasunami M, Kikuchi I, Sarapata D, Yoshida A: The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome. Genomics. 1990 Jun;7(2):152-8. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 6065
Enzyme 16 Name Alcohol dehydrogenase 6
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name ADH6
Enzyme 16 Protein Sequence >Alcohol dehydrogenase 6
MSTTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLD
LLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSK
TQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCGFSTG
FGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATE
CLNPQDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASV
QLKISGQLFFSGRSLKGSVFGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAV
ELMKTGKW
Enzyme 16 Number of Residues 368
Enzyme 16 Molecular Weight 39073
Enzyme 16 Theoretical pI 7.86
Enzyme 16 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 16 General Function Energy production and conversion
Enzyme 16 Specific Function An alcohol + NAD(+) = an aldehyde or ketone + NADH
Enzyme 16 Pathways
Enzyme 16 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + H+
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 178146 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P28332 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name ADH6_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1107 bp
ATGAGTACTACAGGCCAAGTCATCAGATGCAAAGCAGCCATACTCTGGAAGCCTGGTGCA
CCATTTTCTATTGAAGAGGTAGAAGTGGCCCCACCAAAGGCAAAGGAGGTTCGCATAAAG
GTTGTGGCCACCGGACTGTGTGGTACAGAGATGAAAGTGTTGGGGAGTAAACACTTGGAC
CTCTTGTATCCCACCATCTTGGGCCATGAAGGGGCTGGAATCGTTGAGAGTATTGGAGAA
GGAGTAAGCACAGTGAAACCAGGTGACAAAGTTATCACACTCTTTCTGCCACAGTGTGGA
GAATGTACCTCTTGCCTGAATTCTGAGGGCAATTTTTGTATACAATTCAAACAGTCAAAA
ACCCAACTGATGTCTGATGGTACCAGCAGGTTTACCTGCAAGGGAAAATCAATATATCAC
TTTGGTAATACCAGCACCTTCTGTGAATACACAGTGATAAAGGAAATCTCAGTTGCCAAG
ATTGATGCAGTCGCTCCTCTAGAGAAAGTATGCCTAATTAGCTGTGGCTTTTCCACTGGG
TTTGGTGCTGCAATCAATACTGCCAAGGTGACTCCAGGTTCTACCTGTGCTGTGTTTGGC
CTGGGAGGAGTCGGCTTGTCTGTTGTCATGGGTTGTAAAGCAGCAGGAGCAGCCAGGATC
ATTGGAGTGGATGTCAACAAGGAGAAATTTAAGAAGGCACAGGAATTGGGTGCGACTGAG
TGCCTCAACCCTCAGGACTTAAAGAAACCCATTCAAGAAGTTTTATTTGATATGACAGAT
GCTGGTATAGACTTCTGCTTTGAGGCCATTGGAAATCTGGACGTTCTGGCAGCTGCCCTC
GCCTCCTGCAATGAGAGCTATGGGGTCTGTGTGGTTGTTGGGGTGTTGCCTGCCAGTGTT
CAACTCAAAATCAGTGGCCAGTTGTTCTTCTCAGGACGTTCTTTGAAGGGTTCTGTTTTT
GGAGGCTGGAAGAGCAGACAGCACATCCCTAAACTGGTTGCTGATTATATGGCAGAGAAG
TTGAATCTAGATCCACTAATTACTCATACTCTGAATCTTGATAAAATCAATGAAGCAGTT
GAATTAATGAAAACTGGAAAATGGTAA
Enzyme 16 GenBank Gene ID M84402 Link Image
Enzyme 16 GeneCard ID ADH6 Link Image
Enzyme 16 GenAtlas ID ADH6 Link Image
Enzyme 16 HGNC ID HGNC:255 Link Image
Enzyme 16 Chromosome Location 4
Enzyme 16 Locus 4q23
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Yasunami M, Chen CS, Yoshida A: A human alcohol dehydrogenase gene (ADH6) encoding an additional class of isozyme. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7610-4. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6120
Enzyme 17 Name Beta-glucuronidase precursor
Enzyme 17 Synonyms
  1. Beta-G1
Enzyme 17 Gene Name GUSB
Enzyme 17 Protein Sequence >Beta-glucuronidase precursor
MARGSAVAWAALGPLLWGCALGLQGGMLYPQESPSRECKELDGLWSFRADFSDNRRRGFE
EQWYRRPLWESGPTVDMPVPSSFNDISQDWRLRHFVGWVWYEREVILPERWTQDLRTRVV
LRIGSAHSYAIVWVNGVDTLEHEGGYLPFEADISNLVQVGPLPSRLRITIAINNTLTPTT
LPPGTIQYLTDTSKYPKGYFVQNTYFDFFNYAGLQRSVLLYTTPTTYIDDITVTTSVEQD
SGLVNYQISVKGSNLFKLEVRLLDAENKVVANGTGTQGQLKVPGVSLWWPYLMHERPAYL
YSLEVQLTAQTSLGPVSDFYTLPVGIRTVAVTKSQFLINGKPFYFHGVNKHEDADIRGKG
FDWPLLVKDFNLLRWLGANAFRTSHYPYAEEVMQMCDRYGIVVIDECPGVGLALPQFFNN
VSLHHHMQVMEEVVRRDKNHPAVVMWSVANEPASHLESAGYYLKMVIAHTKSLDPSRPVT
FVSNSNYAADKGAPYVDVICLNSYYSWYHDYGHLELIQLQLATQFENWYKKYQKPIIQSE
YGAETIAGFHQDPPLMFTEEYQKSLLEQYHLGLDQKRRKYVVGELIWNFADFMTEQSPTR
VLGNKKGIFTRQRQPKSAAFLLRERYWKIANETRYPHSVAKSQCLENSLFT
Enzyme 17 Number of Residues 651
Enzyme 17 Molecular Weight 74733
Enzyme 17 Theoretical pI 7.02
Enzyme 17 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 17 General Function Carbohydrate transport and metabolism
Enzyme 17 Specific Function Plays an important role in the degradation of dermatan and keratan sulfates
Enzyme 17 Pathways
Enzyme 17 Reactions
  • a beta-D-glucuronoside + H2O = D-glucuronate + an alcohol
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-22
Enzyme 17 Transmembrane Regions Not Available
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 183233 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P08236 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name BGLR_HUMAN Link Image
Enzyme 17 PDB ID 1BHG Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1956 bp
ATGGCCCGGGGGTCGGCGGTTGCCTGGGCGGCGCTCGGGCCGTTGTTGTGGGGCTGCGCG
CTGGGGCTGCAGGGCGGGATGCTGTACCCCCAGGAGAGCCCGTCGCGGGAGTGCAAGGAG
CTGGACGGCCTCTGGAGCTTCCGCGCCGACTTCTCTGACAACCGACGCCGGGGCTTCGAG
GAGCAGTGGTACCGGCGGCCGCTGTGGGAGTCAGGCCCCACCGTGGACATGCCAGTTCCC
TCCAGCTTCAATGACATCAGCCAGGACTGGCGTCTGCGGCATTTTGTCGGCTGGGTGTGG
TACGAACGGGAGGTGATCCTGCCGGAGCGATGGACCCAGGACCTGCGCACAAGAGTGGTG
CTGAGGATTGGCAGTGCCCATTCCTATGCCATCGTGTGGGTGAATGGGGTCGACACGCTA
GAGCATGAGGGGGGCTACCTCCCCTTCGAGGCCGACATCAGCAACCTGGTCCAGGTGGGG
CCCCTGCCCTCCCGGCTCCGAATCACTATCGCCATCAACAACACACTCACCCCCACCACC
CTGCCACCAGGGACCATCCAATACCTGACTGACACCTCCAAGTATCCCAAGGGTTACTTT
GTCCAGAACACATATTTTGACTTTTTCAACTACGCTGGACTGCAGCGGTCTGTACTTCTG
TACACGACACCCACCACCTACATCGATGACATCACCGTCACCACCAGCGTGGAGCAAGAC
AGTGGGCTGGTGAATTACCAGATCTCTGTCAAGGGCAGTAACCTGTTCAAGTTGGAAGTG
CGTCTTTTGGATGCAGAAAACAAAGTCGTGGCGAATGGGACTGGGACCCAGGGCCAACTT
AAGGTGCCAGGTGTCAGCCTCTGGTGGCCGTACCTGATGCACGAACGCCCTGCCTATCTG
TATTCATTGGAGGTGCAGCTGACTGCACAGACGTCACTGGGGCCTGTGTCTGACTTCTAC
ACACTCCCTGTGGGGATCCGCACTGTGGCTGTCACCAAGAGCCAGTTCCTCATCAATGGG
AAACCTTTCTATTTCCACGGTGTCAACAAGCATGAGGATGCGGACATCCGAGGGAAGGGC
TTCGACTGGCCGCTGCTGGTGAAGGACTTCAACCTGCTTCGCTGGCTTGGTGCCAACGCT
TTCCGTACCAGCCACTACCCCTATGCAGAGGAAGTGATGCAGATGTGTGACCGCTATGGG
ATTGTGGTCATCGATGAGTGTCCCGGCGTGGGCCTGGCGCTGCCGCAGTTCTTCAACAAC
GTTTCTCTGCATCACCACATGCAGGTGATGGAAGAAGTGGTGCGTAGGGACAAGAACCAC
CCCGCGGTCGTGATGTGGTCTGTGGCCAACGAGCCTGCGTCCCACCTAGAATCTGCTGGC
TACTACTTGAAGATGGTGATCGCTCACACCAAATCCTTGGACCCCTCCCGGCCTGTGACC
TTTGTGAGCAACTCTAACTATGCAGCAGACAAGGGGGCTCCGTATGTGGATGTGATCTGT
TTGAACAGCTACTACTCTTGGTATCACGACTACGGGCACCTGGAGTTGATTCAGCTGCAG
CTGGCCACCCAGTTTGAGAACTGGTATAAGAAGTATCAGAAGCCCATTATTCAGAGCGAG
TATGGAGCAGAAACGATTGCAGGGTTTCACCAGGATCCACCTCTGATGTTCACTGAAGAG
TACCAGAAAAGTCTGCTAGAGCAGTACCATCTGGGTCTGGATCAAAAACGCAGAAAATAT
GTGGTTGGAGAGCTCATTTGGAATTTTGCCGATTTCATGACTGAACAGTCACCGACGAGA
GTGCTGGGGAATAAAAAGGGGATCTTCACTCGGCAGAGACAACCAAAAAGTGCAGCGTTC
CTTTTGCGAGAGAGATACTGGAAGATTGCCAATGAAACCAGGTATCCCCACTCAGTAGCC
AAGTCACAATGTTTGGAAAACAGCCCGTTTACTTGA
Enzyme 17 GenBank Gene ID M15182 Link Image
Enzyme 17 GeneCard ID GUSB Link Image
Enzyme 17 GenAtlas ID GUSB Link Image
Enzyme 17 HGNC ID HGNC:4696 Link Image
Enzyme 17 Chromosome Location 7
Enzyme 17 Locus 7q21.11
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Oshima A, Kyle JW, Miller RD, Hoffmann JW, Powell PP, Grubb JH, Sly WS, Tropak M, Guise KS, Gravel RA: Cloning, sequencing, and expression of cDNA for human beta-glucuronidase. Proc Natl Acad Sci U S A. 1987 Feb;84(3):685-9. [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. Shipley JM, Miller RD, Wu BM, Grubb JH, Christensen SG, Kyle JW, Sly WS: Analysis of the 5' flanking region of the human beta-glucuronidase gene. Genomics. 1991 Aug;10(4):1009-18. [PubMed Link Image]
  4. Tanaka J, Gasa S, Sakurada K, Miyazaki T, Kasai M, Makita A: Characterization of the subunits and sugar moiety of human placental and leukemic beta-glucuronidase. Biol Chem Hoppe Seyler. 1992 Jan;373(1):57-62. [PubMed Link Image]
