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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Glutamic acid (HMDB00148)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-03-11 14:24:51
Accession Number HMDB00148
Secondary Accession Numbers Not Available
Common Name L-Glutamic acid
Description Glutamic acid (Glu), also referred to as glutamate (the anion), is one of the 20 proteinogenic amino acids. It is not among the essential amino acids. Glutamate is a key molecule in cellular metabolism. In humans, dietary proteins are broken down by digestion into amino acids, which serves as metabolic fuel or other functional roles in the body. Glutamate is the most abundant fast excitatory neurotransmitter in the mammalian nervous system. At chemical synapses, glutamate is stored in vesicles. Nerve impulses trigger release of glutamate from the pre-synaptic cell. In the opposing post-synaptic cell, glutamate receptors, such as the NMDA receptor, bind glutamate and are activated. Because of its role in synaptic plasticity, it is believed that glutamic acid is involved in cognitive functions like learning and memory in the brain. Glutamate transporters are found in neuronal and glial membranes. They rapidly remove glutamate from the extracellular space. In brain injury or disease, they can work in reverse and excess glutamate can accumulate outside cells. This process causes calcium ions to enter cells via NMDA receptor channels, leading to neuronal damage and eventual cell death, and is called excitotoxicity. The mechanisms of cell death include: * Damage to mitochondria from excessively high intracellular Ca2+. * Glu/Ca2+-mediated promotion of transcription factors for pro-apoptotic genes, or downregulation of transcription factors for anti-apoptotic genes. Excitotoxicity due to glutamate occurs as part of the ischemic cascade and is associated with stroke and diseases like amyotrophic lateral sclerosis, lathyrism, and Alzheimer's disease. glutamic acid has been implicated in epileptic seizures. Microinjection of glutamic acid into neurons produces spontaneous depolarization around one second apart, and this firing pattern is similar to what is known as paroxysmal depolarizing shift in epileptic attacks. This change in the resting membrane potential at seizure foci could cause spontaneous opening of voltage activated calcium channels, leading to glutamic acid release and further depolarization. (http://en.wikipedia.org/wiki/Glutamic_acid)
Synonyms
  1. (2S)-2-Aminopentanedioate
  2. (2S)-2-Aminopentanedioic acid
  3. (S)-(+)-Glutamate
  4. (S)-(+)-Glutamic acid
  5. (S)-2-Aminopentanedioate
  6. (S)-2-Aminopentanedioic acid
  7. (S)-Glutamate
  8. (S)-Glutamic acid
  9. 1-Aminopropane-1,3-dicarboxylate
  10. 1-Aminopropane-1,3-dicarboxylic acid
  11. 1-amino-propane-1,3-dicarboxylate
  12. 1-amino-propane-1,3-dicarboxylic acid
  13. 2-Aminoglutarate
  14. 2-Aminoglutaric acid
  15. 2-Aminopentanedioate
  16. 2-Aminopentanedioic acid
  17. Aciglut
  18. E
  19. Glusate
  20. Glutacid
  21. Glutamicol
  22. Glutamidex
  23. Glutaminate
  24. Glutaminic acid
  25. Glutaminol
  26. Glutaton
  27. L-(+)-Glutamate
  28. L-(+)-Glutamic acid
  29. L-Glutamate
  30. L-Glutaminate
  31. L-Glutaminic acid
  32. L-a-Aminoglutarate
  33. L-a-Aminoglutaric acid
  34. L-glu
  35. a-Aminoglutarate
  36. a-Aminoglutaric acid
  37. a-Glutamate
  38. a-Glutamic acid
  39. aminoglutarate
  40. aminoglutaric acid
  41. glt
  42. glu
  43. glut
  44. L-alpha-Aminoglutarate
  45. L-alpha-Aminoglutaric acid
  46. alpha-Aminoglutarate
  47. alpha-Aminoglutaric acid
  48. alpha-Glutamate
  49. alpha-Glutamic acid
Chemical IUPAC Name 2-aminopentanedioic acid
Chemical Formula C5H9NO4
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
  • alpha-aminoacid
Biofunction
  • Component of Alanine and aspartate metabolism
  • Component of Aminoacyl-tRNA biosynthesis
  • Component of Aminosugars metabolism
  • Component of Arginine and proline metabolism
  • Component of beta-Alanine metabolism
  • Component of Butanoate metabolism
  • Component of Cyanoamino acid metabolism
  • Component of Cysteine metabolism
  • Component of D-Glutamine and D-glutamate metabolism
  • Component of Folate biosynthesis
  • Component of Glutamate metabolism
  • Component of Glutathione metabolism
  • Component of Glycine, serine and threonine metabolism
  • Component of Lysine biosynthesis
  • Component of Nitrogen metabolism
  • Component of Novobiocin biosynthesis
  • Component of Pantothenate and CoA biosynthesis
  • Component of Peptidoglycan biosynthesis
  • Component of Phenylalanine metabolism
  • Component of Phenylalanine, tyrosine and tryptophan biosynthesis
  • Component of Porphyrin and chlorophyll metabolism
  • Component of Prostaglandin and leukotriene metabolism
  • Component of Purine metabolism
  • Component of Pyrimidine metabolism
  • Component of Selenoamino acid metabolism
  • Component of Taurine and hypotaurine metabolism
  • Component of Tyrosine metabolism
  • Component of Valine, leucine and isoleucine biosynthesis
  • Component of Vitamin B6 metabolism
Application
Source
  • Endogenous
Average Molecular Weight 147.129
Monoisotopic Molecular Weight 147.053162
Isomeric SMILES N[C@@H](CCC(O)=O)C(O)=O
Canonical SMILES NC(CCC(O)=O)C(O)=O
KEGG Compound ID C00025 Link Image
BioCyc ID GLT Link Image
BiGG ID 33561 Link Image
Wikipedia Link E Link Image
NuGOwiki Link HMDB00148 Link Image
Metagene Link HMDB00148 Link Image
METLIN ID 5174 Link Image
PubChem Compound 33032 Link Image
PubChem Substance 7847075 Link Image
ChEBI ID 16015 Link Image
CAS Registry Number 56-86-0
InChI Identifier InChI=1/C5H9NO4/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H,7,8)(H,9,10)/t3-/m0/s1
Synthesis Reference Horner, L.; Gross, A. Tertiary phosphines. IV. Use of phosphine imines in causing the introduction of primary amino groups. Ann. (1955), 591 117-34.
Melting Point (Experimental) Not Available
Experimental Water Solubility 8.57 mg/mL [BULL,HB et al. (1978)] Source: PhysProp
Predicted Water Solubility 80.600006 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity -3.69 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -3.54 [Predicted by ALOGPS]; -3.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID 1BGV 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 (Predicted from LogP)
  • endoplasmic reticulum
  • Extracellular
  • lysosome
  • mitochondria
Biofluid Location
  • Blood
  • Cellular Cytoplasm
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
Adipose Tissue
Adrenal Medulla
Epidermis
Fibroblasts
Intestine
Kidney
Muscle
Myelin
Nerve Cells
Neuron
Pancreas
Placenta
Platelet
Skeletal Muscle
Spleen
Stratum Corneum
Concentrations (Normal)
Biofluid Blood
Value 24.0 (9.0-39.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Aseptic meningitis
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 65.0 +/- 35.0 uM
Age Newborn:0-30 days old
Sex N/A
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 35.0 +/- 14.0 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 37.0 +/- 14.0 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 60.0 +/- 16.0 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 46.0 +/- 13.0 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 33.0 +/- 12.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 93. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 145.0 +/- 6.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. [PubMed Link Image]
Biofluid Cellular Cytoplasm
Value 1400 (1200-1600) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Zupke C, Sinskey AJ, Stephanopoulos G: Intracellular flux analysis applied to the effect of dissolved oxygen on hybridomas. Appl Microbiol Biotechnol. 1995 Dec;44(1-2):27-36. [PubMed Link Image]
Biofluid CSF
Value 1.8 +/- 0.7 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 0.62 (0.18-1.15) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Rizzo V, Anesi A, Montalbetti L, Bellantoni G, Trotti R, Melzi d'Eril GV: Reference values of neuroactive amino acids in the cerebrospinal fluid by high-performance liquid chromatography with electrochemical and fluorescence detection. J Chromatogr A. 1996 Apr 5;729(1-2):181-8. [PubMed Link Image]
Biofluid CSF
Value 0.34 +/- 0.14 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Alfredsson G, Wiesel FA, Tylec A: Relationships between glutamate and monoamine metabolites in cerebrospinal fluid and serum in healthy volunteers. Biol Psychiatry. 1988 Apr 1;23(7):689-97. [PubMed Link Image]
Biofluid CSF
Value 32.6 +/- 6.9 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
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 40 +/- 52 uM
Age N/A
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Lewis MJ, Morrissey JA, Flegel MD, Jeroncic K, Xiong Y, Cheng D, Eisner R, Gautam B, Tzur D, Sawhney S, Bamforth F, Greiner R, Li L: The human cerebrospinal fluid metabolome. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Aug 15;871(2):164-173. Epub 2008 May 8. [PubMed Link Image]
Biofluid CSF
Value 0.44 +/- 0.29 uM
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 Saliva
Value >10 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
Biofluid Urine
Value 1.711 (0.329-3.092) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value 0.5 (0.13-1.0) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 6.87 +/- 3.51 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 1.38 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 29.8 (27.6-32.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Refractory localization-related epilepsy (RLE)
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 39.7 (36.5-42.9) uM
Age Children:1-13 yrs old
Sex Both
Condition Epilepsy
Comments Juvenile myoclonic epilepsy (JME)
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 56.6 (44.6-68.6) 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 32.7 +/- 18.0 uM
Age Adult:>18 yrs old
Sex Male
Condition Schizophrenia
Comments Not Available
References
  • Alfredsson G, Wiesel FA: Monoamine metabolites and amino acids in serum from schizophrenic patients before and during sulpiride treatment. Psychopharmacology (Berl). 1989;99(3):322-7. [PubMed Link Image]
Biofluid Blood
Value 34.7 +/- 26.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Schizophrenia
Comments Not Available
References
  • Alfredsson G, Wiesel FA: Monoamine metabolites and amino acids in serum from schizophrenic patients before and during sulpiride treatment. Psychopharmacology (Berl). 1989;99(3):322-7. [PubMed Link Image]
Biofluid Blood
Value 33.18 +/- 11.26 uM
Age Elderly:>65 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]
Biofluid Blood
Value 172.0 +/- 6.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Heart failure
Comments Non-diabetic patients with chronic heart failure
References
  • Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. [PubMed Link Image]
Biofluid Cellular Cytoplasm
Value 2500 (2100-2900) uM
Age Adult:>18 yrs old
Sex Both
Condition Anoxia
Comments Not Available
References
  • Zupke C, Sinskey AJ, Stephanopoulos G: Intracellular flux analysis applied to the effect of dissolved oxygen on hybridomas. Appl Microbiol Biotechnol. 1995 Dec;44(1-2):27-36. [PubMed Link Image]
Biofluid CSF
Value 26.8 +/- 5.9 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 23.6 +/- 8.5 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 0.32 +/- 0.09 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 0.22 (0.14-0.29) uM
Age Adult:>18 yrs old
Sex Both
Condition Rett syndrome
Comments Not Available
References
Biofluid CSF
Value 0.37 (0.21-0.53) uM
Age Adult:>18 yrs old
Sex Both
Condition Rett syndrome
Comments Not Available
References
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]
Anoxia
  • Zupke C, Sinskey AJ, Stephanopoulos G: Intracellular flux analysis applied to the effect of dissolved oxygen on hybridomas. Appl Microbiol Biotechnol. 1995 Dec;44(1-2):27-36. [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]
Heart failure
  • Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. [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]
Rett syndrome
Schizophrenia
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Alanine Metabolism SMP00055 Link Image map00250 Link Image
Amino Sugar Metabolism SMP00045 Link Image map00520 Link Image
Ammonia Recycling SMP00009 Link Image map00910 Link Image
Arginine and Proline Metabolism SMP00020 Link Image map00330 Link Image
Cysteine Metabolism SMP00013 Link Image map00270 Link Image
Folate Metabolism SMP00053 Link Image map00670 Link Image
Glucose-Alanine Cycle SMP00127 Link Image
Glutamate Metabolism SMP00072 Link Image map00250 Link Image
Glutathione Metabolism SMP00015 Link Image map00480 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
Histidine Metabolism SMP00044 Link Image map00340 Link Image
Malate-Aspartate Shuttle SMP00129 Link Image
Transcription/Translation SMP00019 Link Image
Urea Cycle SMP00059 Link Image map00330 Link Image
General References
  1. Mross K, Maessen P, van der Vijgh WJ, Gall H, Boven E, Pinedo HM: Pharmacokinetics and metabolism of epidoxorubicin and doxorubicin in humans. J Clin Oncol. 1988 Mar;6(3):517-26. [PubMed Link Image]
  2. Noorlander CW, de Graan PN, Nikkels PG, Schrama LH, Visser GH: Distribution of glutamate transporters in the human placenta. Placenta. 2004 Jul;25(6):489-95. [PubMed Link Image]
  3. 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]
  4. Grasselli G, Vigano L, Capri G, Locatelli A, Tarenzi E, Spreafico C, Bertuzzi A, Giani A, Materazzo C, Cresta S, Perotti A, Valagussa P, Gianni L: Clinical and pharmacologic study of the epirubicin and paclitaxel combination in women with metastatic breast cancer. J Clin Oncol. 2001 Apr 15;19(8):2222-31. [PubMed Link Image]
  5. 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]
  6. 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]
  7. Zupke C, Sinskey AJ, Stephanopoulos G: Intracellular flux analysis applied to the effect of dissolved oxygen on hybridomas. Appl Microbiol Biotechnol. 1995 Dec;44(1-2):27-36. [PubMed Link Image]
  8. Molinari F, Raas-Rothschild A, Rio M, Fiermonte G, Encha-Razavi F, Palmieri L, Palmieri F, Ben-Neriah Z, Kadhom N, Vekemans M, Attie-Bitach T, Munnich A, Rustin P, Colleaux L: Impaired mitochondrial glutamate transport in autosomal recessive neonatal myoclonic epilepsy. Am J Hum Genet. 2005 Feb;76(2):334-9. Epub 2004 Dec 8. [PubMed Link Image]
  9. Frayn KN, Khan K, Coppack SW, Elia M: Amino acid metabolism in human subcutaneous adipose tissue in vivo. Clin Sci (Lond). 1991 May;80(5):471-4. [PubMed Link Image]
  10. Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
  11. Alfredsson G, Wiesel FA, Tylec A: Relationships between glutamate and monoamine metabolites in cerebrospinal fluid and serum in healthy volunteers. Biol Psychiatry. 1988 Apr 1;23(7):689-97. [PubMed Link Image]
  12. Zoia C, Cogliati T, Tagliabue E, Cavaletti G, Sala G, Galimberti G, Rivolta I, Rossi V, Frattola L, Ferrarese C: Glutamate transporters in platelets: EAAT1 decrease in aging and in Alzheimer's disease. Neurobiol Aging. 2004 Feb;25(2):149-57. [PubMed Link Image]
  13. Nicholson JK, O'Flynn MP, Sadler PJ, Macleod AF, Juul SM, Sonksen PH: Proton-nuclear-magnetic-resonance studies of serum, plasma and urine from fasting normal and diabetic subjects. Biochem J. 1984 Jan 15;217(2):365-75. [PubMed Link Image]
  14. Rizzo V, Anesi A, Montalbetti L, Bellantoni G, Trotti R, Melzi d'Eril GV: Reference values of neuroactive amino acids in the cerebrospinal fluid by high-performance liquid chromatography with electrochemical and fluorescence detection. J Chromatogr A. 1996 Apr 5;729(1-2):181-8. [PubMed Link Image]
  15. Agnati LF, Ferre S, Lluis C, Franco R, Fuxe K: Molecular mechanisms and therapeutical implications of intramembrane receptor/receptor interactions among heptahelical receptors with examples from the striatopallidal GABA neurons. Pharmacol Rev. 2003 Sep;55(3):509-50. Epub 2003 Jul 17. [PubMed Link Image]
  16. Rutten EP, Engelen MP, Wouters EF, Schols AM, Deutz NE: Metabolic effects of glutamine and glutamate ingestion in healthy subjects and in persons with chronic obstructive pulmonary disease. Am J Clin Nutr. 2006 Jan;83(1):115-23. [PubMed Link Image]
  17. Agarwal A, Tripathi LM, Pandey VC: Status of ammonia, glutamate, lactate and pyruvate during Plasmodium yoelii infection and pyrimethamine treatment in mice. J Commun Dis. 1997 Sep;29(3):235-41. [PubMed Link Image]
  18. Heuschen UA, Allemeyer EH, Hinz U, Langer K, Heuschen G, Decker-Baumann C, Herfarth C, Stern J: Glutamine distribution in patients with ulcerative colitis and in patients with familial adenomatous polyposis coli before and after restorative proctocolectomy. Int J Colorectal Dis. 2002 Jul;17(4):245-52. Epub 2001 Dec 18. [PubMed Link Image]
  19. Olson RC: A proposed role for nerve growth factor in the etiology of multiple sclerosis. Med Hypotheses. 1998 Dec;51(6):493-8. [PubMed Link Image]
  20. Nakamura K, Matsumura K, Kobayashi S, Kaneko T: Sympathetic premotor neurons mediating thermoregulatory functions. Neurosci Res. 2005 Jan;51(1):1-8. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
  2. Glutathione reductase, mitochondrial
  3. Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 2
  4. 4-aminobutyrate aminotransferase, mitochondrial
  5. Tyrosine aminotransferase
  6. Aspartate aminotransferase, cytoplasmic
  7. Aspartate aminotransferase, mitochondrial
  8. Branched-chain-amino-acid aminotransferase, cytosolic
  9. Alanine--glyoxylate aminotransferase 2, mitochondrial
  10. Ornithine aminotransferase, mitochondrial
  11. Glutamate--cysteine ligase catalytic subunit
  12. N-acetylglutamate synthase, mitochondrial
  13. Branched-chain-amino-acid aminotransferase, mitochondrial
  14. Bifunctional aminoacyl-tRNA synthetase
  15. Asparagine synthetase [glutamine-hydrolyzing]
  16. Glutamate dehydrogenase 2, mitochondrial
  17. Glutamine synthetase
  18. CTP synthase 1
  19. Glutaminase kidney isoform, mitochondrial
  20. Formimidoyltransferase-cyclodeaminase
  21. Glutamate dehydrogenase 1, mitochondrial
  22. Glutamate decarboxylase 2
  23. Glutamate decarboxylase 1
  24. Gamma-glutamyltranspeptidase 1
  25. Glutathione synthetase
  26. Folylpolyglutamate synthase, mitochondrial
  27. Alanine aminotransferase 1
  28. Phosphoserine aminotransferase
  29. Delta-1-pyrroline-5-carboxylate synthase
  30. 5-oxoprolinase
  31. Glutamate [NMDA] receptor subunit zeta-1
  32. Glutamate [NMDA] receptor subunit 3B
  33. Glutamate [NMDA] receptor subunit epsilon-2
  34. Vitamin K-dependent gamma-carboxylase
  35. Glutamate receptor, ionotropic kainate 2
  36. Glutamate carboxypeptidase 2
  37. Metabotropic glutamate receptor 1
  38. Arginine decarboxylase
  39. Glutaminase 2 (Liver, mitochondrial), isoform CRA_b
  40. Hypothetical protein GAD1
  41. Aminoadipate aminotransferase, isoform CRA_b
  42. Excitatory amino acid transporter 3
  43. Mitochondrial glutamate carrier 2
  44. Glutamine-dependent NAD(+) synthetase
  45. CAD protein
  46. Alanine aminotransferase 2
  47. CTP synthase 2
  48. Alanine aminotransferase
  49. Gamma-glutamyltransferase 6
  50. Phosphoribosyl pyrophosphate amidotransferase, isoform CRA_b
  51. Guanine monphosphate synthetase, isoform CRA_b
  52. Glutamine synthetase
  53. Probable glutamyl-tRNA synthetase, mitochondrial
  54. Phosphoserine aminotransferase 1
  55. Aminoadipate-semialdehyde synthase
  56. cDNA, FLJ96771, Homo sapiens ornithine decarboxylase-like protein (ODC-p), mRNA (Arginine decarboxylase, isoform CRA_d)
  57. cDNA, FLJ95223, Homo sapiens N-acetylglutamate synthase (NAGS), mRNA
  58. GGT7 protein
  59. Gamma-glutamyltransferase 5
  60. Putative uncharacterized protein GFPT1
  61. cDNA FLJ75059, highly similar to Homo sapiens phosphoribosylformylglycinamidine synthase (FGAR amidotransferase) (PFAS), mRNA
  62. cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial)
  63. cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
  64. cDNA, FLJ93078, Homo sapiens glutamic-oxaloacetic transaminase 1, soluble(aspartate aminotransferase 1) (GOT1), mRNA (Glutamic-oxaloacetic transaminase 1, soluble (Aspartate aminotransferase 1), isoform CRA_b)
  65. cDNA, FLJ93913, Homo sapiens tyrosine aminotransferase (TAT), nuclear gene encodingmitochondrial protein, mRNA (Tyrosine aminotransferase, isoform CRA_a)
  66. Aspartyl aminopeptidase
  67. Metabotropic glutamate receptor 8
  68. Metabotropic glutamate receptor 4
  69. Metabotropic glutamate receptor 7
Enzyme 1 [top]
Enzyme 1 ID 5388
Enzyme 1 Name Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
Enzyme 1 Synonyms
  1. P5C dehydrogenase
  2. Aldehyde dehydrogenase family 4 member A1
Enzyme 1 Gene Name ALDH4A1
Enzyme 1 Protein Sequence >Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
MLLPAPALRRALLSRPWTGAGLRWKHTSSLKVANEPVLAFTQGSPERDALQKALKDLKGR
MEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKP
IADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVEL
EGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAML
ASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ
NLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSL
WPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGK
CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTG
AVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR
WTSPQVIKETHKPLGDWSYAYMQ
Enzyme 1 Number of Residues 563
Enzyme 1 Molecular Weight 61718.9
Enzyme 1 Theoretical pI 8.20
Enzyme 1 GO Classification
Function
  • 1-pyrroline-5-carboxylate dehydrogenase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glutamine family amino acid metabolic process
  • metabolic process
  • oxidation reduction
  • proline biosynthetic process
  • proline metabolic process
Component
  • cell part
  • cytoplasmic part
  • intracellular part
  • mitochondrial matrix
  • mitochondrial part
Enzyme 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function Irreversible conversion of delta-1-pyrroline-5- carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (S)-1-pyrroline-5-carboxylate + NAD(P)+ + 2 H2O = L-glutamate + NAD(P)H + H+ [RN:R00707 R00708]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 62896531 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P30038 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AL4A1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1692 bp
ATGCTGCTGCCGGCGCCCGCGCTCCGCCGCGCCCTGCTGTCCCGCCCCTGGACCGGGGCC
GGCCTGCGGTGGAAGCACACCTCCTCCCTGAAGGTGGCCAACGAGCCCGTCTTAGCCTTC
ACGCAGGGCAGCCCTGAGCGAGATGCCCTGCAAAAGGCCTTGAAGGACCTGAAGGGCCGG
ATGGAAGCCATCCCATGCGTGGTGGGGGATGAGGAGGTGTGGACGTCGGACGTGCAGTAC
CAAGTGTCGCCTTTTAACCATGGACATAAGGTGGCCAAGTTCTGTTATGCAGACAAGAGC
CTGCTCAACAAAGCCATTGAGGCTGCCCTGGCTGCCCGGAAAGAGTGGGACCTGAAGCCT
ATTGCAGACCGGGCCCAGATCTTCCTGAAGGCGGCAGACATGCTGAGTGGGCCGCGCAGG
GCTGAGATCCTCGCCAAGACCATGGTGGGACAGGGTAAGACCGTGATCCAAGCGGAGATT
GACGCTGCAGCGGAACTCATCGACTTCTTCCGGTTCAATGCCAAGTATGCGGTGGAGCTG
GAGGGGCAGCAGCCCATCAGCGTGCCCCCGAGCACCAACAGCACGGTGTACCGGGGTCTG
GAGGGCTTCGTGGCGGCCATCTCGCCCTTTAACTTCACTGCAATCGGCGGCAACCTGGCG
GGGGCACCGGCCCTGATAGGCAACGTGGTCCTATGGAAGCCCAGTGACACTGCCATGCTG
GCCAGCTATGCTGTCTACCGCATCCTTCGGGAGGCTGGCCTGCCCCCCAACATCATCCAG
TTTGTGCCAGCTGATGGGCCCCTATTTGGGGACACTGTCACCAGCTCAGAGCACCTCTGT
GGCATCAACTTCACAGGCAGTGTGCCCACCTTCAAACACCTGTGGAAGCAGGTGGCCCAG
AACCTGGACCGGTTCCACACCTTCCCACGCCTGGCTGGAGAGTGCGGCGGAAAGAACTTC
CACTTCGTGCACCGCTCGGCCGACGTGGAGAGCGTGGTGAGCGGGACCCTCCGCTCAGCC
TTCGAGTACGGTGGCCAGAAGTGTTCCGCCTGCTCGCGTCTCTACGTGCCGCACTCGCTG
TGGCCGCAGATCAAAGGGCGGCTGCTGGAGGAGCACAGTCGGATCAGAGTGGGCGACCCT
GCAGAGGATTTTGGGACCTTCTTCTCTGCAGTGATTGATGCCAAGTCCTTTGCCCGTATC
AAGAAGTGGCTGGAGCACGCACGCTCCTCACCCAGCCTCACCATCCTGGCCGGGGGCAAG
TGTGATGACTCCGTGGGCTACTTTGTGGAGCCCTGCATCGTGGAGAGCAAGGACCCTCAG
GAGCCCATCATGAAGGAGGAGATCTTCGGGCCTGTACTGTCTGTGTACGTCTACCCGGAT
GACAAGTACAAGGAGACGCTGCAGCTGGTTGACAGCACCACCAGCTATGGCCTCACGGGG
GCAGTGTTCTCCCAGGATAAGGACGTCGTGCAGGAGGCCACAAAGGTGCTGAGGAATGCT
GCCGGCAACTTCTACATCAACGACAAGTCCACTGGCTCGATAGTGGGCCAGCAGCCCTTT
GGGGGGGCCCGAGCCTCTGGAACCAATGACAAGCCAGGGGGCCCACACTACATCCTGCGC
TGGACGTCGCCGCAGGTCATCAAGGAGACACATAAGCCCCTGGGGGACTGGAGCTACGCG
TACATGCAGTGA
Enzyme 1 GenBank Gene ID AK222486 Link Image
Enzyme 1 GeneCard ID ALDH4A1 Link Image
Enzyme 1 GenAtlas ID ALDH4A1 Link Image
Enzyme 1 HGNC ID HGNC:406 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p36
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Hu CA, Lin WW, Valle D: Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase. J Biol Chem. 1996 Apr 19;271(16):9795-800. [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. 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]
  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. Hempel J, Eckey R, Berie D, Romovacek H, Agarwal DP, Goedde HW: Human liver glutamic gamma-semialdehyde dehydrogenase: structural relationship to the yeast enzyme. Comp Biochem Physiol B. 1992 Aug;102(4):791-93. [PubMed Link Image]
  6. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  7. Agarwal DP, Eckey R, Hempel J, Goedde HW: Human liver high Km aldehyde dehydrogenase (ALDH4): properties and structural relationship to the glutamic gamma-semialdehyde dehydrogenase. Adv Exp Med Biol. 1993;328:191-7. [PubMed Link Image]
  8. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  9. Geraghty MT, Vaughn D, Nicholson AJ, Lin WW, Jimenez-Sanchez G, Obie C, Flynn MP, Valle D, Hu CA: Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia. Hum Mol Genet. 1998 Sep;7(9):1411-5. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5428
Enzyme 2 Name Glutathione reductase, mitochondrial
Enzyme 2 Synonyms
  1. GR
  2. GRase
Enzyme 2 Gene Name GSR
Enzyme 2 Protein Sequence >Glutathione reductase, mitochondrial
MALLPRALSAGAGPSWRRAARAFRGFLLLLPEPAALTRALSRAMACRQEPQPQGPPPAAG
AVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHS
EFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDP
KPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAG
YIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKK
TLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVD
EFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPP
IGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQ
GLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR
Enzyme 2 Number of Residues 522
Enzyme 2 Molecular Weight 56256.6
Enzyme 2 Theoretical pI 8.66
Enzyme 2 GO Classification
Function
  • FAD or FADH2 binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • disulfide oxidoreductase activity
  • glutathione disulfide oxidoreductase activity
  • glutathione-disulfide reductase activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on a sulfur group of donors
  • peptide disulfide oxidoreductase activity
  • purine nucleoside binding
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular metabolic process
  • cellular process
  • glutathione metabolic process
  • metabolic process
  • oxidation reduction
  • peptide metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 2 General Function Involved in oxidoreductase activity
Enzyme 2 Specific Function Maintains high levels of reduced glutathione in the cytosol
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ [RN:R00115]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 50301238 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P00390 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name GSHR_HUMAN Link Image
Enzyme 2 PDB ID 1BWC Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1569 bp
ATGGCCCTGCTGCCCCGAGCCCTGAGCGCCGGCGCGGGACCGAGCTGGCGGCGGGCGGCG
CGCGCCTTCCGAGGCTTCCTGCTGCTTCTGCCCGAGCCCGCGGCCCTCACGCGCGCCCTC
TCCCGTGCCATGGCCTGCAGGCAGGAGCCGCAGCCGCAGGGCCCGCCGCCCGCTGCTGGC
GCCGTGGCCTCCTATGACTACCTGGTGATCGGGGGCGGCTCGGGCGGGCTGGCCAGCGCG
CGCAGGGCGGCCGAGCTGGGTGCCAGGGCCGCCGTGGTGGAGAGCCACAAGCTGGGTGGC
ACTTGCGTGAATGTTGGATGTGTACCCAAAAAGGTAATGTGGAACACAGCTGTCCACTCT
GAATTCATGCATGATCATGCTGATTATGGCTTTCCAAGTTGTGAGGGTAAATTCAATTGG
CGTGTTATTAAGGAAAAGCGGGATGCCTATGTGAGCCGCCTGAATGCCATCTATCAAAAC
AATCTCACCAAGTCCCATATAGAAATCATCCGTGGCCATGCAGCCTTCACGAGTGATCCC
AAGCCCACAATAGAGGTCAGTGGGAAAAAGTACACCGCCCCACACATCCTGATCGCCACA
GGTGGTATGCCCTCCACCCCTCATGAGAGCCAGATCCCCGGTGCCAGCTTAGGAATAACC
AGCGATGGATTTTTTCAGCTGGAAGAATTGCCCGGCCGCAGCGTCATTGTTGGTGCAGGT
TACATTGCTGTGGAGATGGCAGGGATCCTGTCAGCCCTGGGTTCTAAGACATCACTGATG
ATACGGCATGATAAGGTACTTAGAAGTTTTGATTCAATGATCAGCACCAACTGCACGGAG
GAGCTGGAGAACGCTGGCGTGGAGGTGCTGAAGTTCTCCCAGGTCAAGGAGGTTAAAAAG
ACTTTGTCGGGCTTGGAAGTCAGCATGGTTACTGCAGTTCCCGGTAGGCTACCAGTCATG
ACCATGATTCCAGATGTTGACTGCCTGCTCTGGGCCATTGGGCGGGTCCCGAATACCAAG
GACCTGAGTTTAAACAAACTGGGGATTCAAACCGATGACAAGGGTCATATCATCGTAGAC
GAATTCCAGAATACCAACGTCAAAGGCATCTATGCAGTTGGGGATGTATGTGGAAAAGCT
CTTCTTACTCCAGTTGCAATAGCTGCTGGCCGAAAACTTGCCCATCGACTTTTTGAATAT
AAGGAAGATTCCAAATTAGATTATAACAACATCCCAACTGTGGTCTTCAGCCACCCCCCT
ATTGGGACAGTGGGACTCACGGAAGATGAAGCCATTCATAAATATGGAATAGAAAATGTG
AAGACCTATTCAACGAGCTTTACCCCGATGTATCACGCAGTTACCAAAAGGAAAACAAAA
TGTGTGATGAAAATGGTCTGTGCTAACAAGGAAGAAAAGGTGGTTGGGATCCATATGCAG
GGACTTGGGTGTGATGAAATGCTGCAGGGTTTTGCTGTTGCAGTGAAGATGGGAGCAACG
AAGGCAGACTTTGACAACACAGTCGCCATTCACCCTACCTCTTCAGAAGAGCTGGTCACA
CTTCGTTGA
Enzyme 2 GenBank Gene ID NM_000637.3 Link Image
Enzyme 2 GeneCard ID GSR Link Image
Enzyme 2 GenAtlas ID GSR Link Image
Enzyme 2 HGNC ID HGNC:4623 Link Image
Enzyme 2 Chromosome Location 8
Enzyme 2 Locus 8p21.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Tutic M, Lu XA, Schirmer RH, Werner D: Cloning and sequencing of mammalian glutathione reductase cDNA. Eur J Biochem. 1990 Mar 30;188(3):523-8. [PubMed Link Image]
  2. Kelner MJ, Montoya MA: Structural organization of the human glutathione reductase gene: determination of correct cDNA sequence and identification of a mitochondrial leader sequence. Biochem Biophys Res Commun. 2000 Mar 16;269(2):366-8. [PubMed Link Image]
  3. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  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. Krauth-Siegel RL, Blatterspiel R, Saleh M, Schiltz E, Schirmer RH, Untucht-Grau R: Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain. Eur J Biochem. 1982 Jan;121(2):259-67. [PubMed Link Image]
  6. Krohne-Ehrich G, Schirmer RH, Untucht-Grau R: Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide. Eur J Biochem. 1977 Oct 17;80(1):65-71. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Thieme R, Pai EF, Schirmer RH, Schulz GE: Three-dimensional structure of glutathione reductase at 2 A resolution. J Mol Biol. 1981 Nov 15;152(4):763-82. [PubMed Link Image]
  9. Karplus PA, Schulz GE: Refined structure of glutathione reductase at 1.54 A resolution. J Mol Biol. 1987 Jun 5;195(3):701-29. [PubMed Link Image]
  10. Savvides SN, Karplus PA: Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor. J Biol Chem. 1996 Apr 5;271(14):8101-7. [PubMed Link Image]
  11. Stoll VS, Simpson SJ, Krauth-Siegel RL, Walsh CT, Pai EF: Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. Biochemistry. 1997 May 27;36(21):6437-47. [PubMed Link Image]
  12. Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA: Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers. Nat Struct Biol. 1998 Apr;5(4):267-71. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5446
Enzyme 3 Name Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 2
Enzyme 3 Synonyms
  1. D-fructose-6-phosphate amidotransferase 2
  2. Glutamine:fructose 6 phosphate amidotransferase 2
  3. GFAT 2
  4. GFAT2
  5. Hexosephosphate aminotransferase 2
Enzyme 3 Gene Name GFPT2
Enzyme 3 Protein Sequence >Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 2
MCGIFAYMNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNHEVKERHIQLVKKR
GKVKALDEELYKQDSMDLKVEFETHFGIAHTRWATHGVPSAVNSHPQRSDKGNEFVVIHN
GIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRETEDITFSTLVERVIQQLEG
AFALVFKSVHYPGEAVATRRGSPLLIGVRSKYKLSTEQIPILYRTCTLENVKNICKTRMK
RLDSSACLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSAS
DDPSRAIQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDH
LKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFF
ISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVASTKAYT
SQFISLVMFGLMMSEDRISLQNRRQEIIRGLRSLPELIKEVLSLEEKIHDLALELYTQRS
LLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCF
AKCQNALQQVTARQGRPIILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFH
LAVLRGYDVDFPRNLAKSVTVE
Enzyme 3 Number of Residues 682
Enzyme 3 Molecular Weight 76929.9
Enzyme 3 Theoretical pI 7.40
Enzyme 3 GO Classification
Function
  • binding
  • carbohydrate binding
  • catalytic activity
  • glutamine-fructose-6-phosphate transaminase (isomerizing) activity
  • sugar binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • carbohydrate biosynthetic process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 3 General Function Involved in metabolic process
Enzyme 3 Specific Function Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins
Enzyme 3 Pathways
Enzyme 3 Reactions
  • L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate [RN:R00768]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID O94808 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name GFPT2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2049 bp
ATGTGCGGAATCTTTGCCTACATGAACTACAGAGTCCCCCGGACGAGGAAGGAGATCTTC
GAAACCCTCATCAAGGGCCTGCAGCGGCTGGAGTACAGAGGCTACGACTCGGCAGGTGTG
GCGATCGATGGGAATAATCACGAAGTCAAAGAAAGACACATTCAGCTGGTCAAGAAAAGG
GGGAAAGTCAAGGCTCTCGATGAAGAACTTTACAAACAAGACAGCATGGACTTAAAAGTG
GAGTTTGAGACACACTTCGGCATTGCCCACACGCGCTGGGCCACCCACGGGGTCCCCAGT
GCTGTCAACAGCCACCCTCAGCGCTCAGACAAAGGCAACGAATTTGTTGTCATCCACAAT
GGGATCATCACAAATTACAAAGATCTGAGGAAATTTCTGGAAAGCAAAGGCTACGAGTTT
GAGTCAGAAACAGATACAGAGACCATCGCCAAGCTGATTAAATATGTGTTCGACAACAGA
GAAACTGAGGACATTACGTTTTCAACGTTGGTCGAGAGAGTCATTCAGCAGTTGGAAGGT
GCATTCGCGCTGGTTTTCAAGAGTGTCCACTACCCAGGAGAAGCCGTTGCCACACGGAGA
GGCAGCCCCCTGCTCATCGGAGTCCGGAGCAAATACAAGCTCTCCACAGAACAGATCCCT
ATCTTATACAGGACGTGCACTCTGGAGAATGTGAAGAATATCTGTAAGACACGGATGAAG
AGGCTGGACAGCTCCGCCTGCCTGCATGCTGTGGGCGACAAGGCCGTGGAATTCTTCTTT
GCTTCTGATGCAAGCGCTATCATAGAGCACACCAACCGGGTCATCTTCCTGGAGGACGAT
GACATCGCCGCAGTGGCTGATGGGAAACTCTCCATTCACCGGGTCAAGCGCTCGGCCAGT
GATGACCCATCTCGAGCCATCCAGACCTTGCAGATGGAACTGCAGCAAATCATGAAAGGT
AACTTCAGTGCGTTTATGCAGAAGGAGATCTTCGAACAGCCAGAATCAGTTTTCAATACT
ATGAGAGGTCGGGTGAATTTTGAAACCAACACAGTGCTCCTGGGTGGCTTGAAGGACCAC
TTGAAGGAGATTCGACGATGCCGACGGCTCATCGTGATTGGCTGTGGAACCAGCTACCAC
GCTGCCGTGGCTACGCGGCAAGTTTTGGAGGAACTGACTGAGCTTCCTGTGATGGTTGAA
CTTGCTAGTGATTTTCTGGACAGGAACACACCTGTGTTCAGGGATGACGTTTGCTTTTTC
ATCAGCCAGTCAGGCGAGACCGCGGACACCCTCCTGGCGCTGCGCTACTGTAAGGACCGC
GGCGCTCTCACCGTGGGCGTCACCAACACCGTGGGCAGCTCCATCTCTCGCGAGACCGAC
TGCGGCGTCCACATCAACGCAGGGCCGGAGATCGGCGTGGCCAGCACCAAGGCTTATACC
AGTCAGTTCATCTCTCTGGTGATGTTTGGTTTGATGATGTCTGAAGACCGAATTTCACTA
CAAAACAGGAGGCAAGAGATCATCCGTGGCTTGAGATCTTTACCTGAGCTGATCAAGGAA
GTGCTGTCTCTGGAGGAGAAGATCCACGACTTGGCCCTGGAGCTCTACACGCAGAGATCG
CTGCTGGTGATGGGGCGGGGCTACAACTATGCCACCTGCCTGGAAGGAGCCCTGAAAATT
AAAGAGATAACCTACATGCACTCAGAAGGCATCCTGGCTGGGGAGCTGAAGCACGGGCCC
CTGGCACTGATTGACAAGCAGATGCCCGTCATCATGGTCATTATGAAGGATCCTTGCTTC
GCCAAATGCCAGAACGCCCTGCAGCAAGTCACGGCCCGCCAGGGTCGCCCCATTATACTG
TGCTCCAAGGACGATACTGAAAGTTCCAAGTTTGCGTATAAGACAATTGAGCTGCCCCAC
ACTGTGGACTGCCTCCAGGGCATCCTGAGCGTGATTCCGCTGCAGCTGCTGTCCTTCCAC
CTGGCTGTTCTCCGAGGATATGACGTTGACTTCCCCAGAAATCTGGCCAAGTCTGTAACT
GTGGAATGA
Enzyme 3 GenBank Gene ID AB016789 Link Image
Enzyme 3 GeneCard ID GFPT2 Link Image
Enzyme 3 GenAtlas ID GFPT2 Link Image
Enzyme 3 HGNC ID HGNC:4242 Link Image
Enzyme 3 Chromosome Location 5
Enzyme 3 Locus 5q34-q35
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Oki T, Yamazaki K, Kuromitsu J, Okada M, Tanaka I: cDNA cloning and mapping of a novel subtype of glutamine:fructose-6-phosphate amidotransferase (GFAT2) in human and mouse. Genomics. 1999 Apr 15;57(2):227-34. [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. 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]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5480
Enzyme 4 Name 4-aminobutyrate aminotransferase, mitochondrial
Enzyme 4 Synonyms
  1. (S)-3-amino-2-methylpropionate transaminase
  2. GABA aminotransferase
  3. GABA-AT
  4. Gamma-amino-N-butyrate transaminase
  5. GABA transaminase
  6. GABA-T
  7. L-AIBAT
