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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Asparagine (HMDB00168)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:44
Accession Number HMDB00168
Secondary Accession Numbers Not Available
Common Name L-Asparagine
Description Asparagine (Asn) is one of the 20 most common natural amino acids on Earth. It has carboxamide as the side chain's functional group. It is considered a non-essential amino acid. Asparagine is not an essential amino acid, which means that it can be synthesized from central metabolic pathway intermediates in humans and is not required in the diet. The precursor to asparagine is oxaloacetate. Oxaloacetate is converted to aspartate using a transaminase enzyme. The enzyme transfers the amino group from glutamate to oxaloacetate producing alpha-ketoglutarate and aspartate. The enzyme asparagine synthetase produces asparagine, AMP, glutamate, and pyrophosphate from aspartate, glutamine, and ATP. In the asparagine synthetase reaction, ATP is used to activate aspartate, forming beta-aspartyl-AMP. glutamine donates an ammonium group which reacts with beta-aspartyl-AMP to form asparagine and free AMP. Since the asparagine side chain can make efficient hydrogen bond interactions with the peptide backbone, asparagines are often found near the beginning and end of alpha-helices, and in turn motifs in beta sheets. Its role can be thought as "capping" the hydrogen bond interactions which would otherwise need to be satisfied by the polypeptide backbone. glutamines have an extra methylene group, have more conformational entropy and thus are less useful in this regard. Asparagine also provides key sites for N-linked glycosylation, modification of the protein chain with the addition of carbohydrate chains. A reaction between asparagine and reducing sugars or reactive carbonyls produces acrylamide (acrylic amide) in food when heated to sufficient temperature, i.e. baking. These occur primarily in baked goods such as french fries, potato chips, and roasted coffee. Asparagine was first isolated in 1806 from asparagus juice, in which it is abundant--hence its name--becoming the first amino acid to be isolated. The smell observed in the urine of some individuals after their consumption of asparagus is attributed to a byproduct of the metabolic breakdown of asparagine, asparagine-amino-succinic-acid monoamide. (However, some scientists disagree and implicate other substances in the smell, especially methanethiol). (http://en.wikipedia.org/wiki/Asparagine)
Synonyms
  1. (-)-Asparagine
  2. (S)-2,4-Diamino-4-oxobutanoate
  3. (S)-2,4-Diamino-4-oxobutanoic acid
  4. (S)-Asparagine
  5. 2-Aminosuccinamate
  6. 2-Aminosuccinamic acid
  7. Agedoite
  8. Altheine
  9. Asn
  10. Asparagine
  11. Asparagine acid
  12. Asparamide
  13. Aspartamate
  14. Aspartamic acid
  15. Aspartic acid amide
  16. Aspartic acid b-amide
  17. Aspartic acid beta amide
  18. B2,4-(S)-diamino-4-oxo-utanoate
  19. B2,4-(S)-diamino-4-oxo-utanoic acid
  20. Crystal VI
  21. L-2,4-Diamino-4-oxobutanoate
  22. L-2,4-Diamino-4-oxobutanoic acid
  23. L-Aspartamine
  24. L-b-Asparagine
  25. L-beta-Asparagine
  26. a-Aminosuccinamate
  27. a-Aminosuccinamic acid
  28. alpha Amminosuccinamate
  29. alpha Amminosuccinamic acid
  30. alpha-Aminosuccinamate
  31. alpha-Aminosuccinamic acid
  32. l-Asparagine
Chemical IUPAC Name 2,4-diamino-4-oxo-butanoic acid
Chemical Formula C4H8N2O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • primary carboxylic acid amide
  • alpha-aminoacid
Biofunction
  • Essential amino acid
  • Component of Alanine and aspartate metabolism
  • Component of Aminoacyl-tRNA biosynthesis
  • Component of Nitrogen metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 132.118
Monoisotopic Molecular Weight 132.053497
Isomeric SMILES N[C@@H](CC(N)=O)C(O)=O
Canonical SMILES NC(CC(N)=O)C(O)=O
KEGG Compound ID C00152 Link Image
BioCyc ID ASN Link Image
BiGG ID 34055 Link Image
Wikipedia Link Asn Link Image
NuGOwiki Link HMDB00168 Link Image
Metagene Link HMDB00168 Link Image
METLIN ID 14 Link Image
PubChem Compound 6267 Link Image
PubChem Substance 3452 Link Image
ChEBI ID 17196 Link Image
CAS Registry Number 70-47-3
InChI Identifier InChI=1/C4H8N2O3/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H2,6,7)(H,8,9)/t2-/m0/s1
Synthesis Reference Wang, Fangda. Preparation of L-b-asparagine. Faming Zhuanli Shenqing Gongkai Shuomingshu (2005), 8 pp.
Melting Point (Experimental) 234-235 oC
Experimental Water Solubility 29.4 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 168.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -3.82 [CHMELIK,J ET AL. (1991)] Source: PhysProp
Predicted LogP/Hydrophobicity -3.36 [Predicted by ALOGPS]; -4.4 [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 1POK Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
All Tissues —
Concentrations (Normal)
Biofluid Blood
Value 41.0 (31.0-51.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
Biofluid Blood
Value 48.0 +/- 7.0 uM
Age Children:1-13 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 46.0 +/- 7.0 uM
Age Children:1-13 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 49.0 +/- 7.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 47.0 +/- 9.0 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 32.9 +/- 7.6 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Canepa A, Filho JC, Gutierrez A, Carrea A, Forsberg AM, Nilsson E, Verrina E, Perfumo F, Bergstrom J: Free amino acids in plasma, red blood cells, polymorphonuclear leukocytes, and muscle in normal and uraemic children. Nephrol Dial Transplant. 2002 Mar;17(3):413-21. [PubMed Link Image]
Biofluid CSF
Value 5.4 +/- 1.4 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 6.20 (5.90-6.50) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Biofluid CSF
Value 19.0 +/- 11.1 uM
Age Children:1-13 yrs old
Sex N/A
Patient information children
Comments Not Available
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 8.1 +/- 4.9 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
Biofluid CSF
Value 9.0 +/- 4.2 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
Biofluid CSF
Value 4.43 (0.0-8.86) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Lewis MJ, Morrissey JA, Flegel MD, Jeroncic K, Xiong Y, Cheng D, Eisner R, Gautam B, Tzur D, Sawhney S, Bamforth F, Greiner R, Li L: The human cerebrospinal fluid metabolome. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Aug 15;871(2):164-173. Epub 2008 May 8. [PubMed Link Image]
Biofluid CSF
Value 5.99 +/- 0.92 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
Biofluid Urine
Value 0.96 +/- 0.65 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Biofluid Urine
Value 9.211 (3.289-15.1) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value 35.0 (16.4-57.2) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Gatti R, Gioia MG: Liquid chromatographic fluorescence determination of amino acids in plasma and urine after derivatization with phanquinone. Biomed Chromatogr. 2008 Feb;22(2):207-13. [PubMed Link Image]
Biofluid Urine
Value 10.0 (4.6-16.32) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Gatti R, Gioia MG: Liquid chromatographic fluorescence determination of amino acids in plasma and urine after derivatization with phanquinone. Biomed Chromatogr. 2008 Feb;22(2):207-13. [PubMed Link Image]
Biofluid Urine
Value 8.75 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 39.9 +/- 3.2 uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Acute seizures
References
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Biofluid Blood
Value 40.8 +/- 11.5 uM
Age Children:1-13 yrs old
Sex Both
Condition Uremia
Comments Not Available
References