  5. Guise KS, Korneluk RG, Waye J, Lamhonwah AM, Quan F, Palmer R, Ganschow RE, Sly WS, Gravel RA: Isolation and expression in Escherichia coli of a cDNA clone encoding human beta-glucuronidase. Gene. 1985;34(1):105-10. [PubMed Link Image]
  6. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
  7. Jain S, Drendel WB, Chen ZW, Mathews FS, Sly WS, Grubb JH: Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs. Nat Struct Biol. 1996 Apr;3(4):375-81. [PubMed Link Image]
  8. Vervoort R, Lissens W, Liebaers I: Molecular analysis of a patient with hydrops fetalis caused by beta-glucuronidase deficiency, and evidence for additional pseudogenes. Hum Mutat. 1993;2(6):443-5. [PubMed Link Image]
  9. Wu BM, Sly WS: Mutational studies in a patient with the hydrops fetalis form of mucopolysaccharidosis type VII. Hum Mutat. 1993;2(6):446-57. [PubMed Link Image]
  10. Tomatsu S, Fukuda S, Sukegawa K, Ikedo Y, Yamada S, Yamada Y, Sasaki T, Okamoto H, Kuwahara T, Yamaguchi S, et al.: Mucopolysaccharidosis type VII: characterization of mutations and molecular heterogeneity. Am J Hum Genet. 1991 Jan;48(1):89-96. [PubMed Link Image]
  11. Shipley JM, Klinkenberg M, Wu BM, Bachinsky DR, Grubb JH, Sly WS: Mutational analysis of a patient with mucopolysaccharidosis type VII, and identification of pseudogenes. Am J Hum Genet. 1993 Mar;52(3):517-26. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6158
Enzyme 18 Name Plasma alpha-L-fucosidase precursor
Enzyme 18 Synonyms
  1. Alpha-L-fucosidase 2
  2. Alpha-L-fucoside fucohydrolase 2
Enzyme 18 Gene Name FUCA2
Enzyme 18 Protein Sequence >Plasma alpha-L-fucosidase precursor
MRPQELPRLAFPLLLLLLLLLPPPPCPAHSATRFDPTWESLDARQLPAWFDQAKFGIFIH
WGVFSVPSFGSEWFWWYWQKEKIPKYVEFMKDNYPPSFKYEDFGPLFTAKFFNANQWADI
FQASGAKYIVLTSKHHEGFTLWGSEYSWNWNAIDEGPKRDIVKELEVAIRNRTDLRFGLY
YSLFEWFHPLFLEDESSSFHKRQFPVSKTLPELYELVNNYQPEVLWSDGDGGAPDQYWNS
TGFLAWLYNESPVRGTVVTNDRWGAGSICKHGGFYTCSDRYNPGHLLPHKWENCMTIDKL
SWGYRREAGISDYLTIEELVKQLVETVSCGGNLLMNIGPTLDGTISVVFEERLRQVGSWL
KVNGEAIYETYTWRSQNDTVTPDVWYTSKPKEKLVYAIFLKWPTSGQLFLGHPKAILGAT
EVKLLGHGQPLNWISLEQNGIMVELPQLTIHQMPCKWGWALALTNVI
Enzyme 18 Number of Residues 467
Enzyme 18 Molecular Weight 54061
Enzyme 18 Theoretical pI 6.10
Enzyme 18 GO Classification
Function
  • alpha-L-fucosidase activity
  • catalytic activity
  • fucosidase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 18 General Function Carbohydrate transport and metabolism
Enzyme 18 Specific Function Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N- acetylglucosamine of the carbohydrate moieties of glycoproteins
Enzyme 18 Pathways
Enzyme 18 Reactions
  • an alpha-L-fucoside + H2O = L-fucose + an alcohol
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-28
Enzyme 18 Transmembrane Regions Not Available
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 22761559 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9BTY2 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name FUCO2_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1404 bp
ATGCGGCCCCAGGAGCTCCCCAGGCTCGCGTTCCCGTTGCTGCTGTTGCTGTTGCTGCTG
CTGCCGCCGCCGCCGTGCCCTGCCCACAGCGCCACGCGCTTCGACCCCACCTGGGAGTCC
CTGGACGCCCGCCAGCTGCCCGCGTGGTTTGACCAGGCCAAGTTCGGCATCTTCATCCAC
TGGGGAGTGTTTTCCGTGCCCAGCTTCGGTAGCGAGTGGTTCTGGTGGTATTGGCAAAAG
GAAAAGATACCGAAGTATGTGGAATTTATGAAAGATAATTACCCTCCTAGTTTCAAATAT
GAAGATTTTGGACCACTATTTACAGCAAAATTTTTTAATGCCAACCAGTGGGCAGATATT
TTTCAGGCCTCTGGTGCCAAATACATTGTCTTAACTTCCAAACATCATGAAGGCTTTACC
TTGTGGGGGTCAGAATATTCGTGGAACTGGAATGCCATAGATGAGGGGCCCAAGAGGGAC
ATTGTCAAGGAACTTGAGGTAGCCATTAGGAACAGAACTGACCTGCGTTTTGGACTGTAC
TATTCCCTTTTTGAATGGTTTCATCCGCTCTTCCTTGAGGATGAATCCAGTTCATTCCAT
AAGCGGCAATTTCCAGTTTCTAAGACATTGCCAGAGCTCTATGAGTTAGTGAACAACTAT
CAGCCTGAGGTTCTGTGGTCGGATGGTGACGGAGGAGCACCGGATCAATACTGGAACAGC
ACAGGCTTCTTGGCCTGGTTATATAATGAAAGCCCAGTTCGGGGCACAGTAGTCACCAAT
GATCGTTGGGGAGCTGGTAGCATCTGTAAGCATGGTGGCTTCTATACCTGCAGTGATCGT
TATAACCCAGGACATCTTTTGCCACATAAATGGGAAAACTGCATGACAATAGACAAACTG
TCCTGGGGCTATAGGAGGGAAGCTGGAATCTCTGACTATCTTACAATTGAAGAATTGGTG
AAGCAACTTGTAGAGACAGTTTCATGTGGAGGAAATCTTTTGATGAATATTGGGCCCACA
CTAGATGGCACCATTTCTGTAGTTTTTGAGGAGCGACTGAGGCAAGTGGGGTCCTGGCTA
AAAGTCAATGGAGAAGCTATTTATGAAACCTATACCTGGCGATCCCAGAACGACACTGTC
ACCCCAGATGTGTGGTACACATCCAAGCCTAAAGAAAAATTAGTCTATGCCATTTTTCCT
AAATGGCCCACATCAGGACAGCTGTTCCTTGGCCATCCCAAAGCTATTCTGGGGGCAACA
GAGGTGAAACTACTGGGCCATGGACAGCCACTTAACTGGATTTCTTTGGAGCAAAATGGC
ATTATGGTAGAACTGCCACAGCTAACCATTCATCAGATGCCGTGTAAATGGGGCTGGGCT
CTAGCCCTAACTAATGTGATCTAA
Enzyme 18 GenBank Gene ID AK075458 Link Image
Enzyme 18 GeneCard ID FUCA2 Link Image
Enzyme 18 GenAtlas ID FUCA2 Link Image
Enzyme 18 HGNC ID HGNC:4008 Link Image
Enzyme 18 Chromosome Location 6
Enzyme 18 Locus 6q24
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6298
Enzyme 19 Name Trans-2-enoyl-CoA reductase, mitochondrial precursor
Enzyme 19 Synonyms
  1. HsNrbf-1
  2. NRBF-1
Enzyme 19 Gene Name MECR
Enzyme 19 Protein Sequence >Trans-2-enoyl-CoA reductase, mitochondrial precursor
MWVCSTLWRVRTPARQWRGLLPASGCHGPAASSYSASAEPARVRALVYGHHGDPAKVVEL
KNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGLLPELPAVGGNEGVAQVVAVGSNVT
GLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQ
LQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEE
ELRRPEMKNFFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLL
IFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEAS
MKPFISSKQILTM
Enzyme 19 Number of Residues 373
Enzyme 19 Molecular Weight 40428
Enzyme 19 Theoretical pI 9.01
Enzyme 19 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 19 General Function Energy production and conversion
Enzyme 19 Specific Function Catalyzes the reduction of trans-2-enoyl-CoA to acyl-CoA with chain length from C6 to C16 in an NADPH-dependent manner with preference to medium chain length substrate. May have a role in the mitochondrial synthesis of fatty acids
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions
  • acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-19
Enzyme 19 Transmembrane Regions Not Available
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 4929595 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9BV79 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name MECR_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1122 bp
ATGTGGGTCTGCAGTACCCTGTGGCGGGTGCGAACCCCGCCCGGCAGTGGCGGGGGCCTG
CTCCCAGCTTCTGGCTGTCACGGACCTGCCGCCTCCTCCTACTCCGCATCCGCCGAGCCT
GCCCGGGTCCGCGGCGTTGTCTATGGGCACCACGGGGATCCAGCCAAGGTCGTCGAACTC
AAGAACCTGGAGCTAGCTGCTGTGAGAGGATCAGATGTCCGTGTGAAGATGCTGGCGGCC
CCTATCAATCCATCTGACATAAATATGATCCAAGGAAACTACGGACTCCTTCCTGAACTG
CCTGCTGTTGGAGGGAACGAAGGTGTTGCACAGGTGGTAGCGGTGGGCAGCAATGTGACC
GGGCTGAAGCCAGGAGACTGGGTGATTCCAGCAAATGCTGGTTTAGGAACCTGGCGGACC
GAGGCTGTGTTCAGCGAGGAAGCACTGATCCAAGTTCCGAGTGACATCCCTCTTCAGAGC
GCTGCCACCCTGGGTGTCAATCCCTGCACAGCCTACAGGATGTTGATGGACTTCGAGCAA
CTGCAGCCAGGGGATTCTGTCATCCAGAATGCATCCAACAGCGGAGTGGGGCAAGCGGTC
ATCCAGATCGCCGCAGCCCTGGGCCTAAGAACCATCAATGTGGTCCGAGACAGACCTGAT
ATCCAGAAGCTGAGTGACAGACTGAAGAGTCTGGGGGCTGAGCATGTCATCACAGAAGAG
GAGCTAAGAAGGCCCGAAATGAAAAACTTCTTTAAGGACATGCCCCAGCCACGGCTTGCT
CTCAACTGTGTTGGTGGGAAAAGCTCCACAGAGCTGCTGCGCCAGTTAGCGCGTGGAGGA
ACCATGGTAACCTATGGGGGGATGGCCAAGCAGCCCGTCGTAGCCTCTGTGAGCCTGCTC
ATTTTTAAGGATCTCAAACTTCGAGGCTTTTGGTTGTCCCAGTGGAAGAAGGATCACAGT
CCAGACCAGTTCAAGGAGCTGATCCTCACACTGTGCGATCTCATCCGCCGAGGCCAGCTC
ACAGCCCCTGCCTGCTCCCAGGTCCCGCTGCAGGACTACCAGTCTGCCTTGGAAGCCTCC
ATGAAGCCCTTCATATCTTCAAAGCAGATTCTCACCATGTGA
Enzyme 19 GenBank Gene ID AF151821 Link Image
Enzyme 19 GeneCard ID MECR Link Image
Enzyme 19 GenAtlas ID MECR Link Image
Enzyme 19 HGNC ID HGNC:19691 Link Image
Enzyme 19 Chromosome Location 1
Enzyme 19 Locus 1p35.1-1p36.1
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