Enzyme 4 Gene Name ABAT
Enzyme 4 Protein Sequence >4-aminobutyrate aminotransferase, mitochondrial
MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMK
QLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQ
NASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYR
SKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPS
FDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGG
DNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMM
TGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLL
DLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVF
RDHHAHLFLNIFSDILADFK
Enzyme 4 Number of Residues 500
Enzyme 4 Molecular Weight 56438.4
Enzyme 4 Theoretical pI 8.04
Enzyme 4 GO Classification
Function
  • 4-aminobutyrate transaminase activity
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular metabolic process
  • gamma-aminobutyric acid metabolic process
  • metabolic process
Component
Enzyme 4 General Function Involved in 4-aminobutyrate transaminase activity
Enzyme 4 Specific Function Catalyzes the conversion of gamma-aminobutyrate and L- beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine
Enzyme 4 Pathways
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 4 Reactions
  • (S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 158254434 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P80404 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name GABT_HUMAN Link Image
Enzyme 4 PDB ID 1OHY Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1503 bp
ATGGCCTCCATGTTGCTCGCCCAGCGCCTGGCCTGCAGCTTCCAGCACAGCTACCGCCTG
CTGGTGCCTGGATCCAGACACATTAGTCAAGCTGCAGCCAAAGTCGACGTTGAATTTGAT
TATGATGGGCCTCTGATGAAGACGGAAGTCCCAGGGCCTAGATCTCAGGAGTTAATGAAA
CAGCTGAATATAATTCAGAATGCAGAGGCTGTGCATTTTTTCTGCAATTACGAAGAGAGC
CGAGGCAATTACCTGGTTGATGTGGACGGCAACCGAATGCTGGATCTTTATTCCCAGATC
TCCTCTGTTCCCATAGGTTACAGCCACCCCGCCCTGCTGAAACTCATCCAACAGCCTCAA
AATGCGAGCATGTTTGTCAACAGACCCGCCCTCGGAATCCTGCCTCCGGAGAACTTTGTG
GAGAAGCTCCGGCAGTCCTTGCTCTCGGTGGCTCCCAAAGGGATGTCCCAGCTCATCACC
ATGGCCTGCGGCTCCTGCTCCAATGAAAACGCCTTAAAGACCATCTTCATGTGGTACCGG
AGCAAGGAAAGAGGGCAGAGGGGCTTCTCCCAGGAGGAGCTGGAGACGTGCATGATTAAC
CAGGCCCCTGGCTGCCCCGACTACAGCATCCTCTCCTTCATGGGCGCGTTCCATGGGAGG
ACCATGGGTTGCTTAGCGACCACGCACTCTAAAGCCATTCACAAGATCGACATCCCTTCC
TTTGACTGGCCCATCGCACCGTTCCCACGGCTGAAATACCCTCTGGAAGAGTTTGTGAAA
GAGAACCAACAGGAGGAGGCCCGCTGTCTGGAAGAGGTGGAGGATCTGATTGTGAAATAT
CGGAAAAAGAAGAAGACGGTGGCCGGGATCATCGTGGAGCCCATCCAGTCCGAGGGTGGA
GACAACCACGCATCCGATGACTTCTTTCGGAAGCTGAGAGACATCGCCAGGAAGCATGGC
TGCGCCTTCTTGGTGGACGAGGTACAGACCGGAGGAGGCTGCACGGGCAAGTTCTGGGCC
CATGAGCACTGGGGCCTGGATGACCCAGCAGACGTGATGACCTTCAGCAAGAAGATGATG
ACTGGGGGCTTCTTCCACAAGGAGGAGTTCAGGCCTAATGCTCCCTACCGGATCTTCAAC
ACCTGGCTGGGGGACCCGTCCAAGAACCTGTTGCTGGCTGAGGTCATCAACATCATCAAG
CGGGAGGACCTGCTAAATAATGCAGCCCATGCCGGGAAGGCCCTGCTCACAGGACTGCTG
GACCTCCAGGCCCGGTACCCCCAGTTCATCAGCAGGGTGAGAGGACGAGGCACCTTTTGC
TCCTTCGATACTCCCGATGATTCCATACGGAATAAGCTCATTTTAATTGCCAGAAACAAA
GGTGTGGTGTTGGGTGGCTGTGGTGACAAATCCATTCGTTTCCGTCCCACGCTGGTCTTC
AGGGATCACCACGCTCACCTGTTCCTCAATATTTTCAGTGACATCTTAGCAGACTTCAAG
TAA
Enzyme 4 GenBank Gene ID AK290501 Link Image
Enzyme 4 GeneCard ID ABAT Link Image
Enzyme 4 GenAtlas ID ABAT Link Image
Enzyme 4 HGNC ID HGNC:23 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 16p13.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Osei YD, Churchich JE: Screening and sequence determination of a cDNA encoding the human brain 4-aminobutyrate aminotransferase. Gene. 1995 Apr 3;155(2):185-7. [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. De Biase D, Barra D, Simmaco M, John RA, Bossa F: Primary structure and tissue distribution of human 4-aminobutyrate aminotransferase. Eur J Biochem. 1995 Jan 15;227(1-2):476-80. [PubMed Link Image]
  5. Medina-Kauwe LK, Tobin AJ, De Meirleir L, Jaeken J, Jakobs C, Nyhan WL, Gibson KM: 4-Aminobutyrate aminotransferase (GABA-transaminase) deficiency. J Inherit Metab Dis. 1999 Jun;22(4):414-27. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5509
Enzyme 5 Name Tyrosine aminotransferase
Enzyme 5 Synonyms
  1. TAT
  2. L-tyrosine:2-oxoglutarate aminotransferase
Enzyme 5 Gene Name TAT
Enzyme 5 Protein Sequence >Tyrosine aminotransferase
MDPYMIQMSSKGNLPSILDVHVNVGGRSSVPGKMKGRKARWSVRPSDMAKKTFNPIRAIV
DNMKVKPNPNKTMISLSIGDPTVFGNLPTDPEVTQAMKDALDSGKYNGYAPSIGFLSSRE
EIASYYHCPEAPLEAKDVILTSGCSQAIDLCLAVLANPGQNILVPRPGFSLYKTLAESMG
IEVKLYNLLPEKSWEIDLKQLEYLIDEKTACLIVNNPSNPCGSVFSKRHLQKILAVAARQ
CVPILADEIYGDMVFSDCKYEPLATLSTDVPILSCGGLAKRWLVPGWRLGWILIHDRRDI
FGNEIRDGLVKLSQRILGPCTIVQGALKSILCRTPGEFYHNTLSFLKSNADLCYGALAAI
PGLRPVRPSGAMYLMVGIEMEHFPEFENDVEFTERLVAEQSVHCLPATCFEYPNFIRVVI
TVPEVMMLEACSRIQEFCEQHYHCAEGSQEECDK
Enzyme 5 Number of Residues 454
Enzyme 5 Molecular Weight 50398.9
Enzyme 5 Theoretical pI 6.24
Enzyme 5 GO Classification
Function
  • 1-aminocyclopropane-1-carboxylate synthase activity
  • L-tyrosine aminotransferase activity
  • L-tyrosine:2-oxoglutarate aminotransferase activity
  • binding
  • carbon-sulfur lyase activity
  • catalytic activity
  • cofactor binding
  • lyase activity
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • aromatic amino acid family catabolic process
  • aromatic amino acid family metabolic process
  • biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid catabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
Component
Enzyme 5 General Function Involved in 1-aminocyclopropane-1-carboxylate synthase activity
Enzyme 5 Specific Function Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has no transaminase activity towards phenylalanine
Enzyme 5 Pathways
Enzyme 5 Reactions
  • L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate [RN:R00734]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 36713 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P17735 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name ATTY_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1365 bp
ATGGACCCATACATGATTCAGATGAGCAGCAAAGGCAACCTCCCCTCAATTCTGGACGTG
CATGTCAACGTTGGTGGGAGAAGCTCTGTGCCGGGAAAAATGAAAGGCAGAAAGGCCAGG
TGGTCTGTGAGGCCCTCAGACATGGCCAAGAAAACTTTCAACCCCATCCGAGCCATTGTG
GACAACATGAAGGTGAAACCAAATCCAAACAAAACCATGATTTCCCTGTCCATTGGGGAC
CCTACTGTGTTTGGAAACCTGCCTACAGACCCTGAAGTTACCCAGGCAATGAAAGATGCC
CTGGACTCGGGCAAATATAATGGCTATGCCCCATCCATCGGCTTCCTATCCAGTCGGGAG
GAGATTGCTTCTTATTACCACTGTCCTGAGGCACCCCTAGAAGCTAAGGACGTCATTCTG
ACAAGTGGCTGCAGCCAAGCTATTGACCTTTGTTTAGCTGTGTTGGCCAACCCAGGGCAG
AACATCCTGGTTCCAAGACCTGGTTTCTCTCTCTACAAGACTCTGGCTGAGTCTATGGGA
ATTGAGGTCAAACTCTACAATTTGTTGCCAGAGAAATCTTGGGAAATTGACCTGAAACAA
CTGGAATATCTAATTGATGAAAAGACAGCTTGTCTCATTGTCAATAATCCATCAAACCCC
TGTGGGTCAGTGTTCAGCAAACGTCATCTTCAGAAGATTCTGGCAGTGGCTGCACGGCAG
TGTGTCCCCATCTTAGCTGATGAGATCTATGGAGACATGGTGTTTTCGGATTGCAAATAT
GAACCACTGGCCACCCTCAGCACCGATGTCCCCATCCTGTCCTGTGGAGGGCTGGCCAAG
CGCTGGCTGGTTCCTGGCTGGAGGTTGGGCTGGATCCTCATTCATGACCGAAGAGACATT
TTTGGCAATGAGATCCGAGATGGGCTGGTGAAGCTGAGTCAGCGCATTTTGGGACCCTGT
ACCATTGTCCAGGGAGCTCTGAAAAGCATCCTATGTCGCACCCCGGGAGAGTTTTACCAC
AACACTCTGAGCTTCCTCAAGTCCAATGCTGATCTCTGTTATGGGGCGTTGGCTGCCATC
CCTGGACTCCGGCCAGTCCGCCCTTCTGGGGCTATGTACCTCATGGTTGGAATTGAGATG
GAACATTTCCCAGAATTTGAGAACGATGTGGAGTTCACGGAGCGGTTAGTTGCTGAGCAG
TCTGTCCACTGCCTCCCAGCAACGTGCTTTGAGTACCCGAATTTCATCCGAGTGGTCATC
ACAGTCCCCGAGGTGATGATGCTGGAGGCGTGCAGCCGGATCCAGGAGTTCTGTGAGCAG
CACTACCATTGTGCTGAAGGCAGCCAGGAGGAGTGTGATAAATAG
Enzyme 5 GenBank Gene ID X52520 Link Image
Enzyme 5 GeneCard ID TAT Link Image
Enzyme 5 GenAtlas ID TAT Link Image
Enzyme 5 HGNC ID HGNC:11573 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 16q22.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Rettenmeier R, Natt E, Zentgraf H, Scherer G: Isolation and characterization of the human tyrosine aminotransferase gene. Nucleic Acids Res. 1990 Jul 11;18(13):3853-61. [PubMed Link Image]
  2. Zelenin SM, Mertvetsov NP: [Nucleotide sequence of the human tyrosine aminotransferase gene] Bioorg Khim. 1994 Feb;20(2):196-204. [PubMed Link Image]
  3. Seralini GE, Luu-The V, Labrie F: Cloning and expression of human tyrosine aminotransferase cDNA. Biochim Biophys Acta. 1995 Jan 2;1260(1):97-101. [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. Sivaraman S, Kirsch JF: The narrow substrate specificity of human tyrosine aminotransferase--the enzyme deficient in tyrosinemia type II. FEBS J. 2006 May;273(9):1920-9. [PubMed Link Image]
  6. Natt E, Kida K, Odievre M, Di Rocco M, Scherer G: Point mutations in the tyrosine aminotransferase gene in tyrosinemia type II. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9297-301. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5515
Enzyme 6 Name Aspartate aminotransferase, cytoplasmic
Enzyme 6 Synonyms
  1. Glutamate oxaloacetate transaminase 1
  2. Transaminase A
Enzyme 6 Gene Name GOT1
Enzyme 6 Protein Sequence >Aspartate aminotransferase, cytoplasmic
MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQK
IANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFL
ARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLEN
APEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWA
IRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPP
AQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGM
FSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ
Enzyme 6 Number of Residues 413
Enzyme 6 Molecular Weight 46247.1
Enzyme 6 Theoretical pI 7.01
Enzyme 6 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
Component
Enzyme 6 General Function Involved in transferase activity, transferring nitrogenous groups
Enzyme 6 Specific Function Plays a key role in amino acid metabolism
Enzyme 6 Pathways
Enzyme 6 Reactions
  • L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate [RN:R00355]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID P17174 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name AATC_HUMAN Link Image
Enzyme 6 PDB ID 1AJS Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1242 bp
ATGGCACCTCCGTCAGTCTTTGCCGAGGTTCCGCAGGCCCAGCCTGTCCTGGTCTTCAAG
CTCACTGCCGACTTCAGGGAGGATCCGGACCCCCGCAAGGTCAACCTGGGAGTGGGAGCA
TATCGCACGGATGACTGCCATCCCTGGGTTTTGCCAGTAGTGAAGAAAGTGGAGCAGAAG
ATTGCTAATGACAATAGCCTAAATCACGAGTATCTGCCAATCCTGGGCCTGGCTGAGTTC
CGGAGCTGTGCTTCTCGTCTTGCCCTTGGGGATGACAGCCCAGCACTCAAGGAGAAGCGG
GTAGGAGGTGTGCAATCTTTGGGGGGAACAGGTGCACTTCGAATTGGAGCTGATTTCTTA
GCGCGTTGGTACAATGGAACAAACAACAAGAACACACCTGTCTATGTGTCCTCACCAACC
TGGGAGAATCACAATGCTGTGTTTTCCGCTGCTGGTTTTAAAGACATTCGGTCCTATCGC
TACTGGGATGCAGAGAAGAGAGGATTGGACCTCCAGGGCTTCCTGAATGATCTGGAGAAT
GCTCCTGAGTTCTCCATTGTTGTCCTCCACGCCTGTGCACACAACCCAACTGGGATTGAC
CCAACTCCGGAGCAGTGGAAGCAGATTGCTTCTGTCATGAAGCACCGGTTTCTGTTCCCC
TTCTTTGACTCAGCCTATCAGGGCTTCGCATCTGGAAACCTGGAGAGAGATGCCTGGGCC
ATTCGCTATTTTGTGTCTGAAGGCTTCGAGTTCTTCTGTGCCCAGTCCTTCTCCAAGAAC
TTCGGGCTCTACAATGAGAGAGTCGGGAATCTGACTGTGGTTGGAAAAGAACCTGAGAGC
ATCCTGCAAGTCCTTTCCCAGATGGAGAAGATCGTGCGGATTACTTGGTCCAATCCCCCC
GCCCAGGGAGCACGAATTGTGGCCAGCACCCTCTCTAACCCTGAGCTCTTTGAGGAATGG
ACAGGTAATGTGAAGACAATGGCTGACCGGATTCTGACCATGAGATCTGAACTCAGGGCA
CGACTAGAAGCCCTCAAAACCCCTGGGACCTGGAACCACATCACTGATCAAATTGGCATG
TTCAGCTTCACTGGGTTGAACCCCAAGCAGGTTGAGTATCTGGTCAATGAAAAGCACATC
TACCTGCTGCCAAGTGGTCGAATCAACGTGAGTGGCTTAACCACCAAAAATCTAGATTAC
GTGGCCACCTCCATCCATGAAGCAGTCACCAAAATCCAGTGA
Enzyme 6 GenBank Gene ID M37400 Link Image
Enzyme 6 GeneCard ID GOT1 Link Image
Enzyme 6 GenAtlas ID GOT1 Link Image
Enzyme 6 HGNC ID HGNC:4432 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 10q24.1-q25.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Bousquet-Lemercier B, Pol S, Pave-Preux M, Hanoune J, Barouki R: Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection. Biochemistry. 1990 Jun 5;29(22):5293-9. [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. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [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. Doyle JM, Schinina ME, Bossa F, Doonan S: The amino acid sequence of cytosolic aspartate aminotransferase from human liver. Biochem J. 1990 Sep 15;270(3):651-7. [PubMed Link Image]
  6. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5516
Enzyme 7 Name Aspartate aminotransferase, mitochondrial
Enzyme 7 Synonyms
  1. mAspAT
  2. Fatty acid-binding protein
  3. FABP-1
  4. Glutamate oxaloacetate transaminase 2
  5. Plasma membrane-associated fatty acid-binding protein
  6. FABPpm
  7. Transaminase A
Enzyme 7 Gene Name GOT2
Enzyme 7 Protein Sequence >Aspartate aminotransferase, mitochondrial
MALLHSGRVLPGIAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKM
NLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEV
LKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYR
YYDPKTCGFDFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFA
FFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADE
AKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADRIIGMRTQLVS
NLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGY
LAHAIHQVTK
Enzyme 7 Number of Residues 430
Enzyme 7 Molecular Weight 47517.3
Enzyme 7 Theoretical pI 9.38
Enzyme 7 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
Component
Enzyme 7 General Function Involved in transferase activity, transferring nitrogenous groups
Enzyme 7 Specific Function Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids
Enzyme 7 Pathways
Enzyme 7 Reactions
  • L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate [RN:R00355]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 62898103 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P00505 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name AATM_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1293 bp
ATGGCCCTGCTGCATTCCGGCCGCGTCCTCCCCGGGATCGCCGCCGCCTTCCACCCGGGC
CTCGCCGCCGCGGCCTCTGCCAGAGCCAGCTCCTGGTGGACCCATGTGGAAATGGGACCT
CCAGATCCCATTCTGGGAGTCACTGAAGCCTTTAAGAGGGACACCAATAGCAAAAAGATG
AATCTGGGAGTTGGTGCCTACCGGGATGATAATGGAAAGCCTTACGTTCTGCCTAGCGTC
CGCAAGGCAGAGGCCCAGATTGCCGCAAAAAATTTGGACAAGGAATACCTGCCCATTGGG
GGACTGGCTGAATTTTGCAAGGCATCTGCAGAACTAGCCCTGGGTGAGAACAGCGAAGTC
TTGAAGAGTGGCCGGTTTGTCACTGTGCAGACCATTTCTGGAACTGGAGCCTTAAGGATC
GGAGCCAGTTTTCTGCAAAGATTTTTTAAGTTCAGCCGAGATGTCTTTCTGCCCAAACCA
ACCTGGGGAAACCACACACCCATCTTCAGGGATGCTGGCATGCAGCTACAAGGTTATCGG
TATTATGACCCCAAGACTTGCGGTTTTGACTTCACAGGCGCTGTGGAGGATATTTCAAAA
ATACCAGAGCAGAGTGTTCTTCTTCTGCATGCCTGCGCCCACAATCCCACGGGAGTGGAC
CCGCGTCCGGAACAGTGGAAGGAAATAGCAACAGTGGTGAAGAAAAGGAATCTCTTTGCG
TTCTTTGACATGGCCTACCAAGGCTTTGCCAGTGGTGATGGTGATAAGGATACCTGGGCT
GTGCGCCACTTCATCGAACAGGGCATTAATGTTTGCCTCTGCCAATCATATGCCAAGAAC
ATGGGCTTATATGGTGAGCGTGTAGGAGCCTTCACTATGGTCTGCAAAGATGCGGATGAA
GCCAAAAGGGTAGAGTCACAGTTGAAGATCTTGATCCGTCCCATGTATTCCAACCCTCCC
CTCAATGGGGCCCGGATTGCTGCTGCCATTCTGAACACCCCAGATTTGCGAAAACAATGG
CTGCAAGAAGTGAAAGTCATGGCTGACCGCATCATTGGCATGCGGACTCAACTGGTCTCC
AACCTCAAGAAGGAGGGTTCCACCCACAATTGGCAACACATCACCGACCAAATTGGCATG
TTCTGTTTCACAGGGCTAAAGCCTGAACAGGTGGAGCGGCTGATCAAGGAGTTCTCCATC
TACATGACAAAAGATGGCCGCATCTCTGTGGCAGGGGTCACCTCCAGCAACGTGGGCTAC
CTTGCCCATGCCATTCACCAGGTCACCAAGTAA
Enzyme 7 GenBank Gene ID AK223271 Link Image
Enzyme 7 GeneCard ID GOT2 Link Image
Enzyme 7 GenAtlas ID GOT2 Link Image
Enzyme 7 HGNC ID HGNC:4433 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 16q21
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Pol S, Bousquet-Lemercier B, Pave-Preux M, Pawlak A, Nalpas B, Berthelot P, Hanoune J, Barouki R: Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA. Biochem Biophys Res Commun. 1988 Dec 30;157(3):1309-15. [PubMed Link Image]
  2. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [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. Martini F, Angelaccio S, Barra D, Pascarella S, Maras B, Doonan S, Bossa F: The primary structure of mitochondrial aspartate aminotransferase from human heart. Biochim Biophys Acta. 1985 Nov 8;832(1):46-51. [PubMed Link Image]
  5. Zhou SL, Gordon RE, Bradbury M, Stump D, Kiang CL, Berk PD: Ethanol up-regulates fatty acid uptake and plasma membrane expression and export of mitochondrial aspartate aminotransferase in HepG2 cells. Hepatology. 1998 Apr;27(4):1064-74. [PubMed Link Image]
  6. Amanchy R, Kalume DE, Iwahori A, Zhong J, Pandey A: Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC). J Proteome Res. 2005 Sep-Oct;4(5):1661-71. [PubMed Link Image]
  7. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  8. 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5536
Enzyme 8 Name Branched-chain-amino-acid aminotransferase, cytosolic
Enzyme 8 Synonyms
  1. BCAT(c)
  2. Protein ECA39
Enzyme 8 Gene Name BCAT1
Enzyme 8 Protein Sequence >Branched-chain-amino-acid aminotransferase, cytosolic
MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTV
EWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRM
YRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTK
ALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDN
GCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQ
WGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPK
LASRILSKLTDIQYGREESDWTIVLS
Enzyme 8 Number of Residues 386
Enzyme 8 Molecular Weight 42965.8
Enzyme 8 Theoretical pI 4.95
Enzyme 8 GO Classification
Function
  • branched-chain-amino-acid transaminase activity
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • branched chain family amino acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
Component
Enzyme 8 General Function Involved in catalytic activity
Enzyme 8 Specific Function Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine
Enzyme 8 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 8 Reactions
  • L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate [RN:R01090]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 38176287 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P54687 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name BCAT1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1161 bp
ATGAAGGATTGCAGTAACGGATGCTCCGCAGAGTGTACCGGAGAAGGAGGATCAAAAGAG
GTGGTGGGGACTTTTAAGGCTAAAGACCTAATAGTCACACCAGCTACCATTTTAAAGGAA
AAACCAGACCCCAATAATCTGGTTTTTGGAACTGTGTTCACGGATCATATGCTGACGGTG
GAGTGGTCCTCAGAGTTTGGATGGGAGAAACCTCATATCAAGCCTCTTCAGAACCTGTCA
TTGCACCCTGGCTCATCAGCTTTGCACTATGCAGTGGAATTATTTGAAGGATTGAAGGCA
TTTCGAGGAGTAGATAATAAAATTCGACTGTTTCAGCCAAACCTCAACATGGATAGAATG
TATCGCTCTGCTGTGAGGGCAACTCTGCCGGTATTTGACAAAGAAGAGCTCTTAGAGTGT
ATTCAACAGCTTGTGAAATTGGATCAAGAATGGGTCCCATATTCAACATCTGCTAGTCTG
TATATTCGTCCTACATTCATTGGAACTGAGCCTTCTCTTGGAGTCAAGAAGCCTACCAAA
GCCCTGCTCTTTGTACTCTTGAGCCCAGTGGGACCTTATTTTTCAAGTGGAACCTTTAAT
CCAGTGTCCCTGTGGGCCAATCCCAAGTATGTAAGAGCCTGGAAAGGTGGAACTGGGGAC
TGCAAGATGGGAGGGAATTACGGCTCATCTCTTTTTGCCCAATGTGAAGCAGTAGATAAT
GGGTGTCAGCAGGTCCTGTGGCTCTATGGAGAGGACCATCAGATCACTGAAGTGGGAACT
ATGAATCTTTTTCTTTACTGGATAAATGAAGATGGAGAAGAAGAACTGGCAACTCCTCCA
CTAGATGGCATCATTCTTCCAGGAGTGACAAGGCGGTGCATTCTGGACCTGGCACATCAG
TGGGGTGAATTTAAGGTGTCAGAGAGATACCTCACCATGGATGACTTGACAACAGCCCTG
GAGGGGAACAGAGTGAGAGAGATGTTTGGCTCTGGTACAGCCTGTGTTGTTTGCCCAGTT
TCTGATATACTGTACAAAGGCGAGACAATACACATTCCAACTATGGAGAATGGTCCTAAG
CTGGCAAGCCGCATCTTGAGCAAATTAACTGATATCCAGTATGGAAGAGAAGAGAGCGAC
TGGACAATTGTGCTATCCTGA
Enzyme 8 GenBank Gene ID NM_005504.6 Link Image
Enzyme 8 GeneCard ID BCAT1 Link Image
Enzyme 8 GenAtlas ID BCAT1 Link Image
Enzyme 8 HGNC ID HGNC:976 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 12p12.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Schuldiner O, Eden A, Ben-Yosef T, Yanuka O, Simchen G, Benvenisty N: ECA39, a conserved gene regulated by c-Myc in mice, is involved in G1/S cell cycle regulation in yeast. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7143-8. [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. Scherer SE, Muzny DM, 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, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  4. 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]
  5. Goto M, Miyahara I, Hirotsu K, Conway M, Yennawar N, Islam MM, Hutson SM: Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin. J Biol Chem. 2005 Nov 4;280(44):37246-56. Epub 2005 Sep 1. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5633
Enzyme 9 Name Alanine--glyoxylate aminotransferase 2, mitochondrial
Enzyme 9 Synonyms
  1. AGT 2
  2. (R)-3-amino-2-methylpropionate--pyruvate transaminase
  3. Beta-ALAAT II
  4. Beta-alanine-pyruvate aminotransferase
  5. D-AIBAT
Enzyme 9 Gene Name AGXT2
Enzyme 9 Protein Sequence >Alanine--glyoxylate aminotransferase 2, mitochondrial
MTLIWRHLLRPLCLVTSAPRILEMHPFLSLGTSRTSVTKLSLHTKPRMPPCDFMPERYQS
LGYNRVLEIHKEHLSPVVTAYFQKPLLLHQGHMEWLFDAEGSRYLDFFSGIVTVSVGHCH
PKVNAVAQKQLGRLWHTSTVFFHPPMHEYAEKLAALLPEPLKVIFLVNSGSEANELAMLM
ARAHSNNIDIISFRGAYHGCSPYTLGLTNVGTYKMELPGGTGCQPTMCPDVFRGPWGGSH
CRDSPVQTIRKCSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVNGVVQYPK
GFLKEAFELVRARGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAA
VITTPEIAKSLAKCLQHFNTFGGNPMACAIGSAVLEVIKEENLQENSQEVGTYMLLKFAK
LRDEFEIVGDVRGKGLMIGIEMVQDKISCRPLPREEVNQIHEDCKHMGLLVGRGSIFSQT
FRIAPSMCITKPEVDFAVEVFRSALTQHMERRAK
Enzyme 9 Number of Residues 514
Enzyme 9 Molecular Weight 57155.9
Enzyme 9 Theoretical pI 7.91
Enzyme 9 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
Component
Enzyme 9 General Function Involved in transaminase activity
Enzyme 9 Specific Function L-alanine + glyoxylate = pyruvate + glycine
Enzyme 9 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 9 Reactions
  • L-alanine + glyoxylate = pyruvate + glycine [RN:R00369]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 12406973 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9BYV1 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name AGT2_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1545 bp
ATGACTCTAATCTGGAGACATTTGCTGAGACCCTTGTGCCTGGTCACTTCCGCTCCCAGG
ATCCTTGAGATGCATCCTTTCCTGAGCCTAGGTACTTCCCGGACATCAGTAACCAAGCTC
AGTCTTCATACAAAGCCCAGAATGCCTCCATGTGACTTCATGCCTGAAAGATACCAGTCC
CTTGGCTACAACCGTGTCCTGGAAATCCACAAGGAACATCTTTCTCCTGTGGTGACGGCA
TATTTCCAGAAACCCCTGCTGCTCCACCAGGGGCACATGGAGTGGCTCTTTGATGCTGAA
GGAAGCAGATACCTGGATTTCTTTTCCGGGATTGTTACTGTCAGTGTTGGCCATTGCCAC
CCAAAGGTGAATGCAGTGGCACAAAAGCAGCTCGGCCGCCTGTGGCATACAAGCACCGTC
TTCTTCCACCCTCCAATGCATGAATATGCAGAGAAGCTTGCCGCACTTCTTCCTGAGCCT
CTTAAGGTCATTTTCTTGGTGAACAGTGGCTCAGAAGCCAATGAGCTGGCCATGCTGATG
GCCAGGGCGCACTCAAACAACATAGACATCATTTCTTTCAGAGGAGCCTACCATGGATGC
AGTCCTTACACACTTGGCTTGACAAACGTAGGGACCTACAAGATGGAACTCCCTGGTGGG
ACAGGTTGCCAACCAACAATGTGTCCAGATGTTTTTCGTGGCCCTTGGGGAGGAAGCCAC
TGTCGAGATTCTCCAGTGCAAACAATCAGGAAGTGCAGCTGTGCACCAGACTGCTGCCAA
GCTAAAGATCAGTATATTGAGCAATTCAAAGATACGCTGAGCACATCTGTGGCCAAGTCA
ATTGCTGGATTTTTCGCAGAACCTATTCAAGGTGTGAATGGAGTTGTCCAGTACCCAAAG
GGGTTTCTAAAGGAAGCCTTTGAGCTGGTGCGAGCAAGGGGAGGCGTGTGCATTGCAGAT
GAAGTGCAGACAGGATTTGGAAGGTTGGGCTCTCACTTCTGGGGCTTCCAAACCCACGAT
GTCCTGCCTGACATTGTCACCATGGCTAAAGGGATTGGGAATGGCTTTCCCATGGCAGCA
GTCATAACCACTCCAGAGATTGCCAAATCTTTGGCGAAATGCCTGCAGCACTTCAACACC
TTTGGAGGGAACCCCATGGCCTGTGCCATTGGATCTGCTGTGCTTGAGGTGATTAAAGAA
GAAAATCTACAGGAAAACAGTCAAGAAGTTGGGACCTACATGTTACTAAAGTTTGCTAAG
CTGCGGGATGAATTTGAAATTGTTGGAGACGTCCGAGGCAAAGGTCTCATGATAGGCATA
GAAATGGTGCAGGATAAGATAAGCTGTCGGCCTCTTCCCCGTGAAGAAGTAAATCAGATC
CATGAGGACTGCAAGCACATGGGACTCCTCGTTGGCAGAGGCAGCATTTTTTCTCAGACA
TTTCGCATTGCGCCCTCAATGTGCATCACTAAACCAGAAGTTGATTTTGCAGTAGAAGTA
TTTCGTTCTGCCTTAACCCAACACATGGAAAGAAGAGCTAAGTAA
Enzyme 9 GenBank Gene ID AJ292204 Link Image
Enzyme 9 GeneCard ID AGXT2 Link Image
Enzyme 9 GenAtlas ID AGXT2 Link Image
Enzyme 9 HGNC ID HGNC:14412 Link Image
Enzyme 9 Chromosome Location 5
Enzyme 9 Locus 5p13
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. 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 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5637
Enzyme 10 Name Ornithine aminotransferase, mitochondrial
Enzyme 10 Synonyms
  1. Ornithine delta-aminotransferase
  2. Ornithine--oxo-acid aminotransferase
  3. Ornithine aminotransferase, hepatic form
  4. Ornithine aminotransferase, renal form
Enzyme 10 Gene Name OAT
Enzyme 10 Protein Sequence >Ornithine aminotransferase, mitochondrial
MFSKLAHLQRFAVLSRGVHSSVASATSVATKKTVQGPPTSDDIFEREYKYGAHNYHPLPV
ALERGKGIYLWDVEGRKYFDFLSSYSAVNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVL
GEYEEYITKLFNYHKVLPMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGR
TLSAISSSTDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGEAGVVV
PDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRPDIVLLGKALSGGLYP
VSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIAALEVLEEENLAENADKLGIILRNEL
MKLPSDVVTAVRGKGLLNAIVIKETKDWDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVI
KEDELRESIEIINKTILSF
Enzyme 10 Number of Residues 439
Enzyme 10 Molecular Weight 48534.4
Enzyme 10 Theoretical pI 7.05
Enzyme 10 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
Component
Enzyme 10 General Function Involved in transaminase activity
Enzyme 10 Specific Function L-ornithine + a 2-oxo acid = L-glutamate 5- semialdehyde + an L-amino acid
Enzyme 10 Pathways
Enzyme 10 Reactions
  • L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid [RN:R01343]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 189069120 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P04181 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name OAT_HUMAN Link Image
Enzyme 10 PDB ID 1OAT Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1320 bp
ATGTTTTCCAAACTAGCACATTTGCAGAGGTTTGCTGTACTTAGTCGCGGAGTTCATTCT
TCAGTGGCTTCTGCTACATCTGTTGCAACTAAAAAAACAGTCCAAGGCCCTCCAACCTCT
GATGACATTTTTGAAAGGGAATATAAGTATGGTGCACACAACTACCATCCTTTACCTGTA
GCCCTGGAGAGAGGAAAAGGTATTTACTTATGGGATGTAGAAGGCAGAAAATATTTTGAC
TTCCTGAGTTCTTACAGTGCTGTCAACCAAGGGCATTGTCACCCCAAGATTGTGAATGCT
CTGAAGAGTCAAGTGGACAAATTGACCTTAACATCTAGAGCTTTCTATAATAACGTACTT
GGTGAATATGAGGAGTATATTACTAAACTTTTCAACTACCACAAAGTTCTTCCTATGAAT
ACAGGAGTGGAGGCTGGAGAGACTGCCTGTAAACTAGCTCGTAAGTGGGGCTATACCGTG
AAGGGCATTCAGAAATACAAAGCAAAGATTGTTTTTGCAGCTGGGAACTTCTGGGGTAGG
ACGTTGTCTGCTATCTCCAGTTCCACAGACCCAACCAGTTACGATGGTTTTGGACCATTT
ATGCCGGGATTCGACATCATTCCCTATAATGATCTGCCCGCACTGGAGCGTGCTCTTCAG
GATCCAAATGTGGCTGCGTTCATGGTAGAACCAATTCAGGGTGAAGCAGGCGTTGTTGTT
CCGGATCCAGGTTACCTAATGGGAGTGCGAGAGCTCTGCACCAGGCACCAGGTTCTCTTT
ATTGCTGATGAAATACAGACAGGATTGGCCAGAACTGGTAGATGGCTGGCTGTTGATTAT
GAAAATGTCAGACCTGATATAGTCCTCCTTGGAAAGGCCCTTTCTGGGGGCTTATACCCT
GTGTCTGCAGTGCTGTGTGATGATGACATCATGCTGACCATTAAGCCAGGGGAGCATGGG
TCCACATACGGTGGCAATCCACTAGGCTGCCGAGTGGCCATCGCAGCCCTTGAGGTTTTA
GAAGAAGAAAACCTTGCTGAAAATGCAGACAAATTGGGCATTATCTTGAGAAATGAACTC
ATGAAGCTACCTTCTGATGTTGTAACTGCCGTAAGAGGAAAAGGATTATTAAATGCTATT
GTCATTAAAGAAACCAAAGATTGGGATGCTTGGAAGGTGTGTCTACGACTTCGAGATAAT
GGACTTCTGGCCAAGCCAACCCATGGCGACATTATCAGGTTTGCGCCTCCGCTGGTGATC
AAGGAGGATGAGCTTCGAGAGTCCATTGAAATTATTAACAAGACCATCTTGTCTTTCTGA
Enzyme 10 GenBank Gene ID AK312561 Link Image
Enzyme 10 GeneCard ID OAT Link Image
Enzyme 10 GenAtlas ID OAT Link Image
Enzyme 10 HGNC ID HGNC:8091 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 10q26
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Inana G, Totsuka S, Redmond M, Dougherty T, Nagle J, Shiono T, Ohura T, Kominami E, Katunuma N: Molecular cloning of human ornithine aminotransferase mRNA. Proc Natl Acad Sci U S A. 1986 Mar;83(5):1203-7. [PubMed Link Image]
  2. Ramesh V, Shaffer MM, Allaire JM, Shih VE, Gusella JF: Investigation of gyrate atrophy using a cDNA clone for human ornithine aminotransferase. DNA. 1986 Dec;5(6):493-501. [PubMed Link Image]
  3. Kobayashi T, Nishii M, Takagi Y, Titani K, Matsuzawa T: Molecular cloning and nucleotide sequence analysis of mRNA for human kidney ornithine aminotransferase. An examination of ornithine aminotransferase isozymes between liver and kidney. FEBS Lett. 1989 Sep 25;255(2):300-4. [PubMed Link Image]
  4. Mitchell GA, Looney JE, Brody LC, Steel G, Suchanek M, Engelhardt JF, Willard HF, Valle D: Human ornithine-delta-aminotransferase. cDNA cloning and analysis of the structural gene. J Biol Chem. 1988 Oct 5;263(28):14288-95. [PubMed Link Image]
  5. Zintz CB, Inana G: Analysis of the human ornithine aminotransferase gene family. Exp Eye Res. 1990 Jun;50(6):759-70. [PubMed Link Image]
  6. 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]
  7. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  8. 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]
  9. Ramesh V, Gusella JF, Shih VE: Molecular pathology of gyrate atrophy of the choroid and retina due to ornithine aminotransferase deficiency. Mol Biol Med. 1991 Feb;8(1):81-93. [PubMed Link Image]
  10. Simmaco M, John RA, Barra D, Bossa F: The primary structure of ornithine aminotransferase. Identification of active-site sequence and site of post-translational proteolysis. FEBS Lett. 1986 Apr 7;199(1):39-42. [PubMed Link Image]
  11. Shah SA, Shen BW, Brunger AT: Human ornithine aminotransferase complexed with L-canaline and gabaculine: structural basis for substrate recognition. Structure. 1997 Aug 15;5(8):1067-75. [PubMed Link Image]
  12. Shen BW, Hennig M, Hohenester E, Jansonius JN, Schirmer T: Crystal structure of human recombinant ornithine aminotransferase. J Mol Biol. 1998 Mar 20;277(1):81-102. [PubMed Link Image]
  13. Storici P, Capitani G, Muller R, Schirmer T, Jansonius JN: Crystal structure of human ornithine aminotransferase complexed with the highly specific and potent inhibitor 5-fluoromethylornithine. J Mol Biol. 1999 Jan 8;285(1):297-309. [PubMed Link Image]
  14. Ramesh V, McClatchey AI, Ramesh N, Benoit LA, Berson EL, Shih VE, Gusella JF: Molecular basis of ornithine aminotransferase deficiency in B-6-responsive and -nonresponsive forms of gyrate atrophy. Proc Natl Acad Sci U S A. 1988 Jun;85(11):3777-80. [PubMed Link Image]
  15. Inana G, Chambers C, Hotta Y, Inouye L, Filpula D, Pulford S, Shiono T: Point mutation affecting processing of the ornithine aminotransferase precursor protein in gyrate atrophy. J Biol Chem. 1989 Oct 15;264(29):17432-6. [PubMed Link Image]
  16. Michaud J, Brody LC, Steel G, Fontaine G, Martin LS, Valle D, Mitchell G: Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene. Genomics. 1992 Jun;13(2):389-94. [PubMed Link Image]
  17. Brody LC, Mitchell GA, Obie C, Michaud J, Steel G, Fontaine G, Robert MF, Sipila I, Kaiser-Kupfer M, Valle D: Ornithine delta-aminotransferase mutations in gyrate atrophy. Allelic heterogeneity and functional consequences. J Biol Chem. 1992 Feb 15;267(5):3302-7. [PubMed Link Image]
  18. Michaud J, Thompson GN, Brody LC, Steel G, Obie C, Fontaine G, Schappert K, Keith CG, Valle D, Mitchell GA: Pyridoxine-responsive gyrate atrophy of the choroid and retina: clinical and biochemical correlates of the mutation A226V. Am J Hum Genet. 1995 Mar;56(3):616-22. [PubMed Link Image]
  19. Kobayashi T, Ogawa H, Kasahara M, Shiozawa Z, Matsuzawa T: A single amino acid substitution within the mature sequence of ornithine aminotransferase obstructs mitochondrial entry of the precursor. Am J Hum Genet. 1995 Aug;57(2):284-91. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5759
Enzyme 11 Name Glutamate--cysteine ligase catalytic subunit
Enzyme 11 Synonyms
  1. GCS heavy chain
  2. Gamma-ECS
  3. Gamma-glutamylcysteine synthetase
Enzyme 11 Gene Name GCLC
Enzyme 11 Protein Sequence >Glutamate--cysteine ligase catalytic subunit
MGLLSQGSPLSWEETKRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDH
ENKKVRLVLSGEKVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTV
EANMRKRRKEATSILEENQALCTITSFPRLGCPGFTLPEVKPNPVEGGASKSLFFPDEAI
NKHPRFSTLTRNIRHRRGEKVVINVPIFKDKNTPSPFIETFTEDDEASRASKPDHIYMDA
MGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVI
SASVDDRTREERGLEPLKNNNYRISKSRYDSIDSYLSKCGEKYNDIDLTIDKEIYEQLLQ
EGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDI
GWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQKRDAVL
QGMFYFRKDICKGGNAVVDGCGKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNS
YLENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYS
LILKCNQIANELCECPELLGSAFRKVKYSGSKTDSSN
Enzyme 11 Number of Residues 637
Enzyme 11 Molecular Weight 72765.1
Enzyme 11 Theoretical pI 5.98
Enzyme 11 GO Classification
Function
  • acid-amino acid ligase activity
  • catalytic activity
  • glutamate-cysteine ligase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular metabolic process
  • glutathione biosynthetic process
  • glutathione metabolic process
  • metabolic process
  • peptide metabolic process
Component
Enzyme 11 General Function Involved in glutamate-cysteine ligase activity
Enzyme 11 Specific Function ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
Enzyme 11 Pathways
Enzyme 11 Reactions
  • ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine [RN:R00894]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID P48506 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name GSH1_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1914 bp
ATGGGGCTGCTGTCCCAGGGCTCGCCGCTGAGCTGGGAGGAAACCAAGCGCCATGCCGAC
CACGTGCGGCGGCACGGGATCCTCCAGTTCCTGCACATCTACCACGCCGTCAAGGACCGG
CACAAGGACGTTCTCAAGTGGGGCGATGAGGTGGAATACATGTTGGTATCTTTTGATCAT
GAAAATAAAAAAGTCCGGTTGGTCCTGTCTGGGGAGAAAGTTCTTGAAACTCTGCAAGAG
AAGGGGGAAAGGACAAACCCAAACCATCCTACCCTTTGGAGACCAGAGTATGGGAGTTAC
ATGATTGAAGGGACACCAGGACAGCCCTACGGAGGAACAATGTCCGAGTTCAATACAGTT
GAGGCCAACATGCGAAAACGCCGGAAGGAGGCTACTTCTATATTAGAAGAAAATCAGGCT
CTTTGCACAATAACTTCATTTCCCAGATTAGGCTGTCCTGGGTTCACACTGCCCGAGGTC
AAACCCAACCCAGTGGAAGGAGGAGCTTCCAAGTCCCTCTTCTTTCCAGATGAAGCAATA
AACAAGCACCCTCGCTTCAGTACCTTAACAAGAAATATCCGACATAGGAGAGGAGAAAAG
GTTGTCATCAATGTACCAATATTTAAGGACAAGAATACACCATCTCCATTTATAGAAACA
TTTACTGAGGATGATGAAGCTTCAAGGGCTTCTAAGCCGGATCATATTTACATGGATGCC
ATGGGATTTGGAATGGGCAATTGCTGTCTCCAGGTGACATTCCAAGCCTGCAGTATATCT
GAGGCCAGATACCTTTATGATCAGTTGGCTACTATCTGTCCAATTGTTATGGCTTTGAGT
GCTGCATCTCCCTTTTACCGAGGCTATGTGTCAGACATTGATTGTCGCTGGGGAGTGATT
TCTGCATCTGTAGATGATAGAACTCGGGAGGAGCGAGGACTGGAGCCATTGAAGAACAAT
AACTATAGGATCAGTAAATCCCGATATGACTCAATAGACAGCTATTTATCTAAGTGTGGT
GAGAAATATAATGACATCGACTTGACGATAGATAAAGAGATCTACGAACAGCTGTTGCAG
GAAGGCATTGATCATCTCCTGGCCCAGCATGTTGCTCATCTCTTTATTAGAGACCCACTG
ACACTGTTTGAAGAGAAAATACACCTGGATGATGCTAATGAGTCTGACCATTTTGAGAAT
ATTCAGTCCACAAATTGGCAGACAATGAGATTTAAGCCCCCTCCTCCAAACTCAGACATT
GGATGGAGAGTAGAATTTCGACCCATGGAGGTGCAATTAACAGACTTTGAGAACTCTGCC
TATGTGGTGTTTGTGGTACTGCTCACCAGAGTGATCCTTTCCTACAAATTGGATTTTCTC
ATTCCACTGTCAAAGGTTGATGAGAACATGAAGGTAGCACAGAAAAGAGATGCTGTCTTG
CAGGGAATGTTTTATTTCAGGAAAGATATTTGCAAAGGTGGCAATGCAGTGGTGGATGGT
TGTGGCAAGGCCCAGAACAGCACGGAGCTCGCTGCAGAGGAGTACACCCTCATGAGCATA
GACACCATCATCAATGGGAAGGAAGGTGTGTTTCCTGGACTGATCCCAATTCTGAACTCT
TACCTTGAAAACATGGAAGTGGATGTGGACACCAGATGTAGTATTCTGAACTACCTAAAG
CTAATTAAGAAGAGAGCATCTGGAGAACTAATGACAGTTGCCAGATGGATGAGGGAGTTT
ATCGCAAACCATCCTGACTACAAGCAAGACAGTGTCATAACTGATGAAATGAATTATAGC
CTTATTTTGAAGTGTAACCAAATTGCAAATGAATTATGTGAATGCCCAGAGTTACTTGGA
TCAGCATTTAGGAAAGTAAAATATAGTGGAAGTAAAACTGACTCATCCAACTAG
Enzyme 11 GenBank Gene ID M90656 Link Image
Enzyme 11 GeneCard ID GCLC Link Image
Enzyme 11 GenAtlas ID GCLC Link Image
Enzyme 11 HGNC ID HGNC:4311 Link Image
Enzyme 11 Chromosome Location 6
Enzyme 11 Locus 6p12
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Gipp JJ, Chang C, Mulcahy RT: Cloning and nucleotide sequence of a full-length cDNA for human liver gamma-glutamylcysteine synthetase. Biochem Biophys Res Commun. 1992 May 29;185(1):29-35. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Mulcahy RT, Gipp JJ: Identification of a putative antioxidant response element in the 5'-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene. Biochem Biophys Res Commun. 1995 Apr 6;209(1):227-33. [PubMed Link Image]
  5. Beutler E, Gelbart T, Kondo T, Matsunaga AT: The molecular basis of a case of gamma-glutamylcysteine synthetase deficiency. Blood. 1999 Oct 15;94(8):2890-4. [PubMed Link Image]
  6. Misra I, Griffith OW: Expression and purification of human gamma-glutamylcysteine synthetase. Protein Expr Purif. 1998 Jul;13(2):268-76. [PubMed Link Image]
  7. Ristoff E, Augustson C, Geissler J, de Rijk T, Carlsson K, Luo JL, Andersson K, Weening RS, van Zwieten R, Larsson A, Roos D: A missense mutation in the heavy subunit of gamma-glutamylcysteine synthetase gene causes hemolytic anemia. Blood. 2000 Apr 1;95(7):2193-6. [PubMed Link Image]
  8. Hamilton D, Wu JH, Alaoui-Jamali M, Batist G: A novel missense mutation in the gamma-glutamylcysteine synthetase catalytic subunit gene causes both decreased enzymatic activity and glutathione production. Blood. 2003 Jul 15;102(2):725-30. Epub 2003 Mar 27. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5762
Enzyme 12 Name N-acetylglutamate synthase, mitochondrial
Enzyme 12 Synonyms
  1. Amino-acid acetyltransferase
  2. N-acetylglutamate synthase long form