  • Canepa A, Filho JC, Gutierrez A, Carrea A, Forsberg AM, Nilsson E, Verrina E, Perfumo F, Bergstrom J: Free amino acids in plasma, red blood cells, polymorphonuclear leukocytes, and muscle in normal and uraemic children. Nephrol Dial Transplant. 2002 Mar;17(3):413-21. [PubMed Link Image]
Biofluid CSF
Value 7.9 +/- 6.4 uM
Age Children:1-13 yrs old
Sex N/A
Condition Leukemia
Comments Acute Lymphoblastic Leukemia (ALL) with Central Nervous System (CNS) disease
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 11.1 +/- 6.7 uM
Age Children:1-13 yrs old
Sex N/A
Condition Leukemia
Comments Not Available
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 6.01 +/- 0.65 uM
Age Adult:>18 yrs old
Sex Both
Condition Schizophrenia
Comments Not Available
References
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
Biofluid CSF
Value 1.77 +/- 0.16 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Associated Disorders
Condition References
Alzheimer's disease
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Epilepsy
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Leukemia
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Schizophrenia
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
Uremia
  • Canepa A, Filho JC, Gutierrez A, Carrea A, Forsberg AM, Nilsson E, Verrina E, Perfumo F, Bergstrom J: Free amino acids in plasma, red blood cells, polymorphonuclear leukocytes, and muscle in normal and uraemic children. Nephrol Dial Transplant. 2002 Mar;17(3):413-21. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Ammonia Recycling SMP00009 Link Image map00910 Link Image
Aspartate Metabolism SMP00067 Link Image map00250 Link Image
Transcription/Translation SMP00019 Link Image
General References
  1. Starczynowski DT, Reynolds JG, Gilmore TD: Mutations of tumor necrosis factor alpha-responsive serine residues within the C-terminal transactivation domain of human transcription factor REL enhance its in vitro transforming ability. Oncogene. 2005 Nov 10;24(49):7355-68. [PubMed Link Image]
  2. Fischer D, Schroers A, Blumcke I, Urbach H, Zerres K, Mortier W, Vorgerd M, Schroder R: Consequences of a novel caveolin-3 mutation in a large German family. Ann Neurol. 2003 Feb;53(2):233-41. [PubMed Link Image]
  3. Filho JC, Bergstrom J, Stehle P, Furst P: Simultaneous measurements of free amino acid patternsof plasma, muscle and erythrocytes in healthy human subjects. Clin Nutr. 1997 Dec;16(6):299-305. [PubMed Link Image]
  4. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
  5. Sun S, Han J, Ralph WM Jr, Chandrasekaran A, Liu K, Auborn KJ, Carter TH: Endoplasmic reticulum stress as a correlate of cytotoxicity in human tumor cells exposed to diindolylmethane in vitro. Cell Stress Chaperones. 2004 Mar;9(1):76-87. [PubMed Link Image]
  6. Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
  7. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
  8. Takamatsu S, Inoue N, Katsumata T, Nakamura K, Fujibayashi Y, Takeuchi M: The relationship between the branch-forming glycosyltransferases and cell surface sugar chain structures. Biochemistry. 2005 Apr 26;44(16):6343-9. [PubMed Link Image]
  9. Rip JW, Coulter-Mackie MB, Rupar CA, Gordon BA: Purification and structure of human liver aspartylglucosaminidase. Biochem J. 1992 Dec 15;288 ( Pt 3):1005-10. [PubMed Link Image]
  10. Chiara F, Goumans MJ, Forsberg H, Ahgren A, Rasola A, Aspenstrom P, Wernstedt C, Hellberg C, Heldin CH, Heuchel R: A gain of function mutation in the activation loop of platelet-derived growth factor beta-receptor deregulates its kinase activity. J Biol Chem. 2004 Oct 8;279(41):42516-27. Epub 2004 Jul 28. [PubMed Link Image]
  11. Xu L, Wang Y, Gillespie D, Meissner G: Two rings of negative charges in the cytosolic vestibule of type-1 ryanodine receptor modulate ion fluxes. Biophys J. 2006 Jan 15;90(2):443-53. Epub 2005 Oct 20. [PubMed Link Image]
  12. Poon CJ, Plaas AH, Keene DR, McQuillan DJ, Last K, Fosang AJ: N-linked keratan sulfate in the aggrecan interglobular domain potentiates aggrecanase activity. J Biol Chem. 2005 Jun 24;280(25):23615-21. Epub 2005 Apr 22. [PubMed Link Image]
  13. Ahlman B, Andersson K, Leijonmarck CE, Ljungqvist O, Hedenborg L, Wernerman J: Short-term starvation alters the free amino acid content of the human intestinal mucosa. Clin Sci (Lond). 1994 Jun;86(6):653-62. [PubMed Link Image]
  14. Avramis VI, Panosyan EH: Pharmacokinetic/pharmacodynamic relationships of asparaginase formulations: the past, the present and recommendations for the future. Clin Pharmacokinet. 2005;44(4):367-93. [PubMed Link Image]
  15. Mohrmann K, van Eijndhoven MA, Schinkel AH, Schellens JH: Absence of N-linked glycosylation does not affect plasma membrane localization of breast cancer resistance protein (BCRP/ABCG2). Cancer Chemother Pharmacol. 2005 Oct;56(4):344-50. Epub 2005 May 5. [PubMed Link Image]
  16. Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
  17. Wikipedia Link Image
Metabolic Enzymes
  1. Asparagine synthetase [glutamine-hydrolyzing]
  2. Asparaginyl-tRNA synthetase, cytoplasmic
  3. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit precursor
  4. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit precursor
  5. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit precursor
  6. Neutral amino acid transporter B(0)
  7. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
  8. System N amino acid transporter 1
  9. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
  10. L-asparaginase
  11. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
  12. Full-length cDNA clone CS0DM001YM08 of Fetal liver of Homo sapiens
  13. Probable asparaginyl-tRNA synthetase, mitochondrial
  14. cDNA FLJ34575 fis, clone KIDNE2008362, highly similar to Homo sapiens asparaginase like 1 (ASRGL1), mRNA
  15. Solute carrier family 38, member 3, isoform CRA_b
Enzyme 1 [top]
Enzyme 1 ID 5855
Enzyme 1 Name Asparagine synthetase [glutamine-hydrolyzing]
Enzyme 1 Synonyms
  1. Glutamine- dependent asparagine synthetase
  2. Cell cycle control protein TS11
Enzyme 1 Gene Name ASNS
Enzyme 1 Protein Sequence >Asparagine synthetase [glutamine-hydrolyzing] 
MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQ
PIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGV
FAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPF
LPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFN
NAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAAR
KVADHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVV
IFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPF
LDHRFSSYYLSLPPEMRIPKNGIEKHLLRETFEDSNLIPKEILWRPKEAFSDGITSVKNS
WFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLSHYWMPK
WINATDPSARTLTHYKSAVKA
Enzyme 1 Number of Residues 561
Enzyme 1 Molecular Weight 64371
Enzyme 1 Theoretical pI 6.85
Enzyme 1 GO Classification
Function
  • asparagine synthase (glutamine-hydrolyzing) activity
  • asparagine synthase (glutamine-hydrolyzing) activity
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • asparagine biosynthesis
  • asparagine metabolism
  • aspartate family amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function ATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + L-aspartate + L-glutamine = AMP + diphosphate + L-asparagine + L-glutamate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 179100 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P08243 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ASNS_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1686 bp 
ATGTGTGGCATTTGGGCGCTGTTTGGCAGTGATGATTGCCTTTCTGTTCAGTGTCTGAGT
GCTATGAAGATTGCACACAGAGGTCCAGATGCATTCCGTTTTGAGAATGTCAATGGATAC
ACCAACTGCTGCTTTGGATTTCACCGGTTGGCGGTAGTTGACCCGCTGTTTGGAATGCAG
CCAATTCGAGTGAAGAAATATCCGTATTTGTGGCTCTGTTACAATGGTGAAATCTACAAC
CATAAGAAGATGCAACAGCATTTTGAATTTGAATACCAGACCAAAGTGGATGGTGAGATA
ATCCTTCATCTTTATGACAAAGGAGGAATTGAGCAAACAATTTGTATGTTGGATGGTGTG