  2. Miinalainen IJ, Chen ZJ, Torkko JM, Pirila PL, Sormunen RT, Bergmann U, Qin YM, Hiltunen JK: Characterization of 2-enoyl thioester reductase from mammals. An ortholog of YBR026p/MRF1'p of the yeast mitochondrial fatty acid synthesis type II. J Biol Chem. 2003 May 30;278(22):20154-61. Epub 2003 Mar 24. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 7319
Enzyme 20 Name Lecithin retinol acyltransferase
Enzyme 20 Synonyms
  1. Phosphatidylcholine-- retinol O-acyltransferase
Enzyme 20 Gene Name LRAT
Enzyme 20 Protein Sequence >Lecithin retinol acyltransferase
MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTH
YGIYLGDNRVAHMMPDILLALTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGA
NILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNNCEHFVTYCRYGTPISPQSDK
FCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG
Enzyme 20 Number of Residues 230
Enzyme 20 Molecular Weight 25703
Enzyme 20 Theoretical pI 7.54
Enzyme 20 GO Classification Not Available
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters. Retinyl esters are storage forms of vitamin A. LRAT plays a critical role in vision. It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-retinaldehyde which is the chromophore for rhodopsin and the cone photopigments
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions
  • phosphatidylcholine + retinol-[cellular-retinol-binding-protein] = 2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • 1-31
Enzyme 20 Transmembrane Regions
  • 206-226
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 4240391 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID O95237 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name LRAT_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >693 bp
ATGAAGAACCCCATGCTGGAGGTGGTGTCTTTACTACTGGAGAAGCTGCTCCTCATCTCC
AACTTCACGCTCTTTAGTTCGGGCGCCGCGGGCAAGGACAAAGGGAGGAACAGTTTTTAT
GAAACCAGCTCTTTCCACCGAGGCGACGTGCTGGAGGTGCCCCGGACCCACCTGACCCAC
TATGGCATCTACCTAGGAGACAACCGTGTTGCCCACATGATGCCCGACATCCTGTTGGCC
CTGACAGACGACATGGGGCGCACGCAGAAGGTGGTCTCCAACAAGCGTCTCATCCTGGGC
GTTATTGTCAAAGTGGCCAGCATCCGCGTGGACACAGTGGAGGACTTCGCCTACGGAGCT
AACATCCTGGTCAATCACCTGGACGAGTCCCTCCAGAAAAAGGCACTGCTCAACGAGGAG
GTGGCGCGGAGGGCTGAAAAGCTGCTGGGCTTTACCCCCTACAGCCTGCTGTGGAACAAC
TGCGAGCACTTCGTGACCTACTGCAGATATGGCACCCCGATCAGTCCCCAGTCCGACAAG
TTTTGTGAGACTGTGAAGATAATTATTCGTGATCAGAGAAGTGTTCTTGCTTCAGCAGTC
TTGGGATTGGCGTCTATAGTCTGTACGGGCTTGGTATCATACACTACCCTTCCTGCAATT
TTTATTCCATTCTTCCTATGGATGGCTGGCTAA
Enzyme 20 GenBank Gene ID AF071510 Link Image
Enzyme 20 GeneCard ID LRAT Link Image
Enzyme 20 GenAtlas ID LRAT Link Image
Enzyme 20 HGNC ID HGNC:6685 Link Image
Enzyme 20 Chromosome Location 4
Enzyme 20 Locus 4q32.1
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Ruiz A, Winston A, Lim YH, Gilbert BA, Rando RR, Bok D: Molecular and biochemical characterization of lecithin retinol acyltransferase. J Biol Chem. 1999 Feb 5;274(6):3834-41. [PubMed Link Image]
  2. Mondal MS, Ruiz A, Bok D, Rando RR: Lecithin retinol acyltransferase contains cysteine residues essential for catalysis. Biochemistry. 2000 May 2;39(17):5215-20. [PubMed Link Image]
  3. Thompson DA, Li Y, McHenry CL, Carlson TJ, Ding X, Sieving PA, Apfelstedt-Sylla E, Gal A: Mutations in the gene encoding lecithin retinol acyltransferase are associated with early-onset severe retinal dystrophy. Nat Genet. 2001 Jun;28(2):123-4. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 7989
Enzyme 21 Name Orphan nuclear receptor NR1I3
Enzyme 21 Synonyms
  1. Constitutive androstane receptor
  2. CAR
  3. Constitutive activator of retinoid response
  4. Constitutive active response
  5. Orphan nuclear receptor MB67
Enzyme 21 Gene Name NR1I3
Enzyme 21 Protein Sequence >Orphan nuclear receptor NR1I3
MASREDELRNCVVCGDQATGYHFNALTCEGCKGFFRRTVSKSIGPTCPFAGSCEVSKTQR
RHCPACRLQKCLDAGMRKDMILSAEALALRRAKQAQRRAQQTPVQLSKEQEELIRTLLGA
HTRHMGTMFEQFVQFRPPAHLFIHHQPLPTLAPVLPLVTHFADINTFMVLQVIKFTKDLP
VFRSLPIEDQISLLKGAAVEICHIVLNTTFCLQTQNFLCGPLRYTIEDGARVSPTVGFQV
EFLELLFHFHGTLRKLQLQEPEYVLLAAMALFSPDRPGVTQRDEIDQLQEEMALTLQSYI
KGQQRRPRDRFLYAKLLGLLAELRSINEAYGYQIQHIQGLSAMMPLLQEICS
Enzyme 21 Number of Residues 352
Enzyme 21 Molecular Weight 39943
Enzyme 21 Theoretical pI 8.26
Enzyme 21 GO Classification
Function
  • DNA binding
  • binding
  • ligand-dependent nuclear receptor activity
  • nucleic acid binding
  • receptor activity
  • signal transducer activity
  • steroid hormone receptor activity
  • transcription factor activity
Process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function Binds and transactivates the retinoic acid response elements that control expression of the retinoic acid receptor beta 2 and alcohol dehydrogenase 3 genes. Transactivates both the phenobarbital responsive element module of the human CYP2B6 gene and the CYP3A4 xenobiotic response element
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 458542 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q14994 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name NR1I3_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1047 bp
ATGGCCAGTAGGGAAGATGAGCTGAGGAACTGTGTGGTATGTGGGGACCAAGCCACAGGC
TACCACTTTAATGCGCTGACTTGTGAGGGCTGCAAGGGTTTCTTCAGGAGAACAGTCAGC
AAAAGCATTGGTCCCACCTGCCCCTTTGCTGGAAGCTGTGAAGTCAGCAAGACTCAGAGG
CGCCACTGCCCAGCCTGCAGGTTGCAGAAGTGCTTAGATGCTGGCATGAGGAAAGACATG
ATACTGTCGGCAGAAGCCCTGGCATTGCGGCGAGCAAAGCAGGCCCAGCGGCGGGCACAG
CAAACACCTGTGCAACTGAGTAAGGAGCAAGAAGAGCTGATCCGGACACTCCTGGGGGCC
CACACCCGCCACATGGGCACCATGTTTGAACAGTTTGTGCAGTTTAGGCCTCCAGCTCAT
CTGTTCATCCATCACCAGCCCTTGCCCACCCTGGCCCCTGTGCTGCCTCTGGTCACACAC
TTCGCAGACATCAACACTTTCATGGTACTGCAAGTCATCAAGTTTACTAAGGACCTGCCC
GTCTTCCGTTCCCTGCCCATTGAAGACCAGATCTCCCTTCTCAAGGGAGCAGCTGTGGAA
ATCTGTCACATCGTACTCAATACCACTTTCTGTCTCCAAACACAAAACTTCCTCTGCGGG
CCTCTTCGCTACACAATTGAAGATGGAGCCCGTGTGGGGTTCCAGGTAGAGTTTTTGGAG
TTGCTCTTTCACTTCCATGGAACACTACGAAAACTGCAGCTCCAAGAGCCTGAGTATGTG
CTCTTGGCTGCCATGGCCCTCTTCTCTCCTGACCGACCTGGAGTTACCCAGAGAGATGAG
ATTGATCAGCTGCAAGAGGAGATGGCACTGACTCTGCAAAGCTACATCAAGGGCCAGCAG
CGAAGGCCCCGGGATCGGTTTCTGTATGCGAAGTTGCTAGGCCTGCTGGCTGAGCTCCGG
AGCATTAATGAGGCCTACGGGTACCAAATCCAGCACATCCAGGGCCTGTCTGCCATGATG
CCGCTGCTCCAGGAGATCTGCAGCTGA
Enzyme 21 GenBank Gene ID Z30425 Link Image
Enzyme 21 GeneCard ID NR1I3 Link Image
Enzyme 21 GenAtlas ID NR1I3 Link Image
Enzyme 21 HGNC ID HGNC:7969 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 1q23.3
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Baes M, Gulick T, Choi HS, Martinoli MG, Simha D, Moore DD: A new orphan member of the nuclear hormone receptor superfamily that interacts with a subset of retinoic acid response elements. Mol Cell Biol. 1994 Mar;14(3):1544-52. [PubMed Link Image]
  2. Choi HS, Seol W, Moore DD: A component of the 26S proteasome binds on orphan member of the nuclear hormone receptor superfamily. J Steroid Biochem Mol Biol. 1996 Jan;56(1-6 Spec No):23-30. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 8781
Enzyme 22 Name Zinc-binding alcohol dehydrogenase domain-containing protein 2
Enzyme 22 Synonyms Not Available
Enzyme 22 Gene Name ZADH2
Enzyme 22 Protein Sequence >Zinc-binding alcohol dehydrogenase domain-containing protein 2
MLRLVPTGARAIVDMSYARHFLDFQGSAIPQAMQKLVVTRLSPNFREAVTLSRDCPVPLP
GDGDLLVRNRFVGVNASDINYSAGRYDPSVKPPFDIGFEGIGEVVALGLSASARYTVGQA
VAYMAPGSFAEYTVVPASIATPVPSVKPEYLTLLVSGTTAYISLKELGGLSEGKKVLVTA
AAGGTGQFAMQLSKKAKCHVIGTCSSDEKSAFLKSLGCDRPINYKTEPVGTVLKQEYPEG
VDVVYESVGGAMFDLAVDALATKGRLIVIGFISGYQTPTGLSPVKAGTLPAKLLKKSASV
QGFFLNHYLSKYQAAMSHLLEMCVSGDLVCEVDLGDLSPEGRFTGLESIFRAVNYMYMGK
NTGKIVVELPHSVNSKL
Enzyme 22 Number of Residues 377
Enzyme 22 Molecular Weight 40141
Enzyme 22 Theoretical pI 8.32
Enzyme 22 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 22 General Function Energy production and conversion
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals Not Available
Enzyme 22 Transmembrane Regions Not Available