  3. N-acetylglutamate synthase short form
  4. N-acetylglutamate synthase conserved domain form
Enzyme 12 Gene Name NAGS
Enzyme 12 Protein Sequence >N-acetylglutamate synthase, mitochondrial
MATALMAVVLRAAAVAPRLRGRGGTGGARRLSCGARRRAARGTSPGRRLSTAWSQPQPPP
EEYAGADDVSQSPVAEEPSWVPSPRPPVPHESPEPPSGRSLVQRDIQAFLNQCGASPGEA
RHWLTQFQTCHHSADKPFAVIEVDEEVLKCQQGVSSLAFALAFLQRMDMKPLVVLGLPAP
TAPSGCLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVS
VETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLR
DSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVITAASTLLTE
LFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLASLRPRLHSIYV
SEGYNAAAILTMEPVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNP
INPWYFKHSDGSFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSFHKPASDPGS
Enzyme 12 Number of Residues 534
Enzyme 12 Molecular Weight 58155.8
Enzyme 12 Theoretical pI 9.12
Enzyme 12 GO Classification
Function
  • N-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • arginine biosynthetic process
  • arginine metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid biosynthetic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glutamine family amino acid metabolic process
  • metabolic process
Component
Enzyme 12 General Function Involved in N-acetyltransferase activity
Enzyme 12 Specific Function Plays a role in the regulation of ureagenesis by producing variable amounts of N-acetylglutamate (NAG), thus modulating carbamoylphosphate synthase I (CPSI) activity
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate [RN:R00259]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 22651771 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q8N159 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name NAGS_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1605 bp
ATGGCGACGGCGCTGATGGCTGTGGTTCTGCGGGCAGCTGCTGTAGCCCCGAGGCTGAGA
GGCCGGGGAGGCACTGGGGGCGCCCGAAGGCTGAGCTGTGGCGCGCGGCGGCGGGCGGCG
AGGGGCACCAGCCCGGGGCGCCGGCTCAGCACCGCCTGGTCGCAGCCCCAGCCCCCGCCC
GAGGAGTACGCGGGCGCGGACGACGTCTCCCAGTCGCCCGTCGCCGAGGAGCCGTCGTGG
GTGCCGAGTCCCAGGCCCCCGGTGCCCCACGAGTCCCCAGAGCCTCCTTCGGGCCGCTCG
CTGGTGCAGCGGGACATCCAGGCCTTCCTGAACCAGTGCGGGGCCAGCCCTGGGGAGGCG
CGCCACTGGCTCACGCAGTTCCAGACCTGCCATCACTCCGCGGACAAGCCCTTCGCCGTC
ATCGAGGTGGACGAGGAGGTGCTCAAGTGCCAGCAGGGCGTATCCAGTCTGGCCTTTGCC
CTGGCCTTCTTGCAGCGCATGGACATGAAGCCGCTGGTGGTCCTGGGGCTGCCGGCCCCT
ACGGCTCCCTCGGGCTGTCTTTCCTTCTGGGAGGCCAAGGCGCAGCTGGCCAAGAGCTGC
AAGGTGCTGGTAGACGCGCTTCGACACAACGCCGCCGCTGCTGTGCCATTTTTTGGCGGC
GGGTCTGTGCTACGCGCTGCCGAGCCGGCTCCCCATGCCAGCTACGGCGGCATCGTCTCG
GTGGAGACAGACCTGCTGCAGTGGTGCCTGGAGTCGGGCAGCATCCCCATCCTGTGCCCC
ATCGGGGAGACGGCCGCGCGCCGCTCCGTGCTTCTCGACTCCCTGGAGGTGACCGCGTCG
CTGGCCAAGGCGCTGCGGCCCACCAAAATCATCTTCCTCAATAACACAGGCGGCCTGCGC
GACAGCAGTCATAAGGTCCTGAGTAACGTGAACCTGCCCGCCGACCTGGACCTGGTGTGC
AACGCCGAGTGGGTGAGCACAAAAGAACGGCAGCAGATGCGGCTCATCGTGGACGTGCTC
AGCCGCCTGCCCCACCACTCCTCGGCCGTCATCACCGCCGCTAGCACGCTGCTCACTGAG
CTCTTTAGCAACAAGGGGTCCGGGACCCTGTTCAAGAACGCCGAGCGAATGCTACGGGTG
CGCAGCCTGGACAAGCTGGACCAGGGCCGTCTAGTGGACCTGGTCAACGCCAGCTTCGGC
AAGAAGCTCAGGGACGACTACCTGGCCTCGCTGCGCCCGCGGCTGCACTCCATCTACGTC
TCCGAGGGGTACAACGCCGCCGCCATTCTGACCATGGAGCCCGTCCTGGGGGGCACCCCG
TACCTGGACAAATTTGTGGTGAGCTCCAGCCGCCAGGGCCAAGGCTCCGGCCAGATGCTG
TGGGAGTGCCTGCGGCGGGACCTTCAGACACTTTTCTGGCGCTCCCGGGTCACCAACCCC
ATCAATCCCTGGTACTTCAAACACAGTGATGGCAGCTTCTCCAACAAGCAGTGGATCTTC
TTCTGGTTTGGCCTGGCTGATATCCGGGACTCCTATGAGTTGGTCAACCACGCCAAGGGA
CTGCCAGACTCCTTTCACAAGCCAGCTTCTGACCCAGGCAGCTGA
Enzyme 12 GenBank Gene ID AY116538 Link Image
Enzyme 12 GeneCard ID NAGS Link Image
Enzyme 12 GenAtlas ID NAGS Link Image
Enzyme 12 HGNC ID HGNC:17996 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 17q21.31
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Haberle J, Schmidt E, Pauli S, Kreuder JG, Plecko B, Galler A, Wermuth B, Harms E, Koch HG: Mutation analysis in patients with N-acetylglutamate synthase deficiency. Hum Mutat. 2003 Jun;21(6):593-7. [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. Caldovic L, Morizono H, Gracia Panglao M, Gallegos R, Yu X, Shi D, Malamy MH, Allewell NM, Tuchman M: Cloning and expression of the human N-acetylglutamate synthase gene. Biochem Biophys Res Commun. 2002 Dec 13;299(4):581-6. [PubMed Link Image]
  4. Schmidt E, Nuoffer JM, Haberle J, Pauli S, Guffon N, Vianey-Saban C, Wermuth B, Koch HG: Identification of novel mutations of the human N-acetylglutamate synthase gene and their functional investigation by expression studies. Biochim Biophys Acta. 2005 Apr 15;1740(1):54-9. Epub 2005 Feb 24. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5763
Enzyme 13 Name Branched-chain-amino-acid aminotransferase, mitochondrial
Enzyme 13 Synonyms
  1. BCAT(m)
  2. Placental protein 18
  3. PP18
Enzyme 13 Gene Name BCAT2
Enzyme 13 Protein Sequence >Branched-chain-amino-acid aminotransferase, mitochondrial
MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKT
FTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRP
WLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSL
GVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLV
QQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQS
LLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIP
TMENGPELILRFQKELKEIQYGIRAHEWMFPV
Enzyme 13 Number of Residues 392
Enzyme 13 Molecular Weight 44287.4
Enzyme 13 Theoretical pI 8.82
Enzyme 13 GO Classification
Function
  • branched-chain-amino-acid transaminase activity
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • branched chain family amino acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
Component
Enzyme 13 General Function Involved in catalytic activity
Enzyme 13 Specific Function Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids
Enzyme 13 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 13 Reactions
  • L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate [RN:R01090]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 13699234 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID O15382 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name BCAT2_HUMAN Link Image
Enzyme 13 PDB ID 1KTA Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1179 bp
ATGGCCGCAGCCGCTCTGGGGCAGATCTGGGCACGAAAGCTTCTCTCTGTCCCTTGGCTT
CTGTGTGGTCCCAGAAGATATGCCTCCTCCAGTTTCAAGGCTGCAGACCTGCAGCTGGAA
ATGACACAGAAGCCTCATAAGAAGCCTGGCCCCGGCGAGCCCCTGGTGTTTGGGAAGACA
TTTACCGACCACATGCTGATGGTGGAATGGAATGACAAGGGCTGGGGCCAGCCCCGAATC
CAGCCCTTCCAGAACCTCACGCTGCACCCAGCCTCCTCCAGCCTCCACTACTCCCTGCAG
CTGTTTGAGGGCATGAAGGCGTTCAAAGGCAAAGACCAGCAGGTGCGCCTCTTCCGCCCC
TGGCTCAACATGGACCGGATGCTGCGCTCAGCCATGCGCCTGTGCCTGCCGAGTTTCGAC
AAGCTGGAGTTGCTGGAGTGCATCCGCCGGCTCATCGAAGTGGACAAGGACTGGGTCCCC
GATGCCGCCGGCACCAGCCTCTATGTGCGGCCTGTGCTCATTGGGAACGAGCCCTCGCTG
GGTGTCAGCCAGCCCACGCGCGCGCTCCTGTTCGTCATTCTCTGCCCAGTGGGTGCCTAC
TTCCCTGGAGGCTCCGTGACCCCGGTCTCCCTCCTGGCCGACCCAGCCTTCATCCGGGCC
TGGGTGGGCGGGGTCGGCAACTACAAGTTAGGTGGGAATTATGGGCCCACCGTGTTAGTG
CAACAGGAGGCACTCAAGCGGGGCTGTGAACAGGTCCTCTGGCTGTATGGGCCCGACCAC
CAGCTCACCGAGGTGGGAACCATGAACATCTTTGTCTACTGGACCCACGAAGATGGGGTG
CTGGAGCTGGTGACGCCCCCGCTGAATGGTGTTATCCTGCCTGGAGTGGTCAGACAGAGT
CTACTGGACATGGCTCAGACCTGGGGTGAGTTCCGGGTGGTGGAGCGCACGATCACCATG
AAGCAGTTGCTGCGGGCCCTGGAGGAGGGCCGCGTGCGGGAAGTCTTTGGCTCGGGCACC
GCTTGCCAGGTCTGCCCAGTGCACCGAATCCTGTACAAAGACAGGAACCTCCACATTCCC
ACCATGGAAAATGGGCCTGAGCTGATCCTCCGCTTCCAGAAGGAGCTGAAGGAGATCCAG
TACGGAATCAGAGCCCACGAGTGGATGTTCCCGGTGTGA
Enzyme 13 GenBank Gene ID AF268047 Link Image
Enzyme 13 GeneCard ID BCAT2 Link Image
Enzyme 13 GenAtlas ID BCAT2 Link Image
Enzyme 13 HGNC ID HGNC:977 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 19q13
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Bledsoe RK, Dawson PA, Hutson SM: Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm). Biochim Biophys Acta. 1997 Apr 25;1339(1):9-13. [PubMed Link Image]
  2. Than NG, Sumegi B, Than GN, Bellyei S, Bohn H: Molecular cloning and characterization of placental tissue protein 18 (PP18a)/human mitochondrial branched-chain aminotransferase (BCATm) and its novel alternatively spliced PP18b variant. Placenta. 2001 Feb-Mar;22(2-3):235-43. [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. 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. Eden A, Simchen G, Benvenisty N: Two yeast homologs of ECA39, a target for c-Myc regulation, code for cytosolic and mitochondrial branched-chain amino acid aminotransferases. J Biol Chem. 1996 Aug 23;271(34):20242-5. [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]
  7. Yennawar N, Dunbar J, Conway M, Hutson S, Farber G: The structure of human mitochondrial branched-chain aminotransferase. Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):506-15. [PubMed Link Image]
  8. Yennawar NH, Conway ME, Yennawar HP, Farber GK, Hutson SM: Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms. Biochemistry. 2002 Oct 1;41(39):11592-601. [PubMed Link Image]
  9. Goto M, Miyahara I, Hirotsu K, Conway M, Yennawar N, Islam MM, Hutson SM: Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin. J Biol Chem. 2005 Nov 4;280(44):37246-56. Epub 2005 Sep 1. [PubMed Link Image]
  10. Yennawar NH, Islam MM, Conway M, Wallin R, Hutson SM: Human mitochondrial branched chain aminotransferase isozyme: structural role of the CXXC center in catalysis. J Biol Chem. 2006 Dec 22;281(51):39660-71. Epub 2006 Oct 18. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5839
Enzyme 14 Name Bifunctional aminoacyl-tRNA synthetase
Enzyme 14 Synonyms
  1. Cell proliferation-inducing gene 32 protein
  2. Glutamyl-tRNA synthetase
  3. Glutamate--tRNA ligase
  4. GluRS
  5. Prolyl-tRNA synthetase
  6. Proline--tRNA ligase
Enzyme 14 Gene Name EPRS
Enzyme 14 Protein Sequence >Bifunctional aminoacyl-tRNA synthetase
MATLSLTVNSGDPPLGALLAVEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLAR
VATTAGLYGSNLMEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLA
DLCVWATLKGNAAWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEK
KQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTN
PEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMK
AEREQRIDSKHRKNPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCK
IQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYI
WEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGS
SRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVG
LKPVWYSPKVFIEGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKLNLENKD
YKKTTKVTWLAETTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPC
LKDLKKGDIIQLQRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTK
VEATKNETSAPFKERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAA
VKQLLSLKAEYKEKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKL
KAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPE
AKVLFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAED
KDKKKKEKENKSEKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKK
EENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPM
FVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDL
PIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEEL
LAIPVVKGRKTEKEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPK
IPGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDK
EALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFV
AVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSG
KIVQIPFCGEIDCEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKN
PAKYYTLFGRSY
Enzyme 14 Number of Residues 1512
Enzyme 14 Molecular Weight 170589.7
Enzyme 14 Theoretical pI 7.34
Enzyme 14 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • aminoacyl-tRNA ligase activity
  • binding
  • catalytic activity
  • glutamate-tRNA ligase activity
  • ligase activity
  • ligase activity, forming aminoacyl-tRNA and related compounds
  • ligase activity, forming carbon-oxygen bonds
  • nucleoside binding
  • nucleotide binding
  • proline-tRNA ligase activity
  • purine nucleoside binding
Process
  • RNA metabolic process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • cellular macromolecule metabolic process
  • glutamyl-tRNA aminoacylation
  • macromolecule biosynthetic process
  • macromolecule metabolic process
  • metabolic process
  • ncRNA metabolic process
  • prolyl-tRNA aminoacylation
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolic process
  • translation
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 14 General Function Involved in nucleotide binding
Enzyme 14 Specific Function Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction:the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA
Enzyme 14 Pathways
Enzyme 14 Reactions
  • ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu [RN:R05578]
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 P07814 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name SYEP_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >4539 bp
ATGGCGACGCTCTCTCTGACCGTGAATTCAGGAGACCCTCCGCTAGGAGCTTTGCTGGCA
GTAGAACACGTGAAAGACGATGTCAGCATTTCCGTTGAAGAAGGGAAAGAGAATATTCTT
CATGTTTCTGAAAATGTGATATTCACAGATGTGAATTCTATACTTCGCTACTTGGCTAGA
GTTGCAACTACAGCTGGGTTATATGGCTCTAATCTGATGGAACATACTGAGATTGATCAC
TGGTTGGAGTTCAGTGCTACAAAATTATCTTCATGTGATTCCTTTACTTCTACAATTAAT
GAACTCAATCATTGCCTGTCTCTGAGAACATACTTAGTTGGAAACTCCTTGAGTTTAGCA
GATTTATGTGTTTGGGCCACCCTAAAAGGAAATGCTGCCTGGCAAGAACAGTTGAAACAG
AAGAAAGCTCCAGTTCATGTAAAACGTTGGTTTGGCTTTCTTGAAGCCCAGCAGGCCTTC
CAGTCAGTAGGTACCAAGTGGGATGTTTCAACAACCAAAGCTCGAGTGGCACCTGAGAAA
AAGCAAGATGTTGGGAAATTTGTTGAGCTTCCAGGTGCGGAGATGGGAAAGGTTACCGTC
AGATTTCCTCCAGAGGCCAGTGGTTACTTACACATTGGGCATGCAAAAGCTGCTCTTCTG
AACCAGCACTACCAGGTTAACTTTAAAGGGAAACTGATCATGAGATTTGATGACACAAAT
CCTGAAAAAGAAAAGGAAGATTTTGAGAAGGTTATCTTGGAAGATGTTGCAATGTTGCAT
ATCAAACCAGATCAATTTACTTATACTTCGGATCATTTTGAAACTATAATGAAGTATGCA
GAGAAGCTAATTCAAGAAGGGAAGGCTTATGTGGATGATACTCCTGCTGAACAGATGAAA
GCAGAACGTGAGCAGAGGATAGAATCTAAACATAGAAAAAACCCTATTGAGAAGAATCTA
CAAATGTGGGAAGAAATGAAAAAAGGGAGCCAGTTTGGTCAGTCCTGTTGTTTGCGAGCA
AAAATTGACATGAGTAGTAACAATGGATGCATGAGAGATCCAACCCTTTATCGCTGCAAA
ATTCAACCACATCCAAGAACTGGAAATAAATACAATGTTTATCCAACATATGATTTTGCC
TGCCCCATAGTTGACAGCATCGAAGGTGTTACACATGCCCTGAGAACAACAGAATACCAT
GACAGAGATGAGCAGTTTTACTGGATTATTGAAGCTTTAGGCATAAGAAAACCATATATT
TGGGAATATAGTCGGCTAAATCTCAACAACACAGTGCTATCCAAAAGAAAACTCACATGG
TTTGTCAATGAAGGACTAGTAGATGGATGGGATGACCCAAGATTTCCTACGGTTCGTGGT
GTACTGAGAAGAGGGATGACAGTTGAAGGACTGAAACAGTTTATTGCTGCTCAGGGCTCC
TCACGTTCAGTCGTGAACATGGAGTGGGACAAAATCTGGGCGTTTAACAAAAAGGTTATT
GACCCAGTGGCTCCACGATATGTTGCATTACTGAAGAAAGAAGTGATCCCAGTGAATGTA
CCTGAAGCTCAGGAGGAGATGAAAGAAGTAGCCAGACACCCAAAGAATCCTGAGGTTGGC
TTGAAGCCTGTGTGGTATAGTCCCAAAGTTTTCATTGAAGGTGCTGATGCAGAGACTTTT
TCGGAGGGTGAGATGGTTACATTTATAAATTGGGGCAACCTCAACATTACAAAAATACAC
AAAAATGCAGATGGAAAAATCATATCTCTTGATGCAAAGTTGAATTTGGAAAACAAAGAC
TACAAGAAAACCACTAAGGTCACTTGGCTTGCAGAGACTACACATGCTCTTCCTATTCCA
GTAATCTGTGTCACTTATGAGCACTTGATCACAAAGCCAGTGCTAGGAAAAGACGAGGAC
TTTAAGCAGTATGTCAACAAGAACAGTAAGCATGAAGAGCTAATGCTAGGGGATCCCTGC
CTTAAGGATTTGAAAAAAGGAGATATTATACAACTCCAGAGAAGAGGATTCTTCATATGT
GATCAACCTTATGAACCTGTTAGCCCATATAGTTGCAAGGAAGCCCCGTGTGTTTTGATA
TACATTCCTGATGGGCACACAAAGGAAATGCCAACATCAGGGTCAAAGGAAAAGACCAAA
GTAGAAGCCACAAAAAATGAGACCTCTGCTCCTTTTAAGGAAAGACCAACACCTTCTCTG
AATAATAATTGTACTACATCTGAGGATTCCTTGGTCCTTTACAATAGAGTGGCTGTTCAA
GGAGATGTGGTTCGTGAATTAAAAGCCAAGAAAGCACCAAAGGAAGATGTAGATGCAGCT
GTAAAACAGCTTTTGTCTTTGAAAGCTGAATATAAGGAGAAAACTGGCCAGGAATATAAA
CCTGGAAACCCTCCTGCTGAAATAGGACAGAATATTTCTTCTAATTCCTCAGCAAGTATT
CTGGAAAGTAAATCTCTGTATGATGAAGTTGCTGCACAAGGGGAGGTGGTTCGTAAGCTA
AAAGCTGAAAAATCCCCTAAGGCTAAAATAAATGAAGCTGTAGAATGCTTACTGTCCCTG
AAGGCTCAGTATAAAGAAAAAACTGGGAAGGAGTACATACCTGGTCAGCCCCCATTATCT
CAAAGTTCGGATTCAAGCCCAACCAGAAATTCTGAACCTGCTGGTTTAGAAACACCAGAA
GCGAAAGTACTTTTTGACAAAGTAGCTTCTCAAGGGGAAGTAGTTCGGAAACTTAAAACT
GAAAAAGCCCCTAAGGATCAAGTAGATATAGCTGTTCAAGAACTCCTTCAGCTAAAGGCA
CAGTACGAGTCTTTGATAGGAGTAGAGTATAAGCCTGTGTCGGCCACTGGAGCTGAGGAC
AAAGATAAGAAGAAGAAAGAAAAAGAAAATAAATCTGAAAAGCAGAATAAGCCTCAGAAA
CAAAATGATGGCCAAAGGAAAGACCCTTCTAAAAACCAAGGAGGTGGGCTCTCATCAAGT
GGAGCAGGAGAAGGGCAGGGGCCTAAGAAACAGACCAGGTTGGGTCTTGAGGCAAAAAAA
GAAGAAAATCTTGCTGATTGGTATTCTCAGGTCATCACAAAATCAGAAATGATTGAATAC
CATGACGTAAGTGGCTGTTATATTCTTCGTCCCTGGGCCTATGCCATTTGGGAAGCCATC
AAGGACTTTTTTGATGCTGAGATCAAGAAACTTGGTGTTGAAAACTGCTACTTCCCCATG
TTTGTGTCTCAAAGTGCATTAGAGAAAGAGAAGACTCATGTTGCTGACTTTGCCCCAGAG
GTTGCTTGGGTTACAAGATCTGGCAAAACCGAGCTGGCAGAACCAATTGCCATTCGTCCT
ACTAGTGAAACAGTAATGTATCCTGCATATGCAAAATGGGTACAATCACACAGAGACCTG
CCCATCAAGCTCAATCAGTGGTGCAATGTGGTGCGTTGGGAATTCAAGCATCCTCAGCCT
TTCCTACGTACTCGTGAATTTCTTTGGCAGGAAGGGCACAGTGCTTTTGTTACCGTGGAA
GAGGCAGCGGAAGAGGTCTTGCAGATACTTGACTTATATGCTCAGGTATATGAAGAACTC
CTGGCAATTCCTGTTGTTAAAGGAAGAAAGACGGAAAAGGAAAAATTTGCAGGAGGAGAC
TATACAACTACAATAGAAGCATTTATATCTGCTAGTGGAAGAGCTATCCAGGGAGGAACA
TCACATCATTTAGGGCAGAATTTTTCCAAAATGTTTGAAATCGTTTTTGAAGATCCAAAG
ATACCAGGAGAGAAGCAATTTGCCTATCAAAACTCCTGGGGCCTGACAACTCGAACTATT
GGTGTTATGACCATGGTTCATGGGGACAACATGGGTTTAGTATTACCACCCCGTGTAGCA
TGTGTTCAGGTGGTGATTATTCCTTGTGGCATTACCAATGCACTTTCTGAAGAAGACAAA
GAAGCGCTGATTGCAAAATGCAATGATTATCGAAGGCGATTACTCAGTGTTAACATCCGC
GTTAGAGCTGATTTACGAGATAATTATTCTCCAGGTTGGAAATTCAATCACTGGGAGCTC
AAGGGAGTTCCCATTAGACTTGAAGTTGGGCCACGTGATATGAAGAGCTGTCAGTTTGTA
GCCGTCAGACGAGATACTGGAGAAAAGCTGACAGTTGCTGAAAATGAGGCAGAGACTAAA
CTTCAAGCTATTTTGGAAGACATCCAGGTCACCCTTTTCACAAGGGCTTCTGAAGACCTT
AAGACTCATATGGTTGTGGCTAATACAATGGAAGACTTTCAGAAGATACTAGATTCTGGA
AGGATTGTTCAGATTCCATTCTGTGGGGAAATTGACTGTGAGGACTGGATCAAAAAGACC
ACTGCCAGGGATCAAGATCTTGAACCTGGTGCTCCATCCATGGGAGCTAAAAGCCTTTGC
ATCCCCTTCAAACCACTCTGTGAACTGCAGCCTGGAGCCAAATGTGTCTGTGGCAAGAAC
CCTGCCAAGTACTACACCTTATTTGGTCGCAGCTACTGA
Enzyme 14 GenBank Gene ID CR933648 Link Image
Enzyme 14 GeneCard ID EPRS Link Image
Enzyme 14 GenAtlas ID EPRS Link Image
Enzyme 14 HGNC ID HGNC:3418 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 1q41-q42
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. 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]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Fett R, Knippers R: The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors. J Biol Chem. 1991 Jan 25;266(3):1448-55. [PubMed Link Image]
  5. Thommes P, Fett R, Schray B, Kunze N, Knippers R: The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes. Nucleic Acids Res. 1988 Jun 24;16(12):5391-406. [PubMed Link Image]
  6. Cerini C, Kerjan P, Astier M, Gratecos D, Mirande M, Semeriva M: A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase. EMBO J. 1991 Dec;10(13):4267-77. [PubMed Link Image]
  7. Kaiser E, Eberhard D, Knippers R: Exons encoding the highly conserved part of human glutaminyl-tRNA synthetase. J Mol Evol. 1992 Jan;34(1):45-53. [PubMed Link Image]
  8. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  9. Kato T, Daigo Y, Hayama S, Ishikawa N, Yamabuki T, Ito T, Miyamoto M, Kondo S, Nakamura Y: A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis. Cancer Res. 2005 Jul 1;65(13):5638-46. [PubMed Link Image]
  10. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  11. 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]
  12. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  13. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  14. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
  19. 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]
  20. Jeong EJ, Hwang GS, Kim KH, Kim MJ, Kim S, Kim KS: Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats. Biochemistry. 2000 Dec 26;39(51):15775-82. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5855
Enzyme 15 Name Asparagine synthetase [glutamine-hydrolyzing]
Enzyme 15 Synonyms
  1. Cell cycle control protein TS11
  2. Glutamine-dependent asparagine synthetase
Enzyme 15 Gene Name ASNS
Enzyme 15 Protein Sequence >Asparagine synthetase [glutamine-hydrolyzing]
MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQ
PIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGV
FAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPF
LPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFN
NAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAAR
KVADHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVV
IFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPF
LDHRFSSYYLSLPPEMRIPKNGIEKHLLRETFEDSNLIPKEILWRPKEAFSDGITSVKNS
WFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLSHYWMPK
WINATDPSARTLTHYKSAVKA
Enzyme 15 Number of Residues 561
Enzyme 15 Molecular Weight 64369.4
Enzyme 15 Theoretical pI 6.85
Enzyme 15 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 15 General Function Involved in asparagine synthase (glutamine-hydrolyzing) activity
Enzyme 15 Specific Function ATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate
Enzyme 15 Pathways
Enzyme 15 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 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 179100 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P08243 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name ASNS_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 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 15 GenBank Gene ID M27396 Link Image
Enzyme 15 GeneCard ID ASNS Link Image
Enzyme 15 GenAtlas ID ASNS Link Image
Enzyme 15 HGNC ID HGNC:753 Link Image
Enzyme 15 Chromosome Location 7
Enzyme 15 Locus 7q21.3
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5939
Enzyme 16 Name Glutamate dehydrogenase 2, mitochondrial
Enzyme 16 Synonyms
  1. GDH 2
Enzyme 16 Gene Name GLUD2
Enzyme 16 Protein Sequence >Glutamate dehydrogenase 2, mitochondrial
MYRYLAKALLPSRAGPAALGSAANHSAALLGRGRGQPAAASQPGLALAARRHYSELVADR
EDDPNFFKMVEGFFDRGASIVEDKLVKDLRTQESEEQKRNRVRGILRIIKPCNHVLSLSF
PIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFG
GAKAGVKINPKNYTENELEKITRRFTMELAKKGFIGPGVDVPAPDMNTGEREMSWIADTY
ASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFR
DKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILG
FPKAKPYEGSILEVDCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLER
NILVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLLSVQESLERKFGK
HGGTIPIVPTAEFQDSISGASEKDIVHSALAYTMERSARQIMHTAMKYNLGLDLRTAAYV
NAIEKVFKVYSEAGVTFT
Enzyme 16 Number of Residues 558
Enzyme 16 Molecular Weight 61433.5
Enzyme 16 Theoretical pI 8.67
Enzyme 16 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
Enzyme 16 General Function Involved in oxidoreductase activity
Enzyme 16 Specific Function Important for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission
Enzyme 16 Pathways
Enzyme 16 Reactions
  • L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H + H+ [RN:R00243 R00248]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID P49448 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name DHE4_HUMAN Link Image
Enzyme 16 PDB ID 1L1F Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1677 bp
ATGTACCGCTACCTGGCCAAAGCGCTGCTGCCGTCCCGGGCCGGGCCCGCTGCCCTGGGC
TCCGCGGCCAACCACTCGGCCGCGTTGCTGGGCCGGGGCCGCGGACAGCCCGCCGCCGCC
TCGCAGCCGGGGCTCGCATTGGCCGCCCGGCGCCACTACAGCGAGTTGGTGGCCGACCGC
GAGGACGACCCCAACTTCTTCAAGATGGTGGAGGGCTTCTTCGATCGCGGCGCCAGCATC
GTGGAGGACAAGTTGGTGAAGGACCTGAGGACCCAGGAAAGCGAGGAGCAGAAGCGGAAC
CGGGTGCGCGGCATCCTGCGGATCATCAAGCCCTGCAACCATGTGCTGAGTCTCTCCTTC
CCCATCCGGCGCGACGACGGCTCCTGGGAGGTCATCGAAGGCTACCGGGCCCAGCACAGC
CAGCACCGCACGCCCTGCAAGGGAGGTATCCGTTACAGCACTGATGTGAGTGTAGATGAA
GTAAAAGCTTTGGCTTCTCTGATGACATACAAGTGTGCAGTGGTTGATGTGCCGTTTGGG
GGTGCTAAAGCTGGTGTTAAGATCAATCCCAAGAACTATACCGAAAATGAATTGGAAAAG
ATCACAAGGAGGTTCACCATGGAGCTAGCAAAGAAGGGCTTTATTGGTCCTGGCGTTGAT
GTGCCTGCTCCAGACATGAACACAGGTGAGCGGGAGATGTCCTGGATTGCTGATACCTAT
GCCAGCACCATAGGGCACTATGATATTAATGCACACGCCTGTGTTACTGGTAAACCCATC
AGCCAAGGGGGAATCCATGGACGCATCTCTGCTACTGGCCGTGGTGTCTTCCATGGGATT
GAAAACTTCATCAATGAAGCTTCTTACATGAGCATTTTAGGAATGACACCAGGGTTTAGA
GATAAAACATTTGTTGTTCAGGGATTTGGTAATGTGGGCCTACACTCTATGAGATATTTA
CATCGTTTTGGTGCTAAATGTATTGCTGTTGGTGAGTCTGATGGGAGTATATGGAATCCA
GATGGTATTGACCCAAAGGAACTGGAAGACTTCAAATTGCAACATGGGTCCATTCTGGGC
TTCCCCAAGGCAAAGCCCTATGAAGGAAGCATCTTGGAGGTCGACTGTGACATACTGATC
CCAGCTGCCACTGAGAAGCAGTTGACCAAATCCAACGCACCCAGAGTCAAAGCCAAGATC
ATTGCTGAAGGTGCCAATGGGCCAACAACTCCAGAAGCTGATAAGATCTTCCTGGAGAGA
AACATTTTGGTTATTCCAGATCTCTACTTGAATGCTGGAGGAGTGACAGTATCTTACTTT
GAGTGGCTGAAGAATCTAAATCATGTCAGCTATGGCCGTTTGACCTTCAAATATGAAAGG
GATTCTAACTACCACTTGCTCCTGTCTGTTCAAGAGAGTTTAGAAAGAAAATTTGGAAAG
CATGGTGGAACTATTCCCATTGTACCCACGGCAGAGTTCCAAGACAGTATATCGGGTGCA
TCTGAGAAAGACATTGTGCACTCTGCCTTGGCATACACAATGGAGCGTTCTGCCAGGCAA
ATTATGCACACAGCCATGAAGTATAACCTGGGATTGGACCTGAGAACAGCTGCCTATGTC
AATGCCATTGAAAAAGTCTTCAAAGTGTACAGTGAAGCTGGTGTGACCTTCACATAG
Enzyme 16 GenBank Gene ID AK313356 Link Image
Enzyme 16 GeneCard ID GLUD2 Link Image
Enzyme 16 GenAtlas ID GLUD2 Link Image
Enzyme 16 HGNC ID HGNC:4336 Link Image
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Shashidharan P, Michaelidis TM, Robakis NK, Kresovali A, Papamatheakis J, Plaitakis A: Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene. J Biol Chem. 1994 Jun 17;269(24):16971-6. [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. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [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. 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 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5943
Enzyme 17 Name Glutamine synthetase
Enzyme 17 Synonyms
  1. GS
  2. Glutamate decarboxylase
  3. Glutamate--ammonia ligase
Enzyme 17 Gene Name GLUL
Enzyme 17 Protein Sequence >Glutamine synthetase
MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEW
NFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRI
MDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHY
RACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDP
KPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRL
TGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCL
LNETGDEPFQYKN
Enzyme 17 Number of Residues 373
Enzyme 17 Molecular Weight 42064.1
Enzyme 17 Theoretical pI 6.88
Enzyme 17 GO Classification
Function
  • acid-ammonia (or amide) ligase activity
  • acid-ammonia (or amide) ligase activity
  • ammonia ligase activity
  • catalytic activity
  • glutamate-ammonia ligase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glutamine biosynthetic process
  • glutamine family amino acid metabolic process
  • glutamine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
Component
Enzyme 17 General Function Involved in glutamate-ammonia ligase activity
Enzyme 17 Specific Function This enzyme has 2 functions:it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner. Essential for proliferation of fetal skin fibroblasts
Enzyme 17 Pathways
Enzyme 17 Reactions
  • ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine [RN:R00253]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 31833 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P15104 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name GLNA_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1122 bp
ATGACCACCTCAGCAAGTTCCCACTTAAATAAAGGCATCAAGCAGGTGTACATGTCCCTG
CCTCAGGGTGAGAAAGTCCAGGCCATGTATATCTGGATCGATGGTACTGGAGAAGGACTG
CGCTGCAAGACCCGGACCCTGGACAGTGAGCCCAAGTGTGTGGAAGAGTTGCCTGAGTGG
AATTTCGATGGCTCCAGTACTTTACAGTCTGAGGGTTCCAACAGTGACATGTATCTCGTG
CCTGCTGCCATGTTTCGGGACCCCTTCCGTAAGGACCCTAACAAGCTGGTGTTATGTGAA
GTTTTCAAGTACAATCGAAGGCCTGCAGAGACCAATTTGAGGCACACCTGTAAACGGATA
ATGGACATGGTGAGCAACCAGCACCCCTGGTTTGGCATGGAGCAGGAGTATACCCTCATG
GGGACAGATGGGCACCCCTTTGGTTGGCCTTCCAACGGCTTCCCAGGGCCCCAGGGTCCA
TATTACTGTGGTGTGGGAGCAGACAGAGCCTATGGCAGGGACATCGTGGAGGCCCATTAC
CGGGCCTGCTTGTATGCTGGAGTCAAGATTGCGGGGACTAATGCCGAGGTCATGCCTGCC
CAGTGGGAATTTCAGATTGGACCTTGTGAAGGAATCAGCATGGGAGATCATCTCTGGGTG
GCCCGTTTCATCTTGCATCGTGTGTGTGAAGACTTTGGAGTGATAGCAACCTTTGATCCT
AAGCCCATTCCTGGGAACTGGAATGGTGCAGGCTGCCATACCAACTTCAGCACCAAGGCC
ATGCGGGAGGAGAATGGTCTGAAGTACATCGAGGAGGCCATTGAGAAACTAAGCAAGCGG
CACCAGTACCACATCCGTGCCTATGATCCCAAGGGAGGCCTGGACAATGCCCGACGTCTA
ACTGGATTCCATGAAACCTCCAACATCAACGACTTTTCTGGTGGTGTAGCCAATCGTAGC
GCCAGCATACGCATTCCCCGGACTGTTGGCCAGGAGAAGAAGGGTTACTTTGAAGATCGT
CGCCCCTCTGCCAACTGCGACCCCTTTTCGGTGACAGAAGCCCTCATCCGCACGTGTCTT
CTCAATGAAACCGGCGATGAGCCCTTCCAGTACAAAAATTAA
Enzyme 17 GenBank Gene ID Y00387 Link Image
Enzyme 17 GeneCard ID GLUL Link Image
Enzyme 17 GenAtlas ID GLUL Link Image
Enzyme 17 HGNC ID HGNC:4341 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 1q31
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Gibbs CS, Campbell KE, Wilson RH: Sequence of a human glutamine synthetase cDNA. Nucleic Acids Res. 1987 Aug 11;15(15):6293. [PubMed Link Image]
  2. Van den Hoff MJ, Geerts WJ, Das AT, Moorman AF, Lamers WH: cDNA sequence of the long mRNA for human glutamine synthase. Biochim Biophys Acta. 1991 Oct 8;1090(2):249-51. [PubMed Link Image]
  3. Christa L, Simon MT, Flinois JP, Gebhardt R, Brechot C, Lasserre C: Overexpression of glutamine synthetase in human primary liver cancer. Gastroenterology. 1994 May;106(5):1312-20. [PubMed Link Image]
  4. 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]
  5. 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]
  6. 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]
  7. Boksha IS, Schonfeld HJ, Langen H, Muller F, Tereshkina EB, Burbaeva GSh: Glutamine synthetase isolated from human brain: octameric structure and homology of partial primary structure with human liver glutamine synthetase. Biochemistry (Mosc). 2002 Sep;67(9):1012-20. [PubMed Link Image]
  8. Vermeulen T, Gorg B, Vogl T, Wolf M, Varga G, Toutain A, Paul R, Schliess F, Haussinger D, Haberle J: Glutamine synthetase is essential for proliferation of fetal skin fibroblasts. Arch Biochem Biophys. 2008 Oct 1;478(1):96-102. Epub 2008 Jul 17. [PubMed Link Image]
  9. Olkku A, Mahonen A: Wnt and steroid pathways control glutamate signalling by regulating glutamine synthetase activity in osteoblastic cells. Bone. 2008 Sep;43(3):483-93. Epub 2008 May 7. [PubMed Link Image]
  10. Haberle J, Gorg B, Rutsch F, Schmidt E, Toutain A, Benoist JF, Gelot A, Suc AL, Hohne W, Schliess F, Haussinger D, Koch HG: Congenital glutamine deficiency with glutamine synthetase mutations. N Engl J Med. 2005 Nov 3;353(18):1926-33. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5949
Enzyme 18 Name CTP synthase 1
Enzyme 18 Synonyms
  1. CTP synthetase 1
  2. UTP--ammonia ligase 1
Enzyme 18 Gene Name CTPS
Enzyme 18 Protein Sequence >CTP synthase 1
MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFV
LDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDA
IQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHV
SLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ
VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCS
IALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQK
LCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDAN
STEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRH
RFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPY
FGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD
Enzyme 18 Number of Residues 591
Enzyme 18 Molecular Weight 66689.9
Enzyme 18 Theoretical pI 6.42
Enzyme 18 GO Classification
Function
  • CTP synthase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
Component
Enzyme 18 General Function Involved in CTP synthase activity
Enzyme 18 Specific Function Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen
Enzyme 18 Pathways
Enzyme 18 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 30293 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P17812 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PYRG1_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1776 bp
ATGAAGTACATTCTGGTTACTGGTGGTGTTATATCAGGAATTGGAAAAGGAATCATTGCC
AGCAGTGTGGGCACAATACTCAAGTCATGTGGTTTACATGTAACTTCAATCAAAATTGAC
CCCTACATTAACATTGATGCAGGAACATTCTCTCCTTATGAGCATGGTGAGGTTTTTGTG
CTGGATGATGGTGGGGAAGTAGACCTTGACCTGGGTAACTATGAGCGGTTCCTTGACATC
CGCCTCACCAAGGACAATAATCTGACCACTGGAAAGATATACCAGTATGTCATTAACAAG
GAACGGAAAGGAGATTACTTGGGGAAAACTGTCCAAGTTGTCCCTCATATCACAGATGCA
ATCCAGGAGTGGGTGATGAGACAGGCGTTAATACCTGTAGATGAAGATGGCCTGGAACCT
CAAGTGTGTGTTATTGAGCTTGGTGGAACCGTGGGGGACATAGAAAGCATGCCCTTTATT
GAGGCCTTCCGTCAGTTCCAATTCAAGGTCAAAAGAGAGAACTTTTGTAACATCCACGTC
AGTCTAGTTCCCCAGCCAAGTTCAACAGGGGAACAGAAGACTAAACCTACCCAGAATAGT
GTTCGGGAACTTAGAGGACTTGGGCTTTCCCCAGATCTGGTTGTATGCAGGTGCTCAAAT
CCACTTGACACATCAGTGAAGGAGAAAATATCAATGTTCTGCCATGTTGAGCCTGAACAA
GTGATCTGTGTCCACGATGTCTCATCCATCTACCGAGTCCCCTTGTTGTTAGAGGAGCAA
GGGGTTGTAGATTATTTTCTTCGAAGACTTGACCTTCCTATTGAGAGGCAGCCAAGAAAA
ATGCTGATGAAATGGAAAGAGATGGCTGACAGATATGATCGCTTGCTGGAGACCTGCTCT
ATTGCCCTTGTGGCGAAATACACCGAGTTCTCAGACTCCTATGCCTCTGTCATTAAGGCT
CTGGAGCATTCTGCACTGGCCATCAACCACAAATTGGAAATCAAGTACATAGATTCTGCG
GACTTGGAGCCCATCACCTCGCAAGAAGAGCCCGTGCGCTACCACGAAGCTTGGCAGAAG
CTCTGTAGTGCTCATGGAGTGCTGGTTCCAGGAGGATTTGGTGTTCGAGGAACAGAAGGA
AAAATCCAAGCAATTGCCTGGGCTCGGAATCAGAAAAAGCCTTTTTTGGGCGTGTGCTTA
GGGATGCAGTTGGCAGTGGTTGAATTCTCAAGAAACGTGCTGGGATGGCAAGATGCCAAT
TCTACAGAGTTTGACCCTACGACCAGTCATCCCGTGGTCGTAGACATGCCAGAACACAAC
CCAGGGCAGATGGGCGGAACCATGAGGCTGGGCAAGAGGAGAACCCTGTTCCAGACCAAG
AACTCAGTCATGAGGAAACTCTATGGAGACGCAGACTACTTGGAAGAGAGGCACCGCCAC
CGATTTGAGGTGAATCCAGTCTGGAAAAAGTGTTTGGAAGAACAAGGCTTGAAGTTTGTT
GGCCAAGATGTTGAAGGAGAGAGAATGGAAATTGTGGAGTTAGAAGATCATCCCTTTTTT
GTTGGGGTTCAGTACCACCCTGAGTTCCTGTCCAGGCCTATCAAGCCCTCCCCACCATAC
TTTGGCCTCCTCCTGGCCTCTGTGGGGCGGCTCTCACATTACCTCCAGAAAGGCTGCAGG
CTCTCACCCAGGGACACCTATAGTGACAGGAGTGGAAGCAGCTCCCCTGACTCTGAAATC
ACCGAACTGAAGTTTCCATCAATAAATCATGACTGA
Enzyme 18 GenBank Gene ID X52142 Link Image
Enzyme 18 GeneCard ID CTPS Link Image
Enzyme 18 GenAtlas ID CTPS Link Image
Enzyme 18 HGNC ID HGNC:2519 Link Image
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 1p34.1
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Yamauchi M, Yamauchi N, Meuth M: Molecular cloning of the human CTP synthetase gene by functional complementation with purified human metaphase chromosomes. EMBO J. 1990 Jul;9(7):2095-9. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  5. Han GS, Sreenivas A, Choi MG, Chang YF, Martin SS, Baldwin EP, Carman GM: Expression of Human CTP synthetase in Saccharomyces cerevisiae reveals phosphorylation by protein kinase A. J Biol Chem. 2005 Nov 18;280(46):38328-36. Epub 2005 Sep 22. [PubMed Link Image]
  6. Kim JE, Tannenbaum SR, White FM: Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res. 2005 Jul-Aug;4(4):1339-46. [PubMed Link Image]
  7. Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J: Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. Proteomics. 2005 Sep;5(14):3589-99. [PubMed Link Image]
  8. 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]
  9. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  10. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  11. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5953
Enzyme 19 Name Glutaminase kidney isoform, mitochondrial
Enzyme 19 Synonyms
  1. GLS
  2. K-glutaminase
  3. L-glutamine amidohydrolase
Enzyme 19 Gene Name GLS
Enzyme 19 Protein Sequence >Glutaminase kidney isoform, mitochondrial
MMRLRGSGMLRDLLLRSPAGVSATLRRAQPLVTLCRRPRGGGRPAAGPAAAARLHPWWGG
GGWPAEPLARGLSSSPSEILQELGKGSTHPQPGVSPPAAPAAPGPKDGPGETDAFGNSEG
KELVASGENKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMD
MLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKK
QSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDL
GTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQ
FLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSI
EVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPA
KSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKL
DPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVE
VVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQT
VHKNLDGLL
Enzyme 19 Number of Residues 669
Enzyme 19 Molecular Weight 73460.6
Enzyme 19 Theoretical pI 7.82
Enzyme 19 GO Classification
Function
  • catalytic activity
  • glutaminase 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
  • glutamine family amino acid metabolic process
  • glutamine metabolic process
  • metabolic process
Component
Enzyme 19 General Function Involved in glutaminase activity
Enzyme 19 Specific Function Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine
Enzyme 19 Pathways
Enzyme 19 Reactions
  • L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 156104878 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID O94925 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name GLSK_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >2010 bp
ATGATGCGGCTGCGAGGCTCGGGGATGCTGCGGGACCTGCTCCTGCGGTCGCCCGCCGGC
GTGAGCGCGACTCTGCGGCGGGCACAGCCCTTGGTCACCCTGTGCCGGCGTCCCCGAGGC
GGGGGACGGCCGGCCGCGGGCCCGGCTGCCGCCGCGCGACTCCACCCGTGGTGGGGCGGG
