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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 Link Image
SDF File Show Link Image
PDB File Show Link Image
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 subunit 1
  4. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
  5. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
  6. Neutral amino acid transporter B(0)
  7. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
  8. Sodium-coupled neutral amino acid transporter 3
  9. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
  10. L-asparaginase
  11. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
  12. 60 kDa lysophospholipase
  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. Cell cycle control protein TS11
  2. Glutamine-dependent asparagine synthetase
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 64369.4
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
  • asparagine biosynthetic process
  • asparagine metabolic process
  • aspartate family amino acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
Component
Enzyme 1 General Function Involved in asparagine synthase (glutamine-hydrolyzing) activity
Enzyme 1 Specific Function ATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (1) ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate [RN:R00578]
  • (2) (1a) L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
  • (3) (1b) ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine [RN:R00483]
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. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  4. 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]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 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 62942.4
Enzyme 2 Theoretical pI 6.17
Enzyme 2 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • aminoacyl-tRNA ligase activity
  • asparagine-tRNA ligase activity
  • aspartate-tRNA ligase activity
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming aminoacyl-tRNA and related compounds
  • ligase activity, forming carbon-oxygen bonds
  • nucleic acid binding
  • nucleoside binding
  • nucleotide binding
  • purine nucleoside binding
Process
  • RNA metabolic process
  • asparaginyl-tRNA aminoacylation
  • aspartyl-tRNA aminoacylation
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • cellular macromolecule metabolic process
  • macromolecule biosynthetic process
  • macromolecule metabolic process
  • metabolic process
  • ncRNA metabolic process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolic process
  • translation
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 2 General Function Involved in nucleotide binding
Enzyme 2 Specific Function ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn)
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + L-asparagine + tRNAAsn = AMP + diphosphate + L-asparaginyl-tRNAAsn [RN:R03648]
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 1
Enzyme 2 Locus 18q21.31
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]
  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. Xu G, Shin SB, Jaffrey SR: Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini. Proc Natl Acad Sci U S A. 2009 Nov 17;106(46):19310-5. Epub 2009 Nov 5. [PubMed Link Image]
  5. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6885
Enzyme 3 Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
Enzyme 3 Synonyms
  1. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit
  2. Ribophorin I
  3. RPN-I
  4. Ribophorin-1
Enzyme 3 Gene Name RPN1
Enzyme 3 Protein Sequence >Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
MEAPAAGLFLLLLLGTWAPAPGSASSEAPPLINEDVKRTVDLSSHLAKVTAEVVLAHLGG
GSTSRATSFLLALEPELEARLAHLGVQVKGEDEEENNLEVRETKIKGKSGRFFTVKLPVA
LDPGAKISVIVETVYTHVLHPYPTQITQSEKQFVVFEGNHYFYSPYPTKTQTMRVKLASR
NVESYTKLGNPTRSEDLLDYGPFRDVPAYSQDTFKVHYENNSPFLTITSMTRVIEVSHWG
NIAVEENVDLKHTGAVLKGPFSRYDYQRQPDSGISSIRSFKTILPAAAQDVYYRDEIGNV
STSHLLILDDSVEMEIRPRFPLFGGWKTHYIVGYNLPSYEYLYNLGDQYALKMRFVDHVF
DEQVIDSLTVKIILPEGAKNIEIDSPYEISRAPDELHYTYLDTFGRPVIVAYKKNLVEQH
IQDIVVHYTFNKVLMLQEPLLVVAAFYILFFTVIIYVRLDFSITKDPAAEARMKVACITE
QVLTLVNKRIGLYRHFDETVNRYKQSRDISTLNSGKKSLETEHKALTSEIALLQSRLKTE
GSDLCDRVSEMQKLDAQVKELVLKSAVEAERLVAGKLKKDTYIENEKLISGKRQELVTKI
DHILDAL
Enzyme 3 Number of Residues 607
Enzyme 3 Molecular Weight 68568.8
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