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 21707266 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q8N4Q0 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name ZADH2_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1134 bp
ATGCTGCGGCTGGTGCCCACCGGGGCCCGGGCCATCGTGGACATGTCGTACGCCCGCCAC
TTCCTGGACTTCCAGGGCTCCGCCATTCCCCAAGCCATGCAGAAGCTGGTGGTGACCCGG
CTGAGCCCCAACTTCCGCGAGGCCGTCACCCTGAGCCGGGACTGCCCGGTGCCGCTCCCC
GGGGACGGAGACCTCCTCGTCCGGAACCGATTTGTTGGTGTTAACGCATCTGACATCAAC
TATTCAGCAGGCCGCTATGACCCCTCAGTTAAGCCTCCCTTTGACATAGGTTTCGAAGGC
ATTGGGGAGGTGGTGGCCCTAGGCCTCTCTGCTAGTGCCAGATACACAGTTGGCCAAGCT
GTGGCTTACATGGCACCTGGTTCTTTTGCTGAGTACACAGTTGTGCCTGCCAGCATTGCA
ACTCCAGTGCCCTCAGTGAAACCCGAGTATCTTACCCTGCTGGTAAGTGGCACCACCGCA
TACATCAGCCTGAAAGAGCTCGGAGGACTGTCGGAAGGGAAAAAAGTTTTGGTGACAGCA
GCAGCTGGGGGAACGGGCCAGTTTGCCATGCAGCTTTCAAAGAAGGCAAAGTGCCATGTA
ATTGGAACCTGCTCTTCTGATGAAAAGTCTGCTTTTCTGAAATCTCTTGGCTGTGATCGT
CCTATCAACTATAAAACTGAACCCGTAGGTACCGTCCTTAAGCAGGAGTACCCTGAAGGT
GTCGATGTGGTCTATGAATCTGTTGGGGGAGCCATGTTTGACTTGGCTGTAGACGCCCTG
GCTACGAAAGGGCGCTTGATAGTAATAGGGTTTATCTCTGGCTACCAAACTCCTACTGGC
CTTTCGCCTGTGAAAGCAGGAACATTGCCAGCCAAACTGCTCAAGAAATCTGCCAGCGTA
CAGGGCTTCTTCCTGAACCATTACCTTTCTAAGTATCAAGCAGCCATGAGCCACTTGCTC
GAGATGTGTGTGAGCGGAGACCTGGTTTGTGAGGTGGACCTTGGAGATCTGTCTCCAGAG
GGCAGGTTTACTGGCCTGGAGTCCATATTCCGTGCTGTCAATTATATGTACATGGGAAAA
AACACTGGAAAAATTGTAGTTGAATTACCTCACTCTGTCAACAGTAAGCTGTAA
Enzyme 22 GenBank Gene ID BC033780 Link Image
Enzyme 22 GeneCard ID ZADH2 Link Image
Enzyme 22 GenAtlas ID ZADH2 Link Image
Enzyme 22 HGNC ID HGNC:28697 Link Image
Enzyme 22 Chromosome Location 18
Enzyme 22 Locus 18q22.3
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References Not Available
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 8823
Enzyme 23 Name Retinol dehydrogenase 13
Enzyme 23 Synonyms Not Available
Enzyme 23 Gene Name RDH13
Enzyme 23 Protein Sequence >Retinol dehydrogenase 13
MSRYLLPLSALGTVAGAAVLLKDYVTGGACPSKATIPGKTVIVTGANTGIGKQTALELAR
RGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDI
LINNAGVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAG
HIDFDDLNWQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH
TGIHGSTFSSTTLGPIFWLLVKSPELAAQPSTYLAVAEELADVSGKYFDGLKQKAPAPEA
EDEEVARRLWAESARLVGLEAPSVREQPLPR
Enzyme 23 Number of Residues 331
Enzyme 23 Molecular Weight 35933
Enzyme 23 Theoretical pI 8.24
Enzyme 23 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 23 General Function Lipid transport and metabolism
Enzyme 23 Specific Function Does not exhibit retinol dehydrogenase (RDH) activity in vitro
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-17
Enzyme 23 Transmembrane Regions Not Available
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 22761451 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q8NBN7 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name RDH13_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >996 bp
ATGAGCCGCTACCTGCTGCCGCTGTCGGCGCTGGGCACGGTAGCAGGCGCCGCCGTGCTG
CTCAAGGACTATGTCACCGGTGGGGCTTGCCCCAGCAAGGCCACCATCCCTGGGAAGACG
GTCATCGTGACGGGCGCCAACACAGGCATCGGGAAGCAGACCGCCTTGGAACTGGCCAGG
AGAGGAGGCAACATCATCCTGGCCTGCCGAGACATGGAGAAGTGTGAGGCGGCAGCAAAG
GACATCCGCGGGGAGACCCTCAATCACCATGTCAACGCCCGGCACCTGGACTTGGCTTCC
CTCAAGTCTATCCGAGTGTTTGCAGCAAAGATCATTGAAGAGGAGGAGCGAGTGGACATT
CTAATCAACAACGCGGGTGTGATGCGGTGCCCCCACTGGACCACCGAGGACGGCTTCGAG
ATGCAGTTTGGCGTTAACCACCTGGGTCACTTTCTCTTGACAAACTTGCTGCTGGACAAG
CTGAAAGCCTCAGCCCCTTCGCGGATCATCAACCTCTCGTCCCTGGCCCATGTTGCTGGG
CACATAGACTTTGACGACTTGAACTGGCAGACGAGGAAGTATAACACCAAAGCCGCCTAC
TGCCAGAGCAAGCTCGCCATCGTCCTCTTCACCAAGGAGCTGAGCCGGCGGCTGCAAGGC
TCTGGTGTGACTGTCAACGCCCTGCACCCCGGCGTGGCCAGGACAGAGCTGGGCAGACAC
ACGGGCATCCATGGCTCCACCTTCTCCAGCACCACACTCGGGCCCATCTTCTGGCTGCTG
GTCAAGAGCCCCGAGCTGGCCGCCCAGCCCAGCACATACCTGGCCGTGGCGGAGGAACTG
GCGGATGTTTCCGGAAAGTACTTCGATGGACTCAAACAGAAGGCCCCGGCCCCCGAGGCT
GAGGATGAGGAGGTGGCCCGGAGGCTTTGGGCTGAAAGTGCCCGCCTGGTGGGCTTAGAG
GCTCCCTCTGTGAGGGAGCAGCCCCTCCCCAGATAA
Enzyme 23 GenBank Gene ID AK075392 Link Image
Enzyme 23 GeneCard ID RDH13 Link Image
Enzyme 23 GenAtlas ID RDH13 Link Image
Enzyme 23 HGNC ID HGNC:19978 Link Image
Enzyme 23 Chromosome Location 19
Enzyme 23 Locus 19q13.42
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 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. Haeseleer F, Jang GF, Imanishi Y, Driessen CA, Matsumura M, Nelson PS, Palczewski K: Dual-substrate specificity short chain retinol dehydrogenases from the vertebrate retina. J Biol Chem. 2002 Nov 22;277(47):45537-46. Epub 2002 Sep 10. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 9419
Enzyme 24 Name Alcohol dehydrogenase iron-containing 1
Enzyme 24 Synonyms Not Available
Enzyme 24 Gene Name ADHFE1
Enzyme 24 Protein Sequence >Alcohol dehydrogenase iron-containing 1
MAAAARARVAYLLRQLQRAACQCPTHSHTYSQAPGLSPSGKTTDYAFEMAVSNIRYGAAV
TKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFM
EAIEFAQKGAFDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYVSAPIGKGKPVSVPLKP
LIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSG
FDVLCHALESYTTLPYHLRSPCPSNPITRPAYQGSNPISDIWAIHALRIVAKYLKRAVRN
PDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMYKAKDYNVDHPLVPHGLS
VVLTSPAVFTFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGL
AAVGYSKADIPALVKGTLPQERVTKLAPCPQSEEDLAALFEASMKLY
Enzyme 24 Number of Residues 467
Enzyme 24 Molecular Weight 50308
Enzyme 24 Theoretical pI Not Available
Enzyme 24 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolism
  • physiological process
Component
Enzyme 24 General Function Energy production and conversion
Enzyme 24 Specific Function Not Available
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions
  • 3,4-Dihydroxymandelaldehyde + H+ + Nicotinamide adenine dinucleotide - reduced <==> 3,4-Dihydroxyphenylethyleneglycol + Nicotinamide adenine dinucleotide
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 25989126 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q8IWW8 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name Q8IWW8_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence Not Available
Enzyme 24 GenBank Gene ID AY033237 Link Image
Enzyme 24 GeneCard ID Not Available
Enzyme 24 GenAtlas ID ADHFE1 Link Image
Enzyme 24 HGNC ID HGNC:16354 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. Deng Y, Wang Z, Gu S, Ji C, Ying K, Xie Y, Mao Y: Cloning and characterization of a novel human alcohol dehydrogenase gene (ADHFe1). DNA Seq. 2002 Oct;13(5):301-6. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 12890
Enzyme 25 Name Fatty acyl-CoA reductase 2
Enzyme 25 Synonyms
  1. Male sterility domain- containing protein 1
Enzyme 25 Gene Name MLSTD1
Enzyme 25 Protein Sequence >Fatty acyl-CoA reductase 2
MSTIAAFYGGKSILITGATGFLGKVLMEKLFRTSPDLKVIYILVRPKAGQTLQQRVFQIL
DSKLFEKVKEVCPNVHEKIRAIYADLNQNDFAISKEDMQELLSCTNIIFHCAATVRFDDT
LRHAVQLNVTATRQLLLMASQMPKLEAFIHISTAYSNCNLKHIDEVIYPCPVEPKKIIDS
LEWLDDAIIDEITPKLIRDWPNIYTYTKALGEMVVQQESRNLNIAIIRPSIVGATWQEPF
PGWVDNINGPNGIIIATGKGFLRAIKATPMAVADVIPVDTVVNLMLAVGWYTAVHRPKST
LVYHITSGNMNPCNWHKMGVQVLATFEKIPFERPFRRPNANFTSNSFTSQYWNAVSHRAP
AIIYDCYLRLTGRKPRMTKLMNRLLRTVSMLEYFINRSWEWSTYNTEMLMSELSPEDQRV
FNFDVRQLNWLEYIENYVLGVKKYLLKEDMAGIPKAKQRLKRLRNIHYLFNTALFLIAWR
LLIARSQMARNVWFFIVSFCYKFLSYFRASSTLKV
Enzyme 25 Number of Residues 515
Enzyme 25 Molecular Weight 59439
Enzyme 25 Theoretical pI Not Available
Enzyme 25 GO Classification Not Available
Enzyme 25 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 25 Specific Function Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. The preferred substrates are C16, C18, C18:1 and C18:2 but low activity can be observed with C10-C14 substrates
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • 465-484 491-510