TTTGCATTTGTTTTACTGGATACTGCCAATAAGAAAGTGTTCCTGGGTAGAGATACATAT
GGAGTCAGACCTTTGTTTAAAGCAATGACAGAAGATGGATTTTTGGCTGTATGTTCAGAA
GCTAAAGGTCTTGTTACATTGAAGCACTCCGCGACTCCCTTTTTAAAAGTGGAGCCTTTT
CTTCCTGGACACTATGAAGTTTTGGATTTAAAGCCAAATGGCAAAGTTGCATCCGTGGAA
ATGGTTAAATATCATCACTGTCGGGATGTACCCCTGCACGCCCTCTATGACAATGTGGAG
AAACTCTTTCCAGGTTTTGAGATAGAAACTGTGAAGAACAACCTCAGGATCCTTTTTAAT
AATGCTGTAAAGAAACGTTTGATGACAGACAGAAGGATTGGCTGCCTTTTATCAGGGGGC
TTGGACTCCAGCTTGGTTGCTGCCACTCTGTTGAAGCAGCTGAAAGAAGCCCAAGTACAG
TATCCTCTCCAGACATTTGCAATTGGCATGGAAGACAGCCCCGATTTACTGGCTGCTAGA
AAGGTGGCAGATCATATTGGAAGTGAACATTATGAAGTCCTTTTTAACTCTGAGGAAGGC
ATTCAGGCTCTGGATGAAGTCATATTTTCCTTGGAAACTTATGACATTACAACAGTTCGT
GCTTCAGTAGGTATGTATTTAATTTCCAAGTATATTCGGAAGAACACAGATAGCGTGGTG
ATCTTCTCTGGAGAAGGATCAGATGAACTTACGCAGGGTTACATATATTTTCACAAGGCT
CCTTCTCCTGAAAAAGCCGAGGAGGAGAGTGAGAGGCTTCTGAGGGAACTCTATTTGTTT
GATGTTCTCCGCGCAGATCGAACTACTGCTGCCCATGGTCTTGAACTGAGAGTCCCATTT
CTAGATCATCGATTTTTTTCCTATTACTTGTCTCTGCCACCAGAAATGAGAATTCCAAAG
AATGGGATAGAAAAACATCTCCTGAGAGAGACGTTTGAGGATTCCAATCTGATACCCAAA
GAGATTCTCTGGCGACCAAAAGAAGCCTTCAGTGATGGAATAACTTCAGTTAAGAATTCC
TGGTTTAAGATTTTACAGGAATACGTTGAACATCAGGTTGATGATGCAATGATGGCAAAT
GCAGCCCAGAAATTTCCCTTCAATACTCCTAAAACCAAAGAAGGATATTACTACCGTCAA
GTCTTTGAACGCCATTACCCAGGCCGGGCTGACTGGCTGAGCCATTACTGGATGCCCAAG
TGGATCAATGCCACTGACCCTTCTGCCCGCACGCTGACCCACTACAAGTCAGCTGTCAAA
GCTTAG
Enzyme 1 GenBank Gene ID M27396 Link Image
Enzyme 1 GeneCard ID ASNS Link Image
Enzyme 1 GenAtlas ID ASNS Link Image
Enzyme 1 HGNC ID HGNC:753 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7q21.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Andrulis IL, Chen J, Ray PN: Isolation of human cDNAs for asparagine synthetase and expression in Jensen rat sarcoma cells. Mol Cell Biol. 1987 Jul;7(7):2435-43. [PubMed Link Image]
  2. Zhang YP, Lambert MA, Cairney AE, Wills D, Ray PN, Andrulis IL: Molecular structure of the human asparagine synthetase gene. Genomics. 1989 Apr;4(3):259-65. [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. Greco A, Ittmann M, Basilico C: Molecular cloning of a gene that is necessary for G1 progression in mammalian cells. Proc Natl Acad Sci U S A. 1987 Mar;84(6):1565-9. [PubMed Link Image]
  5. Greco A, Gong SS, Ittmann M, Basilico C: Organization and expression of the cell cycle gene, ts11, that encodes asparagine synthetase. Mol Cell Biol. 1989 Jun;9(6):2350-9. [PubMed Link Image]
  6. Van Heeke G, Schuster SM: Expression of human asparagine synthetase in Escherichia coli. J Biol Chem. 1989 Apr 5;264(10):5503-9. [PubMed Link Image]
  7. Van Heeke G, Schuster SM: The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity. J Biol Chem. 1989 Nov 25;264(33):19475-7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5883
Enzyme 2 Name Asparaginyl-tRNA synthetase, cytoplasmic
Enzyme 2 Synonyms
  1. Asparagine-- tRNA ligase
  2. AsnRS
Enzyme 2 Gene Name NARS
Enzyme 2 Protein Sequence >Asparaginyl-tRNA synthetase, cytoplasmic 
MVLAELYVSDREGSDATGDGTKEKPFKTGLKALMTVGKEPFPTIYVDSQKENERWNVISK
SQLKNIKKMWHREQMKSESREKKEAEDSLRREKNLEEAKKITIKNDPSLPEPKCVKIGAL
EGYRGQRVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTESSVA
VYGMLNLTPKGKQAPGGHELSCDFWELIGLAPAGGADNLINEESDVDVQLNNRHMMIRGE
NMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSS
QLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCD
VVDRILKSPAGSIVHELNPNFQPPKRPFKRMNYSDAIVWLKEHDVKKEDGTFYEFGEDIP
EAPERLMTDTINEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSMRIF
DSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP
RFVQRCTP
Enzyme 2 Number of Residues 548
Enzyme 2 Molecular Weight 62944
Enzyme 2 Theoretical pI 6.17
Enzyme 2 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • asparagine-tRNA ligase activity
  • aspartate-tRNA ligase activity
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleic acid binding
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
Process
  • RNA metabolism
  • asparaginyl-tRNA aminoacylation
  • aspartyl-tRNA aminoacylation
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Translation, ribosomal structure and biogenesis
Enzyme 2 Specific Function ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn)
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn)
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 2764505 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O43776 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name SYNC_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1647 bp 
ATGGTGCTAGCAGAGCTGTACGTCTCTGACCGAGAGGGAAGCGATGCCACGGGAGATGGA
ACCAAGGAGAAACCATTTAAAACAGGTCTAAAGGCTTTGATGACAGTAGGGAAAGAACCA
TTTCCTACCATTTACGTAGATTCACAAAAAGAAAATGAGAGGTGGAATGTTATTTCTAAA
TCACAGTTGAAGAACATTAAAAAGATGTGGCATAGGGAACAAATGAAGAGTGAATCCCGG
GAAAAGAAAGAGGCAGAAGATAGTTTACGAAGAGAAAAGAACCTGGAAGAAGCAAAGAAG
ATTACCATTAAAAATGATCCAAGTCTCCCAGAGCCAAAATGTGTGAAGATTGGTGCGTTA
GAAGGATATAGAGGCCAAAGAGTAAAGGTGTTTGGCTGGGTCCACAGGCTGCGCAGGCAA
GGAAAGAATTTAATGTTTCTGGTGTTGCGAGATGGTACAGGTTATCTTCAGTGTGTCTTG
GCGGATGAGTTGTGTCAGTGCTACAATGGAGTTCTCTTGTCCACGGAGAGCAGTGTTGCA
GTGTATGGAATGCTAAATCTTACCCCAAAGGGCAAGCAGGCTCCAGGTGGCCATGAGCTG
AGTTGTGACTTCTGGGAACTAATTGGGTTGGCCCCTGCTGGAGGAGCTGACAACCTGATC
AATGAGGAGTCTGACGTTGATGTCCAGCTCAACAACAGACACATGATGATCCGAGGAGAA
AACATGTCCAAAATCCTAAAAGCACGATCCATGGTCACCAGGTGCTTTAGAGATCACTTC
TTTGATAGGGGGTACTATGAAGTTACTCCTCCAACATTAGTGCAAACACAAGTAGAAGGT
GGTGCCACACTCTTCAAGCTTGACTATTTTGGGGAAGAGGCATTTTTGACTCAATCCTCT
CAGTTGTACTTGGAGACCTGCCTCCCAGCCCTGGGAGATGTTTTTTGTATTGCTCAGTCA
TACCGGGCAGAGCAGTCCAGAACACGAAGGCACCTGGCTGAGTACACTCACGTGGAAGCT
GAGTGTCCTTTCCTGACTTTTGACGACCTCCTGAACCGGTTGGAGGACTTGGTTTGTGAT
GTGGTAGATCGAATATTGAAGTCACCTGCAGGGAGCATAGTGCATGAGCTCAACCCGAAC
TTTCAGCCCCCCAAACGGCCTTTCAAACGGATGAACTATTCAGATGCTATCGTTTGGCTA
AAAGAACATGATGTAAAGAAAGAAGATGGAACTTTCTATGAATTTGGAGAAGATATCCCA
GAAGCTCCTGAGAGACTGATGACAGACACCATTAATGAACCAATCTTGCTGTGTCGATTT
CCTGTGGAGATCAAGTCCTTCTACATGCAGCGATGTCCTGAGGATTCCCGTCTTACTGAA
TCTGTCGACGTGTTGATGCCCAATGTTGGTGAGATTGTGGGAGGCTCAATGCGTATCTTT
GATAGTGAAGAAATACTGGCAGGTTATAAAAGGGAAGGGATTGACCCCACTCCCTATTAC
TGGTATACGGATCAGAGAAAATACGGTACATGTCCCCATGGAGGATATGGCTTGGGCTTG
GAACGATTCTTAACGTGGATTCTGAATAGGTATCACATCCGAGACGTGTGCTTATACCCT
CGATTTGTCCAGCGTTGCACGCCATAA
Enzyme 2 GenBank Gene ID AJ000334 Link Image
Enzyme 2 GeneCard ID NARS Link Image
Enzyme 2 GenAtlas ID NARS Link Image
Enzyme 2 HGNC ID HGNC:7643 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Beaulande M, Tarbouriech N, Hartlein M: Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression in Escherichia coli and characterization as human autoantigen. Nucleic Acids Res. 1998 Jan 15;26(2):521-4. [PubMed Link Image]
  2. Shiba K, Motegi H, Yoshida M, Noda T: Human asparaginyl-tRNA synthetase: molecular cloning and the inference of the evolutionary history of Asx-tRNA synthetase family. Nucleic Acids Res. 1998 Nov 15;26(22):5045-51. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6885
Enzyme 3 Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit precursor
Enzyme 3 Synonyms
  1. Ribophorin I
  2. RPN-I
Enzyme 3 Gene Name RPN1
Enzyme 3 Protein Sequence >Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit precursor 
MEAPAAGLFLLLLLGTWAPAPGSASSEAPPLINEDVKRTVDLSSHLAKVTAEVVLAHLGG
GSTSRATSFLLALEPELEARLAHLGVQVKGEDEEENNLEVRETKIKGKSGRFFTVKLPVA
LDPGAKISVIVETVYTHVLHPYPTQITQSEKQFVVFEGNHYFYSPYPTKTQTMRVKLASR
NVESYTKLGNPTRSEDLLDYGPFRDVPAYSQDTFKVHYENNSPFLTITSMTRVIEVSHWG
NIAVEENVDLKHTGAVLKGPFSRYDYQRQPDSGISSIRSFKTILPAAAQDVYYRDEIGNV
STSHLLILDDSVEMEIRPRFPLFGGWKTHYIVGYNLPSYEYLYNLGDQYALKMRFVDHVF
DEQVIDSLTVKIILPEGAKNIEIDSPYEISRAPDELHYTYLDTFGRPVIVAYKKNLVEQH
IQDIVVHYTFNKVLMLQEPLLVVAAFYILFFTVIIYVRLDFSITKDPAAEARMKVACITE
QVLTLVNKRIGLYRHFDETVNRYKQSRDISTLNSGKKSLETEHKALTSEIALLQSRLKTE
GSDLCDRVSEMQKLDAQVKELVLKSAVEAERLVAGKLKKDTYIENEKLISGKRQELVTKI
DHILDAL
Enzyme 3 Number of Residues 607
Enzyme 3 Molecular Weight 68570
Enzyme 3 Theoretical pI 6.34
Enzyme 3 GO Classification