GGCGGCTGGCCGGCGGAGCCCCTCGCGCGGGGCCTGTCCAGCTCTCCTTCGGAGATCTTG
CAGGAGCTGGGCAAGGGGAGCACGCATCCGCAGCCCGGGGTGTCGCCACCCGCTGCCCCG
GCGGCGCCCGGCCCCAAGGACGGCCCCGGGGAGACGGACGCGTTTGGCAACAGCGAGGGC
AAAGAGCTGGTGGCCTCAGGTGAAAATAAAATAAAACAGGGTCTGTTACCTAGCTTGGAA
GATTTGCTGTTCTATACAATTGCTGAAGGACAAGAGAAAATACCTGTTCATAAATTTATT
ACAGCACTCAAATCTACAGGATTGCGAACGTCTGATCCCAGGTTGAAAGAGTGTATGGAT
ATGTTAAGATTAACTCTTCAAACAACATCAGATGGTGTCATGCTAGACAAAGATCTTTTT
AAAAAATGTGTTCAGAGCAACATTGTTTTGTTGACACAAGCATTTAGAAGAAAGTTTGTG
ATTCCTGACTTTATGTCTTTTACCTCACACATTGATGAGTTATATGAAAGTGCTAAAAAG
CAGTCTGGAGGAAAGGTTGCAGATTATATTCCTCAACTGGCCAAATTCAGTCCCGATTTG
TGGGGTGTGTCTGTTTGTACAGTAGATGGACAGAGGCATTCTACTGGAGATACCAAAGTT
CCCTTCTGTCTTCAGTCCTGTGTAAAACCTTTGAAATATGCCATTGCTGTTAATGATCTT
GGAACTGAATATGTGCATCGATATGTTGGAAAAGAGCCGAGTGGACTAAGATTCAACAAA
CTATTTTTGAATGAAGATGATAAACCACATAATCCTATGGTAAATGCTGGAGCAATTGTT
GTGACTTCACTAATAAAGCAAGGAGTAAATAATGCTGAAAAATTTGACTATGTCATGCAG
TTTTTGAATAAGATGGCTGGTAATGAATATGTTGGATTCAGTAATGCAACGTTTCAGTCT
GAAAGAGAAAGTGGAGATCGAAATTTTGCAATAGGATATTACTTAAAAGAAAAGAAGTGT
TTTCCAGAAGGCACAGACATGGTTGGTATATTAGACTTCTACTTCCAGCTGTGCTCCATT
GAAGTGACTTGTGAATCAGCCAGTGTGATGGCTGCGACACTGGCTAATGGTGGTTTCTGC
CCAATTACTGGTGAAAGAGTACTGAGCCCTGAAGCAGTTCGAAATACATTGAGTTTGATG
CATTCCTGTGGCATGTATGACTTCTCAGGGCAGTTTGCTTTCCATGTTGGTCTTCCTGCA
AAATCTGGAGTTGCTGGGGGCATTCTTTTAGTTGTCCCCAATGTTATGGGTATGATGTGC
TGGTCTCCTCCTCTGGATAAGATGGGCAACAGTGTTAAGGGAATTCACTTTTGTCACGAT
CTTGTTTCTCTGTGTAATTTCCATAACTATGATAATTTGAGACACTTTGCAAAAAAACTT
GATCCTCGAAGAGAAGGTGGTGATCAAAGGGTAAAGTCAGTGATAAATCTTTTGTTTGCT
GCATATACTGGAGATGTGTCTGCACTTCGAAGATTTGCTTTGTCAGCTATGGACATGGAA
CAGCGGGACTATGATTCTAGAACAGCACTCCATGTAGCTGCTGCAGAGGGTCATGTTGAA
GTTGTTAAATTTTTGCTGGAAGCCTGCAAAGTAAACCCTTTCCCCAAGGACAGGTGGAAT
AACACTCCCATGGATGAAGCACTGCACTTTGGACACCATGATGTATTTAAAATTCTCCAA
GAATACCAAGTCCAGTACACACCTCAAGGAGATTCTGACAACGGGAAGGAAAATCAAACC
GTCCATAAGAATCTTGATGGATTGTTGTAA
Enzyme 19 GenBank Gene ID NM_014905.3 Link Image
Enzyme 19 GeneCard ID GLS Link Image
Enzyme 19 GenAtlas ID GLS Link Image
Enzyme 19 HGNC ID HGNC:4331 Link Image
Enzyme 19 Chromosome Location 2
Enzyme 19 Locus 2q32-q34
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Elgadi KM, Meguid RA, Qian M, Souba WW, Abcouwer SF: Cloning and analysis of unique human glutaminase isoforms generated by tissue-specific alternative splicing. Physiol Genomics. 1999 Aug 31;1(2):51-62. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [PubMed Link Image]
  3. Holcomb T, Taylor L, Trohkimoinen J, Curthoys NP: Isolation, characterization and expression of a human brain mitochondrial glutaminase cDNA. Brain Res Mol Brain Res. 2000 Mar 10;76(1):56-63. [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. Hillman RT, Green RE, Brenner SE: An unappreciated role for RNA surveillance. Genome Biol. 2004;5(2):R8. Epub 2004 Feb 2. [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 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5959
Enzyme 20 Name Formimidoyltransferase-cyclodeaminase
Enzyme 20 Synonyms
  1. Formiminotransferase-cyclodeaminase
  2. FTCD
  3. LCHC1
  4. Glutamate formimidoyltransferase
  5. Glutamate formiminotransferase
  6. Glutamate formyltransferase
  7. Formimidoyltetrahydrofolate cyclodeaminase
  8. Formiminotetrahydrofolate cyclodeaminase
Enzyme 20 Gene Name FTCD
Enzyme 20 Protein Sequence >Formimidoyltransferase-cyclodeaminase
MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVE
GALNAARVASRLIDMSRHQGEHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELD
VPVYLYGEAARMDSRRTLPAIRAGEYEALPKKLQQADWAPDFGPSSFVPSWGATATGARK
FLIAFNINLLGTKEQAHRIALNLREQGRGKDQPGRLKKVQGIGWYLDEKNLAQVSTNLLD
FEVTALHTVYEETCREAQELSLPVVGSQLVGLVPLKALLDAAAFYCEKENLFILEEEQRI
RLVVSRLGLDSLCPFSPKERIIEYLVPERGPERGLGSKSLRAFVGEVGARSAAPGGGSVA
AAAAAMGAALGSMVGLMTYGRRQFQSLDTTMRRLIPPFREASAKLTTLVDADAEAFTAYL
EAMRLPKNTPEEKDRRTAALQEGLRRAVSVPLTLAETVASLWPALQELARCGNLACRSDL
QVAAKALEMGVFGAYFNVLINLRDITDEAFKDQIHHRVSSLLQEAKTQAALVLDCLETRQ
E
Enzyme 20 Number of Residues 541
Enzyme 20 Molecular Weight 58925.9
Enzyme 20 Theoretical pI 5.45
Enzyme 20 GO Classification
Function
  • amino acid binding
  • binding
  • carboxylic acid binding
  • catalytic activity
  • folic acid binding
  • transferase activity
Process
  • cellular metabolic process
  • metabolic process
Component
Enzyme 20 General Function Involved in catalytic activity
Enzyme 20 Specific Function Binds and promotes bundling of vimentin filaments originating from the Golgi
Enzyme 20 Pathways
Enzyme 20 Reactions
  • 5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH3 [RN:R02302]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 6537208 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID O95954 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name FTCD_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1626 bp
ATGTCCCAGCTGGTGGAATGCGTCCCCAACTTTTCGGAGGGGAAGAACCAGGAGGTGATC
GACGCCATCTCTGGAGCCATCACACAGACCCCGGGCTGCGTGCTGCTGGATGTGGACGCA
GGCCCTTCCACCAACCGCACCGTGTACACCTTCGTGGGGCCGCCGGAGTGCGTGGTGGAG
GGGGCCCTCAACGCTGCCCGGGTAGCTTCCCGACTTATCGACATGAGCAGGCACCAAGGA
GAGCACCCCCGCATGGGGGCCCTAGACGTCTGCCCCTTCATCCCCGTGAGGGGCGTCAGC
GTGGATGAGTGTGTGCTCTGCGCCCAGGCCTTTGGCCAGAGGCTGGCAGAGGAGCTGGAC
GTGCCAGTTTACCTGTACGGCGAGGCAGCCAGGATGGACAGTCGCCGGACCCTGCCGGCC
ATCCGGGCCGGGGAGTACGAGGCCCTCCCTAAGAAGCTCCAGCAGGCCGACTGGGCGCCC
GACTTTGGTCCCAGCTCCTTTGTCCCCAGTTGGGGGGCCACGGCCACGGGGGCGAGGAAG
TTCCTCATTGCTTTTAACATCAACCTGCTCGGCACAAAGGAGCAAGCCCACCGCATCGCG
CTCAACCTGCGGGAGCAGGGCCGCGGGAAGGACCAGCCAGGACGTCTGAAGAAAGTTCAG
GGCATTGGCTGGTACCTGGATGAGAAGAACCTGGCTCAGGTGTCCACCAATCTTCTGGAC
TTTGAGGTCACGGCACTGCACACGGTCTACGAGGAGACCTGCCGAGAAGCACAGGAGCTG
AGCCTCCCAGTGGTGGGCTCACAGCTGGTGGGCCTGGTGCCCCTGAAGGCTCTGCTGGAT
GCGGCCGCCTTCTACTGCGAGAAGGAGAACCTCTTCATCCTGGAGGAGGAGCAGCGGATC
AGGCTGGTGGTGAGCCGGCTGGGCCTGGACTCCCTGTGCCCCTTCAGCCCTAAGGAGCGG
ATCATCGAGTACCTGGTCCCTGAGCGCGGGCCTGAGCGAGGCCTGGGCAGCAAGTCCCTG
CGCGCCTTCGTGGGGGAGGTGGGTGCCCGCTCTGCGGCCCCCGGGGGCGGCTCGGTGGCG
GCGGCCGCTGCGGCCATGGGTGCGGCGCTGGGCTCCATGGTGGGCCTCATGACCTACGGG
CGGCGCCAATTCCAGTCCCTGGACACGACGATGCGGCGCCTGATCCCGCCCTTCCGCGAG
GCTTCGGCCAAGCTAACCACGCTGGTGGATGCCGACGCCGAGGCCTTCACCGCCTACCTG
GAAGCAATGAGGCTCCCCAAGAACACACCTGAGGAAAAGGACAGGCGCACGGCGGCCCTA
CAGGAGGGTCTGAGGCGGGCAGTCTCTGTGCCGCTGACGCTGGCGGAGACGGTGGCCTCG
CTGTGGCCGGCGCTGCAGGAACTGGCCCGGTGTGGGAACCTGGCCTGCCGGTCAGACCTC
CAGGTGGCGGCCAAAGCCCTGGAGATGGGCGTGTTTGGCGCATATTTCAACGTGCTCATC
AACCTGAGGGACATCACAGACGAGGCATTTAAGGACCAGATCCACCATCGTGTTTCCAGC
CTCCTGCAGGAAGCCAAGACCCAGGCTGCACTGGTGCTGGACTGCTTGGAGACCCGGCAG
GAGTGA
Enzyme 20 GenBank Gene ID AF169017 Link Image
Enzyme 20 GeneCard ID FTCD Link Image
Enzyme 20 GenAtlas ID FTCD Link Image
Enzyme 20 HGNC ID HGNC:3974 Link Image
Enzyme 20 Chromosome Location 2
Enzyme 20 Locus 21q22.3
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Solans A, Estivill X, de la Luna S: Cloning and characterization of human FTCD on 21q22.3, a candidate gene for glutamate formiminotransferase deficiency. Cytogenet Cell Genet. 2000;88(1-2):43-9. [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. Lapierre P, Hajoui O, Homberg JC, Alvarez F: Formiminotransferase cyclodeaminase is an organ-specific autoantigen recognized by sera of patients with autoimmune hepatitis. Gastroenterology. 1999 Mar;116(3):643-9. [PubMed Link Image]
  4. Hillman RT, Green RE, Brenner SE: An unappreciated role for RNA surveillance. Genome Biol. 2004;5(2):R8. Epub 2004 Feb 2. [PubMed Link Image]
  5. Hagiwara H, Tajika Y, Matsuzaki T, Suzuki T, Aoki T, Takata K: Localization of Golgi 58K protein (formiminotransferase cyclodeaminase) to the centrosome. Histochem Cell Biol. 2006 Aug;126(2):251-9. Epub 2006 Mar 14. [PubMed Link Image]
  6. Hilton JF, Christensen KE, Watkins D, Raby BA, Renaud Y, de la Luna S, Estivill X, MacKenzie RE, Hudson TJ, Rosenblatt DS: The molecular basis of glutamate formiminotransferase deficiency. Hum Mutat. 2003 Jul;22(1):67-73. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5967
Enzyme 21 Name Glutamate dehydrogenase 1, mitochondrial
Enzyme 21 Synonyms
  1. GDH 1
Enzyme 21 Gene Name GLUD1
Enzyme 21 Protein Sequence >Glutamate dehydrogenase 1, mitochondrial
MYRYLGEALLLSRAGPAALGSASADSAALLGWARGQPAAAPQPGLALAARRHYSEAVADR
EDDPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPCNHVLSLSF
PIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFG
GAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTY
ASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFG
DKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILG
FPKAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLER
NIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGK
HGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYV
NAIEKVFKVYNEAGVTFT
Enzyme 21 Number of Residues 558
Enzyme 21 Molecular Weight 61397.3
Enzyme 21 Theoretical pI 7.91
Enzyme 21 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
Enzyme 21 General Function Involved in oxidoreductase activity
Enzyme 21 Specific Function May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate
Enzyme 21 Pathways
Enzyme 21 Reactions
  • L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H + H+ [RN:R00243 R00248]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 31707 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID P00367 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name DHE3_HUMAN Link Image
Enzyme 21 PDB ID 1L1F Link Image
Enzyme 21 PDB File Show
Enzyme 21 3D Structure
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1677 bp
ATGTACCGCTACCTGGGCGAAGCGCTGTTGCTGTCCCGGGCCGGGCCCGCTGCCCTGGGC
TCGGCGTCCGCCGACTCGGCCGCGTTGCTGGGCTGGGCCCGGGGACAGCCCGCCGCCGCC
CCGCAGCCGGGGCTGGCATTGGCCGCCCGGCGCCACTACAGCGAGGCGGTGGCCGACCGC
GAGGACGACCCCAACTTCTTCAAGATGGTGGAGGGCTTCTTCGATCGCGGCGCCAGCATC
GTGGAGGACAAGCTGGTGGAGGACCTGAGGACCCGGGAGAGCGAGGAGCAGAAGCGGAAC
CGGGTGCGCGGCATCCTGCGGATCATCAAGCCCTGCAACCATGTGCTGAGTCTCTCCTTC
CCCATCCGGCGCGACGACGGCTCCTGGGAGGTCATCGAAGGCTACCGGGCCCAGCACAGC
CAGCACCGCACGCCCTGCAAGGGAGGTATCCGTTACAGCACTGATGTGAGTGTAGATGAA
GTAAAAGCTTTGGCTTCTCTGATGACATACAAGTGTGCAGTGGTTGATGTGCCGTTTGGG
GGTGCTAAAGCTGGTGTTAAGATCAATCCCAAGAACTATACTGATAATGAATTGGAAAAG
ATCACAAGGAGGTTCACCATGGAGCTAGCAAAAAAGGGCTTTATTGGTCCTGGCATTGAT
GTGCCTGCTCCAGACATGAGCACAGGTGAGCGGGAGATGTCCTGGATCGCTGATACCTAT
GCCAGCACCATAGGGCACTATGATATTAATGCACACGCCTGTGTTACTGGTAAACCCATC
AGCCAAGGGGGAATCCATGGACGCATCTCTGCTACTGGCCGTGGTGTCTTCCATGGGATT
GAAAATTTCATCAATGAAGCTTCTTACATGAGCATTTTAGGAATGACACCAGGGTTTGGA
GATAAAACATTTGTTGTTCAGGGATTTGGTAATGTGGGCCTACACTCTATGAGATATTTA
CATCGTTTTGGTGCTAAATGTATTGCTGTTGGTGAGTCTGATGGGAGTATATGGAATCCA
GATGGTATTGACCCAAAGGAACTGGAAGACTTCAAATTGCAACATGGGTCCATTCTGGGC
TTCCCCAAGGCAAAGCCCTATGAAGGAAGCATCTTGGAGGCCGACTGTGACATACTGATC
CCAGCTGCCAGTGAGAAGCAGTTGACCAAATCCAACGCACCCAGAGTCAAAGCCAAGATC
ATTGCTGAAGGTGCCAATGGGCCAACAACTCCAGAAGCTGACAAGATCTTCCTGGAGAGA
AACATTATGGTTATTCCAGATCTCTACTTGAATGCTGGAGGAGTGACAGTATCTTACTTT
GAGTGGCTGAAGAATCTAAATCATGTCAGCTATGGCCGTTTGACCTTCAAATATGAAAGG
GATTCTAACTACCACTTGCTCATGTCTGTTCAAGAGAGTTTAGAAAGAAAATTTGGAAAG
CATGGTGGAACTATTCCCATTGTACCCACGGCAGAGTTCCAAGACAGGATATCGGGTGCA
TCTGAGAAAGACATCGTGCACTCTGGCTTGGCATACACAATGGAGCGTTCTGCCAGGCAA
ATTATGCGCACAGCCATGAAGTATAACCTGGGATTGGACCTGAGAACAGCTGCCTATGTT
AATGCCATTGAGAAAGTCTTCAAAGTGTACAATGAAGCTGGTGTGACCTTCACATAG
Enzyme 21 GenBank Gene ID X07674 Link Image
Enzyme 21 GeneCard ID GLUD1 Link Image
Enzyme 21 GenAtlas ID GLUD1 Link Image
Enzyme 21 HGNC ID HGNC:4335 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 10q23.3
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Nakatani Y, Banner C, von Herrath M, Schneider ME, Smith HH, Freese E: Comparison of human brain and liver glutamate dehydrogenase cDNAS. Biochem Biophys Res Commun. 1987 Dec 16;149(2):405-10. [PubMed Link Image]
  2. Amuro N, Yamaura M, Goto Y, Okazaki T: Molecular cloning and nucleotide sequence of the cDNA for human liver glutamate dehydrogenase precursor. Biochem Biophys Res Commun. 1988 May 16;152(3):1395-400. [PubMed Link Image]
  3. Nakatani Y, Schneider M, Banner C, Freese E: Complete nucleotide sequence of human glutamate dehydrogenase cDNA. Nucleic Acids Res. 1988 Jul 11;16(13):6237. [PubMed Link Image]
  4. Mavrothalassitis G, Tzimagiorgis G, Mitsialis A, Zannis V, Plaitakis A, Papamatheakis J, Moschonas N: Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family. Proc Natl Acad Sci U S A. 1988 May;85(10):3494-8. [PubMed Link Image]
  5. Michaelidis TM, Tzimagiorgis G, Moschonas NK, Papamatheakis J: The human glutamate dehydrogenase gene family: gene organization and structural characterization. Genomics. 1993 Apr;16(1):150-60. [PubMed Link Image]
  6. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Julliard JH, Smith EL: Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme. J Biol Chem. 1979 May 10;254(9):3427-38. [PubMed Link Image]
  9. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  10. Banner C, Silverman S, Thomas JW, Lampel KA, Vitkovic L, Huie D, Wenthold RJ: Isolation of a human brain cDNA for glutamate dehydrogenase. J Neurochem. 1987 Jul;49(1):246-52. [PubMed Link Image]
  11. Tzimagiorgis G, Leversha MA, Chroniary K, Goulielmos G, Sargent CA, Ferguson-Smith M, Moschonas NK: Structure and expression analysis of a member of the human glutamate dehydrogenase (GLUD) gene family mapped to chromosome 10p11.2. Hum Genet. 1993 Jun;91(5):433-8. [PubMed Link Image]
  12. 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]
  13. 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]
  14. 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]
  15. Smith TJ, Peterson PE, Schmidt T, Fang J, Stanley CA: Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation. J Mol Biol. 2001 Mar 23;307(2):707-20. [PubMed Link Image]
  16. Fang J, Hsu BY, MacMullen CM, Poncz M, Smith TJ, Stanley CA: Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. Biochem J. 2002 Apr 1;363(Pt 1):81-7. [PubMed Link Image]
  17. Smith TJ, Schmidt T, Fang J, Wu J, Siuzdak G, Stanley CA: The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol. 2002 May 3;318(3):765-77. [PubMed Link Image]
  18. Banerjee S, Schmidt T, Fang J, Stanley CA, Smith TJ: Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation. Biochemistry. 2003 Apr 1;42(12):3446-56. [PubMed Link Image]
  19. Meissner T, Beinbrech B, Mayatepek E: Congenital hyperinsulinism: molecular basis of a heterogeneous disease. Hum Mutat. 1999;13(5):351-61. [PubMed Link Image]
  20. Stanley CA, Lieu YK, Hsu BY, Burlina AB, Greenberg CR, Hopwood NJ, Perlman K, Rich BH, Zammarchi E, Poncz M: Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene. N Engl J Med. 1998 May 7;338(19):1352-7. [PubMed Link Image]
  21. Miki Y, Taki T, Ohura T, Kato H, Yanagisawa M, Hayashi Y: Novel missense mutations in the glutamate dehydrogenase gene in the congenital hyperinsulinism-hyperammonemia syndrome. J Pediatr. 2000 Jan;136(1):69-72. [PubMed Link Image]
  22. Santer R, Kinner M, Passarge M, Superti-Furga A, Mayatepek E, Meissner T, Schneppenheim R, Schaub J: Novel missense mutations outside the allosteric domain of glutamate dehydrogenase are prevalent in European patients with the congenital hyperinsulinism-hyperammonemia syndrome. Hum Genet. 2001 Jan;108(1):66-71. [PubMed Link Image]
  23. MacMullen C, Fang J, Hsu BY, Kelly A, de Lonlay-Debeney P, Saudubray JM, Ganguly A, Smith TJ, Stanley CA: Hyperinsulinism/hyperammonemia syndrome in children with regulatory mutations in the inhibitory guanosine triphosphate-binding domain of glutamate dehydrogenase. J Clin Endocrinol Metab. 2001 Apr;86(4):1782-7. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5975
Enzyme 22 Name Glutamate decarboxylase 2
Enzyme 22 Synonyms
  1. 65 kDa glutamic acid decarboxylase
  2. GAD-65
  3. Glutamate decarboxylase 65 kDa isoform
Enzyme 22 Gene Name GAD2
Enzyme 22 Protein Sequence >Glutamate decarboxylase 2
MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGG
SQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQ
YVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFN
QLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFS
PGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVI
LIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIW
MHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQ
MHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEY
LYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRLSKVAPVIKARMMEY
GTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL
Enzyme 22 Number of Residues 585
Enzyme 22 Molecular Weight 65410.8
Enzyme 22 Theoretical pI 6.89
Enzyme 22 GO Classification
Function
  • binding
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • cofactor binding
  • lyase activity
  • pyridoxal phosphate binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • metabolic process
  • organic acid metabolic process
  • oxoacid metabolic process
Component
Enzyme 22 General Function Involved in carboxy-lyase activity
Enzyme 22 Specific Function Catalyzes the production of GABA
Enzyme 22 Pathways
Enzyme 22 Reactions
  • L-glutamate = 4-aminobutanoate + CO2 [RN:R00261]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID Q05329 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name DCE2_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1758 bp
ATGGCATCTCCGGGCTCTGGCTTTTGGTCTTTCGGGTCGGAAGATGGCTCTGGGGATTCC
GAGAATCCCGGCACAGCGCGAGCCTGGTGCCAAGTGGCTCAGAAGTTCACGGGCGGCATC
GGAAACAAACTGTGCGCCCTGCTCTACGGAGACGCCGAGAAGCCGGCGGAGAGCGGCGGG
AGCCAACCCCCGCGGGCCGCCGCCCGGAAGGCCGCCTGCGCCTGCGACCAGAAGCCCTGC
AGCTGCTCCAAAGTGGATGTCAACTACGCGTTTCTCCATGCAACAGACCTGCTGCCGGCG
TGTGATGGAGAAAGGCCCACTTTGGCGTTTCTGCAAGATGTTATGAACATTTTACTTCAG
TATGTGGTGAAAAGTTTCGATAGATCAACCAAAGTGATTGATTTCCATTATCCTAATGAG
CTTCTCCAAGAATATAATTGGGAATTGGCAGACCAACCACAAAATTTGGAGGAAATTTTG
ATGCATTGCCAAACAACTCTAAAATATGCAATTAAAACAGGGCATCCTAGATACTTCAAT
CAACTTTCTACTGGTTTGGATATGGTTGGATTAGCAGCAGACTGGCTGACATCAACAGCA
AATACTAACATGTTCACCTATGAAATTGCTCCAGTATTTGTGCTTTTGGAATATGTCACA
CTAAAGAAAATGAGAGAAATCATTGGCTGGCCAGGGGGCTCTGGCGATGGGATATTTTCT
CCCGGTGGCGCCATATCTAACATGTATGCCATGATGATCGCACGCTTTAAGATGTTCCCA
GAAGTCAAGGAGAAAGGAATGGCTGCTCTTCCCAGGCTCATTGCCTTCACGTCTGAACAT
AGTCATTTTTCTCTCAAGAAGGGAGCTGCAGCCTTAGGGATTGGAACAGACAGCGTGATT
CTGATTAAATGTGATGAGAGAGGGAAAATGATTCCATCTGATCTTGAAAGAAGGATTCTT
GAAGCCAAACAGAAAGGGTTTGTTCCTTTCCTCGTGAGTGCCACAGCTGGAACCACCGTG
TACGGAGCATTTGACCCCCTCTTAGCTGTCGCTGACATTTGCAAAAAGTATAAGATCTGG
ATGCATGTGGATGCAGCTTGGGGTGGGGGATTACTGATGTCCCGAAAACACAAGTGGAAA
CTGAGTGGCGTGGAGAGGGCCAACTCTGTGACGTGGAATCCACACAAGATGATGGGAGTC
CCTTTGCAGTGCTCTGCTCTCCTGGTTAGAGAAGAGGGATTGATGCAGAATTGCAACCAA
ATGCATGCCTCCTACCTCTTTCAGCAAGATAAACATTATGACCTGTCCTATGACACTGGA
GACAAGGCCTTACAGTGCGGACGCCACGTTGATGTTTTTAAACTATGGCTGATGTGGAGG
GCAAAGGGGACTACCGGGTTTGAAGCGCATGTTGATAAATGTTTGGAGTTGGCAGAGTAT
TTATACAACATCATAAAAAACCGAGAAGGATATGAGATGGTGTTTGATGGGAAGCCTCAG
CACACAAATGTCTGCTTCTGGTACATTCCTCCAAGCTTGCGTACTCTGGAAGACAATGAA
GAGAGAATGAGTCGCCTCTCGAAGGTGGCTCCAGTGATTAAAGCCAGAATGATGGAGTAT
GGAACCACAATGGTCAGCTACCAACCCTTGGGAGACAAGGTCAATTTCTTCCGCATGGTC
ATCTCAAACCCAGCGGCAACTCACCAAGACATTGACTTCCTGATTGAAGAAATAGAACGC
CTTGGACAAGATTTATAA
Enzyme 22 GenBank Gene ID M81882 Link Image
Enzyme 22 GeneCard ID GAD2 Link Image
Enzyme 22 GenAtlas ID GAD2 Link Image
Enzyme 22 HGNC ID HGNC:4093 Link Image
Enzyme 22 Chromosome Location 1
Enzyme 22 Locus 10p11.23
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Karlsen AE, Hagopian WA, Grubin CE, Dube S, Disteche CM, Adler DA, Barmeier H, Mathewes S, Grant FJ, Foster D, et al.: Cloning and primary structure of a human islet isoform of glutamic acid decarboxylase from chromosome 10. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8337-41. [PubMed Link Image]
  2. Bu DF, Erlander MG, Hitz BC, Tillakaratne NJ, Kaufman DL, Wagner-McPherson CB, Evans GA, Tobin AJ: Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2115-9. [PubMed Link Image]
  3. Bu DF, Tobin AJ: The exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD. Genomics. 1994 May 1;21(1):222-8. [PubMed Link Image]
  4. Mauch L, Abney CC, Berg H, Scherbaum WA, Liedvogel B, Northemann W: Characterization of a linear epitope within the human pancreatic 64-kDa glutamic acid decarboxylase and its autoimmune recognition by sera from insulin-dependent diabetes mellitus patients. Eur J Biochem. 1993 Mar 1;212(2):597-603. [PubMed Link Image]
  5. Kim J, Richter W, Aanstoot HJ, Shi Y, Fu Q, Rajotte R, Warnock G, Baekkeskov S: Differential expression of GAD65 and GAD67 in human, rat, and mouse pancreatic islets. Diabetes. 1993 Dec;42(12):1799-808. [PubMed Link Image]
  6. Namchuk M, Lindsay L, Turck CW, Kanaani J, Baekkeskov S: Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65alpha. J Biol Chem. 1997 Jan 17;272(3):1548-57. [PubMed Link Image]
  7. Kanaani J, el-Husseini Ael-D, Aguilera-Moreno A, Diacovo JM, Bredt DS, Baekkeskov S: A combination of three distinct trafficking signals mediates axonal targeting and presynaptic clustering of GAD65. J Cell Biol. 2002 Sep 30;158(7):1229-38. [PubMed Link Image]
  8. Corper AL, Stratmann T, Apostolopoulos V, Scott CA, Garcia KC, Kang AS, Wilson IA, Teyton L: A structural framework for deciphering the link between I-Ag7 and autoimmune diabetes. Science. 2000 Apr 21;288(5465):505-11. [PubMed Link Image]
  9. Fenalti G, Law RH, Buckle AM, Langendorf C, Tuck K, Rosado CJ, Faux NG, Mahmood K, Hampe CS, Banga JP, Wilce M, Schmidberger J, Rossjohn J, El-Kabbani O, Pike RN, Smith AI, Mackay IR, Rowley MJ, Whisstock JC: GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop. Nat Struct Mol Biol. 2007 Apr;14(4):280-6. Epub 2007 Mar 25. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5976
Enzyme 23 Name Glutamate decarboxylase 1
Enzyme 23 Synonyms
  1. 67 kDa glutamic acid decarboxylase
  2. GAD-67
  3. Glutamate decarboxylase 67 kDa isoform
Enzyme 23 Gene Name GAD1
Enzyme 23 Protein Sequence >Glutamate decarboxylase 1
MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEK
SRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEV
VDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGV
RTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWS
SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAA
LGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIA
DICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKE
KGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQI
NKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAP
KIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL
Enzyme 23 Number of Residues 594
Enzyme 23 Molecular Weight 66896.1
Enzyme 23 Theoretical pI 7.67
Enzyme 23 GO Classification
Function
  • binding
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • cofactor binding
  • lyase activity
  • pyridoxal phosphate binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • metabolic process
  • organic acid metabolic process
  • oxoacid metabolic process
Component
Enzyme 23 General Function Involved in carboxy-lyase activity
Enzyme 23 Specific Function Catalyzes the production of GABA
Enzyme 23 Pathways
Enzyme 23 Reactions
  • L-glutamate = 4-aminobutanoate + CO2 [RN:R00261]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 62988850 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q99259 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name DCE1_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1785 bp
ATGGCGTCTTCGACCCCATCTTCGTCCGCAACCTCCTCGAACGCGGGAGCGGACCCCAAT
ACCACTAACCTGCGCCCCACAACGTACGATACCTGGTGCGGCGTGGCCCATGGATGCACC
AGAAAACTGGGGCTCAAGATCTGCGGCTTCTTGCAAAGGACCAACAGCCTGGAAGAGAAG
AGTCGCCTTGTGAGTGCCTTCAAGGAGAGGCAATCCTCCAAGAACCTGCTTTCCTGTGAA
AACAGCGACCGGGATGCCCGCTTCCGGCGCACAGAGACTGACTTCTCTAATCTGTTTGCT
AGAGATCTGCTTCCGGCTAAGAACGGTGAGGAGCAAACCGTGCAATTCCTCCTGGAAGTG
GTGGACATACTCCTCAACTATGTCCGCAAGACATTTGATCGCTCCACCAAGGTGCTGGAC
TTTCATCACCCACACCAGTTGCTGGAAGGCATGGAGGGCTTCAACTTGGAGCTCTCTGAC
CACCCCGAGTCCCTGGAGCAGATCCTGGTTGACTGCAGAGACACCTTGAAGTATGGGGTT
CGCACAGGTCATCCTCGATTTTTCAACCAGCTCTCCACTGGATTGGATATTATTGGCCTA
GCTGGAGAATGGCTGACATCAACGGCCAATACCAACATGTTTACATATGAAATTGCACCA
GTGTTTGTCCTCATGGAACAAATAACACTTAAGAAGATGAGAGAGATAGTTGGATGGTCA
AGTAAAGATGGTGATGGGATATTTTCTCCTGGGGGCGCCATATCCAACATGTACAGCATC
ATGGCTGCTCGCTACAAGTACTTCCCGGAAGTTAAGACAAAGGGCATGGCGGCTGTGCCT
AAACTGGTCCTCTTCACCTCAGAACAGAGTCACTATTCCATAAAGAAAGCTGGGGCTGCA
CTTGGCTTTGGAACTGACAATGTGATTTTGATAAAGTGCAATGAAAGGGGGAAAATAATT
CCAGCTGATTTTGAGGCAAAAATTCTTGAAGCCAAACAGAAGGGATATGTTCCCTTTTAT
GTCAATGCAACTGCTGGCACGACTGTTTATGGAGCTTTTGATCCGATACAAGAGATTGCA
GATATATGTGAGAAATATAACCTTTGGTTGCATGTCGATGCTGCCTGGGGAGGTGGGCTG
CTCATGTCCAGGAAGCACCGCCATAAACTCAACGGCATAGAAAGGGCCAACTCAGTCACC
TGGAACCCTCACAAGATGATGGGCGTGCTGTTGCAGTGCTCTGCCATTCTCGTCAAGGAA
AAGGGTATACTCCAAGGATGCAACCAGATGTGTGCAGGATACCTCTTCCAGCCAGACAAG
CAGTATGATGTCTCCTACGACACCGGGGACAAGGCAATTCAGTGTGGCCGCCACGTGGAT
ATCTTCAAGTTCTGGCTGATGTGGAAAGCAAAGGGCACAGTGGGATTTGAAAACCAGATC
AACAAATGCCTGGAACTGGCTGAATACCTCTATGCCAAGATTAAAAACAGAGAAGAATTT
GAGATGGTTTTCAATGGCGAGCCTGAGCACACAAACGTCTGTTTTTGGTATATTCCACAA
AGCCTCAGGGGTGTGCCAGACAGCCCTCAACGACGGGAAAAGCTACACAAGGTGGCTCCA
AAAATCAAAGCCCTGATGATGGAGTCAGGTACGACCATGGTTGGCTACCAGCCCCAAGGG
GACAAGGCCAACTTCTTCCGGATGGTCATCTCCAACCCAGCCGCTACCCAGTCTGACATT
GACTTCCTCATTGAGGAGATAGAAAGACTGGGCCAGGATCTGTAA
Enzyme 23 GenBank Gene ID AC007405 Link Image
Enzyme 23 GeneCard ID GAD1 Link Image
Enzyme 23 GenAtlas ID GAD1 Link Image
Enzyme 23 HGNC ID HGNC:4092 Link Image
Enzyme 23 Chromosome Location 2
Enzyme 23 Locus 2q31
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Bu DF, Erlander MG, Hitz BC, Tillakaratne NJ, Kaufman DL, Wagner-McPherson CB, Evans GA, Tobin AJ: Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2115-9. [PubMed Link Image]
  2. Bu DF, Tobin AJ: The exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD. Genomics. 1994 May 1;21(1):222-8. [PubMed Link Image]
  3. Kelly C, Carter ND, Johnstone AP, Nussey SS: Cloning of large isoform of human brain glutamic acid decarboxylase. Lancet. 1991 Dec 7;338(8780):1468-9. [PubMed Link Image]
  4. Kelly CD, Edwards Y, Johnstone AP, Harfst E, Nogradi A, Nussey SS, Povey S, Carter ND: Nucleotide sequence and chromosomal assignment of a cDNA encoding the large isoform of human glutamate decarboxylase. Ann Hum Genet. 1992 Jul;56(Pt 3):255-65. [PubMed Link Image]
  5. Yamashita K, Cram DS, Harrison LC: Molecular cloning of full-length glutamic acid decarboxylase 67 from human pancreas and islets. Biochem Biophys Res Commun. 1993 May 14;192(3):1347-52. [PubMed Link Image]
  6. Kawasaki E, Moriuchi R, Watanabe M, Saitoh K, Brunicardi FC, Watt PC, Yamaguchi T, Mullen Y, Akazawa S, Miyamoto T, et al.: Cloning and expression of large isoform of glutamic acid decarboxylase from human pancreatic islet. Biochem Biophys Res Commun. 1993 May 14;192(3):1353-9. [PubMed Link Image]
  7. Chessler SD, Lernmark A: Alternative splicing of GAD67 results in the synthesis of a third form of glutamic-acid decarboxylase in human islets and other non-neural tissues. J Biol Chem. 2000 Feb 18;275(7):5188-92. [PubMed Link Image]
  8. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  9. 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]
  10. Cram DS, Barnett LD, Joseph JL, Harrison LC: Cloning and partial nucleotide sequence of human glutamic acid decarboxylase cDNA from brain and pancreatic islets. Biochem Biophys Res Commun. 1991 May 15;176(3):1239-44. [PubMed Link Image]
  11. Persson H, Pelto-Huikko M, Metsis M, Soder O, Brene S, Skog S, Hokfelt T, Ritzen EM: Expression of the neurotransmitter-synthesizing enzyme glutamic acid decarboxylase in male germ cells. Mol Cell Biol. 1990 Sep;10(9):4701-11. [PubMed Link Image]
  12. Fenalti G, Law RH, Buckle AM, Langendorf C, Tuck K, Rosado CJ, Faux NG, Mahmood K, Hampe CS, Banga JP, Wilce M, Schmidberger J, Rossjohn J, El-Kabbani O, Pike RN, Smith AI, Mackay IR, Rowley MJ, Whisstock JC: GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop. Nat Struct Mol Biol. 2007 Apr;14(4):280-6. Epub 2007 Mar 25. [PubMed Link Image]
  13. Lynex CN, Carr IM, Leek JP, Achuthan R, Mitchell S, Maher ER, Woods CG, Bonthon DT, Markham AF: Homozygosity for a missense mutation in the 67 kDa isoform of glutamate decarboxylase in a family with autosomal recessive spastic cerebral palsy: parallels with Stiff-Person Syndrome and other movement disorders. BMC Neurol. 2004 Nov 30;4(1):20. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 6005
Enzyme 24 Name Gamma-glutamyltranspeptidase 1
Enzyme 24 Synonyms
  1. GGT 1
  2. Gamma-glutamyltransferase 1
  3. CD224 antigen
  4. Gamma-glutamyltranspeptidase 1 heavy chain
  5. Gamma-glutamyltranspeptidase 1 light chain
Enzyme 24 Gene Name GGT1
Enzyme 24 Protein Sequence >Gamma-glutamyltranspeptidase 1
MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCSKIGRDALRD
GGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFN
SSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALEN
KRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKD
IQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSR
ESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISD
DTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNE
MDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTA
TALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTF
IAVVQAIVRTAGGWAAASDSRKGGEPAGY
Enzyme 24 Number of Residues 569
Enzyme 24 Molecular Weight 61409.7
Enzyme 24 Theoretical pI 7.14
Enzyme 24 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
Component
Enzyme 24 General Function Involved in gamma-glutamyltransferase activity
Enzyme 24 Specific Function Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive
Enzyme 24 Pathways
Enzyme 24 Reactions
  • (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid [RN:R04159]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • 5-26
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 183138 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P19440 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name GGT1_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1710 bp
ATGAAGAAGAAGTTAGTGGTGCTGGGCCTGCTGGCCGTGGTCCTGGTGCTGGTCATTGTC
GGCCTCTGTCTCTGGCTGCCCTCAGCCTCCAAGGAACCTGACAACCATGTGTACACCAGG
GCTGCCGTGGCCGCGGATGCCAAGCAGTGCTCGAAGATTGGGAGGGATGCACTGCGGGAC
GGTGGCTCTGCGGTGGATGCAGCCATTGCAGCCCTGTTGTGTGTGGGGCTCATGAATGCC
CACAGCATGGGCATCGGGGGTGGCCTCTTCCTCACCATCTACAACAGCACCACACGAAAA
GCTGAGGTCATCAACGCCCGCGAGGTGGCCCCCAGGCTGGCCTTTGCCACCATGTTCAAC
AGCTCGGAGCAGTCCCAGAAGGGGGGGCTGTCGGTGGCGGTGCCTGGGGAGATCCGAGGC
TATGAGCTGGCACACCAGCGGCATGGGCGGCTGCCCTGGGCTCGCCTCTTCCAGCCCAGC
ATCCAGCTGGCCCGCCAGGGCTTCCCCGTGGGCAAGGGCTTGGCGGCAGCCCTGGAAAAC
AAGCGGACCGTCATCGAGCAGCAGCCTGTCTTGTGTGAGGTGTTCTGCCGGGATAGAAAG
GTGCTTCGGGAGGGGGAGAGACTGACCCTGCCGCAGCTGGCTGACACCTACGAGACGCTG
GCCATCGAGGGTGCCCAGGCCTTCTACAACGGCAGCCTCACGGCCCAGATTGTGAAGGAC
ATCCAGGCGGCCGGGGGCATTGTGACAGCTGAGGACCTGAACAACTACCGTGCTGAGCTG
ATCGAGCACCCGCTGAACATCAGCCTGGGAGACGCGGTGCTGTACATGCCCAGTGCGCCG
CTCAGCGGGCCCGTGCTGGCCCTCATCCTCAACATCCTCAAAGGGTACAACTTCTCCCGG
GAGAGCGTGGAGAGCCCCGAGCAGAAGGGCCTGACGTACCACCGCATCGTAGAGGCTTTC
CGGTTTGCCTACGCCAAGAGGACCCTGCTTGGGGACCCCAAGTTTGTGGATGTGACTGAG
GTGGTCCGCAACATGACCTCCGAGTTCTTCGCTGCCCAGCTCCGGGCCCAGATCTCTGAC
GACACCACTCACCCGATCTCCTACTACAAGCCCGAGTTCTACACGCCGGATGACGGGGGC
ACTGCTCACCTGTCTGTCGTCGCAGAGGACGGCAGTGCTGTGTCCGCCACCAGCACCATC
AACCTCTACTTTGGCTCCAAGGTCCGCTCCCCGGTCAGCGGGATCCTGTTCAATAATGAA
ATGGACGACTTCAGCTCTCCCAGCATCACCAACGAGTTTGGGGTACCCCCCTCACCTGCC
AATTTCATCCAGCCAGGGAAGCAGCCGCTCTCGTCCATGTGCCCGACGATCATGGTGGGC
CAGGACGGCCAGGTCCGGATGGTGGTGGGAGCTGCTGGGGGCACACAGATCACCACGGCC
ACTGCACTGGCCATCATCTACAACCTCTGGTTCGGCTATGACGTGAAGCGGGCCGTGGAG
GAGCCCCGGCTGCACAACCAGCTTCTGCCCAACGTCACGACAGTGGAGAGAAACATTGAC
CAGGCAGTGACTGCAGCCCTGGAGACCCGGCACCATCACACCCAGATCGCGTCCACCTTC
ATCGCTGTGGTGCAAGCCATCGTCCGCACGGCTGGTGGCTGGGCAGCTGCCTCGGACTCC
AGGAAAGGCGGGGAGCCTGCCGGCTACTGA
Enzyme 24 GenBank Gene ID J04131 Link Image
Enzyme 24 GeneCard ID GGT1 Link Image
Enzyme 24 GenAtlas ID GGT1 Link Image
Enzyme 24 HGNC ID HGNC:4250 Link Image
Enzyme 24 Chromosome Location 2
Enzyme 24 Locus 22q11.23
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Rajpert-De Meyts E, Heisterkamp N, Groffen J: Cloning and nucleotide sequence of human gamma-glutamyl transpeptidase. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8840-4. [PubMed Link Image]
  2. Sakamuro D, Yamazoe M, Matsuda Y, Kangawa K, Taniguchi N, Matsuo H, Yoshikawa H, Ogasawara N: The primary structure of human gamma-glutamyl transpeptidase. Gene. 1988 Dec 15;73(1):1-9. [PubMed Link Image]
  3. Pitot HC, Goodspeed D, Dunn T, Hendrich S, Maronpot RR, Moran S: Regulation of the expression of some genes for enzymes of glutathione metabolism in hepatotoxicity and hepatocarcinogenesis. Toxicol Appl Pharmacol. 1989 Jan;97(1):23-34. [PubMed Link Image]
  4. Goodspeed DC, Dunn TJ, Miller CD, Pitot HC: Human gamma-glutamyl transpeptidase cDNA: comparison of hepatoma and kidney mRNA in the human and rat. Gene. 1989 Mar 15;76(1):1-9. [PubMed Link Image]
  5. Pawlak A, Cohen EH, Octave JN, Schweickhardt R, Wu SJ, Bulle F, Chikhi N, Baik JH, Siegrist S, Guellaen G: An alternatively processed mRNA specific for gamma-glutamyl transpeptidase in human tissues. J Biol Chem. 1990 Feb 25;265(6):3256-62. [PubMed Link Image]
  6. Courtay C, Oster T, Michelet F, Visvikis A, Diederich M, Wellman M, Siest G: Gamma-glutamyltransferase: nucleotide sequence of the human pancreatic cDNA. Evidence for a ubiquitous gamma-glutamyltransferase polypeptide in human tissues. Biochem Pharmacol. 1992 Jun 23;43(12):2527-33. [PubMed Link Image]
  7. Wetmore LA, Gerard C, Drazen JM: Human lung expresses unique gamma-glutamyl transpeptidase transcripts. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7461-5. [PubMed Link Image]
  8. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  9. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  10. 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]
  11. Tate SS, Khadse V, Wellner D: Renal gamma-glutamyl transpeptidases: structural and immunological studies. Arch Biochem Biophys. 1988 May 1;262(2):397-408. [PubMed Link Image]
  12. Chikhi N, Holic N, Guellaen G, Laperche Y: Gamma-glutamyl transpeptidase gene organization and expression: a comparative analysis in rat, mouse, pig and human species. Comp Biochem Physiol B Biochem Mol Biol. 1999 Apr;122(4):367-80. [PubMed Link Image]
  13. Tate SS, Ross ME: Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit. J Biol Chem. 1977 Sep 10;252(17):6042-5. [PubMed Link Image]
  14. Tate SS, Galbraith RA: In vitro translation and processing of human hepatoma cell (Hep G2) gamma-glutamyl transpeptidase. Biochem Biophys Res Commun. 1988 Aug 15;154(3):1167-73. [PubMed Link Image]
  15. Ikeda Y, Fujii J, Taniguchi N: Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis. J Biol Chem. 1993 Feb 25;268(6):3980-5. [PubMed Link Image]
  16. Ikeda Y, Fujii J, Taniguchi N, Meister A: Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit. J Biol Chem. 1995 May 26;270(21):12471-5. [PubMed Link Image]
  17. Ikeda Y, Fujii J, Anderson ME, Taniguchi N, Meister A: Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase. J Biol Chem. 1995 Sep 22;270(38):22223-8. [PubMed Link Image]
  18. Ikeda Y, Fujii J, Taniguchi N: Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase. J Biochem (Tokyo). 1996 Jun;119(6):1166-70. [PubMed Link Image]
  19. Kristiansen TZ, Bunkenborg J, Gronborg M, Molina H, Thuluvath PJ, Argani P, Goggins MG, Maitra A, Pandey A: A proteomic analysis of human bile. Mol Cell Proteomics. 2004 Jul;3(7):715-28. Epub 2004 Apr 14. [PubMed Link Image]
  20. 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]
  21. 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]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 6071
Enzyme 25 Name Glutathione synthetase
Enzyme 25 Synonyms
  1. GSH synthetase
  2. GSH-S
  3. Glutathione synthase
Enzyme 25 Gene Name GSS
Enzyme 25 Protein Sequence >Glutathione synthetase
MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSA
LLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVF
LGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKIL
SNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFE
DISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQ
LAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSR
FVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVV
QCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV
Enzyme 25 Number of Residues 474
Enzyme 25 Molecular Weight 52384.3
Enzyme 25 Theoretical pI 5.73
Enzyme 25 GO Classification
Function
  • ATP binding