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 12053191 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q96K12 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name FACR2_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence Not Available
Enzyme 25 GenBank Gene ID AL136843 Link Image
Enzyme 25 GeneCard ID Not Available
Enzyme 25 GenAtlas ID MLSTD1 Link Image
Enzyme 25 HGNC ID HGNC:25531 Link Image
Enzyme 25 Chromosome Location Not Available
Enzyme 25 Locus Not Available
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 12898
Enzyme 26 Name Acyl-CoA wax alcohol acyltransferase 2
Enzyme 26 Synonyms
  1. Long-chain- alcohol O-fatty-acyltransferase 2
  2. Wax synthase
  3. hWS
  4. Multifunctional O-acyltransferase
  5. Diacylglycerol O-acyltransferase 2-like protein 4
  6. Diacylglycerol O-acyltransferase candidate 4
  7. hDC4
Enzyme 26 Gene Name DGAT2L4
Enzyme 26 Protein Sequence >Acyl-CoA wax alcohol acyltransferase 2
MLLPSKKDLKTALDVFAVFQWSFSALLITTTVIAVNLYLVVFTPYWPVTVLILTWLAFDW
KTPQRGGRRFTCVRHWRLWKHYSDYFPLKLLKTHDICPSRNYILVCHPHGLFAHGWFGHF
ATEASGFSKIFPGITPYILTLGAFFWMPFLREYVMSTGACSVSRSSIDFLLTHKGTGNMV
IVVIGGLAECRYSLPGSSTLVLKNRSGFVRMALQHGVPLIPAYAFGETDLYDQHIFTPGG
FVNRFQKWFQSMVHIYPCAFYGRGFTKNSWGLLPYSRPVTTIVGEPLPMPKIENPSQEIV
AKYHTLYIDALRKLFDQHKTKFGISETQELEII
Enzyme 26 Number of Residues 333
Enzyme 26 Molecular Weight 38094
Enzyme 26 Theoretical pI 9.69
Enzyme 26 GO Classification Not Available
Enzyme 26 General Function Not Available
Enzyme 26 Specific Function Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has no activity using decyl alcohol and significantly prefers the C16 and C18 alcohols. May also have 2-acylglycerol O-acyltransferase (MGAT) and acyl- CoA:retinol acyltransferase (ARAT) activities, to catalyze the synthesis of diacylglycerols and retinyl esters; however this activity is unclear in vivo
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions
  • acyl-CoA + a long-chain alcohol = CoA + a long-chain ester [RN:R01999] ALL_REAC R01999
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • 15-35 38-58 130-150
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 49854214 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q6E213 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name AWAT2_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence Not Available
Enzyme 26 GenBank Gene ID AY605053 Link Image
Enzyme 26 GeneCard ID Q6E213 Link Image
Enzyme 26 GenAtlas ID DGAT2L4 Link Image
Enzyme 26 HGNC ID HGNC:23251 Link Image
Enzyme 26 Chromosome Location Not Available
Enzyme 26 Locus Not Available
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References Not Available
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 13474
Enzyme 27 Name Klotho precursor
Enzyme 27 Synonyms Not Available
Enzyme 27 Gene Name KL
Enzyme 27 Protein Sequence >Klotho precursor
MPASAPPRRPRPPPPSLSLLLVLLGLGGRRLRAEPGDGAQTWARFSRPPAPEAAGLFQGT
FPDGFLWAVGSAAYQTEGGWQQHGKGASIWDTFTHHPLAPPGDSRNASLPLGAPSPLQPA
TGDVASDSYNNVFRDTEALRELGVTHYRFSISWARVLPNGSAGVPNREGLRYYRRLLERL
RELGVQPVVTLYHWDLPQRLQDAYGGWANRALADHFRDYAELCFRHFGGQVKYWITIDNP
YVVAWHGYATGRLAPGIRGSPRLGYLVAHNLLLAHAKVWHLYNTSFRPTQGGQVSIALSS
HWINPRRMTDHSIKECQKSLDFVLGWFAKPVFIDGDYPESMKNNLSSILPDFTESEKKFI
KGTADFFALCFGPTLSFQLLDPHMKFRQLESPNLRQLLSWIDLEFNHPQIFIVENGWFVS
GTTKRDDAKYMYYLKKFIMETLKAIKLDGVDVIGYTAWSLMDGFEWHRGYSIRRGLFYVD
FLSQDKMLLPKSSALFYQKLIEKNGFPPLPENQPLEGTFPCDFAWGVVDNYIQVDTTLSQ
FTDLNVYLWDVHHSKRLIKVDGVVTKKRKSYCVDFAAIQPQIALLQEMHVTHFRFSLDWA
LILPLGNQSQVNHTILQYYRCMASELVRVNITPVVALWQPMAPNQGLPRLLARQGAWENP
YTALAFAEYARLCFQELGHHVKLWITMNEPYTRNMTYSAGHNLLKAHALAWHVYNEKFRH
AQNGKISIALQADWIEPACPFSQKDKEVAERVLEFDIGWLAEPIFGSGDYPWVMRDWLNQ
RNNFLLPYFTEDEKKLIQGTFDFLALSHYTTILVDSEKEDPIKYNDYLEVQEMTDITWLN
SPSQVAVVPWGLRKVLNWLKFKYGDLPMYIISNGIDDGLHAEDDQLRVYYMQNYINEALK
AHILDGINLCGYFAYSFNDRTAPRFGLYRYAADQFEPKASMKHYRKIIDSNGFPGPETLE
RFCPEEFTVCTECSFFHTRKSLLAFIAFLFFASIISLSLIFYYSKKGRRSYK
Enzyme 27 Number of Residues 1012
Enzyme 27 Molecular Weight 116182
Enzyme 27 Theoretical pI 8.05
Enzyme 27 GO Classification
Function
  • catalytic activity
  • glucosidase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 27 General Function Carbohydrate transport and metabolism
Enzyme 27 Specific Function The Klotho peptide generated by cleavage of the membrane-bound isoform may be an anti-aging circulating hormone which would extend life span by inhibiting insulin/IGF1 signaling
Enzyme 27 Pathways
Enzyme 27 Reactions
  • a beta-D-glucuronoside + H2O = D-glucuronate + an alcohol [RN:R01478] ALL_REAC R01478
  • (other) R04979 R07818(G)
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • 1-33
Enzyme 27 Transmembrane Regions
  • 982-1002
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 2618596 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q9UEF7 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name KLOT_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >3039 bp
ATGCCCGCCAGCGCCCCGCCGCGCCGCCCGCGGCCGCCGCCGCCGTCGCTGTCGCTGCTG
CTGGTGCTGCTGGGCCTGGGCGGCCGCCGCCTGCGTGCGGAGCCGGGCGACGGCGCGCAG
ACCTGGGCCCGTGTCTCGCGGCCTCCTGCCCCCGAGGCCGCGGGCCTCTTCCAGGGCACC
TTCCCCGACGGCTTCCTCTGGGCCGTGGGCAGCGCCGCCTACCAGACCGAGGGCGGCTGG
CAGCAGCACGGCAAGGGTGCGTCCATCTGGGACACGTTCACCCACCACCCCCTGGCACCC
CCGGGAGACTCCCGGAACGCCAGTCTGCCGTTGGGCGCCCCGTCGCCGCTGCAGCCCGCC
ACCGGGGACGTAGCCAGCGACAGCTACAACAACGTCTTCCGCGACACGGAGGCGCTGCGC
GAGCTCGGGGTCACTCACTACCGCTTCTCCATCTCGTGGGCGCGAGTGCTCCCCAATGGC
AGCGCGGGCGTCCCCAACCGCGAGGGGCTGCGCTACTACCGGCGCCTGCTGGAGCGGCTG
CGGGAGCTGGGCGTGCAGCCCGTGGTCACCCTGTACCACTGGGACCTGCCCCAGCGCCTG
CAGGACGCCTACGGCGGCTGGGCCAACCGCGCCCTGGCCGACCACTTCAGGGATTACGCG
GAGCTCTGCTTCCGCCACTTCGGCGGTCAGGTCAAGTACTGGATCACCATCGACAACCCC
TACGTGGTGGCCTGGCACGGCTACGCCACCGGGCGCCTGGCCCCCGGCATCCGGGGCAGC
CCGCGGCTCGGGTACCTGGTGGCGCACAACCTCCTCCTGGCTCATGCCAAAGTCTGGCAT
CTCTACAATACTTCTTTCCGTCCCACTCAGGGAGGTCAGGTGTCCATTGCCCTAAGCTCT
CACTGGATCAATCCTCGAAGAATGACCGACCACAGCATCAAAGAATGTCAAAAATCTCTG
GACTTTGTACTAGGTTGGTTTGCCAAACCCGTATTTATTGATGGTGACTATCCCGAGAGC
ATGAAGAATAACCTTTCATCTATTCTGCCTGATTTTACTGAATCTGAGAAAAAGTTCATC
AAAGGAACTGCTGACTTTTTTGCTCTTTGCTTTGGACCCACCTTGAGTTTTCAACTTTTG
GACCCTCACATGAAGTTCCGCCAATTGGAATCTCCCAACCTGAGGCAACTGCTTTCCTGG
ATTGACCTTGAATTTAACCATCCTCAAATATTTATTGTGGAAAATGGCTGGTTTGTCTCA
GGGACCACCAAGAGAGATGATGCCAAATATATGTATTACCTCAAAAAGTTCATCATGGAA
ACCTTAAAAGCCATCAAGCTGGATGGGGTGGATGTCATCGGGTATACCGCATGGTCCCTC
ATGGATGGTTTCGAGTGGCACAGAGGTTACAGCATCAGGCGTGGACTCTTCTATGTTGAC
TTTCTAAGCCAGGACAAGATGTTGTTGCCAAAGTCTTCAGCCTTGTTCTACCAAAAGCTG
ATAGAGAAAAATGGCTTCCCTCCTTTACCTGAAAATCAGCCCCTAGAAGGGACATTTCCC
TGTGACTTTGCTTGGGGAGTTGTTGACAACTACATTCAAGTAGATACCACTCTGTCTCAG
TTTACCGACCTGAATGTTTACCTGTGGGATGTCCACCACAGTAAAAGGCTTATTAAAGTG
GATGGGGTTGTGACCAAGAAGAGGAAATCCTACTGTGTTGACTTTGCTGCCATCCAGCCC
CAGATCGCTTTACTCCAGGAAATGCACGTTACACATTTTCGCTTCTCCCTGGACTGGGCC
CTGATTCTCCCTCTGGGTAACCAGTCCCAGGTGAACCACACCATCCTGCAGTACTATCGC
TGCATGGCCAGCGAGCTTGTCCGTGTCAACATCACCCCAGTGGTGGCCCTGTGGCAGCCT
ATGGCCCCGAACCAAGGACTGCCGCGCCTCCTGGCCAGGCAGGGCGCCTGGGAGAACCCC
TACACTGCCCTGGCCTTTGCAGAGTATGCCCGACTGTGCTTTCAAGAGCTCGGCCATCAC
GTCAAGCTTTGGATAACGATGAATGAGCCGTATACAAGGAATATGACATACAGTGCTGGC
CACAACCTTCTGAAGGCCCATGCCCTGGCTTGGCATGTGTACAATGAAAAGTTTAGGCAT
GCTCAGAATGGGAAAATATCCATAGCCTTGCAGGCTGATTGGATAGAACCTGCCTGCCCT
TTCTCCCAAAAGGACAAAGAGGTGGCCGAGAGAGTTTTGGAATTTGACATTGGCTGGCTG
GCTGAGCCCATTTTCGGCTCTGGAGATTATCCATGGGTGATGAGGGACTGGCTGAACCAA
AGAAACAATTTTCTTCTTCCTTATTTCACTGAAGATGAAAAAAAGCTAATCCAGGGTACC
TTTGACTTTTTGGCTTTAAGCCATTATACCACCATCCTTGTAGACTCAGAAAAAGAAGAT
CCAATAAAATACAATGATTACCTAGAAGTGCAAGAAATGACCGACATCACGTGGCTCAAC
TCCCCCAGTCAGGTGGCGGTAGTGCCCTGGGGGTTGCGCAAAGTGCTGAACTGGCTGAAG
TTCAAGTACGGAGACCTCCCCATGTACATAATATCCAACGGAATCGATGACGGGCTGCAT
GCTGAGGACGACCAGCTGAGGGTGTATTATATGCAGAATTACATAAACGAAGCTCTCAAA
GCCCACATACTGGATGGTATCAATCTTTGCGGATACTTTGCTTATTCGTTTAACGACCGC
ACAGCTCCGAGGTTTGGCCTCTATCGTTATGCTGCAGATCAGTTTGAGCCCAAGGCATCC