Function
  • catalytic activity
  • dolichyl-diphosphooligosaccharide-protein glycotransferase activity
  • oligosaccharyl transferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • endoplasmic reticulum
  • integral to membrane
  • intracellular membrane-bound organelle
  • intrinsic to membrane
  • membrane
  • membrane-bound organelle
  • organelle
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Essential subunit of N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains
Enzyme 3 Pathways
Enzyme 3 Reactions
  • dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharidechain attached by N-glycosyl linkage to protein L-asparagine
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-23
Enzyme 3 Transmembrane Regions
  • 439-457
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 36053 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P04843 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name RIB1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1824 bp 
ATGGAGGCGCCAGCCGCCGGCTTGTTTCTGCTCCTGTTGCTTGGGACTTGGGCCCCGGCG
CCGGGCAGCGCCTCCTCCGAGGCACCGCCGCTGATCAATGAGGACGTGAAGCGCACAGTG
GACCTAAGCAGCCACCTGGCTAAGGTGACGGCCGAGGTGGTCCTGGCGCACCTGGGCGGC
GGCTCCACGTCCCGAGCTACCTCTTTCCTGCTGGCTTTGGAGCCTGAGCTCGAGGCCCGG
CTGGCGCACCTGGGCGTGCAGGTAAAGGGAGAAGATGAGGAAGAGAACAATTTGGAAGTA
CGTGAAACCAAAATTAAGGGTAAAAGTGGGAGATTCTTCACAGTCAAGCTCCCAGTTGCT
CTTGATCCTGGGGCCAAGATTTCAGTCATTGTGGAAACAGTCTACACCCATGTGCTTCAT
CCATATCCAACCCAGATCACCCAGTCAGAGAAACAGTTTGTGGTGTTTGAGGGGAACCAT
TATTTCTACTCTCCCTATCCAACGAAGACACAAACCATGCGTGTGAAGCTTGCCTCTCGA
AATGTGGAGAGCTACACCAAGCTGGGGAACCCCACGCGCTCTGAGGACCTACTGGATTAT
GGGCCTTTCAGAGATGTGCCTGCCTATAGTCAGGATACTTTTAAAGTACATTATGAGAAC
AACAGCCCTTTCCTGACCATCACCAGCATGACCCGAGTCATTGAAGTCTCTCACTGGGGT
AATATTGCTGTGGAAGAAAATGTGGACTTAAAGCACACAGGAGCTGTGCTTAAGGGGCCT
TTCTCACGCTATGATTACCAGAGACAGCCAGATAGTGGAATATCCTCCATCCGTTCTTTT
AAGACCATCCTTCCTGCTGCTGCCCAGGATGTTTATTACCGGGATGAGATTGGCAATGTT
TCTACCAGCCACCTCCTTATTTTGGATGACTCTGTAGAGATGGAAATCCGGCCTCGCTTC
CCTCTCTTTGGCGGGTGGAAGACCCATTACATCGTTGGCTACAACCTCCCAAGCTATGAG
TACCTCTATAATTTGGGTGACCAGTATGCACTGAAGATGAGGTTTGTGGACCATGTGTTT
GATGAACAAGTGATAGATTCTCTGACTGTGAAGATCATCCTGCCTGAAGGAGCCAAGAAC
ATTGAAATTGATAGTCCCTATGAAATCAGCCGTGCCCCAGATGAGCTGCACTACACCTAT
CTGGATACATTTGGCCGCCCTGTGATTGTTGCCTACAAGAAAAATCTGGTAGAACAGCAC
ATTCAGGACATTGTGGTCCACTACACGTTCAACAAGGTGCTCATGCTGCAGGAGCCCCTG
CTGGTGGTGGCGGCCTTCTACATCCTGTTCTTCACCGTTATCATCTATGTTCGGCTGGAC
TTCTCCATCACCAAGGATCCAGCCGCAGAAGCCAGGATGAAGGTAGCCTGCATCACAGAG
CAGGTCTTGACCCTGGTCAACAAGAGAATAGGCCTTTACCGTCACTTTGACGAGACCGTC
AATAGGTACAAGCAATCCCGGGACATCTCCACCCTCAACAGTGGCAAGAAGAGCCTGGAG
ACTGAACACAAGGCCTTGACCAGTGAGATTGCACTGCTGCAGTCCAGGCTGAAGACAGAG
GGCTCTGATCTGTGCGACAGAGTGAGCGAAATGCAGAAGCTGGATGCACAGGTCAAGGAG
CTGGTGCTGAAGTCGGCGGTGGAGGCTGAGCGCCTGGTGGCTGGCAAGCTCAAGAAAGAC
ACGTACATTGAGAATGAGAAGCTCATCTCAGGAAAGCGCCAGGAGCTGGTCACCAAGATC
GACCACATCCTGGATGCCCTGTAG
Enzyme 3 GenBank Gene ID Y00281 Link Image
Enzyme 3 GeneCard ID RPN1 Link Image
Enzyme 3 GenAtlas ID RPN1 Link Image
Enzyme 3 HGNC ID HGNC:10381 Link Image
Enzyme 3 Chromosome Location 3
Enzyme 3 Locus 3q21.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Crimaudo C, Hortsch M, Gausepohl H, Meyer DI: Human ribophorins I and II: the primary structure and membrane topology of two highly conserved rough endoplasmic reticulum-specific glycoproteins. EMBO J. 1987 Jan;6(1):75-82. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6887
Enzyme 4 Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit precursor
Enzyme 4 Synonyms
  1. Oligosaccharyl transferase 48 kDa subunit
  2. DDOST 48 kDa subunit
Enzyme 4 Gene Name DDOST
Enzyme 4 Protein Sequence >Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit precursor 
MEPSTAARAWALFWLLLPLLGAVCASGPRTLVLLDNLNVRETHSLFFRSLKDRGFELTFK
TADDPSLSLIKYGEFLYDNLIIFSPSVEDFGGNINVETISAFIDGGGSVLVAASSDIGDP
LRELGSECGIEFDEEKTAVIDHHNYDISDLGQHTLIVADTENLLKAPTIVGKSSLNPILF
RGVGMVADPDNPLVLDILTGSSTSYSFFPDKPITQYPHAVGKNTLLIAGLQARNNARVIF
SGSLDFFSDSFFNSAVQKAAPGSQRYSQTGNYELAVALSRWVFKEEGVLRVGPVSHHRVG
ETAPPNAYTVTDLVEYSIVIQQLSNGKWVPFDGDDIQLEFVRIDPFVRTFLKKKGGKYSV
QFKLPDVYGVFQFKVDYNRLGYTHLYSSTQVSVRPLQHTQYERFIPSAYPYYASAFPMML
GLFIFSIVFLHMKEKEKSD
Enzyme 4 Number of Residues 439
Enzyme 4 Molecular Weight 48810
Enzyme 4 Theoretical pI 5.42
Enzyme 4 GO Classification
Function
  • catalytic activity
  • dolichyl-diphosphooligosaccharide-protein glycotransferase activity
  • oligosaccharyl transferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid N-linked glycosylation
  • protein amino acid N-linked glycosylation via asparagine
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • endoplasmic reticulum membrane
  • membrane
  • organelle membrane
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Essential subunit of N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains
Enzyme 4 Pathways
Enzyme 4 Reactions
  • dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharidechain attached by N-glycosyl linkage to protein L-asparagine
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-26
Enzyme 4 Transmembrane Regions
  • 411-430
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 473947 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P39656 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name OST48_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1371 bp 
ATGGGGTACTTCCGGTGTGCAGGTGCTGGGTCCTTCGGCAGGAGGAGGAAGATGGAGCCC
AGCACCGCGGCCCGGGCTTGGGCCCTCTTTTGGTTGCTGCTGCCCTTGCTTGGCGCGGTT
TGCGCCAGCGGACCCCGCACCTTAGTGCTGCTGGACAACCTCAACGTGCGGGAGACTCAT
TCGCTTTTCTTCCGGAGCCTGAAGGACCGGGGCTTTGAGCTCACATTCAAGACCGCTGAT
GACCCCAGCCTGTCTCTCATAAAGTATGGGGAATTCCTCTATGACAATCTCATCATTTTC
TCCCCTTCGGTAGAAGATTTTGGAGGCAACATCAACGTGGAGACCATCAGTGCCTTTATT
GACGGCGGAGGCAGTGTGCTGGTAGCTGCCAGCTCCGACATTGGTGACCCTCTTCGAGAG
CTGGGCAGTGAGTGCGGGATTGAGTTTGACGAGGAGAAAACGGCTGTCATTGACCATCAC
AACTATGACATCTCAGACCTTGGCCAGCATACGCTCATCGTGGCTGACACTGAGAACCTG
CTGAAGGCCCCAACCATCGTTGGGAAATCATCTCTAAATCCCATCCTCTTTCGAGGTGTT
GGGATGGTGGCCGATCCTGATAACCCTTTGGTGCTGGACATCCTGACGGGCTCTTCCACC
TCTTACTCCTTCTTCCCGGACAAGCCTATCACCCAGTATCCACATGCGGTGGGGAAGAAC
ACCCTCCTCATTGCTGGGCTCCAGGCCAGGAACAATGCCCGCGTCATCTTCAGCGGCTCC
CTCGACTTCTTCAGCGACTCCTTCTTCAACTCAGCAGTGCAGAAGGCGGCGCCCGGCTCC
CAGAGGTATTCCCAGACAGGCAACTATGAACTAGCTGTGGCCCTCTCCCGCTGGGTGTTC
AAGGAGGAGGGTGTCCTCCGTGTGGGGCCTGTGTCCCATCATCGGGTGGGCGAGACAGCC
CCACCCAATGCCTACACTGTCACTGACCTAGTGGAGTATAGCATCGTGATCCAGCAGCTC
TCAAATGGCAAATGGGTCCCCTTTGATGGCGATGACATTCAGCTGGAGTTTGTCCGCATT
GATCCTTTTGTGAGGACCTTCCTGAAGAAGAAAGGTGGCAAATACAGTGTTCAGTTCAAG
TTGCCCGACGTGTATGGTGTATTCCAGTTTAAAGTGGATTACAACCGGCTAGGCTACACA
CACCTGTACTCTTCCACTCAGGTATCCGTGCGGCCACTCCAGCACACGCAGTATGAGCGC
TTCATCCCCTCGGCCTACCCCTACTACGCCAGCGCCTTCCCCATGATGCTGGGGCTCTTC
ATCTTCAGCATCGTCTTCTTGCACATGAAGGAGAAGGAGAAGTCCGACTGA
Enzyme 4 GenBank Gene ID D29643 Link Image
Enzyme 4 GeneCard ID DDOST Link Image
Enzyme 4 GenAtlas ID DDOST Link Image
Enzyme 4 HGNC ID HGNC:2728 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 1p36.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H, et al.: Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995;2(1):37-43. [PubMed Link Image]
  2. Yamagata T, Tsuru T, Momoi MY, Suwa K, Nozaki Y, Mukasa T, Ohashi H, Fukushima Y, Momoi T: Genome organization of human 48-kDa oligosaccharyltransferase (DDOST). Genomics. 1997 Nov 1;45(3):535-40. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6888
Enzyme 5 Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit precursor
Enzyme 5 Synonyms
  1. Ribophorin II
  2. RPN-II
  3. RIBIIR
Enzyme 5 Gene Name RPN2
Enzyme 5 Protein Sequence >Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit precursor 
MAPPGSSTVFLLALTIIASTWALTPTHYLTKHDVERLKASLDRPFTNLESAFYSIVGLSS
LGAQVPDAKKACTYIRSNLDPSNVDSLFYAAQASQALSGCEISISNETKDLLLAAVSEDS
SVTQIYHAVAALSGFGLPLASQEALSALTARLSKEETVLATVQALQTASHLSQQADLRSI
VEEIEDLVARLDELGGVYLQFEEGLETTALFVAATYKLMDHVGTEPSIKEDQVIQLMNAI