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum
  • integral to membrane
  • intracellular membrane-bounded organelle
  • intrinsic to membrane
  • membrane part
  • membrane-bounded organelle
  • organelle
Enzyme 3 General Function Involved in dolichyl-diphosphooligosaccharide-protein glycotransferase activity
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 oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine [RN:R04216]
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 RPN1_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]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. 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. Basrur V, Yang F, Kushimoto T, Higashimoto Y, Yasumoto K, Valencia J, Muller J, Vieira WD, Watabe H, Shabanowitz J, Hearing VJ, Hunt DF, Appella E: Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. J Proteome Res. 2003 Jan-Feb;2(1):69-79. [PubMed Link Image]
  6. Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R: Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell. 2003 Jul;12(1):101-11. [PubMed Link Image]
  7. Shibatani T, David LL, McCormack AL, Frueh K, Skach WR: Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry. 2005 Apr 26;44(16):5982-92. [PubMed Link Image]
  8. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  9. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  10. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6887
Enzyme 4 Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
Enzyme 4 Synonyms
  1. DDOST 48 kDa subunit
  2. Oligosaccharyl transferase 48 kDa subunit
Enzyme 4 Gene Name DDOST
Enzyme 4 Protein Sequence >Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
MGYFRCARAGSFGRRRKMEPSTAARAWALFWLLLPLLGAVCASGPRTLVLLDNLNVRETH
SLFFRSLKDRGFELTFKTADDPSLSLIKYGEFLYDNLIIFSPSVEDFGGNINVETISAFI
DGGGSVLVAASSDIGDPLRELGSECGIEFDEEKTAVIDHHNYDISDLGQHTLIVADTENL
LKAPTIVGKSSLNPILFRGVGMVADPDNPLVLDILTGSSTSYSFFPDKPITQYPHAVGKN
TLLIAGLQARNNARVIFSGSLDFFSDSFFNSAVQKAAPGSQRYSQTGNYELAVALSRWVF
KEEGVLRVGPVSHHRVGETAPPNAYTVTDLVEYSIVIQQLSNGKWVPFDGDDIQLEFVRI
DPFVRTFLKKKGGKYSVQFKLPDVYGVFQFKVDYNRLGYTHLYSSTQVSVRPLQHTQYER
FIPSAYPYYASAFSMMLGLFIFSIVFLHMKEKEKSD
Enzyme 4 Number of Residues 456
Enzyme 4 Molecular Weight 50800.3
Enzyme 4 Theoretical pI 6.52
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
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid N-linked glycosylation
  • protein amino acid N-linked glycosylation via asparagine
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • membrane
  • organelle membrane
Enzyme 4 General Function Involved in dolichyl-diphosphooligosaccharide-protein glycotransferase activity
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 oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine [RN:R04216]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-42
Enzyme 4 Transmembrane Regions
  • 428-447
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 20070197 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
TTCATCCCCTCGGCCTACCCCTACTACGCCAGCGCCTTCTCCATGATGCTGGGGCTCTTC
ATCTTCAGCATCGTCTTCTTGCACATGAAGGAGAAGGAGAAGTCCGACTGA
Enzyme 4 GenBank Gene ID NM_005216.4 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. 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]
  2. 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]
  3. 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]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6888
Enzyme 5 Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
Enzyme 5 Synonyms
  1. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit
  2. RIBIIR
  3. Ribophorin II
  4. RPN-II
  5. Ribophorin-2
Enzyme 5 Gene Name RPN2
Enzyme 5 Protein Sequence >Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
MAPPGSSTVFLLALTIIASTWALTPTHYLTKHDVERLKASLDRPFTNLESAFYSIVGLSS
LGAQVPDAKKACTYIRSNLDPSNVDSLFYAAQASQALSGCEISISNETKDLLLAAVSEDS
SVTQIYHAVAALSGFGLPLASQEALSALTARLSKEETVLATVQALQTASHLSQQADLRSI
VEEIEDLVARLDELGGVYLQFEEGLETTALFVAATYKLMDHVGTEPSIKEDQVIQLMNAI
FSKKNFESLSEAFSVASAAAVLSHNRYHVPVVVVPEGSASDTHEQAILRLQVTNVLSQPL
TQATVKLEHAKSVASRATVLQKTSFTPVGDVFELNFMNVKFSSGYYDFLVEVEGDNRYIA
NTVELRVKISTEVGITNVDLSTVDKDQSIAPKTTRVTYPAKAKGTFIADSHQNFALFFQL
VDVNTGAELTPHQTFVRLHNQKTGQEVVFVAEPDNKNVYKFELDTSERKIEFDSASGTYT
LYLIIGDATLKNPILWNVADVVIKFPEEEAPSTVLSQNLFTPKQEIQHLFREPEKRPPTV
VSNTFTALILSPLLLLFALWIRIGANVSNFTFAPSTIIFHLGHAAMLGLMYVYWTQLNMF
QTLKYLAILGSVTFLAGNRMLAQQAVKRTAH