  • acid-amino acid ligase activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • glutathione synthase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleoside binding
  • purine nucleoside binding
Process
  • cellular metabolic process
  • glutathione biosynthetic process
  • glutathione metabolic process
  • metabolic process
  • peptide metabolic process
Component
Enzyme 25 General Function Involved in catalytic activity
Enzyme 25 Specific Function ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
Enzyme 25 Pathways
Enzyme 25 Reactions
  • ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione [RN:R00497]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein Not Available
Enzyme 25 UniProtKB/Swiss-Prot ID P48637 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name GSHB_HUMAN Link Image
Enzyme 25 PDB ID 2HGS Link Image
Enzyme 25 PDB File Show
Enzyme 25 3D Structure
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1425 bp
ATGGCCACCAACTGGGGGAGCCTCTTGCAGGATAAACAGCAGCTAGAGGAGCTGGCACGG
CAGGCCGTGGACCGGGCCCTGGCTGAGGGAGTATTGCTGAGGACCTCACAGGAGCCCACT
TCCTCGGAGGTGGTGAGCTATGCCCCATTCACGCTCTTCCCCTCACTGGTCCCCAGTGCC
CTGCTGGAGCAAGCCTATGCTGTGCAGATGGACTTCAACCTGCTAGTGGATGCTGTCAGC
CAGAACGCTGCCTTCCTGGAGCAAACTCTTTCCAGCACCATCAAACAGGATGACTTTACC
GCTCGTCTCTTTGACATCCACAAGCAAGTCCTAAAAGAGGGCATTGCCCAGACTGTGTTC
CTGGGCCTGAATCGCTCAGACTACATGTTCCAGCGCAGCGCAGATGGCTCCCCAGCCCTG
AAACAGATCGAAATCAACACCATCTCTGCCAGCTTTGGGGGCCTGGCCTCCCGGACCCCA
GCTGTGCACCGACATGTTCTCAGTGTCCTGAGTAAGACCAAAGAAGCTGGCAAGATCCTC
TCTAATAATCCCAGCAAGGGACTGGCCCTGGGAATTGCCAAAGCCTGGGAGCTCTACGGC
TCACCCAATGCTCTGGTGCTACTGATTGCTCAAGAGAAGGAAAGAAACATATTTGACCAG
CGTGCCATAGAGAATGAGCTACTGGCCAGGAACATCCATGTGATCCGACGAACATTTGAA
GATATCTCTGAAAAGGGGTCTCTGGACCAAGACCGAAGGCTGTTTGTGGATGGCCAGGAA
ATTGCTGTGGTTTACTTCCGGGATGGCTACATGCCTCGTCAGTACAGTCTACAGAATTGG
GAAGCACGTCTACTGCTGGAGAGGTCACATGCTGCCAAGTGCCCAGACATTGCCACCCAG
CTGGCTGGGACTAAGAAGGTGCAGCAGGAGCTAAGCAGGCCGGGCATGCTGGAGATGTTG
CTCCCTGGCCAGCCTGAGGCTGTGGCCCGCCTCCGCGCCACCTTTGCTGGCCTCTACTCA
CTGGATGTGGGTGAAGAAGGGGACCAGGCCATCGCCGAGGCCCTTGCTGCCCCTAGCCGG
TTTGTGCTAAAGCCCCAGAGAGAGGGTGGAGGTAACAACCTATATGGGGAGGAAATGGTA
CAGGCCCTGAAACAGCTGAAGGACAGTGAGGAGAGGGCCTCCTACATCCTCATGGAGAAG
ATCGAACCTGAGCCTTTTGAGAATTGCCTGCTACGGCCTGGCAGCCCTGCCCGAGTGGTC
CAGTGCATTTCAGAGCTGGGCATCTTTGGGGTCTATGTCAGGCAGGAAAAGACACTCGTG
ATGAACAAGCACGTGGGGCATCTACTTCGAACCAAAGCCATCGAGCATGCAGATGGTGGT
GTGGCAGCGGGAGTGGCAGTCCTGGACAACCCATACCCTGTGTGA
Enzyme 25 GenBank Gene ID L42531 Link Image
Enzyme 25 GeneCard ID GSS Link Image
Enzyme 25 GenAtlas ID GSS Link Image
Enzyme 25 HGNC ID HGNC:4624 Link Image
Enzyme 25 Chromosome Location 2
Enzyme 25 Locus 20q11.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Gali RR, Board PG: Sequencing and expression of a cDNA for human glutathione synthetase. Biochem J. 1995 Aug 15;310 ( Pt 1):353-8. [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. 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]
  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]
  6. Polekhina G, Board PG, Gali RR, Rossjohn J, Parker MW: Molecular basis of glutathione synthetase deficiency and a rare gene permutation event. EMBO J. 1999 Jun 15;18(12):3204-13. [PubMed Link Image]
  7. Shi ZZ, Habib GM, Rhead WJ, Gahl WA, He X, Sazer S, Lieberman MW: Mutations in the glutathione synthetase gene cause 5-oxoprolinuria. Nat Genet. 1996 Nov;14(3):361-5. [PubMed Link Image]
  8. Dahl N, Pigg M, Ristoff E, Gali R, Carlsson B, Mannervik B, Larsson A, Board P: Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction. Hum Mol Genet. 1997 Jul;6(7):1147-52. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 6130
Enzyme 26 Name Folylpolyglutamate synthase, mitochondrial
Enzyme 26 Synonyms
  1. Folylpoly-gamma-glutamate synthetase
  2. FPGS
  3. Tetrahydrofolylpolyglutamate synthase
  4. Tetrahydrofolate synthase
Enzyme 26 Gene Name FPGS
Enzyme 26 Protein Sequence >Folylpolyglutamate synthase, mitochondrial
MSRARSHLRAALFLAAASARGITTQVAARRGLSAWPVPQEPSMEYQDAVRMLNTLQTNAG
YLEQVKRQRGDPQTQLEAMELYLARSGLQVEDLDRLNIIHVTGTKGKGSTCAFTECILRS
YGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGSCVSMPPYFRF
LTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTSLLGDTVEKIA
WQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPMLEALEEGGPPLTLGLEGE
HQRSNAALALQLAHCWLQRQDRHGAGEPKASRPGLLWQLPLAPVFQPTSHMRLGLRNTEW
PGRTQVLRRGPLTWYLDGAHTASSAQACVRWFRQALQGRERPSGGPEVRVLLFNATGDRD
PAALLKLLQPCQFDYAVFCPNLTEVSSTGNADQQNFTVTLDQVLLRCLEHQQHWNHLDEE
QASPDLWSAPSPEPGGSASLLLAPHPPHTCSASSLVFSCISHALQWISQGRDPIFQPPSP
PKGLLTHPVAHSGASILREAAAIHVLVTGSLHLVGGVLKLLEPALSQ
Enzyme 26 Number of Residues 587
Enzyme 26 Molecular Weight 64608.5
Enzyme 26 Theoretical pI 8.00
Enzyme 26 GO Classification
Function
  • ATP binding
  • acid-amino acid ligase activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleoside binding
  • purine nucleoside binding
  • tetrahydrofolylpolyglutamate synthase activity
Process
  • biosynthetic process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative biosynthetic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
Enzyme 26 General Function Involved in tetrahydrofolylpolyglutamate synthase activity
Enzyme 26 Specific Function Conversion of folates to polyglutamate derivatives. This allows tissues to concentrate folate at higher levels than in plasma
Enzyme 26 Pathways
Enzyme 26 Reactions
  • ATP + tetrahydropteroyl-[gamma-Glu]n + L-glutamate = ADP + phosphate + tetrahydropteroyl-[gamma-Glu]n+1 [RN:R04241]
Enzyme 26 Pfam Domain Function Not Available
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 39992602 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q05932 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name FOLC_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1764 bp
ATGTCGCGGGCGCGGAGCCACCTGCGCGCCGCTCTATTCCTGGCAGCGGCGTCTGCGCGC
GGCGTAACGACCCAGGTCGCGGCGCGGCGGGGCTTGAGCGCGTGGCCGGTGCCGCAGGAG
CCGAGCATGGAGTACCAGGATGCCGTGCGCATGCTCAATACCCTGCAGACCAATGCCGGC
TACCTGGAGCAGGTGAAGCGCCAGCGGGGTGACCCTCAGACACAGTTGGAAGCCATGGAA
CTGTACCTGGCACGGAGTGGGCTGCAGGTGGAGGACTTGGACCGGCTGAACATCATCCAC
GTCACTGGGACGAAGGGGAAGGGCTCCACCTGTGCCTTCACGGAATGTATCCTCCGAAGC
TATGGCCTGAAGACGGGATTCTTTAGCTCTCCCCACCTGGTGCAGGTTCGGGAGCGGATC
CGCATCAATGGGCAGCCCATCAGTCCTGAGCTCTTCACCAAGTACTTCTGGCGCCTCTAC
CACCGGCTGGAGGAGACCAAGGATGGCAGCTGTGTCTCCATGCCCCCCTACTTCCGCTTC
CTGACACTCATGGCCTTCCACGTCTTCCTCCAAGAGAAGGTGGACCTGGCAGTGGTGGAG
GTGGGCATTGGCGGGGCTTATGACTGCACCAACATCATCAGGAAGCCTGTGGTGTGCGGA
GTCTCCTCTCTTGGCATCGACCACACCAGCCTCCTGGGGGATACGGTGGAGAAGATCGCA
TGGCAGAAAGGGGGCATCTTTAAGCAAGGTGTCCCTGCCTTCACTGTGCTCCAACCTGAA
GGTCCCCTGGCAGTGCTGAGGGACCGAGCCCAGCAGATCTCATGTCCTCTATACCTGTGT
CCGATGCTGGAGGCCCTCGAGGAAGGGGGGCCGCCGCTGACCCTGGGCCTGGAGGGGGAG
CACCAGCGGTCCAACGCCGCCTTGGCCTTGCAGCTGGCCCACTGCTGGCTGCAGCGGCAG
GACCGCCATGGTGCTGGGGAGCCAAAGGCATCCAGGCCAGGGCTCCTGTGGCAGCTGCCC
CTGGCACCTGTGTTCCAGCCCACATCCCACATGCGGCTCGGGCTTCGGAACACGGAGTGG
CCGGGCCGGACGCAGGTGCTGCGGCGCGGGCCCCTCACCTGGTACCTGGACGGTGCGCAC
ACCGCCAGCAGCGCGCAGGCCTGCGTGCGCTGGTTCCGCCAGGCGCTGCAGGGCCGCGAG
AGGCCGAGCGGTGGCCCCGAGGTTCGAGTCTTGCTCTTCAATGCTACCGGGGACCGGGAC
CCGGCGGCCCTGCTGAAGCTGCTGCAGCCCTGCCAGTTTGACTATGCCGTCTTCTGCCCT
AACCTGACAGAGGTGTCATCCACAGGCAACGCAGACCAACAGAACTTCACAGTGACACTG
GACCAGGTCCTGCTCCGCTGCCTGGAACACCAGCAGCACTGGAACCACCTGGACGAAGAG
CAGGCCAGCCCGGACCTCTGGAGTGTCCCCAGCCCAGAGCCCGGTGGGTCCGCATCCCTG
CTTCTGGCGCCCCACCCACCCCACACCTGCAGTGCCAGCTCCCTCGTCTTCAGCTGCATT
TCACATGCCTTGCAATGGATCAGCCAAGGCCGAGACCCCATCTTCCAGCCACCTAGTCCC
CCAAAGGGCCTCCTCACCCACCCTGTGGCTCACAGTGGGGCCAGCATACTCCGTGAGGCT
GCTGCCATCCATGTGCTAGTCACTGGCAGCCTGCACCTGGTGGGTGGTGTCCTGAAGCTG
CTGGAGCCCGCACTGTCCCAGTAG
Enzyme 26 GenBank Gene ID BC064393 Link Image
Enzyme 26 GeneCard ID FPGS Link Image
Enzyme 26 GenAtlas ID FPGS Link Image
Enzyme 26 HGNC ID HGNC:3824 Link Image
Enzyme 26 Chromosome Location 9
Enzyme 26 Locus 9q34.1
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [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. Garrow TA, Admon A, Shane B: Expression cloning of a human cDNA encoding folylpoly(gamma-glutamate) synthetase and determination of its primary structure. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9151-5. [PubMed Link Image]
  4. Freemantle SJ, Taylor SM, Krystal G, Moran RG: Upstream organization of and multiple transcripts from the human folylpoly-gamma-glutamate synthetase gene. J Biol Chem. 1995 Apr 21;270(16):9579-84. [PubMed Link Image]
  5. Taylor SM, Freemantle SJ, Moran RG: Structural organization of the human folypoly-gamma-glutamate synthetase gene: evidence for a single genomic locus. Cancer Res. 1995 Dec 15;55(24):6030-4. [PubMed Link Image]
  6. Cichowicz DJ, Shane B: Mammalian folylpoly-gamma-glutamate synthetase. 1. Purification and general properties of the hog liver enzyme. Biochemistry. 1987 Jan 27;26(2):504-12. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 6131
Enzyme 27 Name Alanine aminotransferase 1
Enzyme 27 Synonyms
  1. ALT1
  2. Glutamate pyruvate transaminase 1
  3. GPT 1
  4. Glutamic--alanine transaminase 1
  5. Glutamic--pyruvic transaminase 1
Enzyme 27 Gene Name GPT
Enzyme 27 Protein Sequence >Alanine aminotransferase 1
MASSTGDRSQAVRHGLRAKVLTLDGMNPRVRRVEYAVRGPIVQRALELEQELRQGVKKPF
TEVIRANIGDAQAMGQRPITFLRQVLALCVNPDLLSSPNFPDDAKKRAERILQACGGHSL
GAYSVSSGIQLIREDVARYIERRDGGIPADPNNVFLSTGASDAIVTVLKLLVAGEGHTRT
GVLIPIPQYPLYSATLAELGAVQVDYYLDEERAWALDVAELHRALGQARDHCRPRALCVI
NPGNPTGQVQTRECIEAVIRFAFEERLFLLADEVYQDNVYAAGSQFHSFKKVLMEMGPPY
AGQQELASFHSTSKGYMGECGFRGGYVEVVNMDAAVQQQMLKLMSVRLCPPVPGQALLDL
VVSPPAPTDPSFAQFQAEKQAVLAELAAKAKLTEQVFNEAPGISCNPVQGAMYSFPRVQL
PPRAVERAQELGLAPDMFFCLRLLEETGICVVPGSGFGQREGTYHFRMTILPPLEKLRLL
LEKLSRFHAKFTLEYS
Enzyme 27 Number of Residues 496
Enzyme 27 Molecular Weight 54636.4
Enzyme 27 Theoretical pI 7.20
Enzyme 27 GO Classification
Function
  • 1-aminocyclopropane-1-carboxylate synthase activity
  • binding
  • carbon-sulfur lyase activity
  • catalytic activity
  • cofactor binding
  • lyase activity
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthetic process
  • metabolic process
Component
Enzyme 27 General Function Involved in 1-aminocyclopropane-1-carboxylate synthase activity
Enzyme 27 Specific Function Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles
Enzyme 27 Pathways
Enzyme 27 Reactions
  • L-alanine + 2-oxoglutarate = pyruvate + L-glutamate [RN:R00258]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein Not Available
Enzyme 27 UniProtKB/Swiss-Prot ID P24298 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name ALAT1_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1491 bp
ATGGCCTCGAGCACAGGTGACCGGAGCCAGGCGGTGAGGCATGGACTGAGGGCGAAGGTG
CTGACGCTGGACGGCATGAACCCGCGTGTGCGGAGAGTGGAGTACGCAGTGCGTGGCCCC
ATAGTGCAGCGAGCCTTGGAGCTGGAGCAGGAGCTGCGCCAGGGTGTGAAGAAGCCTTTC
ACCGAGGTCATCCGTGCCAACATCGGGGACGCACAGGCTATGGGGCAGAGGCCCATCACC
TTCCTGCGCCAGGTCTTGGCCCTCTGTGTTAACCCTGATCTTCTGAGCAGCCCCAACTTC
CCTGACGATGCCAAGAAAAGGGCGGAGCGCATCTTGCAGGCGTGTGGGGGCCACAGTCTG
GGGGCCTACAGCGTCAGCTCCGGCATCCAGCTGATCCGGGAGGACGTGGCGCGGTACATT
GAGAGGCGTGACGGAGGCATCCCTGCGGACCCCAACAACGTCTTCCTGTCCACAGGGGCC
AGCGATGCCATCGTGACGGTGCTGAAGCTGCTGGTGGCCGGCGAGGGCCACACACGCACG
GGTGTGCTCATCCCCATCCCCCAGTACCCACTCTACTCGGCCACGCTGGCAGAGCTGGGC
GCAGTGCAGGTGGATTACTACCTGGACGAGGAGCGTGCCTGGGCGCTGGACGTGGCCGAG
CTTCACCGTGCACTGGGCCAGGCGCGTGACCACTGCCGCCCTCGTGCGCTCTGTGTCATC
AACCCTGGCAACCCCACCGGGCAGGTGCAGACCCGCGAGTGCATCGAGGCCGTGATCCGC
TTCGCCTTCGAAGAGCGGCTCTTTCTGCTGGCGGACGAGGTGTACCAGGACAACGTGTAC
GCCGCGGGTTCGCAGTTCCACTCATTCAAGAAGGTGCTCATGGAGATGGGGCCGCCCTAC
GCCGGGCAGCAGGAGCTTGCCTCCTTCCACTCCACCTCCAAGGGCTACATGGGCGAGTGC
GGGTTCCGCGGCGGCTATGTGGAGGTGGTGAACATGGACGCTGCAGTGCAGCAGCAGATG
CTGAAGCTGATGAGTGTGCGGCTGTGCCCGCCGGTGCCAGGACAGGCCCTGCTGGACCTG
GTGGTCAGCCCGCCCGCGCCCACCGACCCCTCCTTTGCGCAGTTCCAGGCTGAGAAGCAG
GCAGTGCTGGCAGAGCTGGCGGCCAAGGCCAAGCTCACCGAGCAGGTCTTCAATGAGGCT
CCTGGCATCAGCTGCAACCCAGTGCAGGGCGCCATGTACTCCTTCCCGCGCGTGCAGCTG
CCCCCGCGGGCGGTGGAGCGCGCTCAGGAGCTGGGCCTGGCCCCCGATATGTTCTTCTGC
CTGCGCCTCCTGGAGGAGACCGGCATCTGCGTGGTGCCAGGGAGCGGCTTTGGGCAGCGG
GAAGGCACCTACCACTTCCGGATGACCATTCTGCCCCCCTTGGAGAAACTGCGGCTGCTG
CTGGAGAAGCTGAGCAGGTTCCATGCCAAGTTCACCCTCGAGTACTCCTAG
Enzyme 27 GenBank Gene ID BT006992 Link Image
Enzyme 27 GeneCard ID GPT Link Image
Enzyme 27 GenAtlas ID GPT Link Image
Enzyme 27 HGNC ID HGNC:4552 Link Image
Enzyme 27 Chromosome Location 8
Enzyme 27 Locus 8q24.3
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Sohocki MM, Sullivan LS, Harrison WR, Sodergren EJ, Elder FF, Weinstock G, Tanase S, Daiger SP: Human glutamate pyruvate transaminase (GPT): localization to 8q24.3, cDNA and genomic sequences, and polymorphic sites. Genomics. 1997 Mar 1;40(2):247-52. [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. Ishiguro M, Takio K, Suzuki M, Oyama R, Matsuzawa T, Titani K: Complete amino acid sequence of human liver cytosolic alanine aminotransferase (GPT) determined by a combination of conventional and mass spectral methods. Biochemistry. 1991 Oct 29;30(43):10451-7. [PubMed Link Image]
  4. Yang RZ, Blaileanu G, Hansen BC, Shuldiner AR, Gong DW: cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase. Genomics. 2002 Mar;79(3):445-50. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 6132
Enzyme 28 Name Phosphoserine aminotransferase
Enzyme 28 Synonyms
  1. Phosphohydroxythreonine aminotransferase
  2. PSAT
Enzyme 28 Gene Name PSAT1
Enzyme 28 Protein Sequence >Phosphoserine aminotransferase
MDAPRQVVNFGPGPAKLPHSVLLEIQKELLDYKGVGISVLEMSHRSSDFAKIINNTENLV
RELLAVPDNYKVIFLQGGGCGQFSAVPLNLIGLKAGRCADYVVTGAWSAKAAEEAKKFGT
INIVHPKLGSYTKIPDPSTWNLNPDASYVYYCANETVHGVEFDFIPDVKGAVLVCDMSSN
FLSKPVDVSKFGVIFAGAQKNVGSAGVTVVIVRDDLLGFALRECPSVLEYKVQAGNSSLY
NTPPCFSIYVMGLVLEWIKNNGGAAAMEKLSSIKSQTIYEIIDNSQGFYVCPVEPQNRSK
MNIPFRIGNAKGDDALEKRFLDKALELNMLSLKGHRSVGGIRASLYNAVTIEDVQKLAAF
MKKFLEMHQL
Enzyme 28 Number of Residues 370
Enzyme 28 Molecular Weight 40422.4
Enzyme 28 Theoretical pI 7.77
Enzyme 28 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
Process
  • L-serine biosynthetic process
  • L-serine metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
Enzyme 28 General Function Involved in metabolic process
Enzyme 28 Specific Function Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine
Enzyme 28 Pathways
Enzyme 28 Reactions
  • (1) O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate [RN:R04173]
  • (2) 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 17402893 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q9Y617 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name SERC_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1113 bp
ATGGACGCCCCCAGGCAGGTGGTCAACTTTGGGCCTGGTCCCGCCAAGCTGCCGCACTCA
GTGTTGTTAGAGATACAAAAGGAATTATTAGACTACAAAGGAGTTGGCATTAGTGTTCTT
GAAATGAGTCACAGGTCATCAGATTTTGCCAAGATTATTAACAATACAGAGAATCTTGTG
CGGGAATTGCTAGCTGTTCCAGACAACTATAAGGTGATTTTTCTGCAAGGAGGTGGGTGC
GGCCAGTTCAGTGCTGTCCCCTTAAACCTCATTGGCTTGAAAGCAGGAAGGTGTGCTGAC
TATGTGGTGACAGGAGCTTGGTCAGCTAAGGCCGCAGAAGAAGCCAAGAAGTTTGGGACT
ATAAATATCGTTCACCCTAAACTTGGGAGTTATACAAAAATTCCAGATCCAAGCACCTGG
AACCTCAACCCAGATGCCTCCTACGTGTATTATTGCGCAAATGAGACGGTGCATGGTGTG
GAGTTTGACTTTATACCCGATGTCAAGGGAGCAGTACTGGTTTGTGACATGTCCTCAAAC
TTCCTGTCCAAGCCAGTGGATGTTTCCAAGTTTGGTGTGATTTTTGCTGGTGCCCAGAAG
AATGTTGGCTCTGCTGGGGTCACCGTGGTGATTGTCCGTGATGACCTGCTGGGGTTTGCC
CTCCGAGAGTGCCCCTCGGTCCTGGAATACAAGGTGCAGGCTGGAAACAGCTCCTTGTAC
AACACGCCTCCATGTTTCAGCATCTACGTCATGGGCTTGGTTCTGGAGTGGATTAAAAAC
AATGGAGGTGCCGCGGCCATGGAGAAGCTTAGCTCCATCAAATCTCAAACAATTTATGAG
ATTATTGATAATTCTCAAGGATTCTACGTTTGTCCAGTGGAGCCCCAAAATAGAAGCAAG
ATGAATATTCCATTCCGCATTGGCAATGCCAAAGGAGATGATGCTTTAGAAAAAAGATTT
CTTGATAAAGCTCTTGAACTCAATATGTTGTCCTTGAAAGGGCATAGGTCTGTGGGAGGC
ATCCGGGCCTCTCTGTATAATGCTGTCACAATTGAAGACGTTCAGAAGCTGGCCGCCTTC
ATGAAAAAATTTTTGGAGATGCATCAGCTATGA
Enzyme 28 GenBank Gene ID NM_058179.2 Link Image
Enzyme 28 GeneCard ID PSAT1 Link Image
Enzyme 28 GenAtlas ID PSAT1 Link Image
Enzyme 28 HGNC ID HGNC:19129 Link Image
Enzyme 28 Chromosome Location 9
Enzyme 28 Locus 9q21.2
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Baek JY, Jun DY, Taub D, Kim YH: Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of L-serine biosynthesis. Biochem J. 2003 Jul 1;373(Pt 1):191-200. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [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. 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]
  5. 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]
  6. Hart CE, Race V, Achouri Y, Wiame E, Sharrard M, Olpin SE, Watkinson J, Bonham JR, Jaeken J, Matthijs G, Van Schaftingen E: Phosphoserine aminotransferase deficiency: a novel disorder of the serine biosynthesis pathway. Am J Hum Genet. 2007 May;80(5):931-7. Epub 2007 Mar 30. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 6135
Enzyme 29 Name Delta-1-pyrroline-5-carboxylate synthase
Enzyme 29 Synonyms
  1. P5CS
  2. Aldehyde dehydrogenase family 18 member A1
  3. Glutamate 5-kinase
  4. GK
  5. Gamma-glutamyl kinase
  6. Gamma-glutamyl phosphate reductase
  7. GPR
  8. Glutamate-5-semialdehyde dehydrogenase
  9. Glutamyl-gamma-semialdehyde dehydrogenase
Enzyme 29 Gene Name ALDH18A1
Enzyme 29 Protein Sequence >Delta-1-pyrroline-5-carboxylate synthase
MLSQVYRCGFQPFNQHLLPWVKCTTVFRSHCIQPSVIRHVRSWSNIPFITVPLSRTHGKS
FAHRSELKHAKRIVVKLGSAVVTRGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAV
AFGKQRLRHEILLSQSVRQALHSGQNQLKEMAIPVLEARACAAAGQSGLMALYEAMFTQY
SICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAEPNSDLQGVNV
ISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQSVTFGTK
SRVGMGGMEAKVKAALWALQGGTSVVIANGTHPKVSGHVITDIVEGKKVGTFFSEVKPAG
PTVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGRLAA
PLLKRLSLSTSKLNSLAIGLRQIAASSQDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIF
ESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAVQLVNTRE
EVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMYVDSEASVDKVTRL
VRDSKCEYPAACNALETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSPSE
VKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVF
WNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSDFSEHGSL
KYLHENLPIPQRNTN
Enzyme 29 Number of Residues 795
Enzyme 29 Molecular Weight 87301.5
Enzyme 29 Theoretical pI 7.13
Enzyme 29 GO Classification
Function
  • catalytic activity
  • glutamate 5-kinase activity
  • glutamate-5-semialdehyde dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
  • phosphotransferase activity, carboxyl group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid biosynthetic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glutamine family amino acid metabolic process
  • metabolic process
  • oxidation reduction
  • proline biosynthetic process
  • proline metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 29 General Function Involved in oxidoreductase activity
Enzyme 29 Specific Function ATP + L-glutamate = ADP + L-glutamate 5- phosphate
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions
  • ATP + L-glutamate = ADP + L-glutamate 5-phosphate [RN:R00239]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 1304314 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P54886 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name P5CS_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >2388 bp
ATGTTGAGTCAAGTTTACCGCTGTGGGTTCCAGCCCTTCAACCAACATCTTCTGCCCTGG
GTCAAGTGTACAACCGTCTTCAGATCTCATTGTATCCAGCCTTCAGTCATCAGACATGTT
CGTTCTTGGAGCAACATCCCGTTTATCACTGTACCCCTCAGTCGTACACATGGCAAGTCC
TTCGCCCACCGCAGTGAGCTGAAGCATGCCAAGAGAATCGTGGTGAAGCTCGGCAGTGCC
GTGGTGACCCGAGGGGATGAATGTGGCCTGGCCCTGGGGCGCTTGGCATCTATTGTTGAG
CAGGTATCAGTGCTGCAGAATCAGGGCAGAGAGATGATGCTGGTGACCAGTGGAGCCGTA
GCCTTTGGCAAACAAACGTTGCGCCATGAGATCCTTCTGTCTCAGAGCGTGCGGCAGGCC
CTCCACTCGGGGCAGAACCAGCTGAAAGAAATGGCAATTCCAGTCTTAGAGGCACGAGCC
TGTGCAGCTGCCGGACAGAGTGGGCTGATGGCCTTGTATGAGGCTATGTTTACCCAGTAC
AGCATCTGTGCTGCCCAGATTTTGGTGACCAATTTGGATTTCCATGATGAGCAGAAGCGC
CGGAACCTCAATGGAACACTTCATGAACTCCTTAGAATGAACATTGTCCCCATTGTCAAC
ACAAATGATGCTGTTGTCCCCCCAGCTGAGCCCAACAGTGACCTGCAGGGGGTAAATGTT
ATTAGTGTTAAAGATAATGATAGCCTGGCTGCCCGACTGGCTGTGGAAATGAAAACTGAT
CTCTTGATTGTCCTTCCAGATGTAGAAGGCCTTTTTGACAGCCCCCCAGGTTCAGATGAT
GCAAAGCTTATTGATATATTTTATCCCGGAGATCAGCAGTCTGTGACATTTGGACCCAAG
TCTAGAGTGGGAAATGGGTGCATGGAAGCCAAGGTGAAAAGCACCCTCTGGGCTTTGCAA
GGTGGCACTTCTGTTGTTATTGCCAATGGAACCCACCCAAAGGTGTCTGGGCACGTCATC
ACAGACATTGTGGAGGGGAAGAAAGTTGGTACCTTCTTTTCAGAAGTAAAGCCTGCAGGC
CCTACTGTTGAGCAGCAGGGAGAAATGGCGCGATCTGGAGGAAGGATGTTGGCCACCTTG
GAACCTGAGCAGAGAGCAGAAATTATCCATCATCTGGCTGATCTGTTGACGGACCAGCGT
GATGAGATCCTGTTAGCCAACAAAAAAGACTTGGAGGAGGCAGAGGGGAGACTTGCAGCT
CCTCTGCTGAAACGTTTAAGCCTCTCCACATCCAAATTGAACAGCCTGGCCATCGGTCTG
CGACAGATCGCAGCCTCCTCCCAGGACAGCGTGGGACGTGTTTTGCGCCGCACCCGAATC
GCCAAAAACTTGGAACTGGAACAAGTGACTGTCCCAATTGGAGTTCTGCTGGTGATCTTT
GAATCTCGTCCTGACTGTCCTACCCCAGGTGGCAGCTTTGCTATCGCAAGTGGCAATGGC
TTGTTACTCAAAGGAGGGAAGGAGGCTGCACACAGCAACCGGATTCTCCACCTCCTGACC
CAGGAGGCTCTCTCAATCCATGGAGTCAAGGAGGCCGTGCAACTGGTGAATACCAGAGAA
GAAGTTGAAGATCTTTGCCGCCTAGACAAAATGATAGATCTGATCATTCCACGTGGCTCT
TCCCAGCTGGTCAGAGACATCCAGAAAGCTGCTAAGGGGATTCCAGTGATGGGGCACAGC
GAAGGGATCTGTCACATGTATGTGGATTCCGAGGCCAGTGTTGATAAGGTCACCAGGCTA
GTCAGAGACTCTAAATGTGAATATCCAGCTGCCTGTAATGCTTTGGAGACTTTGTTAATC
CACCGGGATCTGCTCAGGACACCATTATTTGACCAGATCATTGATATGCTGAGAGTGGAA
CAGGTAAAAATTCATGCAGGCCCCAAATTTGCCTCCTATCTGACCTTCAGCCCCTCCGAA
GTGAAGTCACTCCGAACTGAGTATGGGGACCTGGAATTATGCATTGAAGTAGTGGACAAC
GTTCAGGATGCCATTGACCACATCCACAAGTATGGCAGCTCCCACACGGATGTCATCGTC
ACAGAGGACGAAAACACAGCGGAGTTCTTCCTGCAGCACGTAGACAGTGCCTGTGTGTTC
TGGAATGCCAGCACTCGCTTTTCTGATGGTTACCGCTTTGGACTGGGAGCTGAAGTGGGA
ATCAGTACATCGAGAATCCACGCCCGGGGACCAGTAGGACTTGAGGGACTGCTTACTACT
AAGTGGCTGCTGCGAGGGAAGGACCACGTGGTCTCAGATTTCTCAGAGCATGGAAGTTTA
AAATATCTTCATGAGAACCTCCCTATTCCTCAGAGAAACACCAACTGA
Enzyme 29 GenBank Gene ID X94453 Link Image
Enzyme 29 GeneCard ID ALDH18A1 Link Image
Enzyme 29 GenAtlas ID ALDH18A1 Link Image
Enzyme 29 HGNC ID HGNC:9722 Link Image
Enzyme 29 Chromosome Location 1
Enzyme 29 Locus 10q24.3
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Aral B, Schlenzig JS, Liu G, Kamoun P: Database cloning human delta 1-pyrroline-5-carboxylate synthetase (P5CS) cDNA: a bifunctional enzyme catalyzing the first 2 steps in proline biosynthesis. C R Acad Sci III. 1996 Mar;319(3):171-8. [PubMed Link Image]
  2. Hu CA, Lin WW, Obie C, Valle D: Molecular enzymology of mammalian Delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition. J Biol Chem. 1999 Mar 5;274(10):6754-62. [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. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [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. Baumgartner MR, Hu CA, Almashanu S, Steel G, Obie C, Aral B, Rabier D, Kamoun P, Saudubray JM, Valle D: Hyperammonemia with reduced ornithine, citrulline, arginine and proline: a new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline-5-carboxylate synthase. Hum Mol Genet. 2000 Nov 22;9(19):2853-8. [PubMed Link Image]
  7. Bicknell LS, Pitt J, Aftimos S, Ramadas R, Maw MA, Robertson SP: A missense mutation in ALDH18A1, encoding Delta1-pyrroline-5-carboxylate synthase (P5CS), causes an autosomal recessive neurocutaneous syndrome. Eur J Hum Genet. 2008 Oct;16(10):1176-86. Epub 2008 May 14. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 6136
Enzyme 30 Name 5-oxoprolinase
Enzyme 30 Synonyms
  1. 5-oxo-L-prolinase
  2. 5-OPase
  3. Pyroglutamase
Enzyme 30 Gene Name OPLAH
Enzyme 30 Protein Sequence >5-oxoprolinase
MGSPEGRFHFAIDRGGTFTDVFAQCPGGHVRVLKLLSEDPANYADAPTEGIRRILEQEAG
MLLPRDQPLDSSHIASIRMGTTVATNALLERKGERVALLVTRGFRDLLHIGTQARGDLFD
LAVPMPEVLYEEVLEVDERVVLHRGEAGTGTPVKGRTGDLLEVQQPVDLGALRGKLEGLL
SRGIRSLAVVLMHSYTWAQHEQQVGVLARELGFTHVSLSSEAMPMVRIVPRGHTACADAY
LTPAIQRYVQGFCRGFQGQLKDVQVLFMRSDGGLAPMDTFSGSSAVLSGPAGGVVGYSAT
TYQQEGGQPVIGFDMGGTSTDVSRYAGEFEHVFEASTAGVTLQAPQLDINTVAAGGGSRL
FFRSGLFVVGPESAGAHPGPACYRKGGPVTVTDANLVLGRLLPASFPCIFGPGENQPLSP
EASRKALEAVATEVNSFLTNGPCPASPLSLEEVAMGFVRVANEAMCRPIRALTQARGHDP
SAHVLACFGGAGGQHACAIARALGMDTVHIHRHSGLLSALGLALADVVHEAQEPCSLLYA
PETFVQLDQRLSRLEEQCVDALQAQGFPRSQISTESFLHLRYQGTDCALMVSAHQHPATA
RSPRAGDFGAAFVERYMREFGFVIPERPVVVDDVRVRGTGRSGLRLEDAPKAQTGPPRVD
KMTQCYFEGGYQETPVYLLAELGYGHKLHGPCLIIDSNSTILVEPGCQAEVTKTGDICIS
VGAEVPGTVGPQLDPIQLSIFSHRFMSIAEQMGRILQRTAISTNIKERLDFSCALFGPDG
GLVSNAPHIPVHLGAMQETVQFQIQHLGADLHPGDVLLSNHPSAGGSHLPDLTVITPVFW
PGQTRPVFYVASRGHHADIGGITPGSMPPHSTMLQQEGAVFLSFKLVQGGVFQEEAVTEA
LRAPGKVPNCSGTRNLHDNLSDLRAQVAANQKGIQLVGELIGQYGLDVVQAYMGHIQANA
ELAVRDMLRAFGTSRQARGLPLEVSSEDHMDDGSPIRLRVQISLSQGSAVFDFSGTGPEV
FGNLNAPRAVTLSALIYCLRCLVGRDIPLNQGCLAPVRVVIPRGSILDPSPEAAVVGGNV
LTSQRVVDVILGAFGACAASQGCMNNVTLGNAHMGYYETVAGGAGAGPSWHGRSGVHSHM
TNTRITDPEILESRYPVILRRFELRRGSGGRGRFRGGDGVTRELLFREEALLSVLTERRA
FRPYGLHGGEPGARGLNLLIRKNGRTVNLGGKTSVTVYPGDVFCLHTPGGGGYGDPEDPA
PPPGSPPQALAFPEHGSVYEYRRAQEAV
Enzyme 30 Number of Residues 1288
Enzyme 30 Molecular Weight 137456.2
Enzyme 30 Theoretical pI 6.56
Enzyme 30 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 30 General Function Involved in hydrolase activity
Enzyme 30 Specific Function Catalyzes the cleavage of 5-oxo-L-proline to form L- glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate
Enzyme 30 Pathways
Enzyme 30 Reactions
  • ATP + 5-oxo-L-proline + 2 H2O = ADP + phosphate + L-glutamate [RN:R00251]
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein Not Available
Enzyme 30 UniProtKB/Swiss-Prot ID O14841 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name OPLA_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >3867 bp
ATGGGCAGCCCCGAGGGCCGCTTCCACTTTGCCATCGACCGTGGGGGTACCTTCACAGAC
GTCTTTGCCCAGTGCCCAGGGGGGCACGTGCGGGTCTTAAAACTGCTCTCAGAGGACCCT
GCCAACTATGCGGACGCGCCAACCGAAGGCATCCGCCGCATCCTGGAGCAGGAGGCCGGC
ATGCTCCTGCCCCGGGACCAGCCGCTGGACTCCAGTCATATCGCCAGCATCCGCATGGGC
ACCACAGTGGCCACCAACGCACTGCTGGAGCGGAAGGGGGAGCGGGTGGCGCTGCTGGTG
ACACGTGGCTTCCGAGACCTGCTGCACATTGGCACCCAAGCCCGTGGGGACCTCTTTGAC
CTGGCCGTGCCCATGCCTGAGGTGCTGTATGAAGAGGTGCTGGAGGTGGACGAACGCGTG
GTGCTGCACCGTGGAGAGGCGGGCACCGGGACGCCTGTGAAAGGCCGCACGGGGGACCTG
CTGGAAGTGCAGCAGCCTGTGGACCTGGGGGCCCTGCGTGGGAAGCTGGAGGGGCTGCTA
TCTCGAGGCATCCGCAGCCTGGCTGTGGTGCTCATGCACTCGTACACGTGGGCCCAGCAT
GAGCAGCAGGTGGGTGTGCTGGCCCGGGAGCTGGGCTTCACGCACGTGTCACTGTCCTCG
GAGGCCATGCCCATGGTGCGCATCGTCCCTCGGGGGCACACGGCCTGTGCCGACGCCTAC
CTCACGCCCGCCATCCAGCGCTACGTGCAGGGCTTCTGCCGTGGCTTCCAGGGCCAACTC
AAGGATGTGCAGGTGTTGTTCATGCGCTCCGATGGCGGCCTGGCGCCCATGGACACCTTC
AGCGGCTCCAGTGCTGTGCTCTCGGGCCCGGCCGGCGGCGTGGTGGGCTACTCAGCCACC
ACCTACCAGCAGGAGGGTGGCCAGCCTGTCATCGGCTTTGACATGGGAGGCACGTCCACG
GATGTGAGCCGCTATGCTGGGGAATTCGAGCACGTCTTCGAGGCCAGCACAGCTGGCGTC
ACCCTCCAGGCCCCGCAGCTGGACATCAACACCGTGGCAGCGGGAGGGGGTTCCCGCCTC
TTCTTCAGGTCTGGCCTCTTTGTGGTTGGGCCCGAGTCAGCAGGAGCCCACCCAGGACCC
GCCTGCTACCGCAAAGGGGGCCCTGTGACAGTGACGGATGCTAATCTGGTCCTGGGTCGC
CTGCTGCCTGCCTCCTTCCCCTGCATTTTTGGGCCGGGAGAGAACCAACCACTTTCCCCT
GAGGCCTCCCGCAAAGCCCTGGAGGCTGTGGCCACTGAGGTCAACAGCTTCCTGACCAAC
GGGCCCTGCCCGGCCTCCCCGCTGAGCCTGGAGGAGGTGGCCATGGGGTTCGTGCGCGTG
GCCAACGAGGCCATGTGCCGGCCCATCCGTGCACTCACGCAGGCAAGAGGCCATGACCCC
TCAGCCCATGTGCTGGCCTGCTTTGGGGGAGCTGGTGGGCAGCATGCATGTGCCATCGCC
CGGGCCCTGGGCATGGACACGGTGCACATCCACAGGCACAGTGGGCTGCTGTCGGCCCTG
GGGCTGGCCCTGGCTGACGTGGTGCATGAGGCACAGGAACCCTGCTCCCTGCTCTACGCG
CCTGAGACCTTCGTGCAGCTGGACCAGAGGCTGAGCCGCCTGGAGGAGCAGTGTGTGGAT
GCTCTGCAGGCCCAGGGCTTCCCCAGGTCCCAGATCAGCACTGAGAGCTTCCTGCACCTG
CGCTACCAGGGCACGGACTGTGCTCTGATGGTGTCTGCCCACCAGCACCCAGCCACAGCC
CGCTCGCCCCGTGCGGGGGACTTCGGGGCAGCCTTTGTGGAGCGGTACATGAGGGAGTTT
GGCTTTGTCATACCTGAGCGGCCGGTGGTCGTGGACGATGTGCGAGTGCGGGGCACCGGC
CGCAGTGGTCTTCGCCTCGAGGATGCCCCCAAAGCCCAGACCGGGCCTCCCCGGGTGGAC
AAGATGACCCAGTGCTACTTTGAGGGGGGCTACCAGGAGACCCCTGTGTACCTGCTGGCA
GAGCTGGGCTATGGGCACAAGCTCCATGGGCCCTGCCTCATCATCGACAGTAACAGCACC
ATCCTGGTGGAGCCAGGTTGCCAGGCAGAGGTGACCAAGACAGGGGACATCTGCATCTCC
GTGGGGGCCGAAGTCCCCGGCACAGTGGGCCCCCAGCTGGACCCTATCCAGCTGTCCATC
TTCTCACACCGCTTCATGAGCATTGCTGAGCAGATGGGCCGCATCCTGCAGCGCACAGCC
ATCTCCACCAACATCAAGGAGCGTCTGGACTTCTCCTGTGCCCTCTTTGGGCCCGATGGG
GGGCTGGTGTCCAATGCCCCCCACATCCCTGTGCACCTGGGTGCCATGCAGGAGACGGTG
CAGTTCCAGATTCAGCACCTGGGGGCCGATCTCCACCCTGGCGACGTGCTACTGAGCAAC
CATCCCAGTGCCGGGGGCAGCCACCTGCCAGACCTGACTGTTATCACACCGGTGTTTTGG
CCGGGTCAGACGCGGCCTGTGTTCTATGTGGCCAGCCGAGGGCACCACGCAGACATCGGG
GGCATCACACCAGGCTCCATGCCCCCCCACTCCACCATGCTGCAACAGGAGGGTGCCGTC
TTTCTGTCCTTCAAACTTGTCCAGGGGGGCGTCTTCCAGGAGGAGGCGGTGACGGAGGCC
CTGCGGGCGCCAGGCAAGGTCCCCAACTGCAGCGGAACCAGAAACCTGCACGACAACCTG
TCGGACCTCCGTGCCCAGGTGGCAGCCAACCAGAAGGGCATCCAGCTGGTGGGGGAGCTC
ATTGGGCAGTACGGCCTGGACGTGGTGCAGGCCTACATGGGCCATATTCAGGCAAACGCT
GAGCTGGCCGTGCGAGACATGTTGCGTGCCTTTGGAACCTCCCGGCAGGCCCGGGGCCTG
CCCCTGGAGGTGTCCTCGGAAGACCACATGGACGACGGTTCCCCCATCCGCCTCCGTGTG
CAGATCAGCCTGAGTCAGGGCAGCGCTGTGTTTGACTTCAGCGGCACTGGGCCGGAGGTG
TTTGGTAATCTCAACGCACCGCGGGCCGTAACCCTGTCCGCCCTCATCTACTGCCTGCGC
TGTCTGGTGGGCCGCGACATCCCACTCAACCAGGGCTGCCTGGCGCCAGTGCGCGTGGTC
ATTCCCCGAGGCTCCATCCTGGACCCGTCGCCCGAGGCGGCGGTGGTGGGCGGCAACGTG
CTCACGTCGCAGCGCGTGGTGGATGTCATCCTGGGGGCCTTTGGGGCCTGCGCCGCCTCC
CAGGGCTGCATGAACAACGTGACCCTGGGCAACGCCCACATGGGCTACTACGAGACGGTG
GCGGGCGGCGCGGGCGCGGGTCCCAGCTGGCACGGGCGCAGCGGTGTGCACAGCCACATG
ACCAACACACGCATCACCGACCCTGAGATCCTGGAGAGCCGGTACCCGGTCATCCTGCGC
CGCTTCGAGCTGCGGCGGGGCTCGGGGGGCAGAGGCCGCTTCCGAGGCGGCGACGGCGTC
ACCCGCGAGCTGCTCTTTCGTGAGGAGGCGCTGCTGTCAGTGCTGACCGAGCGCCGCGCC
TTCCGGCCATACGGGCTCCACGGGGGCGAGCCTGGCGCCCGCGGCCTAAACCTGCTGATC
CGCAAAAACGGCCGGACGGTGAATCTGGGCGGCAAGACGTCGGTGACCGTGTACCCCGGG
GATGTGTTCTGTCTCCACACGCCCGGCGGCGGTGGCTATGGGGACCCGGAGGACCCCGCC
CCACCGCCGGGGTCGCCCCCGCAAGCACTGGCCTTTCCCGAGCACGGCAGCGTCTATGAG
TATCGCCGGGCCCAGGAGGCCGTGTGA
Enzyme 30 GenBank Gene ID AB122018 Link Image
Enzyme 30 GeneCard ID OPLAH Link Image
Enzyme 30 GenAtlas ID OPLAH Link Image
Enzyme 30 HGNC ID HGNC:8149 Link Image
Enzyme 30 Chromosome Location 8
Enzyme 30 Locus 8q24.3
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Watanabe T, Abe K, Ishikawa H, Iijima Y: Bovine 5-oxo-L-prolinase: simple assay method, purification, cDNA cloning, and detection of mRNA in the coronary artery. Biol Pharm Bull. 2004 Mar;27(3):288-94. [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. 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]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 6960
Enzyme 31 Name Glutamate [NMDA] receptor subunit zeta-1
Enzyme 31 Synonyms
  1. N-methyl-D-aspartate receptor subunit NR1
  2. NMD-R1
Enzyme 31 Gene Name GRIN1
Enzyme 31 Protein Sequence >Glutamate [NMDA] receptor subunit zeta-1
MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQL
NATSVTHKPNAIQMALSVCEDLISSQVYAILVSHPPTPNDHFTPTPVSYTAGFYRIPVLG
LTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL
ETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNM
TGSGYVWLVGEREISGNALRYAPDGILGLQLINGKNESAHISDAVGVVAQAVHELLEKEN
ITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRK
LVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTC
KEEFTVNGDPVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVA
DGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTI
LVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDA
LTLSSAMWFSWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRP
EERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQA
VRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSH
ENGFMEDLDKTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRH
KDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDT
STGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES
Enzyme 31 Number of Residues 938
Enzyme 31 Molecular Weight 105371.9
Enzyme 31 Theoretical pI 9.20
Enzyme 31 GO Classification
Function
  • excitatory extracellular ligand-gated ion channel activity
  • extracellular ligand-gated ion channel activity
  • extracellular-glutamate-gated ion channel activity
  • glutamate receptor activity
  • ion channel activity
  • ion transmembrane transporter activity
  • ionotropic glutamate receptor activity
  • ligand-gated ion channel activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • substrate-specific transmembrane transporter activity
  • transmembrane receptor activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transport
Component
  • cell part
  • membrane
  • outer membrane-bounded periplasmic space
  • periplasmic space
Enzyme 31 General Function Involved in ionotropic glutamate receptor activity
Enzyme 31 Specific Function NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • 1-18
Enzyme 31 Transmembrane Regions
  • 560-580 637-657 813-833
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 123240314 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q05586 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name NMDZ1_HUMAN Link Image
Enzyme 31 PDB ID 1PB7 Link Image
Enzyme 31 PDB File Show
Enzyme 31 3D Structure
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >2817 bp
ATGAGCACCATGCGCCTGCTGACGCTCGCCCTGCTGTTCTCCTGCTCCGTCGCCCGTGCC
GCGTGCGACCCCAAGATCGTCAACATTGGCGCGGTGCTGAGCACGCGGAAGCACGAGCAG
ATGTTCCGCGAGGCCGTGAACCAGGCCAACAAGCGGCACGGCTCCTGGAAGATTCAGCTC
AATGCCACCTCCGTCACGCACAAGCCCAACGCCATCCAGATGGCTCTGTCGGTGTGCGAG
GACCTCATCTCCAGCCAGGTCTACGCCATCCTAGTTAGCCATCCACCTACCCCCAACGAC
CACTTCACTCCCACCCCTGTCTCCTACACAGCCGGCTTCTACCGCATACCCGTGCTGGGG
CTGACCACCCGCATGTCCATCTACTCGGACAAGAGCATCCACCTGAGCTTCCTGCGCACC
GTGCCGCCCTACTCCCACCAGTCCAGCGTGTGGTTTGAGATGATGCGTGTCTACAGCTGG
AACCACATCATCCTGCTGGTCAGCGACGACCACGAGGGCCGGGCGGCTCAGAAACGCCTG
GAGACGCTGCTGGAGGAGCGTGAGTCCAAGGCAGAGAAGGTGCTGCAGTTTGACCCAGGG
ACCAAGAACGTGACGGCCCTGCTGATGGAGGCGAAAGAGCTGGAGGCCCGGGTCATCATC
CTTTCTGCCAGCGAGGACGATGCTGCCACTGTATACCGCGCAGCCGCGATGCTGAACATG
ACGGGCTCCGGGTACGTGTGGCTGGTCGGCGAGCGCGAGATCTCGGGGAACGCCCTGCGC
TACGCCCCAGACGGCATCCTCGGGCTGCAGCTCATCAACGGCAAGAACGAGTCGGCCCAC
ATCAGCGACGCCGTGGGCGTGGTGGCCCAGGCCGTGCACGAGCTCCTCGAGAAGGAGAAC
ATCACCGACCCGCCGCGGGGCTGCGTGGGCAACACCAACATCTGGAAGACCGGGCCGCTC
TTCAAGAGAGTGCTGATGTCTTCCAAGTATGCGGATGGGGTGACTGGTCGCGTGGAGTTC
AATGAGGATGGGGACCGGAAGTTCGCCAACTACAGCATCATGAACCTGCAGAACCGCAAG
CTGGTGCAAGTGGGCATCTACAATGGCACCCACGTCATCCCTAATGACAGGAAGATCATC
TGGCCAGGCGGAGAGACAGAGAAGCCTCGAGGGTACCAGATGTCCACCAGACTGAAGATT
GTGACGATCCACCAGGAGCCCTTCGTGTACGTCAAGCCCACGCTGAGTGATGGGACATGC
AAGGAGGAGTTCACAGTCAACGGCGACCCAGTCAAGAAGGTGATCTGCACCGGGCCCAAC
GACACGTCGCCGGGCAGCCCCCGCCACACGGTGCCTCAGTGTTGCTACGGCTTTTGCATC
GACCTGCTCATCAAGCTGGCACGGACCATGAACTTCACCTACGAGGTGCACCTGGTGGCA
GATGGCAAGTTCGGCACACAGGAGCGGGTGAACAACAGCAACAAGAAGGAGTGGAATGGG
ATGATGGGCGAGCTGCTCAGCGGGCAGGCAGACATGATCGTGGCGCCGCTAACCATAAAC
AACGAGCGCGCGCAGTACATCGAGTTTTCCAAGCCCTTCAAGTACCAGGGCCTGACTATT
CTGGTCAAGAAGGAGATTCCCCGGAGCACGCTGGACTCGTTCATGCAGCCGTTCCAGAGC
ACACTGTGGCTGCTGGTGGGGCTGTCGGTGCACGTGGTGGCCGTGATGCTGTACCTGCTG
GACCGCTTCAGCCCCTTCGGCCGGTTCAAGGTGAACAGCGAGGAGGAGGAGGAGGACGCA
CTGACCCTGTCCTCGGCCATGTGGTTCTCCTGGGGCGTCCTGCTCAACTCCGGCATCGGG
GAAGGCGCCCCCAGAAGCTTCTCAGCGCGCATCCTGGGCATGGTGTGGGCCGGCTTTGCC
ATGATCATCGTGGCCTCCTACACCGCCAACCTGGCGGCCTTCCTGGTGCTGGACCGGCCG
GAGGAGCGCATCACGGGCATCAACGACCCTCGGCTGAGGAACCCCTCGGACAAGTTTATC
TACGCCACGGTGAAGCAGAGCTCCGTGGATATCTACTTCCGGCGCCAGGTGGAGCTGAGC
ACCATGTACCGGCATATGGAGAAGCACAACTACGAGAGTGCGGCGGAGGCCATCCAGGCC
GTGAGAGACAACAAGCTGCATGCCTTCATCTGGGACTCGGCGGTGCTGGAGTTCGAGGCC
TCGCAGAAGTGCGACCTGGTGACGACTGGAGAGCTGTTTTTCCGCTCGGGCTTCGGCATA
GGCATGCGCAAAGACAGCCCCTGGAAGCAGAACGTCTCCCTGTCCATCCTCAAGTCCCAC
GAGAATGGCTTCATGGAAGACCTGGACAAGACGTGGGTTCGGTATCAGGAATGTGACTCG
CGCAGCAACGCCCCTGCGACCCTTACTTTTGAGAACATGGCCGGGGTCTTCATGCTGGTA
GCTGGGGGCATCGTGGCCGGGATCTTCCTGATTTTCATCGAGATTGCCTACAAGCGGCAC
AAGGATGCTCGCCGGAAGCAGATGCAGCTGGCCTTTGCCGCCGTTAACGTGTGGCGGAAG
AACCTGCAGGATAGAAAGAGTGGTAGAGCAGAGCCTGACCCTAAAAAGAAAGCCACATTT
AGGGCTATCACCTCCACCCTGGCTTCCAGCTTCAAGAGGCGTAGGTCCTCCAAAGACACG
AGCACCGGGGGTGGACGCGGCGCTTTGCAAAACCAAAAAGACACAGTGCTGCCGCGACGC
GCTATTGAGAGGGAGGAGGGCCAGCTGCAGCTGTGTTCCCGTCATAGGGAGAGCTGA
Enzyme 31 GenBank Gene ID AL929554 Link Image
Enzyme 31 GeneCard ID GRIN1 Link Image
Enzyme 31 GenAtlas ID GRIN1 Link Image
Enzyme 31 HGNC ID HGNC:4584 Link Image
Enzyme 31 Chromosome Location 9
Enzyme 31 Locus 9q34.3
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Foldes RL, Rampersad V, Kamboj RK: Cloning and sequence analysis of cDNAs encoding human hippocampus N-methyl-D-aspartate receptor subunits: evidence for alternative RNA splicing. Gene. 1993 Sep 15;131(2):293-8. [PubMed Link Image]
  2. Karp SJ, Masu M, Eki T, Ozawa K, Nakanishi S: Molecular cloning and chromosomal localization of the key subunit of the human N-methyl-D-aspartate receptor. J Biol Chem. 1993 Feb 15;268(5):3728-33. [PubMed Link Image]
  3. Planells-Cases R, Sun W, Ferrer-Montiel AV, Montal M: Molecular cloning, functional expression, and pharmacological characterization of an N-methyl-D-aspartate receptor subunit from human brain. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5057-61. [PubMed Link Image]