FSKKNFESLSEAFSVASAAAVLSHNRYHVPVVVVPEGSASDTHEQAILRLQVTNVLSQPL
TQATVKLEHAKSVASRATVLQKTSFTPVGDVFELNFMNVKFSSGYYDFLVEVEGDNRYIA
NTVELRVKISTEVGITNVDLSTVDKDQSIAPKTTRVTYPAKAKGTFIADSHQNFALFFQL
VDVNTGAELTPHQTFVRLHNQKTGQEVVFVAEPDNKNVYKFELDTSERKIEFDSASGTYT
LYLIIGDATLKNPILWNVADVVIKFPEEEAPSTVLSQNLFTPKQEIQHLFREPEKRPPTV
VSNTFTALILSPLLLLFALWIRIGANVSNFTFAPSTIIFHLGHAAMLGLMYVYWTQLNMF
QTLKYLAILGSVTFLAGNRMLAQQAVKRTAH
Enzyme 5 Number of Residues 631
Enzyme 5 Molecular Weight 69285
Enzyme 5 Theoretical pI 5.46
Enzyme 5 GO Classification
Function
  • catalytic activity
  • dolichyl-diphosphooligosaccharide-protein glycotransferase activity
  • oligosaccharyl transferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid N-linked glycosylation
  • protein amino acid N-linked glycosylation via asparagine
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • endoplasmic reticulum membrane
  • membrane
  • oligosaccharyl transferase complex
  • organelle membrane
  • protein complex
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Essential subunit of N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains
Enzyme 5 Pathways
Enzyme 5 Reactions
  • dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharidechain attached by N-glycosyl linkage to protein L-asparagine
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-22
Enzyme 5 Transmembrane Regions
  • 539-561
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 36049 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P04844 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name RIB2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1896 bp 
ATGGCGCCGCCGGGTTCAAGCACTGTCTTCCTGTTGGCCCTGACAATCATAGCCAGCACC
TGGGCTCTGACGCCCACTCACTACCTCACCAAGCATGACGTGGAGAGACTAAAAGCCTCG
CTGGATCGCCCTTTCACAAATTTGGAATCTGCCTTCTACTCCATCGTGGGACTCAGCAGC
CTTGGTGCTCAGGTGCCAGATGCAAAGAAAGCATGTACCTACATCAGATCTAACCTTGAT
CCCAGCAATGTGGATTCCCTCTTCTACGCTGCCCAGGCCAGCCAGGCCCTCTCAGGATGT
GAGATCTCTATTTCAAATGAGACCAAAGATCTGCTTCTGGCAGCTGTCAGTGAGGACTCA
TCTGTTACCCAGATCTACCATGCAGTTGCAGCTCTAAGTGGCTTTGGCCTTCCCTTGGCA
TCCCAAGAAGCACTCAGTGCCCTTACTGCTCGTCTCAGCAAGGAGGAGACTGTGCTGGCA
ACAGTCCAGGCTCTGCAGACAGCATCCCACCTRTCCCAGCAGGCTGACCTGAGGAGCATC
GTGGAGGAGATTGAGGACCTTGTTGCTCGCCTGGATGAACTCGGGGGCCTGTATCTCCAG
TGTGAAGAAGGACTGGAAACAACAGCGTTATTTGTGGCTGCCACCTACAAGCTCATGGAT
CATGTGGGGACTGAGCCATCCATTAAGGAGGATCAGGTCATCCAGCTGATGAACGCGATC
TTCAGCAAGAAGAACTTTGAGTCCCTCTCCGAAGCCTTCAGCGTGGCCTCTGCAGCTTCT
GTGCTCTCGCATAATCGCTACCACGTGCCAGTTGTGGTTGTGCCTGAGGGCTCTGCTTCC
GACACTCATGAACAGGCTATCTTGCGGTTGCAAGTCACCAATGTTCTGTCTCAGCCTCTG
ACTCAGGCCACTGTTAAACTAGAACATGCTAAATCTGTTGCTTCCAGAGCCACTGTCCTC
CAGAAGACATCCTTCACCCCTGTAGGGGATGTTTTTGAACTAAATTTCATGAACGTCAAA
TTTTCCAGTGGTTATTATGACTTCCTTGTCGAAGTTGAAGGTGACAACCGGTATATTGCA
AATACCGTAGAGCTCAGAGTCAAGATCTCCACTGAAGTTGGCATCACAAATGTTGATCTT
TCCACCGTGGATAAGGATCAGAGCATTGCACCCAAAACTACCCGGGTGACATACCCAGCC
AAAGCCAAGGGCACATTCATCGCAGACAGCCACCAGAACTTCGCCTTGTTCTTCCAGCTG
GTAGATATGAACACTGGTGCTGAACTCACTCCTCACCAGACATTTGTCCGACTCCATAAC
CAGAAGACTGGCCAGGAAGTGGTGTTTGTTGCCGAGCCAGACAACAAGAACGTGTACAAG
TTTGAACTGGATACCTCTGAAAGAAAGATTGAATTTGACTCTGCCTCTGGCACCTACACT
CTCTACTTAATCATTGGAGATGCCACTTTGAAGAACCCAATCCTCTGGAATGTGGCTGAT
GTGGTCATCAAGTTCCCTGAGGAAGAAGCTCCCTCGACTGTCTTGTCCCAGAACCTTTTC
ACTCCAAAACAGGAAATTCAGCACCTGTTCCGCGAGCCTGAGAAGAGGCCCCCCACCGTG
GTGTCCAATACATTCACTGCCCTGATCCTCTCGCCGTTGCTTCTGCTCTTCGCTCTGTGG
ATCCGGATTGGTGCCAATGTCTCCAACTTCACTTTTGCTCCTAGCACGATTATATTTCAC
CTGGGACATGCTGCTATGCTGGGACTCATGTATGTCTACTGGACTCAGCTCAACATGTTC
CAGACCTTGAAGTACCTGGCCATCTTGGGCAGTGTGACGTTTCTGGCTGGCAATCGGATG
CTGGCCCAGCAGGCAGTCAAGAGAACAGCACATTAG
Enzyme 5 GenBank Gene ID Y00282 Link Image
Enzyme 5 GeneCard ID RPN2 Link Image
Enzyme 5 GenAtlas ID RPN2 Link Image
Enzyme 5 HGNC ID HGNC:10382 Link Image
Enzyme 5 Chromosome Location 20
Enzyme 5 Locus 20q12-q13.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Crimaudo C, Hortsch M, Gausepohl H, Meyer DI: Human ribophorins I and II: the primary structure and membrane topology of two highly conserved rough endoplasmic reticulum-specific glycoproteins. EMBO J. 1987 Jan;6(1):75-82. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 7373
Enzyme 6 Name Neutral amino acid transporter B(0)
Enzyme 6 Synonyms
  1. ATB(0
  2. Solute carrier family 1 member 5
  3. Sodium-dependent neutral amino acid transporter type 2
  4. RD114/simian type D retrovirus receptor
  5. Baboon M7 virus receptor
Enzyme 6 Gene Name SLC1A5
Enzyme 6 Protein Sequence >Neutral amino acid transporter B(0) 
MVADPPRDSKGLAAAEPTANGGLALASIEDQGAAAGGYCGSRDQVRRCLRANLLVLLTVV
AVVAGVALGLGVSGAGGALALGPERLSAFVFPGELLLRLLRMIILPLVVCSLIGGAASLD
PGALGRLGAWALLFFLVTTLLASALGVGLALALQPGAASAAINASVGAAGSAENAPSKEV
LDSFLDLARNIFPSNLVSAAFRSYSTTYEERNITGTRVKVPVGQEVEGMNILGLVVFAIV
FGVALRKLGPEGELLIRFFNSFNEATMVLVSWIMWYAPVGIMFLVAGKIVEMEDVGLLFA
RLGKYILCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGIVTPLATAFGTSSSSATLPLM
MKCVEENNGVAKHISRFILPIGATVNMDGAALFQCVAAVFIAQLSQQSLDFVKIITILVT
ATASSVGAAGIPAGGVLTLAIILEAVNLPVDHISLILAVDWLVDRSCTVLNVEGDALGAG
LLQNYVDRTESRSTEPELIQVKSELPLDPLPVPTEEGNPLLKHYRGPAGDATVASEKESV
M
Enzyme 6 Number of Residues 541
Enzyme 6 Molecular Weight 56599
Enzyme 6 Theoretical pI 5.14
Enzyme 6 GO Classification
Function
  • carboxylic acid transporter activity
  • dicarboxylic acid transporter activity
  • organic acid transporter activity
  • sodium:dicarboxylate symporter activity
  • transporter activity
Process
  • carboxylic acid transport
  • cellular physiological process
  • dicarboxylic acid transport
  • organic acid transport
  • physiological process
  • transport
Component
  • cell
  • membrane
Enzyme 6 General Function Energy production and conversion
Enzyme 6 Specific Function Has a broad substrate specificity, a preference for zwitterionic amino acids, and a sodium-dependence. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated amino acids, anionic amino acids, and cationic amino acids. Act as a cell surface receptor for feline endogenous virus RD114, baboon M7 endogenous virus and type D simian retroviruses
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 53-73 99-119 133-153 225-245 266-286 306-326 336-356 377-397 399-419 426-446
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 1478281 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q15758 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name AAAT_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1626 bp 
ATGGTGGCCGATCCTCCTCGAGACTCCAAGGGGCTCGCAGCGGCGGAGCCACCGCCAACG
GGGGCCTGGCAGCTGGCCTCCATCGAGGACCAAGGCGCGGCAGCAGGCGGCTACTGCGGT
TCCCGGGACCTGGTGCGCCGCTGCCTTCGAGCCAACCTGCTTGTGCTGCTGACAGTGGTG
GCCGTGGTGGCCGGCGTGGCGCTGGGACTGGGGGTGTCGGGGGCCGGGGGTGCGCTGGCG
TTGGGCCCGGGAGCGCTTGAGGCCTTCGTCTTCCCGGGCGAGCTGCTGCTGCGTCTGCTG
CGGATGATCATCTTGCCGCTGGTGGTGTGCAGCTTGATCGGCGGCGCCGCCAGCCTGGAC
CCCGGCGCGCTCGGCCGTCTGGGCGCCTGGGCGCTGCTCTTTTTCCTGGTCACCACGCTG
CTGGCGTCGGCGCTCGGAGTGGGCTTGGCGCTGGCTCTGCAGCCGGGCGCCGCCTCCGCC
GCCATCAACGCCTCCGTGGGAGCCGCGGGCAGTGCCGAAAATGCCCCCAGCAAGGAGGTG
CTCGATTCGTTCCTGGATCTTGCGAGAAATATCTTCCCTTCCAACCTGGTGTCAGCAGCC
TTTCGCTCATACTCTACCACCTATGAAGAGAGGAATATCACCGGAACCAGGGTGAAGGTG
CCCGTGGGGCAGGAGGTGGAGGGGATGAACATCCTGGGCTTGGTAGTGTTTGCCATCGTC
TTTGGTGTGGCGCTGCGGAAGCTGGGGCCTGAAGGGGAGCTGCTTATCCGCTTCTTCAAC
TCCTTCAATGAGGCCACCATGGTTCTGGTCTCCTGGATCATGTGGTACGCCCCTGTGGGC
ATCATGTTCCTGGTGGCTGGCAAGATCGTGGAGATGGAGGATGTGGGTTTACTCTTTGCC
CGCCTTGGCAAGTACATTCTGTGCTGCCTGCTGGGTCACGCCATCCATGGGCTCCTGGTA
CTGCCCCTCATCTACTTCCTCTTCACCCGCAAAAACCCCTACCGCTTCCTGTGGGGCATC
GTGACGCCGCTGGCCACTGCCTTTGGGACCTCTTCCAGTTCCGCCACGCTGCCGCTGATG
ATGAAGTGCGTGGAGGAGAATAATGGCGTGGCCAAGCACATCAGCCGTTTCATCCTGCCC
ATCGGCGCCACCGTCAACATGGACGGTGCCGCGCTCTTCCAGTGCGTGGCCGCAGTGTTC
ATTGCACAGCTCAGCCAGCAGTCCTTGGACTTCGTAAAGATCATCACCATCCTGGTCACG
GCCACAGCGTCCAGCGTGGGGGCAGCGGGCATCCCTGCTGGAGGTGTCCTCACTCTGGCC
ATCATCCTCGAAGCAGTCAACCTCCCGGTCGACCATATCTCCTTGATCCTGGCTGTGGAC
TGGCTAGTCGACCGGTCCTGTACCGTCCTCAATGTAGAAGGTGACGCTCTGGGGGCAGGA