Enzyme 5 Number of Residues 631
Enzyme 5 Molecular Weight 69283.3
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
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid N-linked glycosylation
  • protein amino acid N-linked glycosylation via asparagine
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • macromolecular complex
  • membrane
  • oligosaccharyltransferase complex
  • organelle membrane
  • protein complex
Enzyme 5 General Function Involved in dolichyl-diphosphooligosaccharide-protein glycotransferase activity
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 oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine [RN:R04216]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-22
Enzyme 5 Transmembrane Regions
  • 541-561 572-592 597-617
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 5834424 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P04844 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name RPN2_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
TCAGTTACCCAGATCTACCATGCAGTTGCAGCTCTAAGTGGCTTTGGCCTTCCCTTGGCA
TCCCAAGAAGCACTCAGTGCCCTTACTGCTCGTCTCAGCAAGGAGGAGACTGTGCTGGCA
ACAGTCCAGGCTCTGCAGACAGCATCCCACCTGTCCCAGCAGGCTGACCTGAGGAGCATC
GTGGAGGAGATTGAGGACCTTGTTGCTCGCCTGGATGAACTCGGGGGCGTGTATCTCCAG
TTTGAAGAAGGACTGGAAACAACAGCGTTATTTGTGGCTGCCACCTACAAGCTCATGGAT
CATGTGGGGACTGAGCCATCCATTAAGGAGGATCAGGTCATCCAGCTGATGAACGCGATC
TTCAGCAAGAAGAACTTTGAGTCCCTCTCCGAAGCCTTCAGCGTGGCCTCTGCAGCTGCT
GTGCTCTCGCATAATCGCTACCACGTGCCAGTTGTGGTTGTGCCTGAGGGCTCTGCTTCC
GACACTCATGAACAGGCTATCTTGCGGTTGCAAGTCACCAATGTTCTGTCTCAGCCTCTG
ACTCAGGCCACTGTTAAACTAGAACATGCTAAATCTGTTGCTTCCAGAGCCACTGTCCTC
CAGAAGACATCCTTCACCCCTGTAGGGGATGTTTTTGAACTAAATTTCATGAACGTCAAA
TTTTCCAGTGGTTATTATGACTTCCTTGTCGAAGTTGAAGGTGACAACCGGTATATTGCA
AATACCGTAGAGCTCAGAGTCAAGATCTCCACTGAAGTTGGCATCACAAATGTTGATCTT
TCCACCGTGGATAAGGATCAGAGCATTGCACCCAAAACTACCCGGGTGACATACCCAGCC
AAAGCCAAGGGCACATTCATCGCAGACAGCCACCAGAACTTCGCCTTGTTCTTCCAGCTG
GTAGATGTGAACACTGGTGCTGAACTCACTCCTCACCAGACATTTGTCCGACTCCATAAC
CAGAAGACTGGCCAGGAAGTGGTGTTTGTTGCCGAGCCAGACAACAAGAACGTGTACAAG
TTTGAACTGGATACCTCTGAAAGAAAGATTGAATTTGACTCTGCCTCTGGCACCTACACT
CTCTACTTAATCATTGGAGATGCCACTTTGAAGAACCCAATCCTCTGGAATGTGGCTGAT
GTGGTCATCAAGTTCCCTGAGGAAGAAGCTCCCTCGACTGTCTTGTCCCAGAACCTTTTC
ACTCCAAAACAGGAAATTCAGCACCTGTTCCGCGAGCCTGAGAAGAGGCCCCCCACCGTG
GTGTCCAATACATTCACTGCCCTGATCCTCTCGCCGTTGCTTCTGCTCTTCGCTCTGTGG
ATCCGGATTGGTGCCAATGTCTCCAACTTCACTTTTGCTCCTAGCACGATTATATTTCAC
CTGGGACATGCTGCTATGCTGGGACTCATGTATGTCTACTGGACTCAGCTCAACATGTTC
CAGACCTTGAAGTACCTGGCCATCTTGGGCAGTGTGACGTTTCTGGCTGGCAATCGGATG
CTGGCCCAGCAGGCAGTCAAGAGAACAGCACATTAG
Enzyme 5 GenBank Gene ID AJ237734 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 2
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. 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. 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]
  5. Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R: Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell. 2003 Jul;12(1):101-11. [PubMed Link Image]
  6. Shibatani T, David LL, McCormack AL, Frueh K, Skach WR: Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry. 2005 Apr 26;44(16):5982-92. [PubMed Link Image]
  7. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  8. Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed Link Image]
  9. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [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. Baboon M7 virus receptor
  3. RD114/simian type D retrovirus receptor
  4. Sodium-dependent neutral amino acid transporter type 2
  5. Solute carrier family 1 member 5
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 56597.6
Enzyme 6 Theoretical pI 5.14
Enzyme 6 GO Classification
Function
  • carboxylic acid transmembrane transporter activity
  • dicarboxylic acid transmembrane transporter activity
  • organic acid transmembrane transporter activity
  • sodium:dicarboxylate symporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • carboxylic acid transport
  • dicarboxylic acid transport
  • establishment of localization
  • organic acid transport
  • transport
Component
  • cell part
  • membrane
Enzyme 6 General Function Involved in sodium:dicarboxylate symporter activity
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 4191556 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
ATGGTGGCCGATCCTCCTCGAGACTCCAAGGGGCTCGCAGCGGCGGAGCCCACCGCCAAC