  4. Zimmer M, Fink TM, Franke Y, Lichter P, Spiess J: Cloning and structure of the gene encoding the human N-methyl-D-aspartate receptor (NMDAR1). Gene. 1995 Jul 4;159(2):219-23. [PubMed Link Image]
  5. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  6. Foldes RL, Rampersad V, Kamboj RK: Cloning and sequence analysis of additional splice variants encoding human N-methyl-D-aspartate receptor (hNR1) subunits. Gene. 1994 Sep 30;147(2):303-4. [PubMed Link Image]
  7. Younkin DP, Tang CM, Hardy M, Reddy UR, Shi QY, Pleasure SJ, Lee VM, Pleasure D: Inducible expression of neuronal glutamate receptor channels in the NT2 human cell line. Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2174-8. [PubMed Link Image]
  8. Tingley WG, Roche KW, Thompson AK, Huganir RL: Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain. Nature. 1993 Jul 1;364(6432):70-3. [PubMed Link Image]
  9. Papadakis M, Hawkins LM, Stephenson FA: Appropriate NR1-NR1 disulfide-linked homodimer formation is requisite for efficient expression of functional, cell surface N-methyl-D-aspartate NR1/NR2 receptors. J Biol Chem. 2004 Apr 9;279(15):14703-12. Epub 2004 Jan 19. [PubMed Link Image]
  10. Opella SJ, Marassi FM, Gesell JJ, Valente AP, Kim Y, Oblatt-Montal M, Montal M: Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat Struct Biol. 1999 Apr;6(4):374-9. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 6964
Enzyme 32 Name Glutamate [NMDA] receptor subunit 3B
Enzyme 32 Synonyms
  1. N-methyl-D-aspartate receptor subtype 3B
  2. NMDAR3B
  3. NR3B
Enzyme 32 Gene Name GRIN3B
Enzyme 32 Protein Sequence >Glutamate [NMDA] receptor subunit 3B
MEFVRALWLGLALALGPGSAGGHPQPCGVLARLGGSVRLGALLPRAPLARARARAALARA
ALAPRLPHNLSLELVVAAPPARDPASLTRGLCQALVPPGVAALLAFPEARPELLQLHFLA
AATETPVLSLLRREARAPLGAPNPFHLQLHWASPLETLLDVLVAVLQAHAWEDVGLALCR
TQDPGGLVALWTSRAGRPPQLVLDLSRRDTGDAGLRARLAPMAAPVGGEAPVPAAVLLGC
DIARARRVLEAVPPGPHWLLGTPLPPKALPTAGLPPGLLALGEVARPPLEAAIHDIVQLV
ARALGSAAQVQPKRALLPAPVNCGDLQPAGPESPGRFLARFLANTSFQGRTGPVWVTGSS
QVHMSRHFKVWSLRRDPRGAPAWATVGSWRDGQLDLEPGGASARPPPPQGAQVWPKLRVV
TLLEHPFVFARDPDEDGQCPAGQLCLDPGTNDSATLDALFAALANGSAPRALRKCCYGYC
IDLLERLAEDTPFDFELYLVGDGKYGALRDGRWTGLVGDLLAGRAHMAVTSFSINSARSQ
VVDFTSPFFSTSLGIMVRARDTASPIGAFMWPLHWSTWLGVFAALHLTALFLTVYEWRSP
YGLTPRGRNRSTVFSYSSALNLCYAILFRRTVSSKTPKCPTGRLLMNLWAIFCLLVLSSY
TANLAAVMVGDKTFEELSGIHDPKLHHPAQGFRFGTVWESSAEAYIKKSFPDMHAHMRRH
SAPTTPRGVAMLTSDPPKLNAFIMDKSLLDYEVSIDADCKLLTVGKPFAIEGYGIGLPQN
SPLTSNLSEFISRYKSSGFIDLLHDKWYKMVPCGKRVFAVTETLQMSIYHFAGLFVLLCL
GLGSALLSSLGEHAFFRLALPRIRKGSRLQYWLHTSQKIHRALNTEPPEGSKEETAEAEP
SGPEVEQQQQQQDQPTAPEGWKRARRAVDKERRVRFLLEPAVVVAPEADAEAEAAPREGP
VWLCSYGRPPAARPTGAPQPGELQELERRIEVARERLRQALVRRGQLLAQLGDSARHRPR
RLLQARAAPAEAPPHSGRPGSQE
Enzyme 32 Number of Residues 1043
Enzyme 32 Molecular Weight 112991.0
Enzyme 32 Theoretical pI 9.50
Enzyme 32 GO Classification
Function
  • excitatory extracellular ligand-gated ion channel activity
  • extracellular ligand-gated ion channel activity
  • extracellular-glutamate-gated ion channel activity
  • glutamate receptor activity
  • ion channel activity
  • ion transmembrane transporter activity
  • ionotropic glutamate receptor activity
  • ligand-gated ion channel activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • substrate-specific transmembrane transporter activity
  • transmembrane receptor activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transport
Component
  • cell part
  • membrane
  • outer membrane-bounded periplasmic space
  • periplasmic space
Enzyme 32 General Function Involved in ionotropic glutamate receptor activity
Enzyme 32 Specific Function NMDA receptor subtype of glutamate-gated ion channels with reduced single-channel conductance, low calcium permeability and low voltage-dependent sensitivity to magnesium. Mediated by glycine
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • 1-22
Enzyme 32 Transmembrane Regions
  • 565-585 649-669 831-851
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 62988346 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID O60391 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name NMD3B_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >3132 bp
ATGGAGTTTGTGCGGGCGCTGTGGCTGGGCCTGGCGCTGGCGCTGGGGCCGGGGTCCGCG
GGGGGCCACCCTCAGCCGTGCGGCGTCCTGGCGCGCCTCGGGGGCTCCGTGCGCCTGGGC
GCCCTCCTGCCCCGCGCGCCTCTCGCCCGCGCCCGCGCCCGCGCCGCCCTGGCCCGGGCC
GCCCTGGCGCCGCGGCTGCCGCACAACCTGAGCTTGGAGCTGGTGGTCGCCGCGCCCCCC
GCCCGCGACCCCGCCTCGCTGACCCGCGGCCTGTGCCAGGCGCTGGTGCCTCCGGGCGTG
GCGGCCCTGCTCGCCTTTCCCGAGGCTCGGCCCGAGCTGCTGCAGCTGCACTTCCTGGCG
GCGGCCACCGAGACCCCCGTGCTCAGCCTGCTGCGGCGGGAGGCGCGCGCGCCCCTCGGA
GCCCCGAACCCATTCCACCTGCAGCTGCACTGGGCCAGCCCCCTGGAGACGCTGCTGGAT
GTGCTGGTGGCGGTGCTGCAGGCGCACGCCTGGGAAGACGTCGGCCTGGCCCTGTGCCGC
ACTCAGGACCCCGGCGGCCTGGTGGCCCTCTGGACAAGCCGGGCTGGCCGGCCCCCACAG
CTGGTCCTGGACCTAAGCCGGCGGGACACGGGAGATGCAGGACTGCGGGCACGCCTGGCC
CCGATGGCGGCGCCAGTGGGGGGTGAAGCACCGGTACCCGCGGCGGTCCTCCTCGGCTGT
GACATCGCCCGTGCCCGTCGGGTGCTGGAGGCCGTACCTCCCGGCCCCCACTGGCTGTTG
GGGACACCACTGCCGCCCAAGGCCCTGCCCACCGCGGGGCTGCCACCAGGGCTGCTGGCG
CTGGGCGAGGTGGCACGACCCCCGCTGGAGGCCGCCATCCATGACATTGTGCAACTGGTG
GCCCGGGCGCTGGGCAGTGCGGCCCAGGTGCAGCCGAAGCGAGCCCTCCTCCCCGCCCCG
GTCAACTGCGGGGACCTGCAGCCGGCCGGGCCCGAGTCCCCGGGGCGCTTCTTGGCACGG
TTCCTGGCCAACACGTCCTTCCAGGGCCGCACGGGCCCCGTGTGGGTGACAGGCAGCTCC
CAGGTACACATGTCTCGGCACTTTAAGGTGTGGAGCCTTCGCCGGGACCCACGGGGCGCC
CCGGCCTGGGCCACGGTGGGCAGCTGGCGGGACGGCCAGCTGGACTTGGAACCGGGAGGT
GCCTCTGCACGGCCCCCGCCCCCACAGGGTGCCCAGGTCTGGCCCAAGCTGCGTGTGGTA
ACGCTGTTGGAACACCCATTTGTGTTTGCCCGTGATCCAGACGAAGACGGGCAGTGCCCA
GCGGGGCAGCTGTGCCTGGACCCTGGCACCAACGACTCGGCCACCCTGGACGCACTGTTC
GCCGCGCTGGCCAACGGCTCAGCGCCCCGTGCCCTGCGCAAGTGCTGCTACGGCTACTGC
ATTGACCTGCTGGAGCGGCTGGCGGAGGACACGCCCTTCGACTTCGAGCTGTACCTCGTG
GGTGACGGCAAGTACGGCGCCCTGCGGGACGGCCGCTGGACCGGCCTGGTCGGGGACCTG
CTGGCCGGCCGGGCCCACATGGCGGTCACCAGCTTCAGTATCAACTCCGCCCGCTCACAG
GTGGTGGACTTCACCAGCCCCTTCTTCTCCACCAGCCTGGGCATCATGGTGCGGGCACGG
GACACGGCCTCACCCATCGGTGCCTTTATGTGGCCCCTGCACTGGTCCACGTGGCTGGGC
GTCTTTGCGGCCCTGCACCTCACCGCGCTCTTCCTCACCGTGTACGAGTGGCGTAGCCCC
TACGGCCTCACGCCACGTGGCCGCAACCGCAGCACCGTCTTCTCCTACTCCTCAGCCCTC
AACCTGTGCTACGCCATCCTCTTCAGACGCACCGTGTCCAGCAAGACGCCCAAGTGCCCC
ACGGGCCGCCTGCTCATGAACCTCTGGGCCATCTTCTGCCTGCTGGTGCTGTCCAGCTAC
ACGGCCAACCTGGCTGCCGTCATGGTCGGGGACAAGACCTTCGAGGAGCTGTCGGGGATC
CACGACCCCAAGCTGCACCACCCGGCGCAGGGCTTCCGCTTCGGCACCGTGTGGGAGAGC
AGCGCCGAGGCGTACATCAAGAAGAGCTTCCCCGACATGCACGCACACATGCGGCGCCAC
AGCGCGCCCACCACGCCCCGCGGCGTCGCCATGCTCACGAGCGACCCCCCCAAGCTCAAC
GCCTTCATCATGGACAAGTCGCTCCTGGACTACGAGGTCTCCATCGACGCCGACTGCAAA
CTGCTGACCGTGGGAAAGCCCTTCGCCATTGAGGGCTATGGGATCGGACTGCCCCAGAAC
TCGCCGCTCACCTCCAACCTGTCCGAGTTCATCAGCCGCTACAAGTCCTCCGGCTTCATC
GACCTGCTCCACGACAAGTGGTACAAGATGGTGCCTTGCGGCAAGCGGGTCTTTGCGGTT
ACAGAGACCCTGCAGATGAGCATCTACCACTTCGCGGGCCTCTTCGTGTTGCTGTGCCTG
GGCCTGGGCAGCGCTCTGCTCAGCTCGCTGGGCGAGCACGCCTTCTTCCGCCTGGCGCTG
CCGCGCATCCGCAAGGGGAGCAGGCTGCAGTACTGGCTGCACACCAGCCAGAAAATCCAC
CGCGCCCTCAACACGGAGCCACCAGAGGGGTCGAAGGAGGAGACGGCAGAGGCGGAGCCC
AGCGGCCCCGAGGTGGAGCAGCAGCAGCAGCAGCAGGACCAGCCAACGGCTCCGGAGGGC
TGGAAACGGGCGCGCCGGGCCGTGGACAAGGAGCGCCGCGTGCGCTTCCTGCTGGAGCCC
GCCGTGGTTGTGGCACCCGAAGCGGACGCGGAGGCGGAGGCTGCGCCGCGAGAGGGCCCC
GTCTGGCTGTGCTCCTACGGCCGCCCGCCCGCCGCAAGGCCCACGGGGGCCCCCCAGCCC
GGGGAGCTGCAGGAGCTGGAGCGCCGCATCGAAGTCGCGCGTGAGCGGCTCCGCCAGGCC
CTGGTGCGGCGCGGCCAGCTCCTGGCACAGCTCGGGGACAGCGCACGTCACCGGCCTCGG
CGCTTGCTTCAGGCCAGAGCGGCCCCCGCGGAGGCCCCACCACACTCTGGCCGACCGGGG
AGCCAGGAATGA
Enzyme 32 GenBank Gene ID NM_138690.1 Link Image
Enzyme 32 GeneCard ID GRIN3B Link Image
Enzyme 32 GenAtlas ID GRIN3B Link Image
Enzyme 32 HGNC ID HGNC:16768 Link Image
Enzyme 32 Chromosome Location 1
Enzyme 32 Locus 19p13.3
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  2. Andersson O, Stenqvist A, Attersand A, von Euler G: Nucleotide sequence, genomic organization, and chromosomal localization of genes encoding the human NMDA receptor subunits NR3A and NR3B. Genomics. 2001 Dec;78(3):178-84. [PubMed Link Image]
  3. Nishi M, Hinds H, Lu HP, Kawata M, Hayashi Y: Motoneuron-specific expression of NR3B, a novel NMDA-type glutamate receptor subunit that works in a dominant-negative manner. J Neurosci. 2001 Dec 1;21(23):RC185. [PubMed Link Image]
  4. Bendel O, Meijer B, Hurd Y, von Euler G: Cloning and expression of the human NMDA receptor subunit NR3B in the adult human hippocampus. Neurosci Lett. 2005 Mar 22;377(1):31-6. Epub 2004 Dec 15. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 6969
Enzyme 33 Name Glutamate [NMDA] receptor subunit epsilon-2
Enzyme 33 Synonyms
  1. N-methyl D-aspartate receptor subtype 2B
  2. NMDAR2B
  3. NR2B
  4. N-methyl-D-aspartate receptor subunit 3
  5. NR3
  6. hNR3
Enzyme 33 Gene Name GRIN2B
Enzyme 33 Protein Sequence >Glutamate [NMDA] receptor subunit epsilon-2
MKPRAECCSPKFWLVLAVLAVSGSRARSQKSPPSIGIAVILVGTSDEVAIKDAHEKDDFH
HLSVVPRVELVAMNETDPKSIITRICDLMSDRKIQGVVFADDTDQEAIAQILDFISAQTL
TPILGIHGGSSMIMADKDESSMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQ
DFVNKIRSTIENSFVGWELEEVLLLDMSLDDGDSKIQNQLKKLQSPIILLYCTKEEATYI
FEVANSVGLTGYGYTWIVPSLVAGDTDTVPAEFPTGLISVSYDEWDYGLPARVRDGIAII
TTAASDMLSEHSFIPEPKSSCYNTHEKRIYQSNMLNRYLINVTFEGRNLSFSEDGYQMHP
KLVIILLNKERKWERVGKWKDKSLQMKYYVWPRMCPETEEQEDDHLSIVTLEEAPFVIVE
SVDPLSGTCMRNTVPCQKRIVTENKTDEEPGYIKKCCKGFCIDILKKISKSVKFTYDLYL
VTNGKHGKKINGTWNGMIGEVVMKRAYMAVGSLTINEERSEVVDFSVPFIETGISVMVSR
SNGTVSPSAFLEPFSADVWVMMFVMLLIVSAVAVFVFEYFSPVGYNRCLADGREPGGPSF
TIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEYV
DQVSGLSDKKFQRPNDFSPPFRFGTVPNGSTERNIRNNYAEMHAYMGKFNQRGVDDALLS
LKTGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAI
LQLFGDGEMEELEALWLTGICHNEKNEVMSSQLDIDNMAGVFYMLGAAMALSLITFICEH
LFYWQFRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEERQSVMNSPTATMNNTHSNILR
LLRTAKNMANLSGVNGSPQSALDFIRRESSVYDISEHRRSFTHSDCKSYNNPPCEENLFS
DYISEVERTFGNLQLKDSNVYQDHYHHHHRPHSIGSASSIDGLYDCDNPPFTTQSRSISK
KPLDIGLPSSKHSQLSDLYGKFSFKSDRYSGHDDLIRSDVSDISTHTVTYGNIEGNAAKR
RKQQYKDSLKKRPASAKSRREFDEIELAYRRRPPRSPDHKRYFRDKEGLRDFYLDQFRTK
ENSPHWEHVDLTDIYKERSDDFKRDSVSGGGPCTNRSHIKHGTGDKHGVVSGVPAPWEKN
LTNVEWEDRSGGNFCRSCPSKLHNYSTTVTGQNSGRQACIRCEACKKAGNLYDISEDNSL
QELDQPAAPVAVTSNASTTKYPQSPTNSKAQKKNRNKLRRQHSYDTFVDLQKEEAALAPR
SVSLKDKGRFMDGSPYAHMFEMSAGESTFANNKSSVPTAGHHHHNNPGGGYMLSKSLYPD
RVTQNPFIPTFGDDQCLLHGSKSYFFRQPTVAGASKARPDFRALVTNKPVVSALHGAVPA
RFQKDICIGNQSNPCVPNNKNPRAFNGSSNGHVYEKLSSIESDV
Enzyme 33 Number of Residues 1484
Enzyme 33 Molecular Weight 166365.9
Enzyme 33 Theoretical pI 6.92
Enzyme 33 GO Classification
Function
  • excitatory extracellular ligand-gated ion channel activity
  • extracellular ligand-gated ion channel activity
  • extracellular-glutamate-gated ion channel activity
  • glutamate receptor activity
  • ion channel activity
  • ion transmembrane transporter activity
  • ionotropic glutamate receptor activity
  • ligand-gated ion channel activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • substrate-specific transmembrane transporter activity
  • transmembrane receptor activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transport
Component
  • cell part
  • membrane
  • outer membrane-bounded periplasmic space
  • periplasmic space
Enzyme 33 General Function Involved in ionotropic glutamate receptor activity
Enzyme 33 Specific Function NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions Not Available
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • 1-26
Enzyme 33 Transmembrane Regions
  • 558-578 635-655 818-838
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 109730561 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q13224 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name NMDE2_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >4455 bp
ATGAAGCCCAGAGCGGAGTGCTGTTCTCCCAAGTTCTGGTTGGTGTTGGCCGTCCTGGCC
GTGTCAGGCAGCAGAGCTCGTTCTCAGAAGAGCCCCCCCAGCATTGGCATTGCTGTCATC
CTCGTGGGCACTTCCGACGAGGTGGCCATCAAGGATGCCCACGAGAAAGATGATTTCCAC
CATCTCTCCGTGGTACCCCGGGTGGAACTGGTAGCCATGAATGAGACCGACCCAAAGAGC
ATCATCACCCGCATCTGTGATCTCATGTCTGACCGGAAGATCCAGGGGGTGGTGTTTGCT
GATGACACAGACCAGGAAGCCATCGCCCAGATCCTCGATTTCATTTCAGCACAGACTCTC
ACCCCGATCCTGGGCATCCACGGGGGCTCCTCTATGATAATGGCAGATAAGGATGAATCC
TCCATGTTCTTCCAGTTTGGCCCATCAATTGAACAGCAAGCTTCCGTAATGCTCAACATC
ATGGAAGAATATGACTGGTACATCTTTTCTATCGTCACCACCTATTTCCCTGGCTACCAG
GACTTTGTAAACAAGATCCGCAGCACCATTGAGAATAGCTTTGTGGGCTGGGAGCTAGAG
GAGGTCCTCCTACTGGACATGTCCCTGGACGATGGAGATTCTAAGATCCAGAATCAGCTC
AAGAAACTTCAAAGCCCCATCATTCTTCTTTACTGTACCAAGGAAGAAGCCACCTACATC
TTTGAAGTGGCCAACTCAGTAGGGCTGACTGGCTATGGCTACACGTGGATCGTGCCCAGT
CTGGTGGCAGGGGATACAGACACAGTGCCTGCGGAGTTCCCCACTGGGCTCATCTCTGTA
TCATATGATGAATGGGACTATGGCCTCCCCGCCAGAGTGAGAGATGGAATTGCCATAATC
ACCACTGCTGCTTCTGACATGCTGTCTGAGCACAGCTTCATCCCTGAGCCCAAAAGCAGT
TGTTACAACACCCACGAGAAGAGAATCTACCAGTCCAATATGCTAAATAGGTATCTGATC
AATGTCACTTTTGAGGGGAGGAATTTGTCCTTCAGTGAAGATGGCTACCAGATGCACCCG
AAACTGGTGATAATTCTTCTGAACAAGGAGAGGAAGTGGGAAAGGGTGGGGAAGTGGAAA
GACAAGTCCCTGCAGATGAAGTACTATGTGTGGCCCCGAATGTGTCCAGAGACTGAAGAG
CAGGAGGATGACCATCTGAGCATTGTGACCCTGGAGGAGGCACCATTTGTCATTGTGGAA
AGTGTGGACCCTCTGAGTGGAACCTGCATGAGGAACACAGTCCCCTGCCAAAAACGCATA
GTCACTGAGAATAAAACAGACGAGGAGCCGGGTTACATCAAAAAATGCTGCAAGGGGTTC
TGTATTGACATCCTTAAGAAAATTTCTAAATCTGTGAAGTTCACCTATGACCTTTACCTG
GTTACCAATGGCAAGCATGGGAAGAAAATCAATGGAACCTGGAATGGTATGATTGGAGAG
GTGGTCATGAAGAGGGCCTACATGGCAGTGGGCTCACTCACCATCAATGAGGAACGATCG
GAGGTGGTCGACTTCTCTGTGCCCTTCATAGAGACAGGCATCAGTGTCATGGTGTCACGC
AGCAATGGGACTGTCTCACCTTCTGCCTTCTTAGAGCCATTCAGTGCTGACGTATGGGTG
ATGATGTTTGTGATGCTGCTCATCGTCTCAGCCGTGGCTGTCTTTGTCTTTGAGTACTTC
AGCCCTGTGGGTTATAACAGGTGCCTCGCTGATGGCAGAGAGCCTGGTGGACCCTCTTTC
ACCATCGGCAAAGCTATTTGGTTGCTCTGGGGTCTGGTGTTTAACAACTCCGTACCTGTG
CAGAACCCAAAGGGGACCACCTCCAAGATCATGGTGTCAGTGTGGGCCTTCTTTGCTGTC
ATCTTCCTGGCCAGCTACACTGCCAACTTAGCTGCCTTCATGATCCAAGAGGAATATGTG
GACCAGGTTTCTGGCCTGAGCGACAAAAAGTTCCAGAGACCTAATGACTTCTCACCCCCT
TTCCGCTTTGGGACCGTGCCCAACGGCAGCACAGAGAGAAATATTCGCAATAACTATGCA
GAAATGCATGCCTACATGGGAAAGTTCAACCAGAGGGGTGTAGATGATGCATTGCTCTCC
CTGAAAACAGGGAAACTGGATGCCTTCATCTATGATGCAGCAGTGCTGAACTATATGGCA
GGCAGAGATGAAGGCTGCAAGCTGGTGACCATTGGCAGTGGGAAGGTCTTTGCTTCCACT
GGCTATGGCATTGCCATCCAAAAAGATTCTGGGTGGAAGCGCCAGGTGGACCTTGCTATC
CTGCAGCTCTTTGGAGATGGGGAGATGGAAGAACTGGAAGCTCTCTGGCTCACTGGCATT
TGTCACAATGAGAAGAATGAGGTCATGAGCAGCCAGCTGGACATTGACAACATGGCAGGG
GTCTTCTACATGTTGGGGGCGGCCATGGCTCTCAGCCTCATCACCTTCATCTGCGAACAC
CTTTTCTATTGGCAGTTCCGACATTGCTTTATGGGTGTCTGTTCTGGCAAGCCTGGCATG
GTCTTCTCCATCAGCAGAGGTATCTACAGCTGCATCCATGGGGTGGCGATCGAGGAGCGC
CAGTCTGTAATGAACTCCCCCACCGCAACCATGAACAACACACACTCCAACATCCTGCGC
CTGCTGCGCACGGCCAAGAACATGGCTAACCTGTCTGGTGTGAATGGCTCACCGCAGAGC
GCCCTGGACTTCATCCGACGGGAGTCATCCGTCTATGACATCTCAGAGCACCGCCGCAGC
TTCACGCATTCTGACTGCAAATCCTACAACAACCCGCCCTGTGAGGAGAACCTCTTCAGT
GACTACATCAGTGAGGTAGAGAGAACGTTCGGGAACCTGCAGCTGAAGGACAGCAACGTG
TACCAAGATCACTACCACCATCACCACCGGCCCCATAGTATTGGCAGTGCCAGCTCCATC
GATGGGCTCTACGACTGTGACAACCCACCCTTCACCACCCAGTCCAGGTCCATCAGCAAG
AAGCCCCTGGACATCGGCCTCCCCTCCTCCAAGCACAGCCAGCTCAGTGACCTGTACGGC
AAATTCTCCTTCAAGAGCGACCGCTACAGTGGCCACGACGACTTGATCCGCTCCGATGTC
TCTGACATCTCAACCCACACCGTCACCTATGGGAACATCGAGGGCAATGCCGCCAAGAGG
CGTAAGCAGCAATATAAGGACAGCCTGAAGAAGCGGCCTGCCTCGGCCAAGTCCCGCAGG
GAGTTTGACGAGATCGAGCTGGCCTACCGTCGCCGACCGCCCCGCTCCCCTGACCACAAG
CGCTACTTCAGGGACAAGGAAGGGCTACGGGACTTCTACCTGGACCAGTTCCGAACAAAG
GAGAACTCACCCCACTGGGAGCACGTAGACCTGACCGACATCTACAAGGAGCGGAGTGAT
GACTTTAAGCGCGACTCCGTCAGCGGAGGAGGGCCCTGTACCAACAGGTCTCATATCAAG
CACGGGACGGGCGACAAACACGGCGTGGTCAGCGGGGTACCTGCACCTTGGGAGAAGAAC
CTGACCAACGTGGAGTGGGAGGACCGGTCCGGGGGCAACTTCTGCCGCAGCTGTCCCTCC
AAGCTGCACAACTACTCCACGACGGTGACGGGTCAGAACTCGGGCAGGCAGGCGTGCATC
CGGTGTGAGGCTTGCAAGAAAGCAGGCAACCTGTATGACATCAGTGAGGACAACTCCCTG
CAGGAACTGGACCAGCCGGCTGCCCCAGTGGCGGTGACGTCAAACGCCTCCACCACTAAG
TACCCTCAGAGCCCGACTAATTCCAAGGCCCAGAAGAAGAACCGGAACAAACTGCGCCGG
CAGCACTCCTACGACACCTTCGTGGACCTGCAGAAGGAAGAAGCCGCCCTGGCCCCGCGC
AGCGTAAGCCTGAAAGACAAGGGCCGATTCATGGATGGGAGCCCCTACGCCCACATGTTT
GAGATGTCAGCTGGCGAGAGCACCTTTGCCAACAACAAGTCCTCAGTGCCCACTGCCGGA
CATCACCACCACAACAACCCCGGCGGCGGGTACATGCTCAGCAAGTCGCTCTACCCTGAC
CGGGTCACGCAAAACCCTTTCATCCCCACTTTTGGGGACGACCAGTGCTTGCTCCATGGC
AGCAAATCCTACTTCTTCAGGCAGCCCACGGTGGCGGGGGCGTCGAAAGCCAGGCCGGAC
TTCCGGGCCCTTGTCACCAACAAGCCGGTGGTCTCGGCCCTTCATGGGGCCGTGCCAGCC
CGTTTCCAGAAGGACATCTGTATAGGGAACCAGTCCAACCCCTGTGTGCCTAACAACAAA
AACCCCAGGGCTTTCAATGGCTCCAGCAATGGGCATGTTTATGAGAAACTTTCTAGTATT
GAGTCTGATGTCTGA
Enzyme 33 GenBank Gene ID BC113618 Link Image
Enzyme 33 GeneCard ID GRIN2B Link Image
Enzyme 33 GenAtlas ID GRIN2B Link Image
Enzyme 33 HGNC ID HGNC:4586 Link Image
Enzyme 33 Chromosome Location 1
Enzyme 33 Locus 12p12
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Adams SL, Foldes RL, Kamboj RK: Human N-methyl-D-aspartate receptor modulatory subunit hNR3: cloning and sequencing of the cDNA and primary structure of the protein. Biochim Biophys Acta. 1995 Jan 2;1260(1):105-8. [PubMed Link Image]
  2. Hess SD, Daggett LP, Crona J, Deal C, Lu CC, Urrutia A, Chavez-Noriega L, Ellis SB, Johnson EC, Velicelebi G: Cloning and functional characterization of human heteromeric N-methyl-D-aspartate receptors. J Pharmacol Exp Ther. 1996 Aug;278(2):808-16. [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. Mandich P, Schito AM, Bellone E, Antonacci R, Finelli P, Rocchi M, Ajmar F: Mapping of the human NMDAR2B receptor subunit gene (GRIN2B) to chromosome 12p12. Genomics. 1994 Jul 1;22(1):216-8. [PubMed Link Image]
  5. Schito AM, Pizzuti A, Di Maria E, Schenone A, Ratti A, Defferrari R, Bellone E, Mancardi GL, Ajmar F, Mandich P: mRNA distribution in adult human brain of GRIN2B, a N-methyl-D-aspartate (NMDA) receptor subunit. Neurosci Lett. 1997 Dec 12;239(1):49-53. [PubMed Link Image]
  6. Wu Y, Dowbenko D, Spencer S, Laura R, Lee J, Gu Q, Lasky LA: Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase. J Biol Chem. 2000 Jul 14;275(28):21477-85. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 7028
Enzyme 34 Name Vitamin K-dependent gamma-carboxylase
Enzyme 34 Synonyms
  1. Gamma-glutamyl carboxylase
  2. Peptidyl-glutamate 4-carboxylase
  3. Vitamin K gamma glutamyl carboxylase
Enzyme 34 Gene Name GGCX
Enzyme 34 Protein Sequence >Vitamin K-dependent gamma-carboxylase
MAVSAGSARTSPSSDKVQKDKAELISGPRQDSRIGKLLGFEWTDLSSWRRLVTLLNRPTD
PASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYT
IMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYW
SVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVEGYSMEYLSRHWLFSP
FKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFS
YVMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSVSCVYKRSRGKSGQKPGLRH
QLGAAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRT
GELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQR
IFDPRVDIVQAAWSPFQRTSWVQPLLMDLSPWRAKLQEIKSSLDNHTEVVFIADFPGLHL
ENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTTSPSPSCYM
YVYVNTTELALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFL
RRQQRLQEIERRRNTPFHERFFRFLLRKLYVFRRSFLMTCISLRNLILGRPSLEQLAQEV
TYANLRPFEAVGELNPSNTDSSHSNPPESNPDPVHSEF
Enzyme 34 Number of Residues 758
Enzyme 34 Molecular Weight 87560.1
Enzyme 34 Theoretical pI 8.10
Enzyme 34 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • gamma-glutamyl carboxylase activity
  • lyase activity
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptidyl-amino acid modification
  • peptidyl-glutamic acid carboxylation
  • peptidyl-glutamic acid modification
  • protein modification process
Component
Enzyme 34 General Function Involved in gamma-glutamyl carboxylase activity
Enzyme 34 Specific Function Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions
  • peptidyl-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O = peptidyl-glutamate + CO2 + O2 + phylloquinone
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • 61-81 114-134 137-157 293-313 362-382
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 62988953 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID P38435 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name VKGC_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >2277 bp
ATGGCGGTGTCTGCCGGGTCCGCGCGGACCTCGCCCAGCTCAGATAAAGTACAGAAAGAC
AAGGCTGAACTGATCTCAGGGCCCAGGCAGGACAGCCGAATAGGGAAACTCTTGGGTTTT
GAGTGGACAGATTTGTCCAGTTGGCGGAGGCTGGTGACCCTGCTGAATCGACCAACGGAC
CCTGCAAGCTTAGCTGTCTTTCGTTTTCTTTTTGGGTTCTTGATGGTGCTAGACATTCCC
CAGGAGCGGGGGCTCAGCTCTCTGGACCGGAAATACCTTGATGGGCTGGATGTGTGCCGC
TTCCCCTTGCTGGATGCCCTACGCCCACTGCCACTTGACTGGATGTATCTTGTCTACACC
ATCATGTTTCTGGGGGCACTGGGCATGATGCTGGGCCTGTGCTACCGGATAAGCTGTGTG
TTATTCCTGCTGCCATACTGGTATGTGTTTCTCCTGGACAAGACATCATGGAACAACCAC
TCCTATCTGTATGGGTTGTTGGCCTTTCAGCTAACATTCATGGATGCAAACCACTACTGG
TCTGTGGACGGTCTGCTGAATGCCCATAGGAGGAATGCCCACGTGCCCCTTTGGAACTAT
GCAGTGCTCCGTGGCCAGATCTTCATTGTGTACTTCATTGCGGGTGTGAAAAAGCTGGAT
GCAGACTGGGTTGAAGGCTATTCCATGGAATATTTGTCCCGGCACTGGCTCTTCAGTCCC
TTCAAACTGCTGTTGTCTGAGGAGCTGACTAGCCTGCTGGTCGTGCACTGGGGTGGGCTG
CTGCTTGACCTCTCAGCTGGTTTCCTGCTCTTTTTTGATGTCTCAAGATCCATTGGACTG
TTCTTTGTGTCCTACTTCCACTGCATGAATTCCCAGCTTTTCAGCATTGGTATGTTCTCC
TACGTCATGCTGGCCAGCAGCCCTCTCTTCTGCTCCCCTGAGTGGCCTCGGAAGCTGGTG
TCCTACTGCCCCCGAAGGTTGCAACAACTGTTGCCCCTCAAGGCAGCCCCTCAGCCCAGT
GTTTCCTGTGTGTATAAGAGGAGCCGGGGCAAAAGTGGCCAGAAGCCAGGGCTGCGCCAT
CAGCTGGGAGCTGCCTTCACCCTGCTCTACCTCCTGGAGCAGCTATTCCTGCCCTATTCT
CATTTTCTCACCCAGGGCTATAACAACTGGACAAATGGGCTGTATGGCTATTCCTGGGAC
ATGATGGTGCACTCCCGCTCCCACCAGCACGTGAAGATCACCTACCGTGATGGCCGCACT
GGCGAACTGGGCTACCTTAACCCTGGGGTATTTACACAGAGTCGGCGATGGAAGGATCAT
GCAGACATGCTGAAGCAATATGCCACTTGCCTGAGCCGCCTGCTTCCCAAGTATAATGTC
ACTGAGCCCCAGATCTACTTTGATATTTGGGTCTCCATCAATGACCGCTTCCAGCAGAGG
ATTTTTGACCCTCGTGTGGACATCGTGCAGGCCGCTTGGTCACCCTTTCAGCGCACATCC
TGGGTGCAACCACTCTTGATGGACCTGTCTCCCTGGAGGGCCAAGTTACAGGAAATCAAG
AGCAGCCTAGACAACCACACTGAGGTGGTCTTCATTGCAGATTTCCCTGGACTGCACTTG
GAGAATTTTGTGAGTGAAGACCTGGGCAACACTAGCATCCAGCTGCTGCAGGGGGAAGTG
ACTGTGGAGCTTGTGGCAGAACAGAAGAACCAGACTCTTCGAGAGGGAGAAAAAATGCAG
TTGCCTGCTGGTGAGTACCATAAGGTGTATACGACATCACCTAGCCCTTCTTGCTACATG
TACGTCTATGTCAACACTACAGAGCTTGCACTGGAGCAAGACCTGGCATATCTGCAAGAA
TTAAAGGAAAAGGTGGAGAATGGAAGTGAAACAGGGCCTCTACCCCCAGAGCTGCAGCCT
CTGTTGGAAGGGGAAGTAAAAGGGGGCCCTGAGCCAACACCTCTGGTTCAGACCTTTCTT
AGACGCCAACAAAGGCTCCAGGAGATTGAACGCCGGCGAAATACTCCTTTCCATGAGCGA
TTCTTCCGCTTCTTGTTGCGAAAGCTCTATGTCTTTCGCCGCAGCTTCCTGATGACTTGT
ATCTCACTTCGAAATCTGATATTAGGCCGTCCTTCCCTGGAGCAGCTGGCCCAGGAGGTG
ACTTATGCAAACTTGAGACCCTTTGAGGCAGTTGGAGAACTGAATCCCTCAAACACGGAT
TCTTCACATTCTAATCCTCCTGAGTCAAATCCTGATCCTGTCCACTCAGAGTTCTGA
Enzyme 34 GenBank Gene ID AC016753 Link Image
Enzyme 34 GeneCard ID GGCX Link Image
Enzyme 34 GenAtlas ID GGCX Link Image
Enzyme 34 HGNC ID HGNC:4247 Link Image
Enzyme 34 Chromosome Location 2
Enzyme 34 Locus 2p12
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Wu SM, Cheung WF, Frazier D, Stafford DW: Cloning and expression of the cDNA for human gamma-glutamyl carboxylase. Science. 1991 Dec 13;254(5038):1634-6. [PubMed Link Image]
  2. Wu SM, Stafford DW, Frazier LD, Fu YY, High KA, Chu K, Sanchez-Vega B, Solera J: Genomic sequence and transcription start site for the human gamma-glutamyl carboxylase. Blood. 1997 Jun 1;89(11):4058-62. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Tie J, Wu SM, Jin D, Nicchitta CV, Stafford DW: A topological study of the human gamma-glutamyl carboxylase. Blood. 2000 Aug 1;96(3):973-8. [PubMed Link Image]
  6. Presnell SR, Tripathy A, Lentz BR, Jin DY, Stafford DW: A novel fluorescence assay to study propeptide interaction with gamma-glutamyl carboxylase. Biochemistry. 2001 Oct 2;40(39):11723-33. [PubMed Link Image]
  7. Tie JK, Mutucumarana VP, Straight DL, Carrick KL, Pope RM, Stafford DW: Determination of disulfide bond assignment of human vitamin K-dependent gamma-glutamyl carboxylase by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J Biol Chem. 2003 Nov 14;278(46):45468-75. Epub 2003 Sep 8. [PubMed Link Image]
  8. Berkner KL: The vitamin K-dependent carboxylase. Annu Rev Nutr. 2005;25:127-49. [PubMed Link Image]
  9. Rishavy MA, Hallgren KW, Yakubenko AV, Shtofman RL, Runge KW, Berkner KL: Bronsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation. Biochemistry. 2006 Nov 7;45(44):13239-48. [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. 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]
  12. Brenner B, Sanchez-Vega B, Wu SM, Lanir N, Stafford DW, Solera J: A missense mutation in gamma-glutamyl carboxylase gene causes combined deficiency of all vitamin K-dependent blood coagulation factors. Blood. 1998 Dec 15;92(12):4554-9. [PubMed Link Image]
  13. Spronk HM, Farah RA, Buchanan GR, Vermeer C, Soute BA: Novel mutation in the gamma-glutamyl carboxylase gene resulting in congenital combined deficiency of all vitamin K-dependent blood coagulation factors. Blood. 2000 Nov 15;96(10):3650-2. [PubMed Link Image]
  14. Mutucumarana VP, Stafford DW, Stanley TB, Jin DY, Solera J, Brenner B, Azerad R, Wu SM: Expression and characterization of the naturally occurring mutation L394R in human gamma-glutamyl carboxylase. J Biol Chem. 2000 Oct 20;275(42):32572-7. [PubMed Link Image]
  15. Rost S, Fregin A, Koch D, Compes M, Muller CR, Oldenburg J: Compound heterozygous mutations in the gamma-glutamyl carboxylase gene cause combined deficiency of all vitamin K-dependent blood coagulation factors. Br J Haematol. 2004 Aug;126(4):546-9. [PubMed Link Image]
  16. Vanakker OM, Martin L, Gheduzzi D, Leroy BP, Loeys BL, Guerci VI, Matthys D, Terry SF, Coucke PJ, Pasquali-Ronchetti I, De Paepe A: Pseudoxanthoma elasticum-like phenotype with cutis laxa and multiple coagulation factor deficiency represents a separate genetic entity. J Invest Dermatol. 2007 Mar;127(3):581-7. Epub 2006 Nov 16. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 7173
Enzyme 35 Name Glutamate receptor, ionotropic kainate 2
Enzyme 35 Synonyms
  1. Excitatory amino acid receptor 4
  2. EAA4
  3. Glutamate receptor 6
  4. GluR-6
  5. GluR6
Enzyme 35 Gene Name GRIK2
Enzyme 35 Protein Sequence >Glutamate receptor, ionotropic kainate 2
MKIIFPILSNPVFRRTVKLLLCLLWIGYSQGTTHVLRFGGIFEYVESGPMGAEELAFRFA
VNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAVQS
ICNALGVPHIQTRWKHQVSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDST
GLIRLQELIKAPSRYNLRLKIRQLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILK
QALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNTENTQVSSIIEKWSMER
LQAPPKPDSGLLDGFMTTDAALMYDAVHVVSVAVQQFPQMTVSSLQCNRHKPWRFGTRFM
SLIKEAHWEGLTGRITFNKTNGLRTDFDLDVISLKEEGLEKIGTWDPASGLNMTESQKGK
PANITDSLSNRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEI
RLVEDGKYGAQDDANGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGISI
LYRKPNGTNPGVFSFLNPLSPDIWMYILLAYLGVSCVLFVIARFSPYEWYNPHPCNPDSD
VVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLT
VERMESPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQSVLVKS
NEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITI
AILQLQEEGKLHMMKEKWWRGNGCPEEESKEASALGVQNIGGIFIVLAAGLVLSVFVAVG
EFLYKSKKNAQLEKRSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRR
LPGKETMA
Enzyme 35 Number of Residues 908
Enzyme 35 Molecular Weight 102582.5
Enzyme 35 Theoretical pI 8.01
Enzyme 35 GO Classification
Function
  • excitatory extracellular ligand-gated ion channel activity
  • extracellular ligand-gated ion channel activity
  • extracellular-glutamate-gated ion channel activity
  • glutamate receptor activity
  • ion channel activity
  • ion transmembrane transporter activity
  • ionotropic glutamate receptor activity
  • ligand-gated ion channel activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • substrate-specific transmembrane transporter activity
  • transmembrane receptor activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transport
Component
  • cell part
  • membrane
Enzyme 35 General Function Involved in ionotropic glutamate receptor activity
Enzyme 35 Specific Function Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L- glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus. Modulates cell surface expression of NETO2
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • 1-31
Enzyme 35 Transmembrane Regions
  • 562-582 636-656 820-840
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein Not Available
Enzyme 35 UniProtKB/Swiss-Prot ID Q13002 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name GRIK2_HUMAN Link Image
Enzyme 35 PDB ID 1YAE Link Image
Enzyme 35 PDB File Show
Enzyme 35 3D Structure
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >2727 bp
ATGAAGATTATTTTCCCGATTCTAAGTAATCCAGTCTTCAGGCGCACCGTTAAACTCCTG
CTCTGTTTACTGTGGATTGGATATTCTCAAGGAACCACACATGTATTAAGATTTGGTGGT
ATTTTTGAATATGTGGAATCTGGCCCAATGGGAGCTGAGGAACTTGCATTCAGATTTGCT
GTGAACACAATTAACAGAAACAGAACATTGCTACCCAATACTACCCTTACCTATGATACC
CAGAAGATAAACCTTTATGATAGTTTTGAAGCATCCAAGAAAGCCTGTGATCAGCTGTCT
CTTGGGGTGGCTGCCATCTTCGGGCCTTCACACAGCTCATCAGCAAACGCAGTGCAGTCC
ATCTGCAATGCTCTGGGAGTTCCCCACATACAGACCCGCTGGAAGCACCAGGTGTCAGAC
AACAAAGATTCCTTCTATGTCAGTCTCTACCCAGACTTCTCTTCACTCAGCCGTGCCATT
TTAGACCTGGTGCAGTTTTTCAAGTGGAAAACCGTCACGGTTGTGTATGATGACAGCACT
GGTCTCATTCGTTTGCAAGAGCTCATCAAAGCTCCATCAAGGTATAATCTTCGACTCAAA
ATTCGTCAGTTACCTGCTGATACAAAGGATGCAAAACCCTTACTAAAAGAAATGAAAAGA
GGCAAGGAGTTTCATGTAATCTTTGATTGTAGCCATGAAATGGCAGCAGGCATTTTAAAA
CAGGCATTAGCTATGGGAATGATGACAGAATACTATCATTATATCTTTACCACTCTGGAC
CTCTTTGCTCTTGATGTTGAGCCCTACCGATACAGTGGTGTTAACATGACAGGGTTCAGA
ATATTAAATACAGAAAATACCCAAGTCTCCTCCATCATTGAAAAGTGGTCGATGGAACGA
TTGCAGGCACCTCCGAAACCCGATTCAGGTTTGCTGGATGGATTTATGACGACTGATGCT
GCTCTAATGTATGATGCTGTGCATGTGGTGTCTGTGGCCGTTCAACAGTTTCCCCAGATG
ACAGTCAGTTCCTTGCAGTGTAATCGACATAAACCCTGGCGCTTCGGGACCCGCTTTATG
AGTCTAATTAAAGAGGCACATTGGGAAGGCCTCACAGGCAGAATAACTTTCAACAAAACC
AATGGCTTGAGAACAGATTTTGATTTGGATGTGATCAGTCTGAAGGAAGAAGGTCTAGAA
AAGATTGGAACGTGGGATCCAGCCAGTGGCCTGAATATGACAGAAAGTCAAAAGGGAAAG
CCAGCGAACATCACAGATTCCTTATCCAATCGTTCTTTGATTGTTACCACCATTTTGGAA
GAGCCTTATGTCCTTTTTAAGAAGTCTGACAAACCTCTCTATGGTAATGATCGATTTGAA
GGCTATTGCATTGATCTCCTCAGAGAGTTATCTACAATCCTTGGCTTTACATATGAAATT
AGACTTGTGGAAGATGGGAAATATGGAGCCCAGGATGATGCCAATGGACAATGGAATGGA
ATGGTTCGTGAACTAATTGATCATAAAGCTGACCTTGCAGTTGCTCCACTGGCTATTACC
TATGTTCGAGAGAAGGTCATCGACTTTTCCAAGCCCTTTATGACACTTGGAATAAGTATT
TTGTACCGCAAGCCCAATGGTACAAACCCAGGCGTCTTCTCCTTCCTGAATCCTCTCTCC
CCTGATATCTGGATGTATATTCTGCTGGCTTACTTGGGTGTCAGTTGTGTGCTCTTTGTC
ATAGCCAGGTTTAGTCCTTATGAGTGGTATAATCCACACCCTTGCAACCCTGACTCAGAC
GTGGTGGAAAACAATTTTACCTTGCTAAATAGTTTCTGGTTTGGAGTTGGAGCTCTCATG
CAGCAAGGTTCTGAGCTCATGCCCAAAGCACTGTCCACCAGGATAGTGGGAGGCATTTGG
TGGTTTTTCACACTTATCATCATTTCTTCGTATACTGCTAACTTAGCCGCCTTTCTGACA
GTGGAACGCATGGAATCCCCTATTGACTCTGCTGATGATTTAGCTAAACAAACCAAGATA
GAATATGGAGCAGTAGAGGATGGTGCAACCATGACTTTTTTCAAGAAATCAAAAATCTCC
ACGTATGACAAAATGTGGGCCTTTATGAGTAGCAGAAGGCAGTCAGTGCTGGTCAAAAGT
AATGAAGAAGGAATCCAGCGAGTCCTCACCTCTGATTATGCTTTCCTAATGGAGTCAACA
ACCATCGAGTTTGTTACCCAGCGGAACTGTAACCTGACACAGATTGGCGGCCTTATAGAC
TCTAAAGGTTATGGCGTTGGCACTCCCATGGGTTCTCCATATCGAGACAAAATTACCATA
GCAATTCTTCAGCTGCAAGAGGAAGGCAAACTGCATATGATGAAGGAGAAATGGTGGAGG
GGCAATGGTTGCCCAGAAGAGGAAAGCAAAGAGGCCAGTGCCCTGGGGGTTCAGAATATT
GGTGGCATCTTCATTGTTCTGGCAGCCGGCTTGGTGCTTTCAGTTTTTGTGGCAGTGGGA
GAATTTTTATACAAATCCAAAAAAAACGCTCAATTGGAAAAGAGGTCCTTCTGTAGTGCC
ATGGTAGAAGAATTGAGGATGTCCCTGAAGTGCCAGCGTCGGTTAAAACATAAGCCACAG
GCCCCAGTTATTGTGAAAACAGAAGAAGTTATCAACATGCACACATTTAACGACAGAAGG
TTGCCAGGTAAAGAAACCATGGCATAA
Enzyme 35 GenBank Gene ID U16126 Link Image
Enzyme 35 GeneCard ID GRIK2 Link Image
Enzyme 35 GenAtlas ID GRIK2 Link Image
Enzyme 35 HGNC ID HGNC:4580 Link Image
Enzyme 35 Chromosome Location 6
Enzyme 35 Locus 6q16.3-q21
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Hoo KH, Nutt SL, Fletcher EJ, Elliott CE, Korczak B, Deverill RM, Rampersad V, Fantaske RP, Kamboj RK: Functional expression and pharmacological characterization of the human EAA4 (GluR6) glutamate receptor: a kainate selective channel subunit. Receptors Channels. 1994;2(4):327-37. [PubMed Link Image]
  2. Paschen W, Blackstone CD, Huganir RL, Ross CA: Human GluR6 kainate receptor (GRIK2): molecular cloning, expression, polymorphism, and chromosomal assignment. Genomics. 1994 Apr;20(3):435-40. [PubMed Link Image]
  3. Barbon A, Vallini I, Barlati S: Genomic organization of the human GRIK2 gene and evidence for multiple splicing variants. Gene. 2001 Aug 22;274(1-2):187-97. [PubMed Link Image]
  4. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  5. Paschen W, Hedreen JC, Ross CA: RNA editing of the glutamate receptor subunits GluR2 and GluR6 in human brain tissue. J Neurochem. 1994 Nov;63(5):1596-602. [PubMed Link Image]
  6. Nutt SL, Kamboj RK: RNA editing of human kainate receptor subunits. Neuroreport. 1994 Dec 20;5(18):2625-9. [PubMed Link Image]
  7. Piserchio A, Pellegrini M, Mehta S, Blackman SM, Garcia EP, Marshall J, Mierke DF: The PDZ1 domain of SAP90. Characterization of structure and binding. J Biol Chem. 2002 Mar 1;277(9):6967-73. Epub 2001 Dec 14. [PubMed Link Image]
  8. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
  9. Motazacker MM, Rost BR, Hucho T, Garshasbi M, Kahrizi K, Ullmann R, Abedini SS, Nieh SE, Amini SH, Goswami C, Tzschach A, Jensen LR, Schmitz D, Ropers HH, Najmabadi H, Kuss AW: A defect in the ionotropic glutamate receptor 6 gene (GRIK2) is associated with autosomal recessive mental retardation. Am J Hum Genet. 2007 Oct;81(4):792-8. Epub 2007 Aug 31. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 7476
Enzyme 36 Name Glutamate carboxypeptidase 2
Enzyme 36 Synonyms
  1. Cell growth-inhibiting gene 27 protein
  2. Folate hydrolase 1
  3. Folylpoly-gamma-glutamate carboxypeptidase
  4. FGCP
  5. Glutamate carboxypeptidase II
  6. GCPII
  7. Membrane glutamate carboxypeptidase
  8. mGCP
  9. N-acetylated-alpha-linked acidic dipeptidase I
  10. NAALADase I
  11. Prostate-specific membrane antigen
  12. PSM
  13. PSMA
  14. Pteroylpoly-gamma-glutamate carboxypeptidase
Enzyme 36 Gene Name FOLH1
Enzyme 36 Protein Sequence >Glutamate carboxypeptidase 2
MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLFGWFIKSSNEATNITPKHNMKA
FLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYP
NKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYA
RTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVK
SYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYY
DAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIG
TLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFAS
WDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKE
LKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKN
WETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDY
AVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIV
LRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVD
PSKAWGEVKRQIYVAAFTVQAAAETLSEVA
Enzyme 36 Number of Residues 750
Enzyme 36 Molecular Weight 84330.0
Enzyme 36 Theoretical pI 6.97
Enzyme 36 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • peptidase activity
Process
  • macromolecule metabolic process
  • metabolic process
  • protein metabolic process
  • proteolysis
Component
Enzyme 36 General Function Involved in peptidase activity
Enzyme 36 Specific Function Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions
  • Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates EFFECTOR Metal [CPD:C00050]
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • 20-43
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein Not Available
Enzyme 36 UniProtKB/Swiss-Prot ID Q04609 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name FOLH1_HUMAN Link Image
Enzyme 36 PDB ID 1Z8L Link Image
Enzyme 36 PDB File Show
Enzyme 36 3D Structure
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >2253 bp
ATGTGGAATCTCCTTCACGAAACCGACTCGGCTGTGGCCACCGCGCGCCGCCCGCGCTGG
CTGTGCGCTGGGGCGCTGGTGCTGGCGGGTGGCTTCTTTCTCCTCGGCTTCCTCTTCGGG
TGGTTTATAAAATCCTCCAATGAAGCTACTAACATTACTCCAAAGCATAATATGAAAGCA
TTTTTGGATGAATTGAAAGCTGAGAACATCAAGAAGTTCTTATATAATTTTACACAGATA
CCACATTTAGCAGGAACAGAACAAAACTTTCAGCTTGCAAAGCAAATTCAATCCCAGTGG
AAAGAATTTGGCCTGGATTCTGTTGAGCTAGCACATTATGATGTCCTGTTGTCCTACCCA
AATAAGACTCATCCCAACTACATCTCAATAATTAATGAAGATGGAAATGAGATTTTCAAC
ACATCATTATTTGAACCACCTCCTCCAGGATATGAAAATGTTTCGGATATTGTACCACCT
TTCAGTGCTTTCTCTCCTCAAGGAATGCCAGAGGGCGATCTAGTGTATGTTAACTATGCA
CGAACTGAAGACTTCTTTAAATTGGAACGGGACATGAAAATCAATTGCTCTGGGAAAATT
GTAATTGCCAGATATGGGAAAGTTTTCAGAGGAAATAAGGTTAAAAATGCCCAGCTGGCA
GGGGCCAAAGGAGTCATTCTCTACTCCGACCCTGCTGACTACTTTGCTCCTGGGGTGAAG
TCCTATCCAGATGGTTGGAATCTTCCTGGAGGTGGTGTCCAGCGTGGAAATATCCTAAAT
CTGAATGGTGCAGGAGACCCTCTCACACCAGGTTACCCAGCAAATGAATATGCTTATAGG
CGTGGAATTGCAGAGGCTGTTGGTCTTCCAAGTATTCCTGTTCATCCAATTGGATACTAT