CTCCTCCAAAATTATGTGGACCGTACGGAGTCGAGAAGCACAGAGCCTGAGTTGATACAA
GTGAAGAGTGAGCTGCCCCTGGATCCGCTGCCAGTCCCCACTGAGGAAGGAAACCCCCTC
CTCAAACACTATCGGGGGCCCGCAGGGGATGCCACGGTCGCCTCTGAGAAGGAATCAGTC
ATGTAA
Enzyme 6 GenBank Gene ID U53347 Link Image
Enzyme 6 GeneCard ID SLC1A5 Link Image
Enzyme 6 GenAtlas ID SLC1A5 Link Image
Enzyme 6 HGNC ID HGNC:10943 Link Image
Enzyme 6 Chromosome Location 19
Enzyme 6 Locus 19q13.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Kekuda R, Prasad PD, Fei YJ, Torres-Zamorano V, Sinha S, Yang-Feng TL, Leibach FH, Ganapathy V: Cloning of the sodium-dependent, broad-scope, neutral amino acid transporter Bo from a human placental choriocarcinoma cell line. J Biol Chem. 1996 Aug 2;271(31):18657-61. [PubMed Link Image]
  2. Rasko JE, Battini JL, Gottschalk RJ, Mazo I, Miller AD: The RD114/simian type D retrovirus receptor is a neutral amino acid transporter. Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2129-34. [PubMed Link Image]
  3. Tailor CS, Nouri A, Zhao Y, Takeuchi Y, Kabat D: A sodium-dependent neutral-amino-acid transporter mediates infections of feline and baboon endogenous retroviruses and simian type D retroviruses. J Virol. 1999 May;73(5):4470-4. [PubMed Link Image]
  4. Tailor CS, Marin M, Nouri A, Kavanaugh MP, Kabat D: Truncated forms of the dual function human ASCT2 neutral amino acid transporter/retroviral receptor are translationally initiated at multiple alternative CUG and GUG codons. J Biol Chem. 2001 Jul 20;276(29):27221-30. Epub 2001 May 11. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 8287
Enzyme 7 Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
Enzyme 7 Synonyms
  1. Oligosaccharyl transferase subunit STT3A
  2. STT3- A
  3. B5
  4. Integral membrane protein 1
  5. TMC
Enzyme 7 Gene Name STT3A
Enzyme 7 Protein Sequence >Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A 
MTKFGFLRLSYEKQDTLLKLLILSMAAVLSFSTRLFAVLRFESVIHEFDPYFNYRTTRFL
AEEGFYKFHNWFDDRAWYPLGRIIGGTIYPGLMITSAAIYHVLHFFHITIDIRNVCVFLA
PLFSSFTSIVTYLLTKELKDAGAGLLAAAMIAVVPGYISRSVAGSYDNEGIAIFCMLLTY
YMWIKAVKTGSICWAAKCALAYFYMVSSWGGYVFLINLIPLHVLVLMLTGRFSHRIYVAY
CTVYCLGTILSRQISFVGFQPVLSSEHMAGFGVFGLCQIHAFVDYLRSKLNPQQFEVLFR
SVISLVGFVLLTVGALLMLTGKISPWTGRFYSLLDPSYAKNNIPIIASVSEHQPTTWSSY
YFDLQLLVFMFPVGLYYCFSNLSDARIFIIMYGVTSMYFSAVMVRLMLVLAPVMSILSGI
GVSQVLSTYMKNLDISRPDKKSKKQQDSTYPIKIEVASGMILVMAFFLITYTFHSTWVTS
EAYSSPSIVLSARGGDGSRIIFDDFREAYYWLRHNTPEDAKVMSWWDYGYQITAMANRTI
LVDNNTWNNTHISRVGQAMASTEEKAYEIMRELDVSYVLVIFGGLTGYSSDDINKFLWMV
RIGGSTDTGKHIKENDYYTPTGEFRVDREGSPVLLNCLMYKMCYYRFGQVYTEAKRPPGF
DRVRNAEIGNKDFELDVLEEGYTTEHWLVRIYKVKDLDNRGLSRT
Enzyme 7 Number of Residues 705
Enzyme 7 Molecular Weight 80472
Enzyme 7 Theoretical pI 8.33
Enzyme 7 GO Classification
Function
  • catalytic activity
  • oligosaccharyl transferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Component of the N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurrs cotranslational and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). SST3A seems to be involved in complex substrate specificity
Enzyme 7 Pathways
Enzyme 7 Reactions
  • dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharidechain attached by N-glycosyl linkage to protein L-asparagine
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-30
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 624704 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P46977 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name STT3A_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2118 bp 
ATGACTAAGTTTGGATTTTTGCGATTGTCCTATGAGAAGCAGGACACACTTTTGAAGCTT
CTCATTCTGTCAATGGCTGCTGTATTATCCTTCTCCACTCGTCTGTTTGCTGTCCTGAGA
TTTGAAAGTGTTATCCATGAGTTTGATCCGTACTTTAATTATCGGACTACCAGGTTCCTG
GCTGAGGAGGGGTTTTATAAATTCCATAACTGGTTTGATGACCGAGCCTGGTACCCTTTG
GGACGAATCATTGGAGGAACAATTTACCCAGGTTTAATGATCACCTCTGCTGCAATCTAC
CATGTACTCCATTTTTTCCACATCACCATCGACATTCGGAATGTCTGTGTGTTCCTGGCC
CCTCTCTTCTCCTCCTTCACCTCCATCGTCACGTACCTCCTTACCAAAGAGCTCAAGGAT
GCAGGGGCTGGGCTTCTTGCTGCTGCCATGATTGCTGTAGTTCCTGGATATATCTCCCGA
TCTGTGGCTGGCTCCTATGATAATGAAGGGATTGCCATCTTTTGCATGCTACTCACCTAC
TACATGTGGATCAAGGCAGTAAAGACTGGTTCCATCTGTTGGGCAGCTAAGTGTGCCCTT
GCTTATTTCTACATGGTCTCGTCATGGGGAGGTTATGTGTTCCTGATCAACTTAATTCCT
CTCCACGTCCTCGTGCTGATGCTCACAGGCCGTTTCTCTCACCGGATCTATGTGGCCTAC
TGTACTGTTTACTGCCTGGGTACTATACTTTCTAGGCAGATCTCCTTTGTGGGTTTCCAG
CCTGTCCTTTCATCAGAGCACATGGCAGGGTTTGGGGTCTTTGGTCTCTGCCAGATCCAT
GCCTTTGTGGATTACCTGCGCAGCAAGTTGAATCCACAACAATTTGAAGTTCTTTTCCGG
AGCGTCATCTCTCTGGTAGGCTTTGTCCTTCTCACCGTGGGAGCTCTCCTCATGCTGACA
GGAAAAATATCTCCCTGGACGGGGCGTTTCTACTCACTGCTGGATCCCTCTTATGCTAAG
AACAACATCCCCATCATTGCTTCTGTGTCTGAGCATCAGCCCACAACCTGGTCCTCATAC
TATTTTGACCTGCAGCTCCTCGTCTTCATGTTTCCAGTTGGCCTCTATTACTGCTTTAGC
AACCTGTCTGATGCCCGGATTTTTATCATCATGTATGGTGTGACCAGCATGTACTTTTCA
GCTGTAATGGTGCGTCTAATGCTAGTGTTGGCACCTGTTATGAGCATTCTCTCTGGCATT
GGAGTCTCCCAGGTGCTGTCCACATACATGAAGAATCTGGACATAAGTCGCCCAGACAAG
AAGAGCAAGAAGCAACAGGATTCCACCTACCCTATTAAGATTGAAGTGGCAAGTGGGATG
ATACTGGTCATGGCTTTCTTTCTCATCACCTACACCTTTCATTCAACCTGGGTGACCAGT
GAGGCCTACTCTTCTCCGTCCATTGTACTATCTGCCCGTGGTGGGGATGGCAGTAGGATC
ATATTTGATGACTTCCGAGAAGCATATTATTGGCTTCGTCATAATACTCCAGAGGATGCG
AAGGTCATGTCCTGGTGGGATTATGGCTATCAGATTACAGCTATGGCAAACCGAACAATT
TTAGTGGACAATAACACATGGAATAATACCCATATTTCTCGAGTAGGGCAGGCAATGGCG
TCCACAGAGGAAAAAGCCTATGAGATCATGAGGGAGCTCGATGTCAGCTATGTGCTGGTC
ATTTTTGGAGGCCTCACTGGGTATTCCTCTGATGATATCAACAAGTTTCTTTGGATGGTC
CGGATTGGAGGGAGCACAGATACAGGCAAACATATCAAGGAGAATGACTATTATACTCCA
ACTGGGGAGTTCCGTGTGGACCGTGAAGGTTCTCCAGTGCTGCTCAACTGCCTCATGTAC
AAGATGTGTTACTATCGCTTTGGACAGGTTTACACAGAAGCCAAGCGTCCTCCAGGCTTT
GACCGTGTCCGAAATGCTGAGATTGGGAATAAAGACTTTGAGCTTGATGTCCTGGAGGAA
GGCTATACCACAGAACATTGGCTGGTCAGGATATACAAGGTAAAGGACCTGGATAATCGA
GGCTTGTCAAGGACATAA
Enzyme 7 GenBank Gene ID L38961 Link Image
Enzyme 7 GeneCard ID STT3A Link Image
Enzyme 7 GenAtlas ID STT3A Link Image
Enzyme 7 HGNC ID HGNC:6172 Link Image
Enzyme 7 Chromosome Location 11
Enzyme 7 Locus 11q23.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Hong G, Deleersnijder W, Kozak CA, Van Marck E, Tylzanowski P, Merregaert J: Molecular cloning of a highly conserved mouse and human integral membrane protein (Itm1) and genetic mapping to mouse chromosome 9. Genomics. 1996 Feb 1;31(3):295-300. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 8562
Enzyme 8 Name System N amino acid transporter 1
Enzyme 8 Synonyms
  1. SN1
  2. N-system amino acid transporter 1
  3. Solute carrier family 38 member 3
Enzyme 8 Gene Name SLC38A3
Enzyme 8 Protein Sequence >System N amino acid transporter 1 
MEAPLQTEMVELVPNGKHSEGLLPVITPMAGNQRVEDPARSCMEGKSFLQKSPSKEPHFT
DFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKS
SGVVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEE
KTSDWYMNGNYLVILVSVTIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFHVPC
PLPPNFNNTTGNFSHVEIVKEKVQLQVEPEASAFCTPSYFTLNSQTAYTIPIMAFAFVCH
PEVLPIYTELKDPSKKKMQHISNLSIAVMYIMYFLAALFGYLTFYNGVESELLHTYSKVD
PFDVLILCVRVAVLTAVTLTVPIVLFPVRRAIQQMLFPNQEFSWLRHVLIAVGLLTCINL
LVIFAPNILGIFGVIGATSAPFLIFIFPAIFYFRIMPTEKEPARSTPKILALCFAMLGFL
LMTMSLSFIIIDWASGTSRHGGNH
Enzyme 8 Number of Residues 504
Enzyme 8 Molecular Weight 55774
Enzyme 8 Theoretical pI 8.01
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Amino acid transport and metabolism
Enzyme 8 Specific Function Sodium-dependent amino acid/proton antiporter. Mediates electrogenic cotransport of glutamine and sodium ions in exchange for protons. Also recognizes histidine, asparagine and alanine. May mediate amino acid transport in either direction under physiological conditions. May play a role in nitrogen metabolism and synaptic transmission
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-111
Enzyme 8 Transmembrane Regions
  • 83-103 106-126 144-164 187-207 213-233 324-344 366-386 408-428 431-451 471-491
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID Q99624 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name S38A3_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AF244548 Link Image