GGGGGCCTGGCGCTGGCCTCCATCGAGGACCAAGGCGCGGCAGCAGGCGGCTACTGCGGT
TCCCGGGACCAGGTGCGCCGCTGCCTTCGAGCCAACCTGCTTGTGCTGCTGACAGTGGTG
GCCGTGGTGGCCGGCGTGGCGCTGGGACTGGGGGTGTCGGGGGCCGGGGGTGCGCTGGCG
TTGGGCCCGGAGCGCTTGAGCGCCTTCGTCTTCCCGGGCGAGCTGCTGCTGCGTCTGCTG
CGGATGATCATCTTGCCGCTGGTGGTGTGCAGCTTGATAGGCGGCGCCGCCAGCCTGGAC
CCCGGCGCGCTCGGCCGTCTGGGCGCCTGGGCGCTGCTCTTTTTCCTGGTCACCACGCTG
CTGGCGTCGGCGCTCGGAGTGGGCTTGGCGCTGGCTCTGCAGCCGGGCGCCGCCTCCGCC
GCCATCAACGCCTCCGTGGGAGCCGCGGGCAGTGCCGAAAATGCCCCCAGCAAGGAGGTG
CTCGATTCGTTCCTGGATCTTGCGAGAAATATCTTCCCTTCCAACCTGGTGTCAGCAGCC
TTTCGCTCATACTCTACCACCTATGAAGAGAGGAATATCACCGGAACCAGGGTGAAGGTG
CCCGTGGGGCAGGAGGTGGAGGGGATGAACATCCTGGGCTTGGTAGTGTTTGCCATCGTC
TTTGGTGTGGCGCTGCGGAAGCTGGGGCCTGAAGGGGAGCTGCTTATCCGCTTCTTCAAC
TCCTTCAATGAGGCCACCATGGTTCTGGTCTCCTGGATCATGTGGTACGCCCCTGTGGGC
ATCATGTTCCTGGTGGCTGGCAAGATCGTGGAGATGGAGGATGTGGGTTTACTCTTTGCC
CGCCTTGGCAAGTACATTCTGTGCTGCCTGCTGGGTCACGCCATCCATGGGCTCCTGGTA
CTGCCCCTCATCTACTTCCTCTTCACCCGCAAAAACCCCTACCGCTTCCTGTGGGGCATC
GTGACGCCGCTGGCCACTGCCTTTGGGACCTCTTCCAGTTCCGCCACGCTGCCGCTGATG
ATGAAGTGCGTGGAGGAGAATAATGGCGTGGCCAAGCACATCAGCCGTTTCATCCTGCCC
ATCGGCGCCACCGTCAACATGGACGGTGCCGCGCTCTTCCAGTGCGTGGCCGCAGTGTTC
ATTGCACAGCTCAGCCAGCAGTCCTTGGACTTCGTAAAGATCATCACCATCCTGGTCACG
GCCACAGCGTCCAGCGTGGGGGCAGCGGGCATCCCTGCTGGAGGTGTCCTCACTCTGGCC
ATCATCCTCGAAGCAGTCAACCTCCCGGTCGACCATGTCTCCTTGATCCTGGCTGTGGGC
TGGCTAGCCGACCGGTCCTGTACCGTCCTCAATGTAGAAGGTGACGCTCTGGGGGCAGGA
CTCCTCCAAAATTACGTGGACCGTACGGAGTCGAGAAGCACAGAGCCTGAGTTGATACAA
GTGAAGAGTGAGCTGCCCCTGGGTCCGCTGCCAGTCCCCACTGAGGAAGGAAACCCCCTC
CTCAAACACTATCGGGGGCCCGCAGGGGATGCCACGGTCGCCTCTGAGAAGGAATCAGTC
ATGTAA
Enzyme 6 GenBank Gene ID AF102826 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 1
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. 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]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. 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]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  11. Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed Link Image]
  12. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [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. Transmembrane protein TMC
Enzyme 7 Gene Name STT3A
Enzyme 7 Protein Sequence >Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
MTKFGFLRLSYEKQDTLLKLLILSMAAVLSFSTRLFAVLRFESVIHEFDPYFNYRTTRFL
AEEGFYKFHNWFDDRAWYPLGRIIGGTIYPGLMITSAAIYHVLHFFHITIDIRNVCVFLA
PLFSSFTTIVTYHLTKELKDAGAGLLAAAMIAVVPGYISRSVAGSYDNEGIAIFCMLLTY
YMWIKAVKTGSICWAAKCALAYFYMVSSWGGYVFLINLIPLHVLVLMLTGRFSHRIYVAY
CTVYCLGTILSMQISFVGFQPVLSSEHMAAFGVFGLCQIHAFVDYLRSKLNPQQFEVLFR
SVISLVGFVLLTVGALLMLTGKISPWTGRFYSLLDPSYAKNNIPIIASVSEHQPTTWSSY
YFDLQLLVFMFPVGLYYCFSNLSDARIFIIMYGVTSMYFSAVMVRLMLVLAPVMCILSGI
GVSQVLSTYMKNLDISRPDKKSKKQQDSTYPIKNEVASGMILVMAFFLITYTFHSTWVTS
EAYSSPSIVLSARGGDGSRIIFDDFREAYYWLRHNTPEDAKVMSWWDYGYQITAMANRTI
LVDNNTWNNTHISRVGQAMASTEEKAYEIMRELDVSYVLVIFGGLTGYSSDDINKFLWMV
RIGGSTDTGKHIKENDYYTPTGEFRVDREGSPVLLNCLMYKMCYYRFGQVYTEAKRPPGF
DRVRNAEIGNKDFELDVLEEAYTTEHWLVRIYKVKDLDNRGLSRT
Enzyme 7 Number of Residues 705
Enzyme 7 Molecular Weight 80528.8
Enzyme 7 Theoretical pI 8.17
Enzyme 7 GO Classification
Function
  • catalytic activity
  • oligosaccharyl transferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 7 General Function Involved in oligosaccharyl transferase activity
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 occurs cotranslationally 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 oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine [RN:R04216]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 18-38 115-135 170-190 209-229 236-259 301-321 360-380 384-404 406-426 454-474
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 158261103 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
CCTCTCTTCTCCTCCTTCACCACCATCGTCACGTACCACCTTACCAAAGAGCTCAAGGAT
GCAGGGGCTGGGCTTCTTGCTGCTGCCATGATTGCTGTAGTTCCTGGATATATCTCCCGA
TCTGTGGCTGGCTCCTATGATAATGAAGGGATTGCCATCTTTTGCATGCTACTCACCTAC
TACATGTGGATCAAGGCAGTAAAGACTGGTTCCATCTGTTGGGCAGCTAAGTGTGCCCTT
GCTTATTTCTACATGGTCTCGTCATGGGGAGGTTATGTGTTCCTGATCAACTTAATTCCT
CTCCACGTCCTCGTGCTGATGCTCACAGGCCGTTTCTCTCACCGGATCTATGTGGCCTAC
TGTACTGTTTACTGCCTGGGCACTATACTTTCTATGCAGATCTCCTTTGTGGGTTTCCAG
CCTGTCCTTTCATCAGAGCACATGGCAGCCTTTGGGGTCTTTGGTCTCTGCCAGATCCAT
GCCTTTGTGGATTACCTGCGCAGCAAGTTGAATCCACAACAATTTGAAGTTCTTTTCCGG
AGCGTCATCTCTCTGGTAGGCTTTGTCCTTCTCACCGTGGGAGCTCTCCTCATGCTGACA