GATGCACAGAAGCTCCTAGAAAAAATGGGTGGCTCAGCACCACCAGATAGCAGCTGGAGA
GGAAGTCTCAAAGTGCCCTACAATGTTGGACCTGGCTTTACTGGAAACTTTTCTACACAA
AAAGTCAAGATGCACATCCACTCTACCAATGAAGTGACAAGAATTTACAATGTGATAGGT
ACTCTCAGAGGAGCAGTGGAACCAGACAGATATGTCATTCTGGGAGGTCACCGGGACTCA
TGGGTGTTTGGTGGTATTGACCCTCAGAGTGGAGCAGCTGTTGTTCATGAAATTGTGAGG
AGCTTTGGAACACTGAAAAAGGAAGGGTGGAGACCTAGAAGAACAATTTTGTTTGCAAGC
TGGGATGCAGAAGAATTTGGTCTTCTTGGTTCTACTGAGTGGGCAGAGGAGAATTCAAGA
CTCCTTCAAGAGCGTGGCGTGGCTTATATTAATGCTGACTCATCTATAGAAGGAAACTAC
ACTCTGAGAGTTGATTGTACACCGCTGATGTACAGCTTGGTACACAACCTAACAAAAGAG
CTGAAAAGCCCTGATGAAGGCTTTGAAGGCAAATCTCTTTATGAAAGTTGGACTAAAAAA
AGTCCTTCCCCAGAGTTCAGTGGCATGCCCAGGATAAGCAAATTGGGATCTGGAAATGAT
TTTGAGGTGTTCTTCCAACGACTTGGAATTGCTTCAGGCAGAGCACGGTATACTAAAAAT
TGGGAAACAAACAAATTCAGCGGCTATCCACTGTATCACAGTGTCTATGAAACATATGAG
TTGGTGGAAAAGTTTTATGATCCAATGTTTAAATATCACCTCACTGTGGCCCAGGTTCGA
GGAGGGATGGTGTTTGAGCTAGCCAATTCCATAGTGCTCCCTTTTGATTGTCGAGATTAT
GCTGTAGTTTTAAGAAAGTATGCTGACAAAATCTACAGTATTTCTATGAAACATCCACAG
GAAATGAAGACATACAGTGTATCATTTGATTCACTTTTTTCTGCAGTAAAGAATTTTACA
GAAATTGCTTCCAAGTTCAGTGAGAGACTCCAGGACTTTGACAAAAGCAACCCAATAGTA
TTAAGAATGATGAATGATCAACTCATGTTTCTGGAAAGAGCATTTATTGATCCATTAGGG
TTACCAGACAGGCCTTTTTATAGGCATGTCATCTATGCTCCAAGCAGCCACAACAAGTAT
GCAGGGGAGTCATTCCCAGGAATTTATGATGCTCTGTTTGATATTGAAAGCAAAGTGGAC
CCTTCCAAGGCCTGGGGAGAAGTGAAGAGACAGATTTATGTTGCAGCCTTCACAGTGCAG
GCAGCTGCAGAGACTTTGAGTGAAGTAGCCTAA
Enzyme 36 GenBank Gene ID M99487 Link Image
Enzyme 36 GeneCard ID FOLH1 Link Image
Enzyme 36 GenAtlas ID FOLH1 Link Image
Enzyme 36 HGNC ID HGNC:3788 Link Image
Enzyme 36 Chromosome Location 1
Enzyme 36 Locus 11p11.2
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Israeli RS, Powell CT, Fair WR, Heston WD: Molecular cloning of a complementary DNA encoding a prostate-specific membrane antigen. Cancer Res. 1993 Jan 15;53(2):227-30. [PubMed Link Image]
  2. Su SL, Huang IP, Fair WR, Powell CT, Heston WD: Alternatively spliced variants of prostate-specific membrane antigen RNA: ratio of expression as a potential measurement of progression. Cancer Res. 1995 Apr 1;55(7):1441-3. [PubMed Link Image]
  3. Bzdega T, Turi T, Wroblewska B, She D, Chung HS, Kim H, Neale JH: Molecular cloning of a peptidase against N-acetylaspartylglutamate from a rat hippocampal cDNA library. J Neurochem. 1997 Dec;69(6):2270-7. [PubMed Link Image]
  4. O'Keefe DS, Su SL, Bacich DJ, Horiguchi Y, Luo Y, Powell CT, Zandvliet D, Russell PJ, Molloy PL, Nowak NJ, Shows TB, Mullins C, Vonder Haar RA, Fair WR, Heston WD: Mapping, genomic organization and promoter analysis of the human prostate-specific membrane antigen gene. Biochim Biophys Acta. 1998 Nov 26;1443(1-2):113-27. [PubMed Link Image]
  5. Luthi-Carter R, Barczak AK, Speno H, Coyle JT: Molecular characterization of human brain N-acetylated alpha-linked acidic dipeptidase (NAALADase). J Pharmacol Exp Ther. 1998 Aug;286(2):1020-5. [PubMed Link Image]
  6. Pangalos MN, Neefs JM, Somers M, Verhasselt P, Bekkers M, van der Helm L, Fraiponts E, Ashton D, Gordon RD: Isolation and expression of novel human glutamate carboxypeptidases with N-acetylated alpha-linked acidic dipeptidase and dipeptidyl peptidase IV activity. J Biol Chem. 1999 Mar 26;274(13):8470-83. [PubMed Link Image]
  7. Devlin AM, Ling EH, Peerson JM, Fernando S, Clarke R, Smith AD, Halsted CH: Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. Hum Mol Genet. 2000 Nov 22;9(19):2837-44. [PubMed Link Image]
  8. O'Keefe DS, Bacich DJ, Heston WD: Comparative analysis of prostate-specific membrane antigen (PSMA) versus a prostate-specific membrane antigen-like gene. Prostate. 2004 Feb 1;58(2):200-10. [PubMed Link Image]
  9. 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]
  10. 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]
  11. Grauer LS, Lawler KD, Marignac JL, Kumar A, Goel AS, Wolfert RL: Identification, purification, and subcellular localization of prostate-specific membrane antigen PSM' protein in the LNCaP prostatic carcinoma cell line. Cancer Res. 1998 Nov 1;58(21):4787-9. [PubMed Link Image]
  12. Luthi-Carter R, Barczak AK, Speno H, Coyle JT: Hydrolysis of the neuropeptide N-acetylaspartylglutamate (NAAG) by cloned human glutamate carboxypeptidase II. Brain Res. 1998 Jun 8;795(1-2):341-8. [PubMed Link Image]
  13. Rawlings ND, Barrett AJ: Structure of membrane glutamate carboxypeptidase. Biochim Biophys Acta. 1997 May 23;1339(2):247-52. [PubMed Link Image]
  14. Speno HS, Luthi-Carter R, Macias WL, Valentine SL, Joshi AR, Coyle JT: Site-directed mutagenesis of predicted active site residues in glutamate carboxypeptidase II. Mol Pharmacol. 1999 Jan;55(1):179-85. [PubMed Link Image]
  15. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
  16. Barinka C, Sacha P, Sklenar J, Man P, Bezouska K, Slusher BS, Konvalinka J: Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity. Protein Sci. 2004 Jun;13(6):1627-35. [PubMed Link Image]
  17. Kinoshita Y, Kuratsukuri K, Landas S, Imaida K, Rovito PM Jr, Wang CY, Haas GP: Expression of prostate-specific membrane antigen in normal and malignant human tissues. World J Surg. 2006 Apr;30(4):628-36. [PubMed Link Image]
  18. Sacha P, Zamecnik J, Barinka C, Hlouchova K, Vicha A, Mlcochova P, Hilgert I, Eckschlager T, Konvalinka J: Expression of glutamate carboxypeptidase II in human brain. Neuroscience. 2007 Feb 23;144(4):1361-72. Epub 2006 Dec 5. [PubMed Link Image]
  19. Mesters JR, Barinka C, Li W, Tsukamoto T, Majer P, Slusher BS, Konvalinka J, Hilgenfeld R: Structure of glutamate carboxypeptidase II, a drug target in neuronal damage and prostate cancer. EMBO J. 2006 Mar 22;25(6):1375-84. Epub 2006 Feb 9. [PubMed Link Image]
  20. Mesters JR, Henning K, Hilgenfeld R: Human glutamate carboxypeptidase II inhibition: structures of GCPII in complex with two potent inhibitors, quisqualate and 2-PMPA. Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):508-13. Epub 2007 Mar 16. [PubMed Link Image]
  21. Barinka C, Rovenska M, Mlcochova P, Hlouchova K, Plechanovova A, Majer P, Tsukamoto T, Slusher BS, Konvalinka J, Lubkowski J: Structural insight into the pharmacophore pocket of human glutamate carboxypeptidase II. J Med Chem. 2007 Jul 12;50(14):3267-73. Epub 2007 Jun 14. [PubMed Link Image]
  22. Barinka C, Byun Y, Dusich CL, Banerjee SR, Chen Y, Castanares M, Kozikowski AP, Mease RC, Pomper MG, Lubkowski J: Interactions between human glutamate carboxypeptidase II and urea-based inhibitors: structural characterization. J Med Chem. 2008 Dec 25;51(24):7737-43. [PubMed Link Image]
  23. Barinka C, Hlouchova K, Rovenska M, Majer P, Dauter M, Hin N, Ko YS, Tsukamoto T, Slusher BS, Konvalinka J, Lubkowski J: Structural basis of interactions between human glutamate carboxypeptidase II and its substrate analogs. J Mol Biol. 2008 Mar 7;376(5):1438-50. Epub 2008 Jan 5. [PubMed Link Image]
  24. Klusak V, Barinka C, Plechanovova A, Mlcochova P, Konvalinka J, Rulisek L, Lubkowski J: Reaction mechanism of glutamate carboxypeptidase II revealed by mutagenesis, X-ray crystallography, and computational methods. Biochemistry. 2009 May 19;48(19):4126-38. [PubMed Link Image]
  25. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 7700
Enzyme 37 Name Metabotropic glutamate receptor 1
Enzyme 37 Synonyms
  1. mGluR1
Enzyme 37 Gene Name GRM1
Enzyme 37 Protein Sequence >Metabotropic glutamate receptor 1
MVGLLLFFFPAIFLEVSLLPRSPGRKVLLAGASSQRSVARMDGDVIIGALFSVHHQPPAE
KVPERKCGEIREQYGIQRVEAMFHTLDKINADPVLLPNITLGSEIRDSCWHSSVALEQSI
EFIRDSLISIRDEKDGINRCLPDGQSLPPGRTKKPIAGVIGPGSSSVAIQVQNLLQLFDI
PQIAYSATSIDLSDKTLYKYFLRVVPSDTLQARAMLDIVKRYNWTYVSAVHTEGNYGESG
MDAFKELAAQEGLCIAHSDKIYSNAGEKSFDRLLRKLRERLPKARVVVCFCEGMTVRGLL
SAMRRLGVVGEFSLIGSDGWADRDEVIEGYEVEANGGITIKLQSPEVRSFDDYFLKLRLD
TNTRNPWFPEFWQHRFQCRLPGHLLENPNFKRICTGNESLEENYVQDSKMGFVINAIYAM
AHGLQNMHHALCPGHVGLCDAMKPIDGSKLLDFLIKSSFIGVSGEEVWFDEKGDAPGRYD
IMNLQYTEANRYDYVHVGTWHEGVLNIDDYKIQMNKSGVVRSVCSEPCLKGQIKVIRKGE
VSCCWICTACKENEYVQDEFTCKACDLGWWPNADLTGCEPIPVRYLEWSNIESIIAIAFS
CLGILVTLFVTLIFVLYRDTPVVKSSSRELCYIILAGIFLGYVCPFTLIAKPTTTSCYLQ
RLLVGLSSAMCYSALVTKTNRIARILAGSKKKICTRKPRFMSAWAQVIIASILISVQLTL
VVTLIIMEPPMPILSYPSIKEVYLICNTSNLGVVAPLGYNGLLIMSCTYYAFKTRNVPAN
FNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITTCFAVSLSVTVALGCMFTPKMYIIIA
KPERNVRSAFTTSDVVRMHVGDGKLPCRSNTFLNIFRRKKAGAGNANSNGKSVSWSEPGG
GQVPKGQHMWHRLSVHVKTNETACNQTAVIKPLTKSYQGSGKSLTFSDTSTKTLYNVEEE
EDAQPIRFSPPGSPSMVVHRRVPSAATTPPLPPHLTAEETPLFLAEPALPKGLPPPLQQQ
QQPPPQQKSLMDQLQGVVSNFSTAIPDFHAVLAGPGGPGNGLRSLYPPPPPPQHLQMLPL
QLSTFGEELVSPPADDDDDSERFKLLQEYVYEHEREGNTEEDELEEEEEDLQAASKLTPD
DSPALTPPSPFRDSVASGSSVPSSPVSESVLCTPPNVSYASVILRDYKQSSSTL
Enzyme 37 Number of Residues 1194
Enzyme 37 Molecular Weight 132365.9
Enzyme 37 Theoretical pI 6.67
Enzyme 37 GO Classification
Function
  • G-protein coupled receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 37 General Function Involved in G-protein coupled receptor activity
Enzyme 37 Specific Function Receptor for glutamate. The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol- calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • 1-18
Enzyme 37 Transmembrane Regions
  • 593-615 630-650 662-680 707-727 751-772 786-808 815-840
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 56203019 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q13255 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name GRM1_HUMAN Link Image
Enzyme 37 PDB ID 1ISS Link Image
Enzyme 37 PDB File Show
Enzyme 37 3D Structure
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >3585 bp
ATGGTCGGGCTCCTTTTGTTTTTTTTCCCAGCGATCTTTTTGGAGGTGTCCCTTCTCCCC
AGAAGCCCCGGCAGGAAAGTGTTGCTGGCAGGAGCGTCGTCTCAGCGCTCGGTGGCCAGA
ATGGACGGAGATGTCATCATTGGAGCCCTCTTCTCAGTCCATCACCAGCCTCCGGCCGAG
AAAGTGCCCGAGAGGAAGTGTGGGGAGATCAGGGAGCAGTATGGCATCCAGAGGGTGGAG
GCCATGTTCCACACGTTGGATAAGATCAACGCGGACCCGGTCCTCCTGCCCAACATCACC
CTGGGCAGTGAGATCCGGGACTCCTGCTGGCACTCTTCCGTGGCTCTGGAACAGAGCATT
GAGTTCATTAGGGACTCTCTGATTTCCATTCGAGATGAGAAGGATGGGATCAACCGGTGT
CTGCCTGACGGCCAGTCCCTCCCCCCAGGCAGGACTAAGAAGCCCATTGCGGGAGTGATC
GGTCCCGGCTCCAGCTCTGTAGCCATTCAAGTGCAGAACCTGCTCCAGCTCTTCGACATC
CCCCAGATCGCTTATTCAGCCACAAGCATCGACCTGAGTGACAAAACTTTGTACAAATAC
TTCCTGAGGGTTGTCCCTTCTGACACTTTGCAGGCAAGGGCCATGCTTGACATAGTCAAA
CGTTACAATTGGACCTATGTCTCTGCAGTCCACACGGAAGGGAATTATGGGGAGAGCGGA
ATGGACGCTTTCAAAGAGCTGGCTGCCCAGGAAGGCCTCTGTATCGCCCATTCTGACAAA
ATCTACAGCAACGCTGGGGAGAAGAGCTTTGACCGACTCTTGCGCAAACTCCGAGAGAGG
CTTCCCAAGGCTAGAGTGGTGGTCTGCTTCTGTGAAGGCATGACAGTGCGAGGACTCCTG
AGCGCCATGCGGCGCCTTGGCGTCGTGGGCGAGTTCTCACTCATTGGAAGTGATGGATGG
GCAGACAGAGATGAAGTCATTGAAGGTTATGAGGTGGAAGCCAACGGGGGAATCACGATA
AAGCTGCAGTCTCCAGAGGTCAGGTCATTTGATGATTATTTCCTGAAACTGAGGCTGGAC
ACTAACACGAGGAATCCCTGGTTCCCTGAGTTCTGGCAACATCGGTTCCAGTGCCGCCTT
CCAGGACACCTTCTGGAAAATCCCAACTTTAAACGAATCTGCACAGGCAATGAAAGCTTA
GAAGAAAACTATGTCCAGGACAGTAAGATGGGGTTTGTCATCAATGCCATCTATGCCATG
GCACATGGGCTGCAGAACATGCACCATGCCCTCTGCCCTGGCCACGTGGGCCTCTGCGAT
GCCATGAAGCCCATCGACGGCAGCAAGCTGCTGGACTTCCTCATCAAGTCCTCATTCATT
GGAGTATCTGGAGAGGAGGTGTGGTTTGATGAGAAAGGAGACGCTCCTGGAAGGTATGAT
ATCATGAATCTGCAGTACACTGAAGCTAATCGCTATGACTATGTGCACGTTGGAACCTGG
CATGAAGGAGTGCTGAACATTGATGATTACAAAATCCAGATGAACAAGAGTGGAGTGGTG
CGGTCTGTGTGCAGTGAGCCTTGCTTAAAGGGCCAGATTAAGGTTATACGGAAAGGAGAA
GTGAGCTGCTGCTGGATTTGCACGGCCTGCAAAGAGAATGAATATGTGCAAGATGAGTTC
ACCTGCAAAGCTTGTGACTTGGGATGGTGGCCCAATGCAGATCTAACAGGCTGTGAGCCC
ATTCCTGTGCGCTATCTTGAGTGGAGCAACATCGAATCCATTATAGCCATCGCCTTTTCA
TGCCTGGGAATCCTTGTTACCTTGTTTGTCACCCTAATCTTTGTACTGTACCGGGACACA
CCAGTGGTCAAATCCTCCAGTCGGGAGCTCTGCTACATCATCCTAGCTGGCATCTTCCTT
GGTTATGTGTGCCCATTCACTCTCATTGCCAAACCTACTACCACCTCCTGCTACCTCCAG
CGCCTCTTGGTTGGCCTCTCCTCTGCGATGTGCTACTCTGCTTTAGTGACTAAAACCAAT
CGTATTGCACGCATCCTGGCTGGCAGCAAGAAGAAGATCTGCACCCGGAAGCCCAGGTTC
ATGAGTGCCTGGGCTCAGGTGATCATTGCCTCAATTCTGATTAGTGTGCAACTAACCCTG
GTGGTAACCCTGATCATCATGGAACCCCCTATGCCCATTCTGTCCTACCCAAGTATCAAG
GAAGTCTACCTTATCTGCAATACCAGCAACCTGGGTGTGGTGGCCCCTTTGGGCTACAAT
GGACTCCTCATCATGAGCTGTACCTACTATGCCTTCAAGACCCGCAACGTGCCCGCCAAC
TTCAACGAGGCCAAATATATCGCGTTCACCATGTACACCACCTGTATCATCTGGCTAGCT
TTTGTGCCCATTTACTTTGGGAGCAACTACAAGATCATCACAACTTGCTTTGCAGTGAGT
CTCAGTGTAACAGTGGCTCTGGGGTGCATGTTCACTCCCAAGATGTACATCATTATTGCC
AAGCCTGAGAGGAATGTCCGCAGTGCCTTCACCACCTCTGATGTTGTCCGCATGCATGTT
GGCGATGGCAAGCTGCCCTGCCGCTCCAACACTTTCCTCAACATCTTCCGAAGAAAGAAG
GCAGGGGCAGGGAATGCCAATTCTAATGGCAAGTCTGTGTCATGGTCTGAACCAGGTGGA
GGACAGGTGCCCAAGGGACAGCATATGTGGCACCGCCTCTCTGTGCACGTGAAGACCAAT
GAGACGGCCTGCAACCAAACAGCCGTCATCAAGCCCCTCACTAAAAGTTACCAAGGCTCT
GGCAAGAGCCTGACCTTTTCAGATACCAGCACCAAGACCCTTTACAACGTAGAGGAGGAG
GAGGATGCCCAGCCGATTCGCTTTAGCCCGCCTGGTAGCCCTTCCATGGTGGTGCACAGG
CGCGTGCCAAGCGCGGCGACCACTCCGCCTCTGCCGTCCCACCTGACCGCAGAGGAGACC
CCCCTCTTCCTGGCCGAACCAGCCCTCCCCAAGGGCTTGCCCCCTCCTCTCCAGCAGCAG
CAGCAACCCCCTCCACAGCAGAAATCGCTGATGGACCAGCTCCAGGGAGTGGTCAGCAAC
TTCAGTACCGCGATCCCGGATTTTCACGCGGTGCTGGCAGGCCCCGGTGGTCCCGGGAAC
GGGCTGCGGTCCCTGTACCCGCCCCCGCCACCTCCGCAGCACCTGCAGATGCTGCCGCTG
CAGCTGAGCACCTTTGGGGAGGAGCTGGTCTCCCCGCCCGCGGACGACGACGACGACAGC
GAGAGGTTTAAGCTCCTCCAGGAGTACGTGTATGAGCACGAGCGGGAAGGGAACACGGAA
GAAGACGAACTGGAAGAGGAGGAGGAGGACCTGCAGGCGGCCAGCAAACTGACCCCGGAT
GATTCGCCTGCGCTGACGCCTCCGTCGCCTTTCCGCGACTCGGTGGCCTCGGGCAGCTCG
GTGCCCAGCTCCCCCGTGTCCGAGTCGGTGCTCTGCACCCCTCCCAACGTATCCTACGCC
TCTGTCATTCTGCGGGACTACAAGCAAAGCTCTTCCACCCTGTAA
Enzyme 37 GenBank Gene ID AL035698 Link Image
Enzyme 37 GeneCard ID GRM1 Link Image
Enzyme 37 GenAtlas ID GRM1 Link Image
Enzyme 37 HGNC ID HGNC:4593 Link Image
Enzyme 37 Chromosome Location 6
Enzyme 37 Locus 6q24
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Desai MA, Burnett JP, Mayne NG, Schoepp DD: Cloning and expression of a human metabotropic glutamate receptor 1 alpha: enhanced coupling on co-transfection with a glutamate transporter. Mol Pharmacol. 1995 Oct;48(4):648-57. [PubMed Link Image]
  2. Stephan D, Bon C, Holzwarth JA, Galvan M, Pruss RM: Human metabotropic glutamate receptor 1: mRNA distribution, chromosome localization and functional expression of two splice variants. Neuropharmacology. 1996;35(12):1649-60. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  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. Ray K, Hauschild BC: Cys-140 is critical for metabotropic glutamate receptor-1 dimerization. J Biol Chem. 2000 Nov 3;275(44):34245-51. [PubMed Link Image]
  6. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [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. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 7724
Enzyme 38 Name Arginine decarboxylase
Enzyme 38 Synonyms
  1. ADC
  2. ARGDC
  3. ODC-paralogue
  4. ODC-p
  5. Ornithine decarboxylase-like protein
Enzyme 38 Gene Name ADC
Enzyme 38 Protein Sequence >Arginine decarboxylase
MAGYLSESDFVMVEEGFSTRDLLKELTLGASQATTDEVAAFFVADLGAIVRKHFCFLKCL
PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQ
IKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRH
LLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFP
GTEGAKVRFEEIASVINSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLD
QPGREEENGSTSKTIVYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWGPA
VDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWGTQACHITYAMSRVAWEALRR
QLMAAEQEDDVEGVCKPLSCGWEITDTLCVGPVFTPASIM
Enzyme 38 Number of Residues 460
Enzyme 38 Molecular Weight 49979.2
Enzyme 38 Theoretical pI 5.41
Enzyme 38 GO Classification
Function
  • catalytic activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • polyamine biosynthetic process
  • polyamine metabolic process
Component
Enzyme 38 General Function Involved in catalytic activity
Enzyme 38 Specific Function Decarboxylates L-arginine to agmatine. Truncated splice isoforms probably lack activity
Enzyme 38 Pathways
Enzyme 38 Reactions
  • L-arginine = agmatine + CO2 [RN:R00566]
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein Not Available
Enzyme 38 UniProtKB/Swiss-Prot ID Q96A70 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name ADC_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >1383 bp
ATGGCTGGCTACCTGAGTGAATCGGACTTTGTGATGGTGGAGGAGGGCTTCAGTACCCGA
GACCTGCTGAAGGAACTCACTCTGGGGGCCTCACAGGCCACCACGGACGAGGTAGCTGCC
TTCTTCGTGGCTGACCTGGGTGCCATAGTGAGGAAGCACTTTTGCTTTCTGAAGTGCCTG
CCACGAGTCCGGCCCTTTTATGCTGTCAAGTGCAACAGCAGCCCAGGTGTGCTGAAGGTT
CTGGCCCAGCTGGGGCTGGGCTTTAGCTGTGCCAACAAGGCAGAGATGGAGTTGGTCCAG
CATATTGGAATCCCTGCCAGTAAGATCATCTGCGCCAACCCCTGTAAGCAAATTGCACAG
ATCAAATATGCTGCCAAGCATGGGATCCAGCTGCTGAGCTTTGACAATGAGATGGAGCTG
GCAAAGGTGGTAAAGAGCCACCCCAGTGCCAAGATGGTTCTGTGCATTGCTACCGATGAC
TCCCACTCCCTGAGCTGCCTGAGCCTAAAGTTTGGAGTGTCACTGAAATCCTGCAGACAC
CTGCTTGAAAATGCGAAGAAGCACCATGTGGAGGTGGTGGGTGTGAGTTTTCACATTGGC
AGTGGCTGTCCTGACCCTCAGGCCTATGCTCAGTCCATCGCAGACGCCCGGCTCGTGTTT
GAAATGGGCACCGAGCTGGGTCACAAGATGCACGTTCTGGACCTTGGTGGTGGCTTCCCT
GGCACAGAAGGGGCCAAAGTGAGATTTGAAGAGATTGCTTCCGTGATCAACTCAGCCTTG
GACCTGTACTTCCCAGAGGGCTGTGGCGTGGACATCTTTGCTGAGCTGGGGCGCTACTAC
GTGACCTCGGCCTTCACTGTGGCAGTCAGCATCATTGCCAAGAAGGAGGTTCTGCTAGAC
CAGCCTGGCAGGGAGGAGGAAAATGGTTCCACCTCCAAGACCATCGTGTACCACCTTGAT
GAGGGCGTGTATGGGATCTTCAACTCAGTCCTGTTTGACAACATCTGCCCTACCCCCATC
CTGCAGAAGAAACCATCCACGGAGCAGCCCCTGTACAGCAGCAGCCTGTGGGGCCCGGCG
GTTGATGGCTGTGATTGCGTGGCTGAGGGCCTGTGGCTGCCGCAACTACACGTAGGGGAC
TGGCTGGTCTTTGACAACATGGGCGCCTACACTGTGGGCATGGGTTCCCCCTTTTGGGGG
ACCCAGGCCTGCCACATCACCTATGCCATGTCCCGGGTGGCCTGGGAAGCGCTGCGAAGG
CAGCTGATGGCTGCAGAACAGGAGGATGACGTGGAGGGTGTGTGCAAGCCTCTGTCCTGC
GGCTGGGAGATCACAGACACCCTGTGCGTGGGCCCTGTCTTCACCCCAGCGAGCATCATG
TGA
Enzyme 38 GenBank Gene ID AY050634 Link Image
Enzyme 38 GeneCard ID ADC Link Image
Enzyme 38 GenAtlas ID ADC Link Image
Enzyme 38 HGNC ID HGNC:29957 Link Image
Enzyme 38 Chromosome Location 1
Enzyme 38 Locus 1p35.1
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Pitkanen LT, Heiskala M, Andersson LC: Expression of a novel human ornithine decarboxylase-like protein in the central nervous system and testes. Biochem Biophys Res Commun. 2001 Oct 12;287(5):1051-7. [PubMed Link Image]
  2. Zhu MY, Iyo A, Piletz JE, Regunathan S: Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine. Biochim Biophys Acta. 2004 Jan 22;1670(2):156-64. [PubMed Link Image]
  3. Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [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. 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]
  6. 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 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 7918
Enzyme 39 Name Glutaminase 2 (Liver, mitochondrial), isoform CRA_b
Enzyme 39 Synonyms
  1. SubName: L-glutaminase
Enzyme 39 Gene Name GLS2
Enzyme 39 Protein Sequence >Glutaminase 2 (Liver, mitochondrial), isoform CRA_b
MRSMKALQKALSRAGSHCGRGGWGHPSRSPLLGGGVRHHLSEAAAQGRETPHSHQPQHQD
HDSSESGMLSRLGDLLFYTIAEGQERIPIHKFTTALKATGLQTSDPRLRDCMSEMHRVVQ
ESSSGGLLDRDLFRKCVSSNIVLLTQAFRKKFVIPDFEEFTGHVDRIFEDVKELTGGKVA
AYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHK
FVGKEPSGLRYNKLSLNEEGIPHNPMVNAGAIVVSSLIKMDCNKAEKFDFVLQYLNKMAG
NEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMMAALDLYFQLCSVEVTCESG
SVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGA
ILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFHNYDNLRHCARKLDPRREGA
EIRNKTVVNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIE
ACKVNPFAKDRWGNIPLDDAVQFNHLEVVKLLQDYQDSYTLSETQAEAAAEALSKENLES
MV
Enzyme 39 Number of Residues 602
Enzyme 39 Molecular Weight 66322.2
Enzyme 39 Theoretical pI 7.32
Enzyme 39 GO Classification
Function
  • catalytic activity
  • glutaminase 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
  • glutamine family amino acid metabolic process
  • glutamine metabolic process
  • metabolic process
Component
Enzyme 39 General Function Involved in glutaminase activity
Enzyme 39 Specific Function Not Available
Enzyme 39 Pathways
Enzyme 39 Reactions
  • L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 29029569 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q8IX91 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name Q8IX91_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >1809 bp
ATGCGCTCCATGAAGGCTCTGCAGAAGGCCCTGAGCCGGGCTGGCAGTCACTGCGGGCGA
GGAGGCTGGGGTCACCCGAGCCGGAGCCCCCTCCTTGGCGGGGGCGTCCGGCACCACCTC
AGTGAGGCCGCGGCGCAGGGCAGAGAGACGCCACACAGCCACCAGCCGCAGCACCAGGAT
CATGATTCATCAGAAAGTGGCATGCTGTCCCGCCTGGGTGATTTGCTCTTTTACACTATT
GCTGAAGGACAGGAACGAATCCCTATCCACAAGTTCACCACTGCACTAAAGGCCACTGGA
CTGCAGACATCAGATCCTCGGCTCCGAGACTGCATGAGCGAGATGCACCGCGTGGTCCAA
GAGTCCAGTAGTGGTGGCCTCTTGGACCGAGATCTCTTCCGAAAGTGTGTGAGCAGCAAC
ATTGTGCTCCTGACCCAGGCATTCCGAAAGAAGTTTGTCATTCCTGATTTTGAGGAGTTC
ACGGGCCATGTGGATCGCATCTTTGAGGATGTCAAAGAGCTCACTGGAGGCAAAGTGGCA
GCCTACATCCCTCAGCTGGCCAAGTCAAACCCAGACCTGTGGGGTGTCTCCCTGTGCACT
GTGGATGGTCAACGGCACTCTGTGGGCCACACAAAGATCCCCTTCTGCCTGCAGTCCTGT
GTGAAGCCCCTCACCTATGCCATCTCCATAAGCACCCTAGGCACTGACTACGTGCACAAG
TTTGTGGGCAAAGAGCCAAGTGGCCTGCGCTACAACAAGCTCTCCCTCAATGAGGAAGGA
ATCCCCCATAACCCCATGGTCAATGCTGGTGCCATTGTTGTCAGCTCCCTGATCAAGATG
GACTGTAACAAAGCAGAGAAGTTTGATTTTGTGTTGCAGTATCTCAACAAAATGGCTGGG
AATGAATACATGGGTTTCAGCAATGCCACATTCCAGTCAGAGAAGGAAACAGGGGATCGG
AATTATGCCATCGGCTATTATCTCAAGGAAAAGAAGTGCTTTCCTAAGGGGGTGGACATG
ATGGCTGCCCTTGATCTCTACTTCCAGCTGTGTTCTGTGGAGGTCACTTGTGAATCAGGC
AGTGTCATGGCAGCCACCCTCGCCAACGGTGGGATCTGCCCCATCACAGGCGAGAGTGTG
CTGAGTGCTGAAGCAGTGCGCAACACCCTCAGCCTCATGCATTCCTGCGGCATGTATGAC
TTCTCTGGCCAGTTTGCCTTCCACGTGGGCCTGCCAGCCAAGTCAGCTGTATCAGGAGCC
ATCCTCCTGGTGGTACCCAATGTCATGGGAATGATGTGCCTGTCACCCCCATTGGACAAG
CTGGGGAACAGCCATAGGGGGACCAGCTTCTGCCAGAAGTTGGTGTCTCTCTTCAATTTC
CACAACTATGACAACCTGAGGCACTGTGCTCGGAAGTTAGACCCACGGCGTGAAGGGGCA
GAAATTCGGAACAAGACTGTGGTCAACCTGTTATTTGCTGCCTATAGTGGCGATGTCTCA
GCTCTTCGAAGGTTTGCCTTGTCAGCCATGGATATGGAACAGAAAGACTATGACTCGCGC
ACAGCTCTGCATGTTGCTGCAGCTGAAGGACACATCGAAGTTGTTAAATTCCTGATCGAG
GCTTGCAAAGTGAATCCTTTTGCCAAGGACAGGTGGGGCAACATTCCCCTGGATGATGCT
GTGCAGTTCAACCATCTGGAGGTGGTCAAACTGCTTCAAGATTACCAGGACTCCTACACA
CTCTCTGAAACTCAGGCTGAGGCAGCAGCTGAGGCCCTGTCCAAAGAGAACTTAGAAAGC
ATGGTATGA
Enzyme 39 GenBank Gene ID AF348119 Link Image
Enzyme 39 GeneCard ID GLS2 Link Image
Enzyme 39 GenAtlas ID GLS2 Link Image
Enzyme 39 HGNC ID HGNC:29570 Link Image
Enzyme 39 Chromosome Location 1
Enzyme 39 Locus 12q13
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Perez-Gomez C, Mates JM, Gomez-Fabre PM, del Castillo-Olivares A, Alonso FJ, Marquez J: Genomic organization and transcriptional analysis of the human l-glutaminase gene. Biochem J. 2003 Mar 15;370(Pt 3):771-84. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 7966
Enzyme 40 Name Hypothetical protein GAD1
Enzyme 40 Synonyms Not Available
Enzyme 40 Gene Name GAD1
Enzyme 40 Protein Sequence >Hypothetical protein GAD1
MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEK
SRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEV
VDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGV
RTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWS
SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAA
LGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIA
DICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKE
KGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQI
NKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAP
KIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL
Enzyme 40 Number of Residues 594
Enzyme 40 Molecular Weight 66897
Enzyme 40 Theoretical pI 7.67
Enzyme 40 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
Enzyme 40 General Function Amino acid transport and metabolism
Enzyme 40 Specific Function Not Available
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 62988850 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q53TQ7 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name Q53TQ7_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >1785 bp
ATGGCGTCTTCGACCCCATCTTCGTCCGCAACCTCCTCGAACGCGGGAGCGGACCCCAAT
ACCACTAACCTGCGCCCCACAACGTACGATACCTGGTGCGGCGTGGCCCATGGATGCACC
AGAAAACTGGGGCTCAAGATCTGCGGCTTCTTGCAAAGGACCAACAGCCTGGAAGAGAAG
AGTCGCCTTGTGAGTGCCTTCAAGGAGAGGCAATCCTCCAAGAACCTGCTTTCCTGTGAA
AACAGCGACCGGGATGCCCGCTTCCGGCGCACAGAGACTGACTTCTCTAATCTGTTTGCT
AGAGATCTGCTTCCGGCTAAGAACGGTGAGGAGCAAACCGTGCAATTCCTCCTGGAAGTG
GTGGACATACTCCTCAACTATGTCCGCAAGACATTTGATCGCTCCACCAAGGTGCTGGAC
TTTCATCACCCACACCAGTTGCTGGAAGGCATGGAGGGCTTCAACTTGGAGCTCTCTGAC
CACCCCGAGTCCCTGGAGCAGATCCTGGTTGACTGCAGAGACACCTTGAAGTATGGGGTT
CGCACAGGTCATCCTCGATTTTTCAACCAGCTCTCCACTGGATTGGATATTATTGGCCTA
GCTGGAGAATGGCTGACATCAACGGCCAATACCAACATGTTTACATATGAAATTGCACCA
GTGTTTGTCCTCATGGAACAAATAACACTTAAGAAGATGAGAGAGATAGTTGGATGGTCA
AGTAAAGATGGTGATGGGATATTTTCTCCTGGGGGCGCCATATCCAACATGTACAGCATC
ATGGCTGCTCGCTACAAGTACTTCCCGGAAGTTAAGACAAAGGGCATGGCGGCTGTGCCT
AAACTGGTCCTCTTCACCTCAGAACAGAGTCACTATTCCATAAAGAAAGCTGGGGCTGCA
CTTGGCTTTGGAACTGACAATGTGATTTTGATAAAGTGCAATGAAAGGGGGAAAATAATT
CCAGCTGATTTTGAGGCAAAAATTCTTGAAGCCAAACAGAAGGGATATGTTCCCTTTTAT
GTCAATGCAACTGCTGGCACGACTGTTTATGGAGCTTTTGATCCGATACAAGAGATTGCA
GATATATGTGAGAAATATAACCTTTGGTTGCATGTCGATGCTGCCTGGGGAGGTGGGCTG
CTCATGTCCAGGAAGCACCGCCATAAACTCAACGGCATAGAAAGGGCCAACTCAGTCACC
TGGAACCCTCACAAGATGATGGGCGTGCTGTTGCAGTGCTCTGCCATTCTCGTCAAGGAA
AAGGGTATACTCCAAGGATGCAACCAGATGTGTGCAGGATACCTCTTCCAGCCAGACAAG
CAGTATGATGTCTCCTACGACACCGGGGACAAGGCAATTCAGTGTGGCCGCCACGTGGAT
ATCTTCAAGTTCTGGCTGATGTGGAAAGCAAAGGGCACAGTGGGATTTGAAAACCAGATC
AACAAATGCCTGGAACTGGCTGAATACCTCTATGCCAAGATTAAAAACAGAGAAGAATTT
GAGATGGTTTTCAATGGCGAGCCTGAGCACACAAACGTCTGTTTTTGGTATATTCCACAA
AGCCTCAGGGGTGTGCCAGACAGCCCTCAACGACGGGAAAAGCTACACAAGGTGGCTCCA
AAAATCAAAGCCCTGATGATGGAGTCAGGTACGACCATGGTTGGCTACCAGCCCCAAGGG
GACAAGGCCAACTTCTTCCGGATGGTCATCTCCAACCCAGCCGCTACCCAGTCTGACATT
GACTTCCTCATTGAGGAGATAGAAAGACTGGGCCAGGATCTGTAA
Enzyme 40 GenBank Gene ID AC007405 Link Image
Enzyme 40 GeneCard ID GAD1 Link Image
Enzyme 40 GenAtlas ID GAD1 Link Image
Enzyme 40 HGNC ID HGNC:4092 Link Image
Enzyme 40 Chromosome Location 2
Enzyme 40 Locus 2q31
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References Not Available
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 8585
Enzyme 41 Name Aminoadipate aminotransferase, isoform CRA_b
Enzyme 41 Synonyms
  1. SubName: Putative uncharacterized protein AADAT
  2. SubName: cDNA, FLJ95590, Homo sapiens L-kynurenine/alpha-aminoadipate aminotransferase (KATII), mRNA
Enzyme 41 Gene Name AADAT
Enzyme 41 Protein Sequence >Aminoadipate aminotransferase, isoform CRA_b
MNYARFITAASAARNPSPIRTMTDILSRGPKSMISLAGGLPNPNMFPFKTAVITVENGKT
IQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCVTSGSQQG
LCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDESGIVPDSLRDILSRWKP
EDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERKKEIYELARKYDFLIIEDDPYYFLQFNK
FRVPTFLSMDVDGRVIRADSFSKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQ
LMISQLLHEWGEEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKV
KGINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVAFQVLAQL
IKESL
Enzyme 41 Number of Residues 425
Enzyme 41 Molecular Weight 47351.2
Enzyme 41 Theoretical pI 6.96
Enzyme 41 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthetic process
  • metabolic process
Component
Enzyme 41 General Function Transcription
Enzyme 41 Specific Function Not Available
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions Not Available
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 63995206 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID Q4W5N8 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name Q4W5N8_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >1278 bp
ATGAATTACGCACGGTTCATCACGGCAGCGAGCGCAGCCAGAAACCCTTCTCCCATCCGG
ACCATGACTGACATATTGAGCAGAGGACCAAAATCGATGATCTCCTTGGCTGGTGGCTTA
CCAAATCCAAACATGTTTCCTTTTAAGACTGCCGTAATCACTGTAGAAAATGGAAAGACC
ATCCAATTTGGAGAAGAGATGATGAAGAGAGCACTTCAGTATTCTCCGAGTGCTGGAATT
CCAGAGCTTTTGTCCTGGCTAAAACAGTTACAAATAAAATTGCATAATCCTCCTACCATC
CATTACCCACCCAGTCAAGGACAAATGGATCTATGTGTCACATCTGGCAGCCAACAAGGT
CTTTGTAAGGTGTTTGAAATGATCATTAATCCTGGAGATAATGTCCTCCTAGATGAACCT
GCTTATTCAGGAACTCTTCAAAGTCTGCACCCACTGGGCTGCAACATTATTAATGTTGCC
AGTGATGAAAGTGGGATTGTTCCAGATTCCCTAAGAGACATACTTTCCAGATGGAAACCA
GAAGATGCAAAGAATCCCCAGAAAAACACCCCCAAATTTCTTTATACTGTTCCAAATGGC
AACAACCCTACTGGAAACTCATTAACCAGTGAACGCAAAAAGGAAATCTATGAGCTTGCA
AGAAAATATGATTTCCTCATAATAGAAGATGATCCTTACTATTTTCTCCAGTTTAACAAG
TTCAGGGTACCAACATTTCTTTCCATGGATGTTGATGGACGTGTCATCAGAGCTGACTCT
TTTTCAAAAATCATTTCCTCTGGGTTGAGAATAGGATTTTTAACTGGTCCAAAACCCTTA
ATAGAGAGAGTTATTTTACACATACAAGTTTCAACATTGCACCCCAGCACTTTTAACCAG
CTCATGATATCACAGCTTCTACACGAATGGGGAGAAGAAGGTTTCATGGCTCATGTAGAC
AGGGTTATTGATTTCTATAGTAACCAGAAGGATGCAATACTGGCAGCTGCAGACAAGTGG
TTAACTGGTTTGGCAGAATGGCATGTTCCTGCTGCTGGAATGTTTTTATGGATTAAAGTT
AAAGGCATTAATGATGTAAAAGAACTGATTGAAGAAAAGGCCGTTAAGATGGGGGTATTA
ATGCTCCCTGGAAATGCTTTCTACGTCGATAGCTCAGCTCCTAGCCCTTACTTGAGAGCA
TCCTTCTCTTCAGCTTCTCCAGAACAGATGGATGTGGCCTTCCAGGTATTAGCACAACTT
ATAAAAGAATCTTTATGA
Enzyme 41 GenBank Gene ID AC084866 Link Image
Enzyme 41 GeneCard ID AADAT Link Image
Enzyme 41 GenAtlas ID Not Available
Enzyme 41 HGNC ID Not Available
Enzyme 41 Chromosome Location 4
Enzyme 41 Locus 4q33
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 8631
Enzyme 42 Name Excitatory amino acid transporter 3
Enzyme 42 Synonyms
  1. Excitatory amino-acid carrier 1
  2. Neuronal and epithelial glutamate transporter
  3. Sodium-dependent glutamate/aspartate transporter 3
  4. Solute carrier family 1 member 1
Enzyme 42 Gene Name SLC1A1
Enzyme 42 Protein Sequence >Excitatory amino acid transporter 3
MGKPARKGCEWKRFLKNNWVLLSTVAAVVLGITTGVLVREHSNLSTLEKFYFAFPGEILM
RMLKLIILPLIISSMITGVAALDSNVSGKIGLRAVVYYFCTTLIAVILGIVLVVSIKPGV
TQKVGEIARTGSTPEVSTVDAMLDLIRNMFPENLVQACFQQYKTKREEVKPPSDPEMNMT
EESFTAVMTTAISKNKTKEYKIVGMYSDGINVLGLIVFCLVFGLVIGKMGEKGQILVDFF
NALSDATMKIVQIIMCYMPLGILFLIAGKIIEVEDWEIFRKLGLYMATVLTGLAIHSIVI
LPLIYFIVVRKNPFRFAMGMAQALLTALMISSSSATLPVTFRCAEENNQVDKRITRFVLP
VGATINMDGTALYEAVAAVFIAQLNDLDLGIGQIITISITATSASIGAAGVPQAGLVTMV
IVLSAVGLPAEDVTLIIAVDWLLDRFRTMVNVLGDAFGTGIVEKLSKKELEQMDVSSEVN
IVNPFALESTILDNEDSDTKKSYVNGGFAVDKSDTISFTQTSQF
Enzyme 42 Number of Residues 524
Enzyme 42 Molecular Weight 57099.8
Enzyme 42 Theoretical pI 5.36
Enzyme 42 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 42 General Function Involved in sodium:dicarboxylate symporter activity
Enzyme 42 Specific Function Transports L-glutamate and also L- and D-aspartate. Essential for terminating the postsynaptic action of glutamate by rapidly removing released glutamate from the synaptic cleft. Acts as a symport by cotransporting sodium. Negatively regulated by ARL6IP5
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions Not Available
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • 19-38 62-82 94-114 210-229 254-273 290-309 316-335 362-381 392-411 420-439
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 18157236 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID P43005 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name EAA3_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >1575 bp
ATGGGGAAACCGGCGAGGAAAGGATGCGAGTGGAAGCGCTTCCTGAAGAATAACTGGGTG
TTGCTGTCCACCGTGGCCGCGGTGGTGCTAGGCATTACCACAGGAGTCTTGGTTCGAGAA
CACAGCAACCTCTCAACTCTAGAGAAATTCTACTTTGCTTTTCCTGGAGAAATTCTAATG
CGGATGCTGAAACTCATCATTTTGCCATTAATTATATCCAGCATGATTACAGGTGTTGCT
GCACTGGATTCCAACGTATCCGGAAAAATTGGTCTGCGCGCTGTCGTGTATTATTTCTGT
ACCACTCTCATTGCTGTTATTCTAGGTATTGTGCTGGTGGTGAGCATCAAGCCTGGTGTC
ACCCAGAAAGTGGGTGAAATTGCGAGGACAGGCAGCACCCCTGAAGTCAGTACAGTGGAT
GCCATGTTAGATCTCATCAGGAATATGTTCCCTGAGAATCTTGTCCAGGCCTGTTTTCAG
CAGTACAAAACTAAGCGTGAAGAAGTGAAGCCTCCCAGCGATCCAGAGATGAACATGACA
GAAGAGTCCTTCACAGCTGTCATGACAACTGCAATTTCCAAGAACAAAACAAAGGAATAC
AAAATTGTTGGCATGTATTCAGATGGCATAAACGTCCTGGGCTTGATTGTCTTTTGCCTT
GTCTTTGGACTTGTCATTGGAAAAATGGGAGAAAAGGGACAAATTCTGGTGGATTTCTTC
AATGCTTTGAGTGATGCAACCATGAAAATCGTTCAGATCATCATGTGTTATATGCCACTA
GGTATTTTGTTCCTGATTGCTGGGAAGATCATAGAAGTTGAAGACTGGGAAATATTCCGC
AAGCTGGGCCTTTACATGGCCACAGTCCTGACTGGGCTTGCAATCCACTCCATTGTAATT
CTCCCGCTGATATATTTCATAGTCGTACGAAAGAACCCTTTCCGATTTGCCATGGGAATG
GCCCAGGCTCTCCTGACAGCTCTCATGATCTCTTCCAGTTCAGCAACACTGCCTGTCACC
TTCCGCTGTGCTGAAGAAAATAACCAGGTGGACAAGAGGATCACTCGATTCGTGTTACCC
GTTGGTGCAACAATCAACATGGATGGGACTGCGCTCTATGAAGCAGTGGCAGCGGTGTTT
ATTGCACAGTTGAATGACCTGGACTTGGGCATTGGGCAGATCATCACCATCAGTATCACG
GCCACATCTGCCAGCATCGGAGCTGCTGGCGTGCCCCAGGCTGGCCTGGTGACCATGGTG
ATTGTGCTGAGTGCCGTGGGCCTGCCCGCCGAGGATGTCACCCTGATCATTGCTGTCGAC
TGGCTCCTGGACCGGTTCAGGACCATGGTCAACGTCCTTGGTGATGCTTTTGGGACGGGC
ATTGTGGAAAAGCTCTCCAAGAAGGAGCTGGAGCAGATGGATGTTTCATCTGAAGTCAAC
ATTGTGAATCCCTTTGCCTTGGAATCCACAATCCTTGACAACGAAGACTCAGACACCAAG
AAGTCTTATGTCAATGGAGGCTTTGCAGTAGACAAGTCTGACACCATCTCATTCACCCAG
ACCTCACAGTTCTAG
Enzyme 42 GenBank Gene ID AB008536 Link Image
Enzyme 42 GeneCard ID SLC1A1 Link Image
Enzyme 42 GenAtlas ID SLC1A1 Link Image
Enzyme 42 HGNC ID HGNC:10939 Link Image
Enzyme 42 Chromosome Location 9
Enzyme 42 Locus 9p24
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Shashidharan P, Huntley GW, Meyer T, Morrison JH, Plaitakis A: Neuron-specific human glutamate transporter: molecular cloning, characterization and expression in human brain. Brain Res. 1994 Oct 31;662(1-2):245-50. [PubMed Link Image]
  2. Kanai Y, Stelzner M, Nussberger S, Khawaja S, Hebert SC, Smith CP, Hediger MA: The neuronal and epithelial human high affinity glutamate transporter. Insights into structure and mechanism of transport. J Biol Chem. 1994 Aug 12;269(32):20599-606. [PubMed Link Image]
  3. Arriza JL, Fairman WA, Wadiche JI, Murdoch GH, Kavanaugh MP, Amara SG: Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex. J Neurosci. 1994 Sep;14(9):5559-69. [PubMed Link Image]
  4. Veenstra-VanderWeele J, Kim SJ, Gonen D, Hanna GL, Leventhal BL, Cook EH Jr: Genomic organization of the SLC1A1/EAAC1 gene and mutation screening in early-onset obsessive-compulsive disorder. Mol Psychiatry. 2001 Mar;6(2):160-7. [PubMed Link Image]
  5. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  6. 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 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 8642
Enzyme 43 Name Mitochondrial glutamate carrier 2
Enzyme 43 Synonyms
  1. GC-2
  2. Glutamate/H(+) symporter 2
  3. Solute carrier family 25 member 18
Enzyme 43 Gene Name SLC25A18
Enzyme 43 Protein Sequence >Mitochondrial glutamate carrier 2
MTHQDLSITAKLINGGVAGLVGVTCVFPIDLAKTRLQNQHGKAMYKGMIDCLMKTARAEG
FFGMYRGAAVNLTLVTPEKAIKLAANDFFRRLLMEDGMQRNLKMEMLAGCGAGMCQVVVT
CPMEMLKIQLQDAGRLAVHHQGSASAPSTSRSYTTGSASTHRRPSATLIAWELLRTQGLA
GLYRGLGATLLRDIPFSIIYFPLFANLNNLGFNELAGKASFAHSFVSGCVAGSIAAVAVT
PLDVLKTRIQTLKKGLGEDMYSGITDCARKLWIQEGPSAFMKGAGCRALVIAPLFGIAQG
VYFIGIGERILKCFD
Enzyme 43 Number of Residues 315
Enzyme 43 Molecular Weight 33848.4
Enzyme 43 Theoretical pI 9.62
Enzyme 43 GO Classification
Function
  • binding
Process
  • establishment of localization
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
  • mitochondrial inner membrane
  • organelle inner membrane
  • organelle membrane
Enzyme 43 General Function Involved in binding
Enzyme 43 Specific Function Involved in the transport of glutamate across the inner mitochondrial membrane. Glutamate is cotransported with H(+)
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • 12-32 61-81 106-126 185-205 225-245 288-308
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 21322707 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID Q9H1K4 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name GHC2_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >948 bp
ATGACCCACCAGGATCTGAGCATCACAGCCAAACTCATCAATGGAGGTGTAGCAGGGCTC
GTGGGGGTGACCTGCGTGTTCCCCATCGACTTGGCCAAGACTCGCCTGCAGAACCAGCAT
GGGAAAGCCATGTACAAAGGAATGATCGACTGCCTGATGAAGACGGCTCGGGCGGAGGGC
TTCTTCGGCATGTACCGAGGGGCTGCAGTGAACCTCACTCTGGTCACTCCAGAGAAGGCC
ATCAAGCTGGCGGCCAACGACTTTTTCCGGCGGCTGCTCATGGAAGATGGGATGCAGCGG
AACCTGAAGATGGAGATGCTTGCCGGGTGTGGGGCTGGGATGTGCCAGGTCGTGGTGACC
TGTCCCATGGAAATGCTCAAGATTCAGCTGCAGGATGCTGGACGCCTGGCCGTCCATCAT
CAGGGCTCGGCCTCAGCACCCTCCACCTCCAGGTCCTACACAACTGGTTCGGCTTCCACC
CACAGGCGCCCCTCTGCCACCCTCATTGCCTGGGAGCTGCTCCGCACTCAGGGCCTGGCT
GGGCTCTACAGGGGCCTGGGTGCCACTCTCCTCAGAGACATTCCTTTCTCCATCATCTAC
TTCCCACTGTTTGCCAACCTTAACAACCTGGGGTTCAACGAGCTCGCCGGTAAGGCGTCC
TTTGCACATTCCTTCGTGTCAGGCTGTGTGGCAGGTTCCATAGCTGCGGTCGCAGTGACG
CCTCTAGATGTTCTGAAAACTCGAATCCAAACCCTCAAGAAAGGCCTGGGCGAGGACATG
TACAGTGGGATCACCGACTGTGCCAGGAAACTCTGGATTCAGGAGGGACCATCTGCCTTC
ATGAAAGGCGCTGGCTGCCGGGCACTGGTCATAGCACCTCTCTTTGGGATTGCTCAAGGG
GTCTATTTTATTGGGATTGGAGAGCGCATCTTAAAGTGTTTTGACTAG
Enzyme 43 GenBank Gene ID AJ428203 Link Image
Enzyme 43 GeneCard ID SLC25A18 Link Image
Enzyme 43 GenAtlas ID SLC25A18 Link Image
Enzyme 43 HGNC ID HGNC:10988 Link Image
Enzyme 43 Chromosome Location 2
Enzyme 43 Locus 22q11.2