Enzyme 8 GeneCard ID SLC38A3 Link Image
Enzyme 8 GenAtlas ID SLC38A3 Link Image
Enzyme 8 HGNC ID HGNC:18044 Link Image
Enzyme 8 Chromosome Location 3
Enzyme 8 Locus 3p21.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Fei YJ, Sugawara M, Nakanishi T, Huang W, Wang H, Prasad PD, Leibach FH, Ganapathy V: Primary structure, genomic organization, and functional and electrogenic characteristics of human system N 1, a Na+- and H+-coupled glutamine transporter. J Biol Chem. 2000 Aug 4;275(31):23707-17. [PubMed Link Image]
  2. Lerman MI, Minna JD: The 630-kb lung cancer homozygous deletion region on human chromosome 3p21.3: identification and evaluation of the resident candidate tumor suppressor genes. The International Lung Cancer Chromosome 3p21.3 Tumor Suppressor Gene Consortium. Cancer Res. 2000 Nov 1;60(21):6116-33. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 8843
Enzyme 9 Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
Enzyme 9 Synonyms
  1. Oligosaccharyl transferase subunit DAD1
  2. Defender against cell death 1
  3. DAD-1
Enzyme 9 Gene Name DAD1
Enzyme 9 Protein Sequence >Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 
MSASVVSVISRFLEEYLSSTPQRLKLLDAYLLYILLTGALQFGYCLLVGTFPFNSFLSGF
ISCVGSFILAVCLRIQINPQNKADFQGISPERAFADFLFASTILHLVVMNFVG
Enzyme 9 Number of Residues 113
Enzyme 9 Molecular Weight 12497
Enzyme 9 Theoretical pI 7.17
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Component of the N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurrs cotranslational and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). Loss of the DAD1 protein triggers apoptosis
Enzyme 9 Pathways
Enzyme 9 Reactions
  • dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide $chain attached by N-glycosyl linkage to protein L-asparagine
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-41
Enzyme 9 Transmembrane Regions
  • 31-51 53-73
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 914935 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P61803 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name DAD1_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >342 bp 
ATGTCGGCGTCGGTAGTGTCTGTCATTTCGCGGTTCTTAGAAGAGTACTTGAGCTCCACT
CCGCAGCGTCTGAAGTTGCTGGACGCGTACCTGCTGTATATACTGCTGACCGGGGCGCTG
CAGTTCGGTTACTGTCTCCTCGTGGGGACCTTCCCCTTCAACTCTTTTCTCTCGGGCTTC
ATCTCTTGTGTGGGGAGTTTCATCCTAGCGGTTTGCCTGAGAATACAGATCAACCCACAG
AACAAAGCGGATTTCCAAGGCATCTCCCCAGAGCGAGCCTTTGCTGATTTTCTCTTTGCC
AGCACCATCCTGCACCTTGTTGTCATGAACTTTGTTGGCTGA
Enzyme 9 GenBank Gene ID D15057 Link Image
Enzyme 9 GeneCard ID DAD1 Link Image
Enzyme 9 GenAtlas ID DAD1 Link Image
Enzyme 9 HGNC ID HGNC:2664 Link Image
Enzyme 9 Chromosome Location 14
Enzyme 9 Locus 14q11-q12
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Nakashima T, Sekiguchi T, Kuraoka A, Fukushima K, Shibata Y, Komiyama S, Nishimoto T: Molecular cloning of a human cDNA encoding a novel protein, DAD1, whose defect causes apoptotic cell death in hamster BHK21 cells. Mol Cell Biol. 1993 Oct;13(10):6367-74. [PubMed Link Image]
  2. 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 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 8930
Enzyme 10 Name L-asparaginase
Enzyme 10 Synonyms
  1. L-asparagine amidohydrolase
  2. Asparaginase-like protein 1
Enzyme 10 Gene Name ASRGL1
Enzyme 10 Protein Sequence >L-asparaginase 
MNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPE
FNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQ
GAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTDCQKNLGTVGAVALDCKGNV
AYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQ
GKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPD
DTTITDLP
Enzyme 10 Number of Residues 308
Enzyme 10 Molecular Weight 32055
Enzyme 10 Theoretical pI Not Available
Enzyme 10 GO Classification
Function
  • asparaginase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • cellular protein metabolism
  • glycoprotein catabolism
  • glycoprotein metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
—
Enzyme 10 General Function Amino acid transport and metabolism
Enzyme 10 Specific Function Acts in asparagine catabolism. May be involved in astroglial production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions
Enzyme 10 Pathways
Enzyme 10 Reactions
  • L-Asparagine + H2O --> L-Aspartate + Ammonium
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 20799290 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q7L266 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name ASGL1_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID AF411076 Link Image
Enzyme 10 GeneCard ID Not Available
Enzyme 10 GenAtlas ID ASRGL1 Link Image
Enzyme 10 HGNC ID HGNC:16448 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Bush LA, Herr JC, Wolkowicz M, Sherman NE, Shore A, Flickinger CJ: A novel asparaginase-like protein is a sperm autoantigen in rats. Mol Reprod Dev. 2002 Jun;62(2):233-47. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 12876
Enzyme 11 Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
Enzyme 11 Synonyms
  1. Oligosaccharyl transferase subunit STT3B
  2. STT3- B
  3. Source of immunodominant MHC-associated peptides homolog
Enzyme 11 Gene Name STT3B
Enzyme 11 Protein Sequence >Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B 
MAEPSAPESKHKSSLNSSPWSGLMALGNSRHGHHGPGAQCAHKAAGGAAPPKPAPAGLSG
GLSQPAGWQSLLSFTILFLAWLAGFSSRLFAVIRFESIIHEFDPWFNYRSTHHLASHGFY
EFLNWFDERAWYPLGRIVGGTVYPGLMITAGLIHWILNTLNITVHIRDVCVFLAPTFSGL
TSISTFLLTRELWNQGAGLLAACFIAIVPGYISRSVAGSFDNEGIAIFALQFTYYLWVKS
VKTGSVFWTMCCCLSYFYMVSAWGGYVFIINLIPLHVFVLLLMQRYSKRVYIAYSTFYIV
GLILSMQIPFVGFQPIRTSEHMAAAGVFALLQAYAFLQYLRDRLTKQEFQTLFFLGVSLA
AGAVFLSVIYLTYTGYIAPWSGRFYSLWDTGYAKIHIPIIASVSEHQPTTWVSFFFDLHI
LVCTFPAGLWFCIKNINDERVFVALYAISAVYFAGVMVRLMLTLTPVVCMLSAIAFSNVF
EHYLGDDMKRENPPVEDSSDEDDKRNQGNLYDKAGKVRKHATEQEKTEEGLGPNIKSIVT
MLMLMLLMMFAVHCTWVTSNAYSSPSVVLASYNHDGTRNILDDFREAYFWLRQNTDEHAR
VMSWWDYGYQIAGMANRTTLVDNNTWNNSHIALVGKAMSSNETAAYKIMRTLDVDYVLVI
FGGVIGYSGDDINKFLWMVRIAEGEHPKDIRESDYFTPQGEFRVDKAGSPTLLNCLMYKM
SYYRFGEMQLDFRTPPGFDRTRNAEIGNKDIKFKHLEEAFTSEHWLVRIYKVKAPDNRET
LDHKPRVTNIFPKQKYLSKKTTKRKRGYIKNKLVFKKGKKISKKTV
Enzyme 11 Number of Residues 826
Enzyme 11 Molecular Weight 93675
Enzyme 11 Theoretical pI Not Available
Enzyme 11 GO Classification
Function
  • catalytic activity
  • oligosaccharyl transferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Component of the N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurrs cotranslational and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). SST3B seems to be involved in complex substrate specificity
Enzyme 11 Pathways
Enzyme 11 Reactions
  • dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine [RN:R04216] ALL_REAC R04216 > R05976(G)
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • 65-85 137-157 169-189 192-212 243-259 263-283 292-312 320-340 351-371 411-431 441-461 464-484 538-558
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 19879589 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q8TCJ2 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name STT3B_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AY074880 Link Image
Enzyme 11 GeneCard ID Not Available
Enzyme 11 GenAtlas ID STT3B Link Image
Enzyme 11 HGNC ID HGNC:30611 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. McBride K, Baron C, Picard S, Martin S, Boismenu D, Bell A, Bergeron J, Perreault C: The model B6(dom1) minor histocompatibility antigen is encoded by a mouse homolog of the yeast STT3 gene. Immunogenetics. 2002 Nov;54(8):562-9. Epub 2002 Oct 2. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 12921
Enzyme 12 Name Full-length cDNA clone CS0DM001YM08 of Fetal liver of Homo sapiens
Enzyme 12 Synonyms
  1. human
  2. HCG23215, isoform CRA_b