ATGAAACATTACAGGAAAATTATTGACAGCAATGGTTTCCCGGGCCCAGAAACTCTGGAA
AGATTTTGTCCAGAAGAATTCACCGTGTGTACTGAGTGCAGTTTTTTTCACACCCGAAAG
TCTTTACTGGCTTTCATAGCTTTTCTATTTTTTGCTTCTATTATTTCTCTCTCCCTTATA
TTTTACTACTCGAAGAAAGGCAGAAGAAGTTACAAATAG
Enzyme 27 GenBank Gene ID AB005142 Link Image
Enzyme 27 GeneCard ID Q9UEF7 Link Image
Enzyme 27 GenAtlas ID KL Link Image
Enzyme 27 HGNC ID HGNC:6344 Link Image
Enzyme 27 Chromosome Location 13
Enzyme 27 Locus 13q12
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Kuro-o M, Matsumura Y, Aizawa H, Kawaguchi H, Suga T, Utsugi T, Ohyama Y, Kurabayashi M, Kaname T, Kume E, Iwasaki H, Iida A, Shiraki-Iida T, Nishikawa S, Nagai R, Nabeshima YI: Mutation of the mouse klotho gene leads to a syndrome resembling ageing. Nature. 1997 Nov 6;390(6655):45-51. [PubMed Link Image]
  2. Matsumura Y, Aizawa H, Shiraki-Iida T, Nagai R, Kuro-o M, Nabeshima Y: Identification of the human klotho gene and its two transcripts encoding membrane and secreted klotho protein. Biochem Biophys Res Commun. 1998 Jan 26;242(3):626-30. [PubMed Link Image]
  3. Yahata K, Mori K, Arai H, Koide S, Ogawa Y, Mukoyama M, Sugawara A, Ozaki S, Tanaka I, Nabeshima Y, Nakao K: Molecular cloning and expression of a novel klotho-related protein. J Mol Med. 2000;78(7):389-94. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 14404
Enzyme 28 Name CDNA FLJ16165 fis, clone BRCOC2019841
Enzyme 28 Synonyms Not Available
Enzyme 28 Gene Name Not Available
Enzyme 28 Protein Sequence >CDNA FLJ16165 fis, clone BRCOC2019841
MHPLPGYWSCYCLLLLFSLGVQGSLGAPSAAPEQVHLSYPGEPGSMTVTWTTWVPTRSEV
QFGLQPSGPLPLRAQGTFVPFVDGGILRRKLYIHRVTLRKLLPGVQYVYRCGSAQGWSRR
FRFRALKNGAHWSPRLAVFGDLGADNPKAVPRLRRDTQQGMYDAVLHVGDFAYNLDQDNA
RVGDRFMRLIEPVAASLPYMTCPGNHEERYNFSNYKARFSMPGDNEGLWYSWDLGPAHII
SFSTEVYFFLHYGRHLVQRQFRWLESDLQKANKNRAARPWIITMGHRPMYCSNADLDDCT
RHESKVRKGLQGKLYGLEDLFYKYGVDLQLWAHEHSYERLWPIYNYQVFNGSREMPYTNP
RGPVHIITGSAGCEERLTPFAVFPRPWSAVRVKEYGYTRLHILNGTHTHIQQVSDDQDGK
IVDDVWVVRPLFGRRMYL
Enzyme 28 Number of Residues 438
Enzyme 28 Molecular Weight 50468
Enzyme 28 Theoretical pI 9.42
Enzyme 28 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Not Available
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • 1-26
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 47076980 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q6ZNF0 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name Q6ZNF0_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1317 bp
ATGCACCCCCTTCCTGGCTACTGGTCCTGTTACTGTCTACTCCTGCTATTCTCCTTGGGA
GTCCAGGGGTCCCTGGGGGCTCCCAGCGCTGCCCCAGAGCAAGTCCATCTGTCTTACCCA
GGTGAGCCAGGCTCCATGACTGTAACTTGGACCACATGGGTCCCAACCCGCTCTGAAGTG
CAATTCGGGTTGCAGCCGTCGGGGCCCCTGCCCCTCCGCGCCCAGGGCACCTTCGTCCCC
TTTGTGGACGGGGGCATTCTCCGGCGGAAGCTCTACATACACCGAGTCACGCTTCGCAAG
CTGCTGCCAGGGGTTCAGTATGTTTATCGCTGTGGCAGTGCGCAGGGCTGGAGCCGTCGG
TTCCGCTTCAGGGCCCTCAAGAATGGGGCCCACTGGAGTCCCCGTCTGGCTGTGTTTGGA
GACCTGGGGGCTGACAACCCGAAGGCCGTCCCCCGGCTGCGCAGGGACACCCAGCAGGGC
ATGTATGACGCCGTTCTCCATGTGGGAGACTTTGCCTACAACCTGGATCAGGACAACGCC
CGTGTTGGGGATAGGTTCATGCGGCTCATTGAACCCGTGGCTGCCAGCCTGCCGTACATG
ACATGCCCTGGGAATCATGAAGAACGCTACAACTTCTCTAACTACAAGGCTCGCTTCAGC
ATGCCGGGGGATAATGAGGGCCTGTGGTACAGCTGGGATCTGGGTCCCGCCCACATCATC
TCCTTCTCCACCGAGGTCTATTTCTTTCTCCATTATGGCCGCCACTTGGTACAGAGGCAG
TTTCGCTGGCTGGAGAGCGACCTCCAGAAAGCCAATAAGAACCGGGCAGCCCGGCCGTGG
ATCATCACTATGGGGCACCGGCCCATGTACTGCTCCAACGCAGATCTGGACGACTGCACA
CGACATGAAAGCAAGGTCCGCAAAGGCCTCCAAGGCAAGCTGTACGGGTTGGAGGATCTT
TTCTACAAATATGGAGTGGATCTGCAGCTGTGGGCTCATGAGCACTCGTATGAACGACTG
TGGCCAATTTACAACTACCAGGTATTTAACGGCAGCCGAGAGATGCCCTACACTAACCCG
CGAGGGCCTGTCCACATCATCACAGGATCTGCTGGCTGTGAGGAGCGGCTGACGCCCTTT
GCTGTCTTCCCGAGGCCCTGGAGTGCCGTGCGTGTGAAGGAGTACGGGTATACGCGGCTG
CACATCCTCAACGGGACCCACACCCACATCCAGCAGGTGTCGGACGACCAGGATGGGAAG
ATCGTAGATGATGTCTGGGTGGTGAGACCCCTGTTTGGCCGGAGGATGTACCTCTAG
Enzyme 28 GenBank Gene ID AK131245 Link Image
Enzyme 28 GeneCard ID Q6ZNF0 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 15247
Enzyme 29 Name Testicular acid phosphatase
Enzyme 29 Synonyms Not Available
Enzyme 29 Gene Name ACPT
Enzyme 29 Protein Sequence >Testicular acid phosphatase
MAGLGFWGHPAGPLLLLLLLVLPPRALPEGPLVFVALVFRHGDRAPLASYPMDPHKEVAS
TLWPRGLGQLTTEGVRQQLELGRFLRSRYEAFLSPEYRREEVYIRSTDFDRTLESAQANL
AGLFPEAAPGSPEARWRPIPVHTVPVAEDKLLRFPMRSCPRYHELLREATEAAEYQEALE
GWTGFLSRLENFTGLSLVGEPLRRAWKVLDTLMCQQAHGLPLPAWASPDVLRTLAQISAL
DIGAHVGPPRAAEKAQLTGGILLNAILANFSRVQRLGLPLKMVMYSAHDSTLLALQGALG
LYDGHTPPYAACLGFEFRKHLGNPAKDGGNVTVSLFYRNDSAHLPLPLSLPGCPAPCPLG
RFYQLTAPARPPAHGVSCHGPYEAAIPPAPVVPLLAGAVAVLVALSLGLGLLAWRPGCLR
ALGGPV
Enzyme 29 Number of Residues 426
Enzyme 29 Molecular Weight 46090
Enzyme 29 Theoretical pI 8.29
Enzyme 29 GO Classification
Function
  • acid phosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
Component
Enzyme 29 General Function Not Available
Enzyme 29 Specific Function Dephosphorylates receptor tyrosine-protein kinase erbB-4 and inhibits the ligand-induced proteolytic cleavage
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • 1-26
Enzyme 29 Transmembrane Regions
  • 394-414
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 12958660 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q9BZG2 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name PPAT_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1281 bp
ATGGCCGGCCTGGGGTTTTGGGGCCACCCTGCTGGACCTCTCCTGCTGCTGCTGCTGCTG
GTGCTGCCACCCCGGGCCCTGCCAGAAGGACCCCTGGTGTTCGTGGCTCTGGTATTCCGC
CATGGCGACCGGGCCCCGCTGGCCTCCTACCCCATGGACCCACACAAGGAGGTGGCCTCC
ACCCTGTGGCCACGAGGCCTGGGCCAGCTGACCACGGAGGGGGTCCGCCAGCAGCTGGAG
CTGGGCCGCTTCCTGAGGAGCCGCTACGAGGCCTTCCTGAGTCCGGAGTACCGGCGGGAG
GAGGTGTACATCCGCAGCACGGACTTTGACCGCACGCTGGAGAGTGCCCAGGCCAACCTT
GCCGGGCTGTTTCCCGAGGCTGCTCCAGGGAGCCCCGAGGCCCGCTGGAGGCCGATCCCG
GTGCACACGGTGCCCGTGGCTGAGGATAAGCTGCTGAGGTTCCCCATGCGCAGCTGTCCC
CGATACCACGAGCTGCTGCGGGAGGCCACCGAGGCCGCCGAGTACCAGGAGGCCCTGGAG
GGCTGGACGGGCTTCCTGAGTCGCCTGGAGAACTTCACGGGACTGTCGCTGGTTGGAGAG
CCACTGCGCAGGGCATGGAAGGTTCTGGACACCCTCATGTGCCAGCAAGCCCACGGTCTT
CCACTACCAGCCTGGGCCTCCCCAGATGTCCTGCGGACTCTTGCCCAGATCTCGGCTTTG
GATATTGGAGCCCACGTGGGCCCACCCCGGGCAGCAGAGAAGGCCCAGCTGACAGGGGGG
ATCCTGCTGAATGCTATCCTTGCAAACTTCTCCCGGGTCCAGCGCCTGGGGCTGCCCCTC
AAGATGGTCATGTACTCAGCTCATGACAGCACCCTGCTGGCCCTCCAGGGGGCCCTGGGC
CTCTATGATGGACACACCCCGCCATATGCTGCCTGCCTCGGCTTTGAGTTCCGGAAGCAC
CTGGGGAATCCCGCCAAAGATGGAGGGAATGTCACCGTCTCCCTCTTCTACCGCAATGAC
TCCGCCCACCTGCCCCTGCCTCTCAGCCTCCCCGGGTGCCCGGCCCCCTGTCCACTAGGC
CGCTTCTACCAGCTGACTGCCCCGGCCCGGCCTCCCGCCCATGGGGTCTCCTGCCATGGC
CCCTATGAGGCTGCCATCCCCCCAGCTCCAGTGGTGCCCCTGCTGGCCGGAGCTGTAGCT
GTGCTGGTGGCACTCAGCTTGGGGCTGGGCCTGCTGGCCTGGAGACCAGGGTGCCTGCGG
GCCTTGGGGGGCCCCGTGTGA
Enzyme 29 GenBank Gene ID AF321918 Link Image
Enzyme 29 GeneCard ID Q9BZG2 Link Image
Enzyme 29 GenAtlas ID ACPT Link Image
Enzyme 29 HGNC ID HGNC:14376 Link Image
Enzyme 29 Chromosome Location 19
Enzyme 29 Locus 19q13.4
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Yousef GM, Diamandis M, Jung K, Diamandis EP: Molecular cloning of a novel human acid phosphatase gene (ACPT) that is highly expressed in the testis. Genomics. 2001 Jun 15;74(3):385-95. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 16056
Enzyme 30 Name Carboxylesterase 7
Enzyme 30 Synonyms
  1. Carboxylesterase-like urinary excreted protein homolog
  2. Cauxin
Enzyme 30 Gene Name CES7
Enzyme 30 Protein Sequence >Carboxylesterase 7
MSGNWVHPGQILIWAIWVLAAPTKGPSAEGPQRNTRLGWIQGKQVTVLGSPVPVNVFLGV
PFAAPPLGSLRFTNPQPASPWDNLREATSYPNLCLQNSEWLLLDQHMLKVHYPKFGVSED
CLYLNIYAPAHADTGSKLPVLVWFPGGAFKTGSASIFDGSALAAYEDVLVVVVQYRLGIF
GFFTTWDQHAPGNWAFKDQVAALSWVQKNIEFFGGDPSSVTIFGESAGAISVSSLILSPM
AKGLFHKAIMESGVAIIPYLEAHDYEKSEDLQVVAHFCGNNASDSEALLRCLRTKPSKEL
LTLSQKTKSFTRVVDGAFFPNEPLDLLSQKAFKAIPSIIGVNNHECGFLLPMKEAPEILS