GGAAAAATATCTCCCTGGACGGGGCGTTTCTACTCACTGCTGGATCCCTCTTATGCTAAG
AACAACATCCCCATCATTGCTTCTGTGTCTGAGCATCAGCCCACAACCTGGTCCTCATAC
TATTTTGACCTGCAGCTCCTCGTCTTCATGTTTCCAGTTGGCCTCTATTACTGCTTTAGC
AACCTGTCTGATGCCCGGATTTTTATCATCATGTATGGTGTGACCAGCATGTACTTTTCA
GCTGTAATGGTGCGTCTAATGCTAGTGTTGGCACCTGTTATGTGCATTCTCTCTGGCATT
GGAGTCTCCCAGGTGCTGTCCACATACATGAAGAATCTGGACATAAGTCGTCCAGACAAG
AAGAGCAAGAAGCAACAGGATTCCACCTACCCTATTAAGAATGAAGTGGCAAGTGGGATG
ATACTGGTCATGGCTTTCTTTCTCATCACCTACACCTTTCATTCAACCTGGGTGACCAGT
GAGGCCTACTCTTCTCCGTCCATTGTACTATCTGCCCGTGGTGGGGATGGCAGTAGGATC
ATATTTGATGACTTCCGAGAAGCATATTATTGGCTTCGTCATAATACTCCAGAGGATGCG
AAGGTCATGTCCTGGTGGGATTATGGCTATCAGATTACAGCTATGGCAAACCGAACAATT
TTAGTGGACAATAACACATGGAATAATACCCATATTTCTCGAGTAGGGCAGGCAATGGCG
TCCACAGAGGAAAAAGCCTATGAGATCATGAGGGAGCTCGATGTCAGCTATGTGCTGGTC
ATTTTTGGAGGCCTCACTGGGTATTCCTCTGATGATATCAACAAGTTTCTTTGGATGGTC
CGGATTGGAGGGAGCACAGATACAGGCAAACATATCAAGGAGAATGACTATTATACTCCA
ACTGGGGAGTTCCGTGTGGACCGTGAAGGTTCTCCAGTGCTGCTCAACTGCCTCATGTAC
AAGATGTGTTACTATCGCTTTGGACAGGTTTACACAGAAGCCAAGCGTCCTCCAGGCTTT
GACCGTGTCCGAAATGCTGAGATTGGGAATAAAGACTTTGAGCTTGATGTCCTGGAGGAA
GCATATACCACAGAACATTGGCTGGTCAGGATATACAAGGTAAAGGACCTGGATAATCGA
GGCTTGTCAAGGACATAA
Enzyme 7 GenBank Gene ID AK290040 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 1
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]
  2. Lissy NA, Bellacosa A, Sonoda G, Miller PD, Jhanwar SC, Testa JR: Isolation, characterization, and mapping to human chromosome 11q24-25 of a cDNA encoding a highly conserved putative transmembrane protein, TMC. Biochim Biophys Acta. 1996 May 2;1306(2-3):137-41. [PubMed Link Image]
  3. 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]
  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. Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R: Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell. 2003 Jul;12(1):101-11. [PubMed Link Image]
  6. Shibatani T, David LL, McCormack AL, Frueh K, Skach WR: Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry. 2005 Apr 26;44(16):5982-92. [PubMed Link Image]
  7. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 8562
Enzyme 8 Name Sodium-coupled neutral amino acid transporter 3
Enzyme 8 Synonyms
  1. N-system amino acid transporter 1
  2. Na(+)-coupled neutral amino acid transporter 3
  3. Solute carrier family 38 member 3
  4. System N amino acid transporter 1
Enzyme 8 Gene Name SLC38A3
Enzyme 8 Protein Sequence >Sodium-coupled neutral amino acid transporter 3
MEAPLQTEMVELVPNGKHSEGLLPVITPMAGNQRVEDPARSCMEGKSFLQKSPSKEPHFT
DFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKS
SGVVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEE
KTSDWYMNGNYLVILVSVTIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFHVPC
PLPPNFNNTTGNFSHVEIVKEKVQLQVEPEASAFCTPSYFTLNSQTAYTIPIMAFAFVCH
PEVLPIYTELKDPSKKKMQHISNLSIAVMYIMYFLAALFGYLTFYNGVESELLHTYSKVD
PFDVLILCVRVAVLTAVTLTVPIVLFPVRRAIQQMLFPNQEFSWLRHVLIAVGLLTCINL
LVIFAPNILGIFGVIGATSAPFLIFIFPAIFYFRIMPTEKEPARSTPKILALCFAMLGFL
LMTMSLSFIIIDWASGTSRHGGNH
Enzyme 8 Number of Residues 504
Enzyme 8 Molecular Weight 55772.4
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
  • None
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 5870893 Link Image
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 >1515 bp
ATGGAGGCGCCTTTGCAGACAGAGATGGTGGAGCTGGTGCCCAATGGCAAACACTCAGAG
GGGCTGCTCCCGGTCATCACCCCCATGGCAGGCAACCAGAGGGTCGAGGACCCTGCACGG
AGCTGTATGGAGGGCAAGAGCTTCCTACAGAAAAGTCCCAGCAAGGAGCCACACTTCACT
GACTTCGAGGGGAAGACATCATTCGGGATGTCAGTGTTCAACCTCAGCAATGCCATCATG
GGCAGCGGCATCCTGGGACTCGCCTATGCCATGGCCAATACGGGCATTATCCTTTTCCTG
TTCCTGTTGACAGCTGTCGCCTTGCTCTCCAGCTACTCCATCCACCTGCTACTCAAGTCC
TCAGGGGTCGTGGGCATCCGTGCCTATGAGCAGCTGGGCTACCGTGCCTTTGGGACCCCA
GGAAAGCTGGCAGCAGCCCTGGCCATCACGCTCCAGAACATCGGAGCCATGTCCAGCTAC
CTGTACATCATCAAGTCTGAGCTGCCACTTGTCATACAGACCTTCCTGAACCTGGAGGAG
AAAACCTCGGACTGGTACATGAACGGGAACTACCTGGTAATCCTTGTCTCTGTCACCATC
ATTCTGCCCCTGGCACTGATGCGGCAGCTTGGCTACCTGGGCTACTCCAGCGGCTTCTCT
CTTAGCTGCATGGTGTTCTTCCTAATTGCAGTCATCTACAAAAAGTTCCACGTGCCCTGC
CCACTGCCCCCCAACTTCAACAACACCACAGGCAACTTCAGCCACGTGGAGATCGTGAAG
GAGAAGGTGCAGCTGCAGGTCGAGCCTGAGGCTTCAGCCTTCTGCACTCCCAGCTACTTC
ACGCTCAACTCACAGACAGCATACACCATCCCCATCATGGCCTTCGCCTTCGTCTGCCAC
CCCGAGGTGCTGCCCATCTATACTGAGCTCAAGGACCCCTCCAAGAAGAAGATGCAGCAC
ATCTCCAACCTGTCCATCGCTGTCATGTACATCATGTACTTCCTGGCTGCCCTCTTCGGC
TACCTCACCTTCTACAACGGGGTGGAGTCGGAGCTGCTGCACACCTACAGCAAGGTGGAC
CCGTTTGACGTCCTGATCCTGTGTGTGCGCGTGGCCGTGCTGACAGCAGTCACGCTCACA