Enzyme 12 Gene Name Not Available
Enzyme 12 Protein Sequence >Full-length cDNA clone CS0DM001YM08 of Fetal liver of Homo sapiens 
MAGPSPPLRAGVGRRLLGVAHPDLRPCLCGELQVEGGPGPVPGMLRTCYVRSPWRRGPSS
ARGEQSGSGHLEQEEVQSGSLLFRLLLFLSRSPASRNQRILYTVLECQPLFDSSDMTIAE
WVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSD
GRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADI
TINRELVRKVDGKAGLVVHSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGN
GPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTDYAAGMAMAGAGVISGFDMTSEAALA
KLSYVLGQPGLSLDVRKELLTKDLRGEMTPPSVEERRPSLQGNTLGGGVSWLLSLSGSQE
ADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAA
Enzyme 12 Number of Residues 469
Enzyme 12 Molecular Weight 50186
Enzyme 12 Theoretical pI 6.83
Enzyme 12 GO Classification
Function
  • asparaginase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 12 General Function Amino acid transport and metabolism
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 28193178 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q86U10 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name Q86U10_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID BX247999 Link Image
Enzyme 12 GeneCard ID Q86U10 Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs Not Available
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 15083
Enzyme 13 Name Probable asparaginyl-tRNA synthetase, mitochondrial
Enzyme 13 Synonyms
  1. Asparagine--tRNA ligase
  2. AsnRS
Enzyme 13 Gene Name NARS2
Enzyme 13 Protein Sequence >Probable asparaginyl-tRNA synthetase, mitochondrial 
MLGVRCLLRSVRFCSSAPFPKHKPSAKLSVRDALGAQNASGERIKIQGWIRSVRSQKEVL
FLHVNDGSSLESLQVVADSGLDSRELTFGSSVEVQGQLIKSPSKRQNVELKAEKIKVIGN
CDAKDFPIKYKERHPLEYLRQYPHFRCRTNVLGSILRIRSEATAAIHSFFKDSGFVHIHT
PIITSNDSEGAGELFQLEPSGKLKVPEENFFNVPAFLTVSGQLHLEVMSGAFTQVFTFGP
TFRAENSQSRRHLAEFYMIEAEISFVDSLQDLMQVIEELFKATTMMVLSKCPEDVELCHK
FIAPGQKDRLEHMLKNNFLIISYTEAVEILKQASQNFTFTPEWGADLRTEHEKYLVKHCG
NIPVFVINYPLTLKPFYMRDNEDGPQHTVAAVDLLVPGVGELFGGGLREERYHFLEERLA
RSGLTEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFPHSCLL
Enzyme 13 Number of Residues 477
Enzyme 13 Molecular Weight 54078
Enzyme 13 Theoretical pI 7.26
Enzyme 13 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • asparagine-tRNA ligase activity
  • aspartate-tRNA ligase activity
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleic acid binding
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
Process
  • RNA metabolism
  • asparaginyl-tRNA aminoacylation
  • aspartyl-tRNA aminoacylation
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 13 General Function Translation, ribosomal structure and biogenesis
Enzyme 13 Specific Function ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn)
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 39644781 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q96I59 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name SYNM_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1434 bp 
ATGCTGGGGGTCCGCTGCCTGCTGCGGTCCGTGCGCTTCTGTTCCTCCGCCCCCTTCCCC
AAGCACAAACCTTCAGCCAAACTGAGCGTGCGGGACGCTCTCGGGGCTCAGAACGCGAGT
GGGGAGCGCATTAAGATCCAGGGATGGATTCGTTCTGTCCGATCCCAGAAGGAAGTCTTG
TTCCTGCATGTAAATGATGGGTCATCTTTGGAAAGCCTTCAGGTTGTTGCAGATTCAGGC
CTTGACAGTAGAGAATTAACTTTTGGGAGTTCTGTGGAAGTACAAGGGCAGCTGATAAAA
AGTCCATCCAAAAGGCAAAATGTGGAACTGAAGGCAGAAAAAATTAAAGTTATTGGAAAT
TGTGATGCCAAGGATTTCCCCATCAAATATAAAGAGAGGCATCCTCTGGAGTACCTGCGA
CAATATCCTCACTTTAGGTGTAGGACTAACGTTCTGGGTTCTATATTGAGGATTCGCAGT
GAAGCGACAGCTGCTATTCATTCTTTCTTTAAGGACAGTGGCTTTGTACATATTCATACT
CCAATAATCACATCCAATGACTCTGAGGGAGCTGGAGAACTTTTTCAACTTGAACCTTCA
GGCAAACTTAAGGTACCTGAGGAGAATTTCTTCAATGTTCCTGCTTTCTTAACTGTCTCA
GGACAACTTCATCTAGAAGTGATGTCAGGAGCTTTTACTCAAGTGTTTACCTTTGGTCCG
ACCTTCCGAGCTGAAAATTCTCAGAGCCGGAGGCACCTGGCAGAGTTTTATATGATAGAA
GCAGAGATTTCTTTTGTTGACAGCCTTCAAGATCTTATGCAGGTTATAGAGGAACTGTTC
AAGGCTACAACAATGATGGTTCTCTCAAAATGTCCTGAAGATGTTGAACTCTGTCACAAA
TTCATAGCACCTGGCCAAAAGGACAGATTAGAACATATGCTAAAAAACAACTTTTTAATC
ATTTCTTATACTGAAGCAGTGGAGATCTTAAAGCAAGCATCCCAGAACTTCACCTTTACC
CCAGAGTGGGGTGCTGACCTACGGACTGAACATGAAAAGTACCTGGTGAAGCACTGTGGC
AACATACCTGTCTTCGTTATTAATTATCCATTAACACTCAAGCCTTTCTACATGAGGGAT
AATGAAGATGGCCCTCAGCACACGGTTGCTGCTGTTGATCTTCTGGTTCCTGGAGTTGGG
GAACTCTTTGGAGGAGGCCTCAGAGAAGAACGATACCATTTCTTAGAGGAGCGCTTAGCC
AGATCGGGACTTACAGAAGTCTACCAATGGTATCTGGACCTTCGTCGATTTGGATCTGTG
CCACATGGAGGTTTTGGGATGGGATTTGAACGCTACCTGCAGTGCATCTTGGGTGTTGAC
AATATCAAAGATGTTATCCCTTTCCCAAGGTTTCCTCATTCATGCCTTTTATAG
Enzyme 13 GenBank Gene ID BC007800 Link Image
Enzyme 13 GeneCard ID Q96I59 Link Image
Enzyme 13 GenAtlas ID NARS2 Link Image
Enzyme 13 HGNC ID HGNC:26274 Link Image
Enzyme 13 Chromosome Location 11
Enzyme 13 Locus 11q14.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 16462
Enzyme 14 Name cDNA FLJ34575 fis, clone KIDNE2008362, highly similar to Homo sapiens asparaginase like 1 (ASRGL1), mRNA
Enzyme 14 Synonyms
  1. SubName: Asparaginase like 1, isoform CRA_a
  2. SubName: cDNA, FLJ93550, highly similar to Homo sapiens asparaginase like 1 (ASRGL1), mRNA
Enzyme 14 Gene Name ASRGL1
Enzyme 14 Protein Sequence >cDNA FLJ34575 fis, clone KIDNE2008362, highly similar to Homo sapiens asparaginase like 1 (ASRGL1), mRNA 
MNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPE
FNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQ
GAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTDCQKNLGTVGAVALDCKGNV
AYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQ
GKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPD
DTTITDLP
Enzyme 14 Number of Residues 308
Enzyme 14 Molecular Weight 32055
Enzyme 14 Theoretical pI 6.17
Enzyme 14 GO Classification
Function
  • asparaginase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • cellular protein metabolism
  • glycoprotein catabolism
  • glycoprotein metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
Component
—
Enzyme 14 General Function Amino acid transport and metabolism
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID B2R7Q0 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name B2R7Q0_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID AK313069 Link Image
Enzyme 14 GeneCard ID B2R7Q0 Link Image
Enzyme 14 GenAtlas ID Not Available
Enzyme 14 HGNC ID Not Available
Enzyme 14 Chromosome Location 11
Enzyme 14 Locus 11q12.3
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References Not Available
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 17098
Enzyme 15 Name Solute carrier family 38, member 3, isoform CRA_b
Enzyme 15 Synonyms
  1. SubName: cDNA, FLJ94006, Homo sapiens solute carrier family 38, member 3 (SLC38A3), mRNA
Enzyme 15 Gene Name SLC38A3
Enzyme 15 Protein Sequence >Solute carrier family 38, member 3, isoform CRA_b 
MEAPLQTEMVELVPNGKHSEGLLPVITPMAGNQRVEDPARSCMEGKSFLQKSPSKEPHFT
DFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKS
SGVVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEE
KTSDWYMNGNYLVILVSVTIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFHVPC
PLPPNFNNTTGNFSHVEIVKEKVQLQVEPEASAFCTPSYFTLNSQTAYTIPIMAFAFVCH
PEVLPIYTELKDPSKKKMQHISNLSIAVMYIMYFLAALFGYLTFYNGVESELLHTYSKVD
PFDVLILCVRVAVLTAVTLTVPIVLFPVRRAIQQMLFPNQEFSWLRHVLIAVGLLTCINL
LVIFAPNILGIFGVIGATSAPFLIFIFPAIFYFRIMPTEKEPARSTPKILALCFAMLGFL
LMTMSLSFIIIDWASGTSRHGGNH
Enzyme 15 Number of Residues 504
Enzyme 15 Molecular Weight 55774
Enzyme 15 Theoretical pI 8.01
Enzyme 15 GO Classification Not Available
Enzyme 15 General Function Amino acid transport and metabolism
Enzyme 15 Specific Function Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID B2R8Q0 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name B2R8Q0_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID AK313461 Link Image
Enzyme 15 GeneCard ID B2R8Q0 Link Image
Enzyme 15 GenAtlas ID Not Available
Enzyme 15 HGNC ID Not Available
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available