GSNKSLALHLIQNILHIPPQYLHLVANEYFHDKHSLTEIRDSLLDLLGDVFFVVPALITA
RYHRDAGAPVYFYEFRHRPQCFEDTKPAFVKADHADEVRFVFGGAFLKGDIVMFEGATEE
EKLLSRKMMKYWATFARTGNPNGNDLSLWPAYNLTEQYLQLDLNMSLGQRLKEPRVDFWT
STIPLILSASDMLHSPLSSLTFLSLLQPFFFFCAP
Enzyme 30 Number of Residues 575
Enzyme 30 Molecular Weight 63927
Enzyme 30 Theoretical pI 6.42
Enzyme 30 GO Classification Not Available
Enzyme 30 General Function Lipid transport and metabolism
Enzyme 30 Specific Function Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • 1-20
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein Not Available
Enzyme 30 UniProtKB/Swiss-Prot ID Q6NT32 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name EST7_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 AY907669 Link Image
Enzyme 30 GeneCard ID Q6NT32 Link Image
Enzyme 30 GenAtlas ID CES7 Link Image
Enzyme 30 HGNC ID HGNC:26459 Link Image
Enzyme 30 Chromosome Location 16
Enzyme 30 Locus 16q12.2
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References Not Available
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 17330
Enzyme 31 Name Acid phosphatase-like protein 2
Enzyme 31 Synonyms Not Available
Enzyme 31 Gene Name ACPL2
Enzyme 31 Protein Sequence >Acid phosphatase-like protein 2
MLFRNRFLLLLALAALLAFVSLSLQFFHLIPVSTPKNGMSSKSRKRIMPDPVTEPPVTDP
VYEALLYCNIPSVAERSMEGHAPHHFKLVSVHVFIRHGDRYPLYVIPKTKRPEIDCTLVA
NRKPYHPKLEAFISHMSKGSGASFESPLNSLPLYPNHPLCEMGELTQTGVVQHLQNGQLL
RDIYLKKHKLLPNDWSADQLYLETTGKSRTLQSGLALLYGFLPDFDWKKIYFRHQPSALF
CSGSCYCPVRNQYLEKEQRRQYLLRLKNSQLEKTYGEMAKIVDVPTKQLRAANPIDSMLC
HFCHNVSFPCTRNGCVDMEHFKVIKTHQIEDERERREKKLYFGYSLLGAHPILNQTIGRM
QRATEGRKEELFALYSAHDVTLSPVLSALGLSEARFPRFAARLIFELWQDREKPSEHSVR
ILYNGVDVTFHTSFCQDHHKRSPKPMCPLENLVRFVKRDMFVALGGSGTNYYDACHREGF
Enzyme 31 Number of Residues 480
Enzyme 31 Molecular Weight 55239.4
Enzyme 31 Theoretical pI 9.24
Enzyme 31 GO Classification
Function
  • acid phosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
Component
Enzyme 31 General Function Involved in acid phosphatase activity
Enzyme 31 Specific Function A phosphate monoester + H(2)O = an alcohol + phosphate
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • 1-23
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 37182044 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q8TE99 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name ACPL2_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1443 bp
ATGCTTTTCCGCAACCGCTTCTTGCTGCTGCTGGCCCTGGCTGCGCTGCTGGCCTTTGTG
AGCCTCAGCCTGCAGTTCTTCCACCTGATCCCGGTGTCGACTCCTAAGAATGGAATGAGT
AGCAAGAGTCGAAAGAGAATCATGCCCGACCCTGTGACGGAGCCCCCTGTGACAGACCCC
GTTTATGAAGCTCTTTTGTACTGCAACATCCCCAGTGTGGCCGAGCGCAGCATGGAAGGT
CATGCCCCGCATCATTTTAAGCTGGTCTCAGTGCATGTGTTCATTCGCCACGGAGACAGG
TACCCACTGTATGTCATTCCCAAAACAAAGCGACCAGAAATTGACTGCACTCTGGTGGCT
AACAGGAAACCGTATCACCCAAAACTGGAAGCTTTCATTAGTCACATGTCAAAAGGATCC
GGAGCCTCTTTCGAAAGCCCCTTGAACTCCTTGCCTCTTTACCCAAATCACCCATTGTGT
GAGATGGGAGAGCTCACACAGACAGGAGTTGTGCAGCATTTGCAGAACGGTCAGCTGCTG
AGGGATATCTATCTAAAGAAACACAAACTCCTGCCCAATGATTGGTCTGCAGACCAGCTC
TATTTAGAGACCACTGGGAAAAGCCGGACCCTACAAAGTGGGCTGGCCTTGCTTTATGGC
TTTCTCCCAGATTTTGACTGGAAGAAGATTTATTTCAGGCACCAGCCAAGTGCGCTGTTC
TGCTCTGGAAGCTGCTATTGCCCGGTAAGAAACCAGTATCTGGAAAAGGAGCAGCGTCGT
CAGTACCTCCTACGTTTGAAAAACAGCCAGCTGGAGAAGACCTACGGGGAGATGGCCAAG
ATCGTGGATGTCCCCACCAAGCAGCTTAGAGCTGCCAACCCCATAGACTCCATGCTCTGC
CACTTCTGCCACAATGTCAGCTTTCCCTGTACCAGAAATGGCTGTGTTGACATGGAGCAC
TTCAAGGTAATTAAGACCCATCAGATCGAGGATGAAAGGGAAAGACGGGAGAAGAAATTG
TACTTCGGGTATTCTCTCCTGGGTGCCCACCCCATCCTGAACCAAACCATCGGCCGGATG
CAGCGTGCCACCGAGGGCAGGAAAGAAGAGCTCTTTGCCCTCTACTCTGCTCATGATGTC
ACTCTGTCACCAGTTCTCAGTGCCTTGGGCCTTTCAGAAGCCAGGTTCCCAAGGTTTGCA
GCCAGGTTGATCTTTGAGCTTTGGCAAGACAGAGAAAAGCCCAGTGAACATTCCGTCCGG
ATTCTTTACAATGGCGTCGATGTCACATTCCACACCTCTTTCTGCCAAGACCACCACAAG
CGTTCTCCCAAGCCCATGTGCCCGCTTGAAAACTTGGTCCGCTTTGTGAAAAGGGACATG
TTTGTAGCCCTGGGTGGCAGTGGTACAAATTATTATGATGCATGTCACAGGGAAGGATTC
TAA
Enzyme 31 GenBank Gene ID AY358460 Link Image
Enzyme 31 GeneCard ID ACPL2 Link Image
Enzyme 31 GenAtlas ID Not Available
Enzyme 31 HGNC ID HGNC:26303 Link Image
Enzyme 31 Chromosome Location 3
Enzyme 31 Locus 3q23
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 17331
Enzyme 32 Name Synaptic vesicle membrane protein VAT-1 homolog-like
Enzyme 32 Synonyms Not Available
Enzyme 32 Gene Name VAT1L
Enzyme 32 Protein Sequence >Synaptic vesicle membrane protein VAT-1 homolog-like
MAKEGVEKAEETEQMIEKEAGKEPAEGGGGDGSHRLGDAQEMRAVVLAGFGGLNKLRLFR
KAMPEPQDGELKIRVKACGLNFIDLMVRQGNIDNPPKTPLVPGFECSGIVEALGDSVKGY
EIGDRVMAFVNYNAWAEVVCTPVEFVYKIPDDMSFSEAAAFPMNFVTAYVMLFEVANLRE
GMSVLVHSAGGGVGQAVAQLCSTVPNVTVFGTASTFKHEAIKDSVTHLFDRNADYVQEVK
RISAEGVDIVLDCLCGDNTGKGLSLLKPLGTYILYGSSNMVTGETKSFFSFAKSWWQVEK
VNPIKLYEENKVIAGFSLLNLLFKQGRAGLIRGVVEKLIGLYNQKKIKPVVDSLWALEEV
KEAMQRIHDRGNIGKLILDVEKTPTPLMANDSTETSEAGEEEEDHEGDSENKERMPFIQ
Enzyme 32 Number of Residues 419
Enzyme 32 Molecular Weight 45899.2
Enzyme 32 Theoretical pI 4.70
Enzyme 32 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 32 General Function Energy production and conversion
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
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 10047227 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q9HCJ6 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name VAT1L_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 AB046796 Link Image
Enzyme 32 GeneCard ID VAT1L Link Image
Enzyme 32 GenAtlas ID Not Available
Enzyme 32 HGNC ID HGNC:29315 Link Image
Enzyme 32 Chromosome Location 1
Enzyme 32 Locus 16q23.1
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Aug 31;7(4):273-81. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 17332
Enzyme 33 Name Putative quinone oxidoreductase
Enzyme 33 Synonyms
  1. Tumor protein p53-inducible protein 3
  2. p53-induced gene 3 protein
Enzyme 33 Gene Name TP53I3
Enzyme 33 Protein Sequence >Putative quinone oxidoreductase
MLAVHFDKPGGPENLYVKEVAKPSPGEGEVLLKVAASALNRADLMQRQGQYDPPPGASNI
LGLEASGHVAELGPGCQGHWKIGDTAMALLPGGGQAQYVTVPEGLLMPIPEGLTLTQAAA
IPEAWLTAFQLLHLVGNVQAGDYVLIHAGLSGVGTAAIQLTRMAGAIPLVTAGSQKKLQM
AEKLGAAAGFNYKKEDFSEATLKFTKGAGVNLILDCIGGSYWEKNVNCLALDGRWVLYGL
MGGGDINGPLFSKLLFKRGSLITSLLRSRDNKYKQMLVNAFTEQILPHFSTEGPQRLLPV
LDRIYPVTEIQEAHKYMEANKNIGKIVLELPQ
Enzyme 33 Number of Residues 332
Enzyme 33 Molecular Weight 35535.9
Enzyme 33 Theoretical pI 7.20
Enzyme 33 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 33 General Function Energy production and conversion
Enzyme 33 Specific Function May be involved in the generation of reactive oxygen species (ROS)
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions Not Available
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 2754812 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q53FA7 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name QORX_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >969 bp
ATGTTAGCCGTGCACTTTGACAAGCCGGGAGGACCGGAAAACCTCTACGTGAAGGAGGTG
GCCAAGCCGAGCCCGGGGGAGGGTGAAGTCCTCCTGAAGGTGGCGGCCAGCGCCCTGAAC
CGGGCGGACTTAATGCAGAGACAAGGCCAGTATGACCCACCTCCAGGAGCCAGCAACATT
TTGGGACTTGAGGCATCTGGACATGTGGCAGAGCTGGGGCCTGGCTGCCAGGGACACTGG
AAGATCGGGGACACAGCCATGGCTCTGCTCCCCGGTGGGGGCCAGGCTCAGTACGTCACT
GTCCCCGAAGGGCTCCTCATGCCTATCCCAGAGGGATTGACCCTGACCCAGGCTGCAGCC
ATCCCAGAGGCCTGGCTCACCGCCTTCCAGCTGTTACATCTTGTGGGAAATGTTCAGGCT
GGAGACTATGTGCTAATCCATGCAGGACTGAGTGGTGTGGGCACAGCTGCTATCCAACTC
ACCCGGATGGCTGGAGCTATTCCTCTGGTCACAGCTGGCTCCCAGAAGAAGCTTCAAATG
GCAGAAAAGCTTGGAGCAGCTGCTGGATTCAATTACAAAAAAGAGGATTTCTCTGAAGCA
ACGCTGAAATTCACCAAAGGTGCTGGAGTTAATCTTATTCTAGACTGCATAGGCGGATCC
TACTGGGAGAAGAACGTCAACTGCCTGGCTCTTGATGGTCGATGGGTTCTCTATGGTCTG
ATGGGAGGAGGTGACATCAATGGGCCCCTGTTTTCAAAGCTACTTTTTAAGCGAGGAAGT
CTGATCACCAGTTTGCTGAGGTCTAGGGACAATAAGTACAAGCAAATGCTGGTGAATGCT
TTCACGGAGCAAATTCTGCCTCACTTCTCCACGGAGGGCCCCCAACGTCTGCTGCCGGTT