GTGCCCATCGTTCTGTTCCCGGTGCGCCGCGCCATCCAGCAGATGCTGTTTCCAAACCAG
GAGTTCAGCTGGCTGCGGCATGTGCTTATTGCCGTTGGCCTGCTCACTTGTATCAACCTG
CTGGTCATCTTTGCCCCCAACATCCTGGGCATCTTTGGGGTCATCGGTGCCACATCTGCC
CCATTCCTCATCTTCATCTTCCCTGCCATCTTCTACTTCCGAATCATGCCCACGGAGAAG
GAGCCTGCAAGATCCACCCCCAAAATCCTGGCCCTGTGTTTTGCTATGCTTGGCTTCTTG
CTGATGACCATGAGCTTGAGCTTCATCATCATTGACTGGGCCTCAGGGACCAGCCGGCAT
GGAGGAAACCACTAG
Enzyme 8 GenBank Gene ID NM_006841.4 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. 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 12496.5
Enzyme 9 Theoretical pI 7.17
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Involved in dolichyl-diphosphooligosaccharide-protein g
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 occurs cotranslationally 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 [RN:R04216]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • 31-51 53-73
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 29501770 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 AY259117 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 1
Enzyme 9 Locus 14q11.2
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. 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. 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. Asparaginase-like protein 1
  2. L-asparagine amidohydrolase
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 32054.3
Enzyme 10 Theoretical pI 6.17
Enzyme 10 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 10 General Function Involved in hydrolase activity
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 + NH3 [RN:R00485]
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 >927 bp
ATGAATCCCATCGTAGTGGTCCACGGCGGCGGAGCCGGTCCCATCTCCAAGGATCGGAAG
GAGCGAGTGCACCAGGGCATGGTCAGAGCCGCCACCGTGGGCTACGGCATCCTCCGGGAG
GGCGGGAGCGCCGTGGATGCCGTAGAGGGAGCTGTCGTCGCCCTGGAAGACGATCCCGAG
TTCAACGCAGGTTGTGGGTCTGTCTTGAACACAAATGGTGAGGTTGAAATGGATGCTAGT
ATCATGGATGGAAAAGACCTGTCTGCAGGAGCAGTGTCCGCAGTCCAGTGTATAGCAAAT
CCCATTAAACTTGCTCGGCTTGTCATGGAAAAGACACCTCATTGCTTTCTGACTGACCAA
GGCGCAGCGCAGTTTGCAGCAGCTATGGGGGTTCCAGAGATTCCTGGAGAAAAACTGGTG
ACAGAGAGAAACAAAAAGCGCCTGGAAAAAGAGAAGCATGAAAAAGGTGCTCAGAAAACA
GATTGTCAAAAAAACTTGGGAACCGTGGGTGCTGTTGCCTTGGACTGCAAAGGGAATGTA
ACCTACGCAACCTCCACAGGCGGTATCGTTAATAAAATGGTCGGCCGCGTTGGGGACTCA
CCGTGTCTAGGAGCTGGAGGTTATGCCGACAATGACATCGGAGCCGTCTCAACCACAGGG
CATGGGGAAAGCATCCTGAAGGTGAACCTGGCTAGACTCACCCTGTTCCACATAGAACAA
GGAAAGACGGTAGAAGAGGCTGCGGACCTATCGTTGGGTTATATGAAGTCAAGGGTTAAA
GGTTTAGGTGGCCTCATCGTGGTTAGCAAAACAGGAGACTGGGTGGCAAAGTGGACCTCC
ACCTCCATGCCCTGGGCAGCCGCCAAGGACGGCAAGCTGCACTTTGGAATTGATCCTGAC
GATACTACTATCACCGACCTTCCCTAA
Enzyme 10 GenBank Gene ID AF411076 Link Image
Enzyme 10 GeneCard ID ASRGL1 Link Image
Enzyme 10 GenAtlas ID ASRGL1 Link Image
Enzyme 10 HGNC ID HGNC:16448 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 11q12.3
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]
  2. Evtimova V, Zeillinger R, Kaul S, Weidle UH: Identification of CRASH, a gene deregulated in gynecological tumors. Int J Oncol. 2004 Jan;24(1):33-41. [PubMed Link Image]
  3. 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]
  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. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 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 93673.5
Enzyme 11 Theoretical pI 9.17
Enzyme 11 GO Classification
Function
  • catalytic activity
  • oligosaccharyl transferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 11 General Function Involved in oligosaccharyl transferase activity
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 occurs cotranslationally 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]
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 30578410 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 >2481 bp
ATGGCGGAGCCCTCGGCCCCGGAGAGCAAGCACAAGTCGTCCCTCAACTCGTCCCCGTGG
AGTGGCCTCATGGCCCTGGGAAACAGCCGGCACGGCCACCACGGGCCCGGGGCCCAGTGC
GCGCACAAGGCGGCGGGCGGCGCGGCGCCGCCGAAGCCGGCCCCGGCGGGGCTGTCCGGG
GGGCTGTCGCAGCCGGCTGGGTGGCAGTCGCTTCTCTCCTTCACCATCCTCTTCCTGGCC
TGGCTTGCCGGCTTCAGCTCGCGCCTCTTCGCCGTCATCCGCTTCGAAAGCATCATCCAC
GAGTTCGACCCGTGGTTTAACTATAGATCAACACATCATCTTGCATCTCATGGGTTCTAT
GAATTTTTAAATTGGTTTGATGAAAGAGCATGGTATCCACTAGGAAGAATAGTAGGTGGT
ACTGTTTACCCAGGGTTGATGATAACCGCTGGCCTTATTCATTGGATTTTAAATACATTG
AACATAACTGTTCACATAAGAGACGTATGTGTGTTCCTTGCACCAACTTTTAGCGGCCTT
ACATCTATATCTACTTTCCTGCTTACAAGAGAACTTTGGAACCAAGGAGCAGGACTTTTA
GCTGCTTGTTTTATTGCTATTGTACCAGGCTACATATCTCGGTCAGTAGCTGGATCCTTT
GATAATGAAGGCATTGCTATTTTTGCACTTCAGTTCACATACTATTTATGGGTAAAATCT
GTAAAAACTGGGTCAGTTTTTTGGACAATGTGCTGCTGCTTATCCTATTTCTATATGGTC
TCTGCTTGGGGTGGTTATGTATTTATCATCAATCTTATTCCACTGCATGTATTTGTGTTG
TTACTGATGCAGAGATACAGCAAAAGAGTCTACATAGCATATAGCACTTTCTACATTGTG
GGTTTAATATTATCAATGCAGATACCTTTTGTGGGATTCCAGCCAATCAGAACAAGTGAA
CACATGGCAGCTGCAGGTGTCTTTGCATTGCTGCAAGCTTATGCTTTCTTGCAGTATCTG
AGAGACCGATTAACAAAACAAGAGTTCCAGACCCTTTTCTTTTTGGGTGTATCACTAGCT
GCAGGTGCTGTGTTCCTTAGTGTCATCTATTTGACTTATACAGGTTACATTGCACCATGG
AGTGGCAGGTTTTATTCATTGTGGGATACTGGGTATGCAAAAATACACATTCCAATTATT
GCATCAGTGTCTGAGCATCAACCTACGACTTGGGTGTCTTTCTTCTTTGATCTACATATT
CTTGTATGTACCTTCCCAGCAGGCCTTTGGTTCTGCATCAAAAATATCAACGATGAAAGA
GTATTTGTTGCTCTATATGCAATCAGTGCTGTCTACTTTGCTGGAGTGATGGTGCGACTG
ATGTTGACTTTGACTCCAGTCGTGTGTATGCTGTCTGCAATTGCCTTTTCAAATGTTTTT
GAGCACTATTTGGGGGATGACATGAAAAGGGAAAATCCACCTGTGGAGGACAGCAGTGAT
GAGGATGACAAAAGAAACCAAGGAAATTTGTATGATAAGGCAGGTAAAGTGAGGAAACAT
GCAACTGAACAGGAAAAAACTGAAGAGGGATTAGGCCCTAATATAAAAAGCATTGTCACC
ATGTTGATGCTGATGCTATTGATGATGTTTGCTGTCCACTGTACCTGGGTCACAAGCAAT
GCCTACTCTAGTCCAAGTGTAGTCCTGGCCTCATACAATCATGATGGCACCAGGAATATC
TTAGATGATTTTAGAGAAGCTTACTTTTGGCTAAGGCAAAATACAGATGAACATGCACGA
GTAATGTCTTGGTGGGATTATGGCTATCAGATAGCTGGAATGGCTAATAGAACTACGTTG
GTGGATAATAACACCTGGAATAACAGCCACATAGCACTGGTGGGAAAAGCTATGTCTTCT
AATGAAACAGCAGCCTATAAAATCATGAGGACTCTAGATGTAGATTATGTTTTGGTTATT
TTTGGAGGGGTTATTGGCTATTCTGGTGATGATATCAACAAATTTCTCTGGATGGTTAGG
ATAGCTGAAGGAGAACATCCCAAAGACATTCGGGAAAGTGACTATTTTACCCCACAGGGA
GAATTCCGTGTAGACAAAGCAGGATCCCCTACTTTGTTGAATTGCCTTATGTATAAAATG
TCATACTACAGATTTGGAGAAATGCAGCTGGATTTTCGTACACCCCCAGGTTTTGACCGA
ACACGTAATGCTGAGATTGGAAATAAGGACATTAAATTCAAACATTTGGAAGAAGCCTTT
ACATCAGAACACTGGCTTGTTAGGATATATAAAGTAAAAGCACCTGATAACAGGGAGACA
TTAGATCACAAACCTCGAGTCACCAACATTTTCCCAAAACAGAAGTATTTGTCAAAGAAG
ACTACCAAAAGGAAGCGTGGCTACATTAAAAATAAGCTGGTTTTTAAGAAAGGCAAGAAA
ATATCTAAGAAGACTGTTTAA
Enzyme 11 GenBank Gene ID NM_178862.1 Link Image
Enzyme 11 GeneCard ID STT3B Link Image
Enzyme 11 GenAtlas ID STT3B Link Image
Enzyme 11 HGNC ID HGNC:30611 Link Image
Enzyme 11 Chromosome Location 3
Enzyme 11 Locus 3p23
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]
  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]
  4. Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R: Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell. 2003 Jul;12(1):101-11. [PubMed Link Image]
  5. Shibatani T, David LL, McCormack AL, Frueh K, Skach WR: Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry. 2005 Apr 26;44(16):5982-92. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  9. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  10. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 12921
Enzyme 12 Name 60 kDa lysophospholipase
Enzyme 12 Synonyms
  1. L-asparaginase
  2. L-asparagine amidohydrolase
  3. Platelet-activating factor acetylhydrolase
  4. PAF acetylhydrolase
Enzyme 12 Gene Name ASPG
Enzyme 12 Protein Sequence >60 kDa lysophospholipase
MARAVGPERRLLAVYTGGTIGMRSELGVLVPGTGLAAILRTLPMFHDEEHARARGLSEDT
LVLPPASRNQRILYTVLECQPLFDSSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMA
FAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQYVIPEVCLFFQNQL
FRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLVVHSSMEQDVGL
LRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCL
QGAVTTDYAAGMAMAGAGVISGFDMTSEAALAKLSYVLGQPGLSLDVRKELLTKDLRGEM
TPPSVEERRPSLQGNTLGGGVSWLLSLSGSQEADALRNALVPSLACAAAHAGDVEALQAL
VELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHP
GVIGLLREAGASLSTQELEEAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHV
AEAAGNLAVVAFLQSLEGAVGAQAPCP
Enzyme 12 Number of Residues 567
Enzyme 12 Molecular Weight 60287.7
Enzyme 12 Theoretical pI 5.59
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
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
Component
Enzyme 12 General Function Involved in asparaginase activity
Enzyme 12 Specific Function Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • L-asparagine + H2O = L-aspartate + NH3 [RN:R00485]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 122937331 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q86U10 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name LPP60_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1740 bp
ATGGCGCGCGCGGTGGGGCCCGAGCGGAGGCTGCTGGCCGTCTACACCGGCGGCACCATT