CTGGACAGAATCTACCCAGTGACCGAAATCCAGGAGGCCCATAGTACATGGAGGCCAACA
AGAACATAG
Enzyme 33 GenBank Gene ID AF010309 Link Image
Enzyme 33 GeneCard ID TP53I3 Link Image
Enzyme 33 GenAtlas ID Not Available
Enzyme 33 HGNC ID HGNC:19373 Link Image
Enzyme 33 Chromosome Location 2
Enzyme 33 Locus 2p23.3
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B: A model for p53-induced apoptosis. Nature. 1997 Sep 18;389(6648):300-5. [PubMed Link Image]
  2. Nicholls CD, Shields MA, Lee PW, Robbins SM, Beattie TL: UV-dependent alternative splicing uncouples p53 activity and PIG3 gene function through rapid proteolytic degradation. J Biol Chem. 2004 Jun 4;279(23):24171-8. Epub 2004 Apr 2. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Chanock SJ, Burdett L, Yeager M, Llaca V, Langerod A, Presswalla S, Kaaresen R, Strausberg RL, Gerhard DS, Kristensen V, Perou CM, Borresen-Dale AL: Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas. Breast Cancer Res. 2007;9(1):R5. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 17333
Enzyme 34 Name Synaptic vesicle membrane protein VAT-1 homolog
Enzyme 34 Synonyms Not Available
Enzyme 34 Gene Name VAT1
Enzyme 34 Protein Sequence >Synaptic vesicle membrane protein VAT-1 homolog
MSDEREVAEAATGEDASSPPPKTEAASDPQHPAASEGAAAAAASPPLLRCLVLTGFGGYD
KVKLQSRPAAPPAPGPGQLTLRLRACGLNFADLMARQGLYDRLPPLPVTPGMEGAGVVIA
VGEGVSDRKAGDRVMVLNRSGMWQEEVTVPSVQTFLIPEAMTFEEAAALLVNYITAYMVL
FDFGNLQPGHSVLVHMAAGGVGMAAVQLCRTVENVTVFGTASASKHEALKENGVTHPIDY
HTTDYVDEIKKISPKGVDIVMDPLGGSDTAKGYNLLKPMGKVVTYGMANLLTGPKRNLMA
LARTWWNQFSVTALQLLQANRAVCGFHLGYLDGEVELVSGVVARLLALYNQGHIKPHIDS
VWPFEKVADAMKQMQEKKNVGKVLLVPGPEKEN
Enzyme 34 Number of Residues 393
Enzyme 34 Molecular Weight 41920.0
Enzyme 34 Theoretical pI 6.25
Enzyme 34 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 34 General Function Energy production and conversion
Enzyme 34 Specific Function Not Available
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 30583577 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q99536 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name VAT1_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence Not Available
Enzyme 34 GenBank Gene ID BT007369 Link Image
Enzyme 34 GeneCard ID VAT1 Link Image
Enzyme 34 GenAtlas ID Not Available
Enzyme 34 HGNC ID HGNC:16919 Link Image
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 17q21
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Smith TM, Lee MK, Szabo CI, Jerome N, McEuen M, Taylor M, Hood L, King MC: Complete genomic sequence and analysis of 117 kb of human DNA containing the gene BRCA1. Genome Res. 1996 Nov;6(11):1029-49. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Friedman LS, Ostermeyer EA, Lynch ED, Welcsh P, Szabo CI, Meza JE, Anderson LA, Dowd P, Lee MK, Rowell SE, et al.: 22 genes from chromosome 17q21: cloning, sequencing, and characterization of mutations in breast cancer families and tumors. Genomics. 1995 Jan 1;25(1):256-63. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 17719
Enzyme 35 Name cDNA FLJ52809, highly similar to Zinc-binding alcohol dehydrogenasedomain-containing protein 2 (EC 1.-.-.-)
Enzyme 35 Synonyms Not Available
Enzyme 35 Gene Name Not Available
Enzyme 35 Protein Sequence >cDNA FLJ52809, highly similar to Zinc-binding alcohol dehydrogenasedomain-containing protein 2 (EC 1.-.-.-)
MAPGSFAEYTVVPASIATPVPSVKPEYLTLLVSGTTAYISLKELGGLSEGKKVLVTAAAG
GTGQFAMQLSKKAKCHVIGTCSSDEKSAFLKSLGCDRPINYKTEPVGTVLKQEYPEGVDV
VYESVGGAMFDLAVDALATKGRLIVIGFISGYQTPTGLSPVKAGTLPAKLLKKSASVQGF
FLNHYLSKYQAAMSHLLEMCVSGDLVCEVDLGDLSPEGRFTGLESIFRAVNYMYMGKNTG
KIVVELPHSVNSKL
Enzyme 35 Number of Residues 254
Enzyme 35 Molecular Weight 26900.0
Enzyme 35 Theoretical pI 8.18
Enzyme 35 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 35 General Function Involved in oxidoreductase activity
Enzyme 35 Specific Function Not Available
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 194380870 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID B4DZ91 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name B4DZ91_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >765 bp
ATGGCACCTGGTTCTTTTGCTGAGTACACAGTTGTGCCTGCCAGCATTGCAACTCCAGTG
CCCTCAGTGAAACCCGAGTATCTTACCCTGCTGGTAAGTGGCACCACCGCATACATCAGC
CTGAAAGAGCTCGGAGGACTGTCGGAAGGGAAAAAAGTTTTGGTGACAGCAGCAGCTGGG
GGAACGGGCCAGTTTGCCATGCAGCTTTCAAAGAAGGCAAAGTGCCATGTAATTGGAACC
TGCTCTTCTGATGAAAAGTCTGCTTTTCTGAAATCTCTTGGCTGTGATCGTCCTATCAAC
TATAAAACTGAACCCGTAGGTACCGTCCTTAAGCAGGAGTACCCTGAAGGTGTCGATGTG
GTCTATGAATCTGTTGGGGGAGCCATGTTTGACTTGGCTGTAGACGCCCTGGCTACGAAA
GGGCGCTTGATAGTAATAGGGTTTATCTCTGGCTACCAAACTCCTACTGGCCTTTCGCCT
GTGAAAGCAGGAACATTGCCAGCCAAACTGCTCAAGAAATCTGCCAGCGTACAGGGCTTC
TTCCTGAACCATTACCTTTCTAAGTATCAAGCAGCCATGAGCCACTTGCTCGAGATGTGT
GTGAGCGGAGACCTGGTTTGTGAGGTGGACCTTGGAGATCTGTCTCCAGAGGGCAGGTTT
ACTGGCCTGGAGTCCATATTCCGTGCTGTCAATTATATGTACATGGGAAAAAACACTGGA
AAAATTGTAGTTGAATTACCTCACTCTGTCAACAGTAAGCTGTAA
Enzyme 35 GenBank Gene ID AK302801 Link Image
Enzyme 35 GeneCard ID Not Available
Enzyme 35 GenAtlas ID Not Available
Enzyme 35 HGNC ID HGNC:28697 Link Image
Enzyme 35 Chromosome Location Not Available
Enzyme 35 Locus Not Available
Enzyme 35 SNPs Not Available
Enzyme 35 General References Not Available
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 17720
Enzyme 36 Name Reticulon-4-interacting protein 1, mitochondrial
Enzyme 36 Synonyms
  1. NOGO-interacting mitochondrial protein
Enzyme 36 Gene Name RTN4IP1
Enzyme 36 Protein Sequence >Reticulon-4-interacting protein 1, mitochondrial
MEFLKTCVLRRNACTAVCFWRSKVVQKPSVRRISTTSPRSTVMPAWVIDKYGKNEVLRFT
QNMMMPIIHYPNEVIVKVHAASVNPIDVNMRSGYGATALNMKRDPLHVKIKGEEFPLTLG
RDVSGVVMECGLDVKYFKPGDEVWAAVPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQAAS
LPYVALTAWSAINKVGGLNDKNCTGKRVLILGASGGVGTFAIQVMKAWDAHVTAVCSQDA
SELVRKLGADDVIDYKSGSVEEQLKSLKPFDFILDNVGGSTETWAPDFLKKWSGATYVTL
VTPFLLNMDRLGIADGMLQTGVTVGSKALKHFWKGVHYRWAFFMASGPCLDDIAELVDAG
KIRPVIEQTFPFSKVPEAFLKVERGHARGKTVINVV
Enzyme 36 Number of Residues 396
Enzyme 36 Molecular Weight 43589.4
Enzyme 36 Theoretical pI 9.58
Enzyme 36 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 36 General Function Energy production and conversion
Enzyme 36 Specific Function Appears to be a potent inhibitor of regeneration following spinal cord injury
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 17046447 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q8WWV3 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name RT4I1_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >681 bp
ATGGAATTTCTGAAGACTTGTGTACTTAGAAGAAATGCATGCACTGCGGTTTGCTTCTGG
AGAAGCAAAGTTGTCCAAAAGCCTTCAGTTAGAAGGATTAGTACTACCTCTCCAAGGAGC
ACTGTCATGCCTGCTTGGGTGATAGATAAATATGGGAAGAATGAAGTGCTTCGATTCACT
CAGAACATGATGGTGCCTATCATACACTATCCAAATGAAGTCATTGTCAAAGTTCACGCT
GCCAGTGTAAATCCTATAGACGTTAATATGAGAAGTGGTTATGGAGCTACAGCTTTAAAT
ATGAAGCGTGATCCTTTACACGTGAAAATCAAAGGAGAAGAATTTCCTCTGACTCTGGGT
CGGGATGTCTCTGGCGTGGTGATGGAGTGTGGGCTTGATGTGAAATACTTCAAGCCTGGA
GATGAGGTCTGGGCTGCAGTTCCTCCTTGGAAACAAGGCACTCTTTCAGAGTTTGTTGTA
GTCAGTGGGAATGAGGTCTCTCACAAACCCAAATCACTCACTCATACTCAAGCTGCCTCT
TTGTCATATGTGGCTCTCACAGCCTGGTCTGCTATAAACAAAGTTGGTGGCCTGAATGAC
AAGAATTGCACAGGAAAACGCATTTCTGGAAAGGAGTCCATTATCGCTGGGCATTTTTCA
TGGCCAGTGGCCCATGTTTAG
Enzyme 36 GenBank Gene ID AF439711 Link Image
Enzyme 36 GeneCard ID RTN4IP1 Link Image
Enzyme 36 GenAtlas ID Not Available
Enzyme 36 HGNC ID HGNC:18647 Link Image
Enzyme 36 Chromosome Location 6
Enzyme 36 Locus 6q21
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Hu WH, Hausmann ON, Yan MS, Walters WM, Wong PK, Bethea JR: Identification and characterization of a novel Nogo-interacting mitochondrial protein (NIMP). J Neurochem. 2002 Apr;81(1):36-45. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available