GGCATGCGGAGTGAGCTCGGCGTGCTTGTGCCCGGGACGGGCCTGGCTGCCATCCTGAGG
ACACTGCCCATGTTCCATGACGAGGAGCACGCCCGAGCCCGCGGCCTCTCTGAGGACACC
CTGGTGCTACCCCCGGCCAGCCGCAACCAGAGGATTCTCTACACCGTGCTGGAGTGCCAG
CCCCTCTTCGACTCCAGTGACATGACCATCGCTGAGTGGGTTTGCCTTGCCCAGACCATC
AAGAGGCACTACGAGCAGTACCACGGCTTTGTGGTCATCCACGGCACCGACACCATGGCC
TTTGCTGCCTCGATGCTGTCCTTCATGCTGGAGAACCTGCAGAAGACTGTCATCCTCACT
GGGGCCCAGGTGCCCATCCATGCCCTGTGGAGCGACGGCCGTGAGAACCTGCTGGGGGCA
CTGCTCATGGCTGGCCAGTATGTGATCCCAGAGGTCTGCCTTTTCTTCCAGAATCAGCTG
TTTCGGGGCAACCGGGCAACCAAGGTAGACGCTCGGAGGTTCGCAGCTTTCTGCTCCCCG
AACCTGCTGCCTCTGGCCACAGTGGGTGCTGACATCACAATCAACAGGGAGCTGGTGCGG
AAGGTGGACGGGAAGGCTGGGCTGGTGGTGCACAGCAGCATGGAGCAGGACGTGGGCCTG
CTGCGCCTCTACCCTGGGATCCCTGCCGCCCTGGTTCGGGCCTTCTTGCAGCCTCCCCTG
AAGGGCGTGGTCATGGAGACCTTCGGTTCAGGGAACGGACCCACCAAGCCCGACCTGCTG
CAGGAGCTGCGGGTGGCCACCGAGCGCGGCCTGGTCATCGTCAACTGTACCCACTGCCTC
CAGGGGGCTGTGACCACAGACTATGCAGCTGGCATGGCCATGGCGGGAGCCGGCGTCATC
TCAGGCTTCGACATGACATCGGAGGCCGCCCTGGCCAAGCTATCGTATGTGCTGGGCCAG
CCAGGGCTGAGCCTGGATGTCAGGAAGGAGCTGCTGACCAAGGACCTTCGGGGGGAGATG
ACGCCACCCTCGGTGGAAGAGCGCCGGCCCTCACTGCAGGGCAACACGCTGGGCGGTGGG
GTCTCCTGGCTCCTCAGTCTGAGCGGCAGCCAGGAGGCAGATGCCCTGCGGAATGCCCTG
GTGCCCAGCCTGGCCTGTGCTGCTGCCCACGCCGGTGACGTGGAGGCGCTGCAGGCGCTT
GTGGAGCTGGGCAGTGACCTGGGCCTGGTGGACTTTAACGGCCAAACCCCACTGCACGCG
GCCGCCCGGGGAGGCCACACAGAGGCAGTCACCATGCTGCTGCAGAGAGGTGTGGACGTG
AACACCCGGGACACGGATGGCTTCAGCCCGCTGCTGCTGGCCGTGCGGGGCAGGCATCCG
GGTGTCATTGGGTTGCTGCGGGAAGCCGGGGCCTCCCTGTCCACCCAGGAGCTGGAGGAA
GCAGGGACGGAGCTGTGCAGGCTGGCATACAGGGCCGACCTCGAAGGCCTGCAGGTGTGG
TGGCAGGCAGGGGCTGACCTGGGGCAGCCGGGCTATGACGGGCACAGCGCCCTGCACGTC
GCAGAGGCAGCCGGGAACCTGGCAGTGGTGGCCTTTCTACAGAGCCTGGAGGGTGCGGTT
GGTGCCCAGGCCCCATGCCCAGAGCCCTCATGTTTTCAGGAAGTGCTGCCTGGTGTCTAA
Enzyme 12 GenBank Gene ID NM_001080464 Link Image
Enzyme 12 GeneCard ID ASPG Link Image
Enzyme 12 GenAtlas ID ASPG Link Image
Enzyme 12 HGNC ID HGNC:20123 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 14q32.33
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [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 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
FLHVNDGSSLESLQVVADSGLDSRELNFGSSVEVQGQLIKSPSKRQNVELKAEKIKVIGN
CDAKDFPIKYKERHPLEYLRQYPHFRCRTNVLGSILRIRSEATAAIHSFFKDSGFVHIHT
PIITSNDSEGAGELFQLEPSGKLKVPEENFFNVPAFLTVSGQLHLEVMSGAFTQVFTFGP
TFRAENSQSRRHLAEFYMIEAEISFVDSLQDLMQVIEELFKATTMMVLSKCPEDVELCHK
FIAPGQKDRLEHMLKNNFLIISYTEAVEILKQASQNFTFTPEWGADLRTEHEKYLVKHCG
NIPVFVINYPLTLKPFYMRDNEDGPQHTVAAVDLLVPGVGELFGGGLREERYHFLEERLA
RSGLTEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFPHSCLL
Enzyme 13 Number of Residues 477
Enzyme 13 Molecular Weight 54089.6
Enzyme 13 Theoretical pI 7.26
Enzyme 13 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • aminoacyl-tRNA ligase activity
  • asparagine-tRNA ligase activity
  • aspartate-tRNA ligase activity
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming aminoacyl-tRNA and related compounds
  • ligase activity, forming carbon-oxygen bonds
  • nucleic acid binding
  • nucleoside binding
  • nucleotide binding
  • purine nucleoside binding
Process
  • RNA metabolic process
  • asparaginyl-tRNA aminoacylation
  • aspartyl-tRNA aminoacylation
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • cellular macromolecule metabolic process
  • macromolecule biosynthetic process
  • macromolecule metabolic process
  • metabolic process
  • ncRNA metabolic process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolic process
  • translation
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 13 General Function Involved in nucleotide binding
Enzyme 13 Specific Function ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn)
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions
  • ATP + L-asparagine + tRNAAsn = AMP + diphosphate + L-asparaginyl-tRNAAsn [RN:R03648]
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 NARS2 Link Image
Enzyme 13 GenAtlas ID NARS2 Link Image
Enzyme 13 HGNC ID HGNC:26274 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 11q14.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [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. Bonnefond L, Fender A, Rudinger-Thirion J, Giege R, Florentz C, Sissler M: Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry. 2005 Mar 29;44(12):4805-16. [PubMed Link Image]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 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