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Fiermonte G, Palmieri L, Todisco S, Agrimi G, Palmieri F, Walker JE: Identification of the mitochondrial glutamate transporter. Bacterial expression, reconstitution, functional characterization, and tissue distribution of two human isoforms. J Biol Chem. 2002 May 31;277(22):19289-94. Epub 2002 Mar 15. [PubMed Link Image]
  2. Footz TK, Brinkman-Mills P, Banting GS, Maier SA, Riazi MA, Bridgland L, Hu S, Birren B, Minoshima S, Shimizu N, Pan H, Nguyen T, Fang F, Fu Y, Ray L, Wu H, Shaull S, Phan S, Yao Z, Chen F, Huan A, Hu P, Wang Q, Loh P, Qi S, Roe BA, McDermid HE: Analysis of the cat eye syndrome critical region in humans and the region of conserved synteny in mice: a search for candidate genes at or near the human chromosome 22 pericentromere. Genome Res. 2001 Jun;11(6):1053-70. [PubMed Link Image]
  3. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  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]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 8813
Enzyme 44 Name Glutamine-dependent NAD(+) synthetase
Enzyme 44 Synonyms
  1. NAD(+) synthase [glutamine-hydrolyzing]
  2. NAD(+) synthetase
Enzyme 44 Gene Name NADSYN1
Enzyme 44 Protein Sequence >Glutamine-dependent NAD(+) synthetase
MGRKVTVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYES
DTLLHSFQVLAALVESPVTQDIICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANE
GNYRELRWFTPWSRSRHTEEYFLPRMIQDLTKQETVPFGDAVLVTWDTCIGSEICEELWT
PHSPHIDMGLDGVEIITNASGSHQVLRKANTRVDLVTMVTSKNGGIYLLANQKGCDGDRL
YYDGCAMIAMNGSVFAQGSQFSLDDVEVLTATLDLEDVRSYRAEISSRNLAASRASPYPR
VKVDFALSCHEDLLAPISEPIEWKYHSPEEEISLGPACWLWDFLRRSQQAGFLLPLSGGV
DSAATACLIYSMCCQVCEAVRSGNEEVLADVRTIVNQISYTPQDPRDLCGRILTTCYMAS
KNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFSLVTGKSPLFAAHGGSSRENLA
LQNVQARIRMVLAYLFAQLSLWSRGVHGGLLVLGSANVDESLLGYLTKYDCSSADINPIG
GISKTDLRAFVQFCIQRFQLPALQSILLAPATAELEPLADGQVSQTDEEDMGMTYAELSV
YGKLRKVAKMGPYSMFCKLLGMWRHICTPRQVADKVKRFFSKYSMNRHKMTTLTPAYHAE
NYSPEDNRFDLRPFLYNTSWPWQFRCIENQVLQLERAEPQSLDGVD
Enzyme 44 Number of Residues 706
Enzyme 44 Molecular Weight 79283.9
Enzyme 44 Theoretical pI 6.40
Enzyme 44 GO Classification
Function
  • ATP binding
  • NAD+ synthase (glutamine-hydrolyzing) activity
  • NAD+ synthase (glutamine-hydrolyzing) activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleoside binding
  • purine nucleoside binding
Process
  • NAD biosynthetic process
  • cellular metabolic process
  • coenzyme biosynthetic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • metabolic process
  • nicotinamide nucleotide biosynthetic process
  • nitrogen compound metabolic process
  • pyridine nucleotide biosynthetic process
Component
Enzyme 44 General Function Involved in NAD+ synthase (glutamine-hydrolyzing) activity
Enzyme 44 Specific Function ATP + deamido-NAD(+) + L-glutamine + H(2)O = AMP + diphosphate + NAD(+) + L-glutamate
Enzyme 44 Pathways
Enzyme 44 Reactions
  • ATP + deamido-NAD+ + L-glutamine + H2O = AMP + diphosphate + NAD+ + L-glutamate [RN:R00257]
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 28849201 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID Q6IA69 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name NADE_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >2121 bp
ATGGGCCGGAAGGTGACCGTGGCCACCTGCGCACTCAACCAGTGGGCCCTGGACTTCGAG
GGCAATTTGCAAAGAATTTTAAAGAGTATTGAAATTGCCAAAAACAGAGGAGCAAGATAC
AGGCTTGGACCAGAGCTGGAAATATGCGGCTACGGATGTTGGGATCATTATTACGAGTCG
GACACCCTCTTGCACTCGTTTCAAGTCCTAGCGGCCCTTGTGGAGTCTCCCGTCACTCAG
GACATCATCTGCGACGTGGGGATGCCTGTAATGCACCGAAACGTCCGCTACAACTGCAGA
GTGGTATTCCTCAACAGGAAGATCCTGCTCATCAGACCCAAGATGGCCTTGGCCAATGAA
GGCAACTACCGCGAGCTGCGCTGGTTCACCCCGTGGTCGAGGAGTCGGCACACAGAGGAG
TACTTTCTGCCTCGGATGATACAGGACCTGACAAAGCAGGAAACCGTACCCTTCGGAGAT
GCGGTGCTGGTGACATGGGACACCTGCATTGGAAGTGAGATCTGTGAGGAGCTCTGGACA
CCCCACAGCCCGCACATCGACATGGGCCTGGATGGCGTGGAGATCATCACCAACGCCTCG
GGCAGCCACCACGTGCTGCGCAAAGCCAACACCAGGGTGGATCTCGTGACTATGGTCACC
AGCAAGAACGGTGGGATTTACTTGCTGGCCAACCAGAAGGGTTGCGACGGGGACCGCCTG
TACTACGACGGCTGTGCCATGATCGCCATGAACGGAAGCGTCTTTGCTCAAGGATCCCAG
TTTTCTCTGGATGACGTGGAAGTCCTGACGGCCACGCTGGATCTGGAGGACGTCCGGAGC
TACAGGGCGGAGATTTCATCTCGAAACCTGGCGGCCAGCAGGGCGAGCCCCTACCCCAGA
GTGAAGGTGGACTTTGCCCTCTCGTGCCACGAGGACTTGCTGGCACCCATCTCTGAGCCC
ATCGAGTGGAAATACCACAGCCCTGAGGAGGAGATAAGCCTTGGACCTGCCTGCTGGCTC
TGGGATTTTTTAAGACGAAGTCAACAGGCAGGGTTTTTGCTGCCCTTGAGTGGCGGGGTG
GACAGCGCAGCCACCGCCTGCCTCATCTACTCCATGTGCTGCCAGGTCTGCGAGGCCGTG
AGGAGTGGAAATGAGGAAGTGCTGGCTGATGTCCGCACCATCGTGAACCAGATCAGCTAC
ACCCCCCAGGATCCCCGAGACCTCTGTGGACGCATACTGACCACCTGCTACATGGCCAGC
AAGAACTCCTCCCAGGAGACGTGCACCCGGGCCAGAGAGTTGGCCCAGCAGATTGGAAGC
CACCACATCAGTCTCAACATCGATCCAGCCGTGAAGGCCGTCATGGGCATCTTCAGCCTG
GTGACGGGGAAGAGCCCTCTGTTTGCAGCTCATGGAGGAAGCAGCAGGGAAAACCTGGCG
CTGCAAAATGTGCAGGCTCGAATACGGATGGTCCTCGCCTATCTGTTTGCTCAGTTGAGC
CTCTGGTCTCGGGGTGTCCACGGTGGGCTCCTCGTGCTGGGATCCGCCAACGTGGATGAG
AGTCTCCTGGGCTACCTGACCAAGTACGACTGCTCCAGTGCGGACATCAACCCCATAGGC
GGGATCAGCAAGACGGACCTCAGGGCCTTCGTCCAGTTCTGCATCCAGCGCTTCCAGCTT
CCTGCCCTGCAGAGCATCCTGTTGGCGCCGGCCACCGCAGAGCTGGAGCCCTTGGCTGAT
GGACAGGTGTCCCAGACCGACGAGGAAGATATGGGGATGACATATGCGGAGCTCTCGGTC
TATGGGAAACTCAGGAAGGTGGCCAAGATGGGGCCCTACAGCATGTTCTGCAAACTCCTC
GGCATGCGGAGACACATCTGCACCCCGAGACAGGTCGCTGACAAAGTGAAGCGGTTTTTC
TCCAAGTACTCCATGAACAGACACAAGATGACCACGCTCACACCCGCGTACCACGCCGAG
AACTACAGCCCTGAGGACAACAGGTTTGATCTGCGACCATTTCTGTACAACACAAGCTGG
CCTTGGCAGTTTCGGTGCATAGAAAATCAGGTGCTACAGCTCGAGAGGGCAGAGCCACAG
TCCCTGGACGGCGTGGACTGA
Enzyme 44 GenBank Gene ID AB091316 Link Image
Enzyme 44 GeneCard ID NADSYN1 Link Image
Enzyme 44 GenAtlas ID NADSYN1 Link Image
Enzyme 44 HGNC ID HGNC:29832 Link Image
Enzyme 44 Chromosome Location 1
Enzyme 44 Locus 11q13.4
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References
  1. Hara N, Yamada K, Terashima M, Osago H, Shimoyama M, Tsuchiya M: Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency. J Biol Chem. 2003 Mar 28;278(13):10914-21. Epub 2003 Jan 23. [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. 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]
  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]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 8876
Enzyme 45 Name CAD protein
Enzyme 45 Synonyms
  1. Glutamine-dependent carbamoyl-phosphate synthase
  2. Aspartate carbamoyltransferase
  3. Dihydroorotase
Enzyme 45 Gene Name CAD
Enzyme 45 Protein Sequence >CAD protein
MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNY
GIPPDEMDEFGLCKWFESSGIHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVD
TRELTKKLREQGSLLGKLVQNGTEPSSLPFLDPNARPLVPEVSIKTPRVFNTGGAPRILA
LDCGLKYNQIRCLCQRGAEVTVVPWDHALDSQEYEGLFLSNGPGDPASYPSVVSTLSRVL
SEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVE
TDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEA
TAGNPGGQTVRERLTERLCPPGIPTPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAI
KALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGGQT
ALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQ
AQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHTSQVLVDKSLKGWKEI
EYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRQTAIKVTQHLG
IVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRN
SVTGGTAAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKAL
RMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRM
KRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAV
KQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQ
QLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLP
NNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQT
VGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAV
ASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFN
LQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVG
VKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIG
SYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSI
LEQLAEKNFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEAL
GQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMV
CAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYLN
ETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEE
ILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVRPELGSRQDVEALWENMAVI
DCFASDHAPHTLEEKCGSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIF
HLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVL
VPPGYGQDVRKWPQGAVPQLPPSAPATSEMTTTPERPRRGIPGLPDGRFHLPPRIHRASD
PGLPAEEPKEKSSRKVAEPELMGTPDGTCYPPPPVPRQASPQNLGTPGLLHPQTSPLLHS
LVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSF
AAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRR
PVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVS
LRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEA
CFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLAT
VLGRF
Enzyme 45 Number of Residues 2225
Enzyme 45 Molecular Weight 242981.7
Enzyme 45 Theoretical pI 6.42
Enzyme 45 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • amino acid binding
  • aspartate carbamoyltransferase activity
  • binding
  • carbamoyl-phosphate synthase activity
  • carboxyl- or carbamoyltransferase activity
  • carboxylic acid binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleoside binding
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • 'de novo' pyrimidine base biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • glutamine family amino acid metabolic process
  • glutamine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase metabolic process
  • pyrimidine base biosynthetic process
  • pyrimidine base metabolic process
Component
Enzyme 45 General Function Involved in hydrolase activity
Enzyme 45 Specific Function This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase)
Enzyme 45 Pathways
Enzyme 45 Reactions
  • (1) 2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate [RN:R00575]
  • (2) L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
  • (3) 2 ATP + HCO3- = 2 ADP + phosphate + carbamoyl phosphate [RN:R07641]
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 1228049 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID P27708 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name PYR1_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >6678 bp
ATGGCGGCCCTAGTGTTGGAGGACGGGTCGGTCCTGCGGGGCCAGCCCTTTGGGGCCGCC
GTGTCGACTGCCGGGGAAGTGGTGTTTCAAACCGGCATGGTCGGCTACCCCGAGGCCCTC
ACTGATCCCTCCTACAAGGCACAGATCTTAGTGCTCACCTATCCTCTGATCGGCAACTAT
GGCATCCCCCCAGATGAAATGGATGAGTTCGGTCTCTGCAAGTGGTTTGAATCCTCGGGC
ATCCACGTAGCAGCACTGGTAGTGGGAGAGTGCTGTCCTACTCCCAGCCACTGGAGTGCC
ACCCGCACCCTGCATGAGTGGCTGCAGCAGCATGGCATCCCTGGCTTGCAAGGAGTAGAC
ACTCGGGAGCTGACCAAGAAGTTGCGGGAACAGGGGTCTCTGCTGGGGAAGCTGGTCCAG
AATGGAACAGAACCTTCATCCCTGCCATTCTTGGACCCCAATGCCCGCCCCCTGGTACCA
GAGGTCTCCATTAAGACTCCACGGGTATTCAATACAGGGGGTGCCCCTCGGATCCTTGCT
TTGGACTGTGGCCTCAAGTATAATCAGATCCGATGCCTCTGCCAGCGTGGGGCTGAGGTC
ACTGTGGTACCCTGGGACCATGCACTAGACAGCCAAGAGTATGAGGGTCTCTTCTTAAGT
AATGGGCCTGGTGACCCTGCCTCCTATCCCAGTGTCGTATCCACACTGAGCCGTGTTTTA
TCTGAGCCTAATCCCCGACCTGTCTTTGGGATCTGCCTGGGACACCAGCTATTGGCCTTA
GCCATTGGGGCCAAGACTTACAAGATGAGATATGGGAACCGAGGCCATAACCAGCCCTGC
TTGTTGGTGGGCTCTGGGCGCTGCTTTCTGACATCCCAGAACCATGGGTTTGCTGTGGAG
ACAGACTCACTGCCAGCAGACTGGGCTCCTCTCTTCACCAACGCCAATGATGGTTCCAAT
GAAGGCATTGTGCACAACAGCTTGCCTTTCTTCAGTGTCCAGTTTCACCCAGAGCACCAA
GCTGGCCCTTCAGATATGGAACTGCTTTTCGATATCTTTCTGGAAACTGTGAAAGAGGCC
ACAGCTGGGAACCCTGGGGGCCAGACAGTTAGAGAGCGGCTGACTGAGCGCCTCTGTCCC
CCTGGGATTCCCACTCCCGGCTCTGGACTTCCACCACCACGAAAGGTTCTGATCCTGGGC
TCAGGGGGCCTCTCCATTGGCCAAGCTGGAGAATTTGACTACTCGGGCTCTCAGGCAATT
AAGGCCCTGAAGGAGGAAAACATCCAGACGTTGCTGATCAACCCCAATATTGCCACAGTG
CAGACCTCCCAGGGGCTGGCCGACAAGGTCTATTTTCTTCCCATAACACCTCATTATGTA
ACCCAGGTGATACGTAATGAACGCCCCGATGGTGTGTTACTGACTTTTGGGGGCCAGACT
GCTCTGAACTGTGGTGTGGAGCTGACCAAGGCCGGGGTGCTGGCTCGGTATGGGGTCCGG
GTCCTGGGCACAACAGTGGAGACCATTGAGCTGACCGAGGATCGACGGGCCTTTGCTGCC
AGAATGGCAGAGATCGGAGAGCATGTGGCCCCGAGCGAGGCAGGAAATTCTCTTGAACAG
GCCCAGGCAGCCGCTGAACGGCTGGGGTACCCTGTGCTAGTGCGTGCAGCCTTTGCCGTG
GGTGGCCTGGGCTCTGGCTTTGCCTCTAACAGGGAGGAGCTCTCTGCTCTCGTGGCCCCA
GCTTTTGCCCATACCAGCCAAGTGCTAGTAGACAAGTCTCTGAAGGGATGGAAGGAGATT
GAGTACGAGGTGGTGAGAGACGCCTATGGCAACTGTGTCACGGTGTGTAACATGGAGAAC
TTGGACCCACTGGGCATCCACACTGGTGAGTCCATAGTGGTGGCCCCTAGCCAGACACTG
AATGACAGGGAGTATCAGCTCCTGAGGCAGACAGCTATCAAGGTGACCCAGCACCTGGGA
ATTGTTGGGGAGTGCAATGTGCAGTATGCCTTGAACCCTGAGTCTGAGCAGTATTACATC
ATTGAAGTGAATGCCAGGCTCTCTCGCAGCTCTGCCCTGGCCAGTAAGGCCACAGGTTAT
CCACTGGCTTATGTGGCAGCCAAGCTAGCATTGGGCATCCCTTTGCCTGAGCTCAGGAAC
TCTGTGACAGGGGGTACAGCAGCCTTTGAACCCAGCGTGGATTATTGTGTGGTGAAGATT
CCTCGATGGGACCTTAGCAAGTTCCTGCGAGTCAGCACAAAGATTGGGAGCTGCATGAAG
AGCGTTGGTGAAGTCATGGGCATTGGGCGTTCATTTGAGGAGGCCTTCCAGAAGGCCCTG
CGCATGGTGGATGAGAACTGTGTGGGCTTTGATCACACAGTGAAACCAGTCAGCGATATG
GAGTTGGAGACTCCAACAGATAAGCGGATTTTTGTGGTGGCAGCTGCTTTGTGGGCTGGT
TATTCAGTGGACCGCCTGTATGAGCTCACACGCATCGACCGCTGGTTCCTGCACCGAATG
AAGCGTATCATCGCACATGCCCAGCTGCTAGAACAACACCGTGGACAGCCTTTGCCGCCA
GACCTGCTGCAACAGGCCAAGTGTCTTGGCTTCTCAGACAAACAGATTGCCCTTGCAGTT
CTGAGCACAGAGCTGGCTGTTCGCAAGCTGCGTCAGGAACTGGGGATCTGTCCAGCAGTG
AAACAGATTGACACAGTTGCAGCTGAGTGGCCAGCCCAGACAAATTACCTATACCTAACG
TATTGGGGCACCACCCATGACCTCACCTTTCGAACACCTCATGTCCTAGTCCTTGGCTCT
GGCGTCTACCGTATTGGCTCCAGTGTTGAGTTTGACTGGTGTGCTGTAGGCTGCATCCAG
CAGCTCCGAAAGATGGGATATAAGACCATCATGGTGAACTATAACCCAGAGACAGTCAGC
ACCGACTATGACATGTGTGATCGACTCTACTTTGATGAGATCTCTTTTGAGGTGGTGATG
GACATCTATGAGCTCGAGAACCCTGAAGGTGTGATCCTATCCATGGGTGGACAGCTGCCC
AACAACATGGCCATGGCGTTGCATCGGCAGCAGTGCCGGGTGCTGGGCACCTCCCCTGAA
GCCATTGACTCGGCTGAGAACCGTTTCAAGTTTTCCCGGCTCCTTGACACCATTGGTATC
AGCCAGCCTCAGTGGAGGGAGCTCAGTGACCTCGAGTCTGCTCGCCAATTCTGCCAGACC
GTGGGGTACCCCTGTGTGGTGCGCCCCTCCTATGTGCTGAGCGGTGCTGCTATGAATGTG
GCCTACGCGGATGGAGACCTGGAGCGCTTCCTGAGCAGCGCAGCAGCCGTCTCCAAAGAG
CATCCCGTGGTCATCTCCAAGTTCATCCAGGAGGCTAAGGAGATTGACGTGGATGCCGTG
GCCTCTGATGGTGTGGTGGCAGCCATCGCCATCTCTGAGCATGTGGAGAATGCAGGTGTG
CATTCAGGTGATGCGACGCTGGTGACCCCCCCACAAGATATCACTGCCAAAACCCTGGAG
CGGATCAAAGCCATTGTGCATGCTGTGGGCCAGGAGCTACAGGTCACAGGACCCTTCAAT
CTGCAGCTCATTGCCAAGGATGACCAGCTGAAAGTTATTGAATGCAACGTACGTGTCTCT
CGCTCCTTCCCCTTCGTTTCCAAGACACTGGGTGTGGACCTAGTAGCCTTGGCCACGCGG
GTCATCATGGGGGAAGAAGTGGAACCTGTGGGGCTAATGACTGGTTCTGGAGTCGTGGGA
GTAAAGGTGCCTCAGTTCTCCTTCTCCCGCTTGGCGGGTGCTGACGTGGTGTTGGGTGTG
GAAATGACCAGTACTGGGGAGGTGGCCGGCTTTGGGGAGAGCCGCTGTGAGGCATACCTC
AAGGCCATGCTAAGCACTGGCTTTAAGATCCCCAAGAAGAATATCCTGCTGACCATTGGC
AGCTATAAGAACAAAAGCGAGCTGCTCCCAACTGTGCGGCTACTGGAGAGCCTGGGCTAC
AGCCTCTATGCCAGTCTCGGCACAGCTGACTTCTACACTGAGCATGGCGTCAAGGTAACA
GCTGTGGACTGGCACTTTGAGGAGGCTGTGGATGGTGAGTGCCCACCACAGCGGAGCATC
CTGGAGCAGCTAGCTGAGAAAAACTTTGAGCTGGTGATTAACCTGTCAATGCGTGGAGCT
GGGGGCCGGCGTCTCTCCTCCTTTGTCACCAAGGGCTACCGCACCCGACGCTTGGCCGCT
GACTTCTCCGTGCCCCTAATCATCGATATCAAGTGCACCAAACTCTTTGTGGAGGCCCTA
GGCCAGATCGGGCCAGCCCCTCCTTTGAAGGTGCATGTTGACTGTATGACCTCCCAAAAG
CTTGTGCGACTGCCGGGATTGATTGATGTCCATGTGCACCTGCGGGAACCAGGTGGGACA
CATAAGGAGGACTTTGCTTCAGGCACAGCCGCTGCCCTGGCTGGGGGTATCACCATGGTG
TGTGCCATGCCTAATACCCGGCCCCCCATCATTGACGGCCCTGCTCTGGCCCTGGCCCAG
AAGCTGGCAGAGGCTGGCGCCCGGTGCGACTTTGCGCTATTCCTTGGGGCCTCGTCTGAA
AATGCAGGAACCTTGGGCACCGTGGCCGGGTCTGCAGCCGGGCTGAAGCTTTACCTCAAT
GAGACCTTCTCTGAGCTGCGGCTGGACAGCGTGGTCCAGTGGATGGAGCATTTCGAGACA
TGGCCCTCCCACCTCCCCATTGTGGCTCACGCAGAGCAGCAAACCGTGGCTGCTGTCCTC
ATGGTGGCTCAGCTCACTCAGCGCTCAGTGCACATATGTCACGTGGCACGGAAGGAGGAG
ATCCTGCTAATTAAAGCTGCAAAGGCACGGGGCTTGCCAGTGACCTGCGAGGTGGCTCCC
CACCACCTGTTCCTAAGCCATGATGACCTGGAGCGCCTGGGGCCTGGGAAGGGGGAGGTC
CGGCCTGAGCTTGGCTCCCGCCAGGATGTGGAAGCCCTGTGGGAGGACATGGCTGTCATC
GACTGCTTTGCCTCAGACCATGCTCCCCATACCTTGGAGGAGAAGTGTGGGTCCAGGCCC
CCACCTGGGTTCCCAGGGTTAGAGACCATGCTGCCACTACTCCTGACGGCTGTAAGCGAG
GGCCGGCTCAGCCTGGACGACCTGCTGCAGCGATTGCACCACAATCCTCGGCGCATCTTT
CACCTGCCCCCGCAGGAGGACACCTATGTGGAGGTGGATCTGGAGCATGAGTGGACAATT
CCCAGCCACATGCCCTTCTCCAAGGCCCACTGGACACCTTTTGAAGGGCAGAAAGTGAAG
GGCACCGTCCGCCGTGTGGTCCTGCGAGGGGAGGTTGCCTATATCGATGGGCAGGTTCTG
GTACCCCCGGGCTATGGACAGGATGTACGGAAGTGGCCACAGGGGGCTGTTCCTCAGCTC
CCACCCTCAGCCCCTGCCACTAGTGAGATGACCACGACACCTGAAAGACCCCGCCGTGGC
ATCCCAGGGCTTCCTGATGGCCGCTTCCATCTGCCGCCCCGAATCCATCGAGCCTCCGAC
CCAGGTTTGCCAGCTGAGGAGCCAAAGGAGAAGTCCTCTCGGAAGGTAGCCGAGCCAGAG
CTGATGGGAACCCCTGATGGCACCTGCTACCCTCCACCACCAGTACCGAGACAGGCATCT
CCCCAGAACCTGGGGACCCCTGGCTTGCTGCACCCCCAGACCTCACCCCTGCTGCACTCA
TTAGTGGGCCAACATATCCTGTCCGTCCAGCAGTTCACCAAGGATCAGATGTCTCACCTG
TTCAATGTGGCACACACACTGCGTATGATGGTGCAGAAGGAGCGGAGCCTCGACATCCTG
AAGGGGAAGGTCATGGCCTCCATGTTCTATGAAGTGAGCACACGGACCAGCAGCTCCTTT
GCAGCAGCCATGGCCCGGCTGGGAGGTGCTGTGCTCAGCTTCTCGGAAGCCACATCGTCC
GTCCAGAAGGGCGAATCCCTGGCTGACTCCGTGCAGACCATGAGCTGCTATGCCGACGTC
GTCGTGCTCCGGCACCCCCAGCCTGGAGCAGTGGAGCTGGCCGCCAAGCACTGCCGGAGG
CCAGTGATCAATGCTGGGGATGGGGTCGGAGAGCACCCCACCCAGGCCCTGCTGGACATC
TTCACCATCCGTGAGGAGCTGGGAACTGTCAATGGCATGACGATCACGATGGTGGGTGAC
CTGAAGCACGGACGCACAGTACATTCCCTGGCCTGCCTGCTCACCCAGTATCGTGTCAGC
CTGCGCTACGTGGCACCTCCCAGCCTGCGCATGCCACCCACTGTGCGGGCCTTCGTGGCC
TCCCGCGGCACCAAGCAGGAGGAATTCGAGAGCATTGAGGAGGCGCTGCCTGACACTGAT
GTGCTCTACATGACTCGAATCCAGAAGGAACGATTTGGCTCTACCCAGGAGTACGAAGCT
TGCTTTGGTCAGTTCATCCTCACTCCCCACATCATGACCCGGGCCAAGAAGAAGATGGTG
GTGATGCACCCGATGCCCCGTGTCAACGAGATAAGCGTGGAAGTGGACTCGGATCCCCGC
GCAGCCTACTTCCGCCAGGCTGAGAACGGCATGTACATCCGCATGGCTCTGTTAGCCACC
GTGCTGGGCCGTTTCTAG
Enzyme 45 GenBank Gene ID D78586 Link Image
Enzyme 45 GeneCard ID CAD Link Image
Enzyme 45 GenAtlas ID CAD Link Image
Enzyme 45 HGNC ID HGNC:1424 Link Image
Enzyme 45 Chromosome Location 2
Enzyme 45 Locus 2p22-p21
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Iwahana H, Fujimura M, Ii S, Kondo M, Moritani M, Takahashi Y, Yamaoka T, Yoshimoto K, Itakura M: Molecular cloning of a human cDNA encoding a trifunctional enzyme of carbamoyl-phosphate synthetase-aspartate transcarbamoylase-dihydroorotase in de Novo pyrimidine synthesis. Biochem Biophys Res Commun. 1996 Feb 6;219(1):249-55. [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. Davidson JN, Rao GN, Niswander L, Andreano C, Tamer C, Chen KC: Organization and nucleotide sequence of the 3' end of the human CAD gene. DNA Cell Biol. 1990 Nov;9(9):667-76. [PubMed Link Image]
  4. 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]
  5. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  6. 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]
  7. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  8. 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]
  9. 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]
  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]
  12. 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]
  13. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 9258
Enzyme 46 Name Alanine aminotransferase 2
Enzyme 46 Synonyms
  1. ALT2
  2. Glutamate pyruvate transaminase 2
  3. GPT 2
  4. Glutamic--alanine transaminase 2
  5. Glutamic--pyruvic transaminase 2
Enzyme 46 Gene Name GPT2
Enzyme 46 Protein Sequence >Alanine aminotransferase 2
MQRAAALVRRGCGPRTPSSWGRSQSSAAAEASAVLKVRPERSRRERILTLESMNPQVKAV
EYAVRGPIVLKAGEIELELQRGIKKPFTEVIRANIGDAQAMGQQPITFLRQVMALCTYPN
LLDSPSFPEDAKKRARRILQACGGNSLGSYSASQGVNCIREDVAAYITRRDGGVPADPDN
IYLTTGASDGISTILKILVSGGGKSRTGVMIPIPQYPLYSAVISELDAIQVNYYLDEENC
WALNVNELRRAVQEAKDHCDPKVLCIINPGNPTGQVQSRKCIEDVIHFAWEEKLFLLADE
VYQDNVYSPDCRFHSFKKVLYEMGPEYSSNVELASFHSTSKGYMGECGYRGGYMEVINLH
PEIKGQLVKLLSVRLCPPVSGQAAMDIVVNPPVAGEESFEQFSREKESVLGNLAKKAKLT
EDLFNQVPGIHCNPLQGAMYAFPRIFIPAKAVEAAQAHQMAPDMFYCMKLLEETGICVVP
GSGFGQREGTYHFRMTILPPVEKLKTVLQKVKDFHINFLEKYA
Enzyme 46 Number of Residues 523
Enzyme 46 Molecular Weight 57903.1
Enzyme 46 Theoretical pI 7.77
Enzyme 46 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthetic process
  • metabolic process
Component
Enzyme 46 General Function Involved in transferase activity, transferring nitrogenous groups
Enzyme 46 Specific Function Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate
Enzyme 46 Pathways
Enzyme 46 Reactions
  • L-alanine + 2-oxoglutarate = pyruvate + L-glutamate [RN:R00258]
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 19046894 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID Q8TD30 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name ALAT2_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >1572 bp
ATGCAGCGGGCGGCGGCGCTGGTCCGGCGGGGCTGTGGTCCCCGGACCCCCAGCTCCTGG
GGCCGCAGCCAGAGCAGCGCGGCCGCCGAGGCCTCGGCGGTGCTCAAGGTGCGGCCCGAG
CGCAGCCGGCGCGAGCGCATCCTCACGCTGGAGTCCATGAACCCGCAGGTGAAGGCGGTG
GAGTACGCCGTGCGGGGACCCATCGTGCTCAAGGCCGGCGAGATCGAGCTCGAGCTGCAG
CGGGGTATCAAAAAGCCATTCACAGAGGTCATCCGAGCCAACATCGGGGACGCCCAGGCT
ATGGGGCAGCAGCCAATCACCTTCCTCCGGCAGGTGATGGCACTATGCACCTACCCAAAC
CTGCTGGACAGCCCCAGCTTCCCAGAAGATGCTAAGAAACGTGCCCGGCGGATCCTGCAG
GCTTGTGGCGGGAACAGCCTGGGGTCCTACAGTGCTAGCCAGGGTGTCAACTGCATCCGT
GAAGATGTGGCTGCCTACATCACCAGGAGGGATGGCGGTGTGCCTGCGGACCCCGACAAC
ATCTACCTGACCACGGGAGCTAGTGACGGCATTTCTACGATCCTGAAGATCCTCGTCTCC
GGGGGCGGCAAGTCACGGACAGGTGTGATGATCCCCATCCCACAATATCCCCTCTATTCA
GCTGTCATCTCTGAGCTCGACGCCATCCAGGTGAATTACTACCTGGACGAGGAGAACTGC
TGGGCGCTGAATGTGAATGAGCTCCGGCGGGCGGTGCAGGAGGCCAAAGACCACTGTGAT
CCTAAGGTGCTCTGCATAATCAACCCTGGGAACCCCACAGGCCAGGTACAAAGCAGAAAG
TGCATAGAAGATGTGATCCACTTTGCCTGGGAAGAGAAGCTCTTTCTCCTGGCTGATGAG
GTGTACCAGGACAACGTGTACTCTCCAGATTGCAGATTCCACTCCTTCAAGAAGGTGCTG
TACGAGATGGGGCCCGAGTACTCCAGCAACGTGGAGCTCGCCTCCTTCCACTCCACCTCC
AAGGGCTACATGGGCGAGTGTGGTTACAGAGGAGGCTACATGGAGGTGATCAACCTGCAC
CCTGAGATCAAGGGCCAGCTGGTGAAGCTGCTGTCGGTGCGCCTGTGCCCCCCAGTGTCT
GGGCAGGCCGCCATGGACATTGTCGTGAACCCCCCGGTGGCAGGAGAGGAGTCCTTTGAG
CAATTCAGCCGAGAGAAGGAGTCGGTCCTGGGTAATCTGGCCAAAAAAGCAAAGCTGACG
GAAGACCTGTTTAACCAAGTCCCAGGAATTCACTGCAACCCCTTGCAGGGGGCCATGTAC
GCCTTCCCTCGGATCTTCATTCCTGCCAAAGCTGTGGAGGCTGCTCAGGCCCATCAAATG
GCTCCAGACATGTTCTACTGCATGAAGCTCCTGGAGGAGACTGGCATCTGTGTCGTGCCC
GGCAGTGGCTTTGGGCAGAGGGAAGGCACTTACCACTTCAGGATGACTATCCTCCCTCCA
GTGGAGAAGCTGAAAACGGTGCTGCAGAAGGTGAAAGACTTCCACATCAACTTCCTGGAG
AAGTACGCGTGA
Enzyme 46 GenBank Gene ID AY029173 Link Image
Enzyme 46 GeneCard ID GPT2 Link Image
Enzyme 46 GenAtlas ID GPT2 Link Image
Enzyme 46 HGNC ID HGNC:18062 Link Image
Enzyme 46 Chromosome Location 1
Enzyme 46 Locus 16q12.1
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Yang RZ, Blaileanu G, Hansen BC, Shuldiner AR, Gong DW: cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase. Genomics. 2002 Mar;79(3):445-50. [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. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [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]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 9663
Enzyme 47 Name CTP synthase 2
Enzyme 47 Synonyms
  1. CTP synthetase 2
  2. UTP--ammonia ligase 2
Enzyme 47 Gene Name CTPS2
Enzyme 47 Protein Sequence >CTP synthase 2
MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFV
LNDGGEVDLDLGNYERFLDINLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDA
VQEWVMNQAKVPVDGNKEEPQICVIELGGTIGDIEGMPFVEAFRQFQFKAKRENFCNIHV
SLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ
VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSASNLLFKWRNMADRYERLQKICS
IALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEKITETEDPVKFHEAWQK
LCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCLGMQLAVIEFARNCLNLKDAD
STEFRPNAPVPLVIDMPEHNPGNLGGTMRLGIRRTVFKTENSILRKLYGDVPFIEERHRH
RFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPY
LGLLLAATGNLNAYLQQGCKLSSSDRYSDASDDSFSEPRIAELEIS
Enzyme 47 Number of Residues 586
Enzyme 47 Molecular Weight 65677.0
Enzyme 47 Theoretical pI 6.91
Enzyme 47 GO Classification
Function
  • CTP synthase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
Component
Enzyme 47 General Function Involved in CTP synthase activity
Enzyme 47 Specific Function Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides
Enzyme 47 Pathways
Enzyme 47 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571]
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 9651727 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID Q9NRF8 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name PYRG2_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >1761 bp
ATGAAGTACATCCTGGTCACGGGTGGGGTCATCTCAGGCATTGGTAAAGGGATCATTGCC
AGCAGCATTGGAACGATTCTAAAATCATGTGGACTCCGAGTTACTGCCATAAAAATCGAC
CCCTATATTAACATCGATGCTGGCACTTTTTCACCTTATGAACACGGTGAAGTCTTCGTC
TTAAATGATGGTGGAGAAGTTGATTTAGACCTTGGAAATTATGAAAGATTTTTGGATATT
AATCTTTATAAAGACAACAATATCACCACGGGGAAGATATATCAGCATGTGATCAATAAA
GAGAGGCGTGGTGATTACCTGGGGAAAACAGTGCAAGTTGTCCCTCACATTACTGATGCT
GTCCAGGAGTGGGTTATGAATCAAGCCAAGGTGCCGGTGGATGGTAATAAGGAAGAGCCC
CAAATATGCGTTATTGAGCTGGGAGGCACCATTGGAGACATCGAAGGAATGCCGTTTGTG
GAGGCGTTTAGACAATTCCAGTTTAAGGCGAAAAGAGAGAATTTCTGTAATATCCACGTT
AGCCTTGTCCCACAGCTCAGTGCTACCGGAGAACAAAAAACCAAACCCACCCAAAACAGC
GTCCGCGCACTGAGGGGTTTAGGCCTGTCTCCAGATCTGATTGTCTGCCGAAGTTCAACG
CCCATTGAGATGGCCGTGAAGGAGAAGATTTCTATGTTTTGTCACGTGAACCCTGAACAG
GTCATATGTATCCATGATGTTTCTTCCACATACCGAGTTCCTGTGCTTTTAGAGGAACAA
AGCATTGTGAAATATTTTAAGGAGAGATTGCACCTGCCCATCGGTGATTCTGCAAGTAAT
TTGCTTTTTAAGTGGAGAAATATGGCTGACAGGTATGAAAGGTTACAGAAAATATGCTCC
ATAGCCCTGGTTGGCAAATACACCAAGCTCAGAGACTGCTACGCCTCTGTGTTCAAAGCC
CTGGAACACTCAGCCCTGGCCATCAACCACAAGTTGAATCTGATGTACATAGACTCCATT
GATCTGGAGAAGATCACTGAAACCGAGGACCCTGTGAAATTTCATGAAGCTTGGCAGAAG
CTATGCAAAGCTGATGGTATTCTTGTGCCTGGAGGCTTTGGAATCAGAGGAACATTGGGA
AAACTCCAGGCGATTTCTTGGGCAAGGACAAAGAAGATTCCTTTTCTGGGAGTTTGTCTT
GGGATGCAACTAGCAGTGATAGAGTTTGCAAGAAACTGCCTTAACTTGAAAGATGCTGAT
TCCACAGAGTTTAGGCCAAATGCCCCAGTTCCTCTGGTGATTGATATGCCCGAGCACAAC
CCTGGCAATTTGGGAGGAACAATGAGACTGGGAATAAGAAGAACTGTTTTCAAAACTGAA
AATTCAATATTAAGGAAACTTTATGGTGATGTTCCTTTTATAGAAGAAAGACACAGACAT
CGGTTCGAGGTAAACCCTAACCTGATCAAACAATTTGAGCAGAATGACTTAAGTTTTGTA
GGTCAGGATGTTGATGGAGACAGGATGGAAATCATTGAACTGGCAAATCATCCTTATTTT
GTTGGTGTCCAGTTCCATCCTGAGTTTTCTTCTAGGCCGATGAAGCCTTCCCCTCCGTAT
CTGGGGCTGTTACTTGCAGCAACTGGGAACCTGAATGCCTACTTGCAACAGGGTTGCAAA
CTGTCTTCCAGTGATAGATACAGTGATGCCAGTGATGACAGCTTTTCAGAGCCAAGGATA
GCTGAGTTGGAAATAAGCTGA
Enzyme 47 GenBank Gene ID AF226667 Link Image
Enzyme 47 GeneCard ID CTPS2 Link Image
Enzyme 47 GenAtlas ID CTPS2 Link Image
Enzyme 47 HGNC ID HGNC:2520 Link Image
Enzyme 47 Chromosome Location Not Available
Enzyme 47 Locus Not Available
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. van Kuilenburg AB, Meinsma R, Vreken P, Waterham HR, van Gennip AH: Identification of a cDNA encoding an isoform of human CTP synthetase. Biochim Biophys Acta. 2000 Jul 24;1492(2-3):548-52. [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. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [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. Han GS, Sreenivas A, Choi MG, Chang YF, Martin SS, Baldwin EP, Carman GM: Expression of Human CTP synthetase in Saccharomyces cerevisiae reveals phosphorylation by protein kinase A. J Biol Chem. 2005 Nov 18;280(46):38328-36. Epub 2005 Sep 22. [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]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 12977
Enzyme 48 Name Alanine aminotransferase
Enzyme 48 Synonyms Not Available
Enzyme 48 Gene Name GPT
Enzyme 48 Protein Sequence >Alanine aminotransferase
MASSTGDRSQAVRHGLRAKVLTLDGMNPRVRRVEYAVRGPIVQRALELEQELRQGVKKPF
TEVIRANIGDAQAMGQRPITFLRQVLALCVNPDLLSSPNFPDDAKKRAERILQACGGHSL
GAYSVSSGIQLIREDVARYIERRDGGIPADPNNVFLSTGASDAIVTVLKLLVAGEGHTRT
GVLIPIPQYPLYSATLAELGAVQVDYYLDEERAWALDVAELHRALGQARDHCRPRALCVI
NPGNPTGQVQTRECIEAVIRFAFEERLFLLADEVYQDNVYAAGSQFHSFKKVLMEMGPPY
AGQQELASFHSTSKGYMGECGFRGGYVEVVNMDAAVQQQMLKLMSVRLCPPVPGQALLDL
VVSPPAPTDPSFAQFQAEKQAVLAELAAKAKLTEQVFNEAPGISCNPVQGAMYSFPRVQL
PPRAVERAQELGLAPDMFFCLRLLEETGICVVPGSGFGQREGTYHFRMTILPPLEKLRLL
LEKLSRFHAKFTLEYS
Enzyme 48 Number of Residues 496
Enzyme 48 Molecular Weight 54637
Enzyme 48 Theoretical pI Not Available
Enzyme 48 GO Classification Not Available
Enzyme 48 General Function Not Available
Enzyme 48 Specific Function Not Available
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions Not Available
Enzyme 48 Pfam Domain Function Not Available
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein Not Available
Enzyme 48 UniProtKB/Swiss-Prot ID B0YJ18 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name B0YJ18_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence Not Available
Enzyme 48 GenBank Gene ID Not Available
Enzyme 48 GeneCard ID B0YJ18 Link Image
Enzyme 48 GenAtlas ID Not Available
Enzyme 48 HGNC ID Not Available
Enzyme 48 Chromosome Location Not Available
Enzyme 48 Locus Not Available
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References Not Available
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 12987
Enzyme 49 Name Gamma-glutamyltransferase 6
Enzyme 49 Synonyms
  1. GGT 6
  2. Gamma-glutamyltranspeptidase 6
  3. Gamma-glutamyltransferase 6 heavy chain
  4. Gamma-glutamyltransferase 6 light chain
Enzyme 49 Gene Name GGT6
Enzyme 49 Protein Sequence >Gamma-glutamyltransferase 6
MERAEEPVVYQKLLPWEPSLESEEEVEEEETSEALVLNPRRHQDSSRNKAGGLPGTWARV
VAALLLLAVGCSLAVRQLQNQGRSTGSLGSVAPPPGGHSHGPGVYHHGAIISPAGRELLV
AGGNVVDAGVGAALCLAVVHPHATGLGAMFWGLFHDSSSGNSTALTSGPAQTLAPGLGLP
AALPTLHLLHARFGRLPWPRLLVGPTTLAQEGFLVDTPLARALVARGTEGLCPLLCHADG
TPLGAGARATNPQLAAVLRSAALAPTSDLAGDALLSLLAGDLGVEVPSAVPRPTLEPAEQ
LPVPQGILFTTPSPSAGPELLALLEAALRSGAPIPDPCPPFLQTAVSPESSALAAVDSSG
SVLLLTSSLNCSFGSAHLSPSTGVLLSNLVAKSTTSAWACPLILRGSLDDTEADVLGLVA
SGTPDVARAMTHTLLRHLAARPPTQAQHQHQGQQEPTEHPSTCGQGTLLQVAAHTEHAHV
SSVPHACCPFQGF
Enzyme 49 Number of Residues 493
Enzyme 49 Molecular Weight 50508.8
Enzyme 49 Theoretical pI 6.04
Enzyme 49 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
Component
Enzyme 49 General Function Involved in gamma-glutamyltransferase activity
Enzyme 49 Specific Function Cleaves glutathione conjugates
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions
  • (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid [RN:R04159]
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • 55-75
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 171543825 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q6P531 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name GGT6_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >1482 bp
ATGGAGCGGGCAGAAGAGCCCGTGGTCTATCAGAAGCTGCTGCCCTGGGAGCCAAGCTTG
GAGTCGGAGGAGGAAGTGGAGGAGGAGGAGACATCAGAGGCGCTGGTTCTAAACCCCCGG
AGGCACCAGGACTCTTCCAGGAACAAGGCTGGCGGGCTGCCCGGAACCTGGGCCCGTGTA
GTGGCAGCCCTGCTGCTGCTGGCTGTTGGCTGCTCCCTGGCTGTGAGGCAGCTCCAGAAT
CAGGGCAGGTCGACAGGAAGCTTGGGCTCTGTGGCCCCTCCACCCGGCGGACACTCCCAC
GGCCCTGGCGTATACCACCACGGTGCCATCATCAGCCCTGCAGGCCGAGAGCTGCTTGTT
GCCGGGGGCAACGTCGTGGATGCTGGAGTTGGAGCTGCATTGTGCCTGGCAGTGGTGCAT
CCTCATGCCACGGGGCTAGGTGCCATGTTTTGGGGCCTCTTCCACGATAGCTCCTCAGGC
AATTCCACGGCCCTGACATCAGGCCCAGCACAGACCCTGGCCCCCGGCCTGGGGCTGCCC
GCGGCTCTGCCCACCCTGCACCTGCTGCATGCACGCTTCGGCCGCCTGCCCTGGCCACGC
CTGCTAGTGGGCCCCACCACGCTGGCTCAGGAGGGCTTCCTGGTGGACACACCCCTGGCA
AGGGCTCTGGTGGCTCGGGGCACAGAAGGCCTCTGTCCACTACTTTGCCATGCTGATGGG
ACACCCCTGGGCGCTGGGGCCCGAGCCACCAACCCACAACTGGCAGCTGTGCTTCGCAGC
GCAGCCCTCGCTCCCACCTCAGACCTTGCTGGGGATGCTCTACTGAGTCTACTGGCGGGA
GACCTGGGGGTGGAGGTGCCCTCGGCTGTGCCCAGGCCCACTTTGGAACCAGCAGAGCAG
CTACCTGTGCCCCAGGGCATCCTGTTCACCACCCCCAGTCCCTCAGCTGGCCCAGAACTG
CTGGCACTGTTGGAGGCAGCCCTGCGCTCCGGGGCGCCCATCCCTGACCCCTGCCCACCG
TTCCTGCAGACTGCTGTGAGCCCCGAGAGCAGTGCCCTGGCCGCCGTGGACAGCAGCGGC
TCTGTGCTCCTTCTCACCTCCTCGCTCAACTGCTCCTTTGGCTCTGCACACCTGTCCCCA
AGCACTGGGGTTCTGCTCAGCAACCTGGTGGCCAAGTCTACCACTAGTGCCTGGGCCTGC
CCCCTCATCCTCCGTGGCAGCCTGGATGACACAGAGGCTGATGTGTTGGGGCTTGTGGCT
TCAGGGACCCCTGATGTGGCCAGGGCCATGACTCACACCCTACTCAGGCATCTGGCAGCA
AGGCCCCCTACCCAGGCCCAGCACCAGCATCAGGGTCAGCAAGAACCAACAGAGCATCCC
AGCACTTGTGGCCAAGGGACCCTGCTCCAGGTGGCAGCCCACACAGAGCACGCCCATGTC
TCCAGTGTCCCCCATGCCTGCTGCCCCTTCCAGGGGTTCTAA
Enzyme 49 GenBank Gene ID NM_001122890.1 Link Image
Enzyme 49 GeneCard ID GGT6 Link Image
Enzyme 49 GenAtlas ID GGT6 Link Image
Enzyme 49 HGNC ID HGNC:26891 Link Image
Enzyme 49 Chromosome Location 1
Enzyme 49 Locus 17p13.2
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. 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. Heisterkamp N, Groffen J, Warburton D, Sneddon TP: The human gamma-glutamyltransferase gene family. Hum Genet. 2008 May;123(4):321-32. Epub 2008 Mar 21. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 13038
Enzyme 50 Name Phosphoribosyl pyrophosphate amidotransferase, isoform CRA_b
Enzyme 50 Synonyms
  1. SubName: cDNA FLJ78123, highly similar to Homo sapiens phosphoribosyl pyrophosphate amidotransferase (PPAT), mRNA
  2. SubName: cDNA, FLJ92602, highly similar to Homo sapiens phosphoribosyl pyrophosphate amidotransferase (PPAT), mRNA
Enzyme 50 Gene Name PPAT
Enzyme 50 Protein Sequence >Phosphoribosyl pyrophosphate amidotransferase, isoform CRA_b
MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPT
FKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVA
HNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEA
PTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFL
SIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVY
TVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQP
NMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASP
PIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKE
KKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW
Enzyme 50 Number of Residues 517
Enzyme 50 Molecular Weight 57398.5
Enzyme 50 Theoretical pI 6.74
Enzyme 50 GO Classification
Function
  • amidophosphoribosyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside metabolic process
  • purine base biosynthetic process
  • purine base metabolic process
Component
Enzyme 50 General Function Involved in amidophosphoribosyltransferase activity
Enzyme 50 Specific Function Not Available
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 158255320 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID A8K4H7 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name A8K4H7_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >1554 bp
ATGGAGCTGGAGGAGTTGGGGATCCGAGAGGAATGTGGCGTGTTCGGGTGCATCGCCTCA
GGAGAGTGGCCCACGCAGCTGGATGTACCGCATGTGATCACTCTGGGACTCGTGGGGCTG
CAGCACCGGGGTCAGGAGAGTGCTGGTATTGTGACTAGTGATGGGAGTTCCGTGCCAACA
TTCAAATCACACAAGGGAATGGGTCTTGTAAATCACGTCTTTACTGAAGACAATTTGAAA
AAATTATATGTTTCAAATCTTGGAATTGGACACACCAGGTATGCCACCACAGGAAAATGT
GAACTAGAAAATTGTCAGCCCTTCGTTGTTGAAACACTTCATGGGAAGATAGCTGTGGCA
CATAATGGCGAATTGGTAAATGCTGCTCGATTAAGGAAAAAGCTTCTGCGTCATGGTATT
GGTCTGTCTACAAGTTCTGATAGTGAAATGATTACCCAGTTACTGGCGTATACCCCTCCT
CAGGAACAAGATGACACCCCAGACTGGGTAGCCAGGATTAAAAACTTGATGAAGGAAGCA
CCCACAGCATACTCCCTGCTTATAATGCACAGAGATGTTATTTATGCAGTACGAGATCCT
TATGGAAATCGTCCCTTATGCATTGGTCGTCTTATTCCAGTGTCTGATATAAATGACAAA
GAGAAAAAAACATCAGAAACAGAAGGATGGGTGGTGTCTTCAGAATCTTGTAGCTTCTTA
TCTATTGGTGCAAGATATTACCGTGAAGTCTTGCCTGGAGAAATTGTGGAAATATCCAGA
CACAATGTCCAAACTCTTGATATTATATCAAGGTCTGAAGGAAACCCAGTGGCTTTTTGT
ATCTTTGAATATGTTTATTTTGCAAGACCAGACAGTATGTTCGAAGACCAAATGGTTTAT
ACAGTAAGATACCGTTGTGGCCAGCAGCTAGCGATTGAAGCACCTGTGGATGCAGATTTG
GTTAGCACTGTTCCAGAATCTGCTACGCCTGCTGCTCTTGCTTACGCAGGAAAGTGTGGA
CTTCCATATGTGGAGGTGCTGTGTAAAAACCGGTATGTAGGGAGAACCTTCATTCAGCCA
AACATGAGGTTAAGACAACTTGGTGTTGCAAAAAAATTTGGAGTATTGTCAGACAACTTT
AAAGGCAAAAGAATTGTTCTTGTAGATGATTCAATTGTCAGAGGCAATACCATCTCACCT
ATAATAAAACTGCTCAAAGAATCTGGTGCAAAAGAGGTACACATTCGAGTAGCTTCACCA
CCAATTAAATATCCATGCTTCATGGGAATAAACATTCCTACAAAAGAAGAGCTCATTGCC
AATAAACCAGAATTTGATCACCTTGCAGAATATCTAGGAGCAAACAGTGTTGTGTATCTG
TCAGTAGAAGGACTGGTTTCATCTGTACAAGAAGGGATAAAGTTTAAAAAACAGAAAGAG
AAAAAGCACGATATTATGATCCAAGAAAATGGAAATGGTCTGGAATGTTTTGAAAAGAGT
GGTCATTGTACAGCTTGTCTCACTGGAAAATATCCTGTAGAATTAGAATGGTAG
Enzyme 50 GenBank Gene ID AK290942 Link Image
Enzyme 50 GeneCard ID PPAT Link Image
Enzyme 50 GenAtlas ID PPAT Link Image
Enzyme 50 HGNC ID HGNC:9238 Link Image
Enzyme 50 Chromosome Location 4
Enzyme 50 Locus 4q12
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References Not Available
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 13039
Enzyme 51 Name Guanine monphosphate synthetase, isoform CRA_b
Enzyme 51 Synonyms
  1. SubName: cDNA FLJ75406, highly similar to Homo sapiens guanine monphosphate synthetase (GMPS), mRNA
  2. SubName: cDNA, FLJ79481, highly similar to GMP synthase (glutamine-hydrolyzing) (EC6.3.5.2)
Enzyme 51 Gene Name GMPS
Enzyme 51 Protein Sequence >Guanine monphosphate synthetase, isoform CRA_b
MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETP
AFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHK
KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANE
SKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAA
HSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPE
EVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVR
ILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPH
TLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDW
ESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVE
VVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
Enzyme 51 Number of Residues 693
Enzyme 51 Molecular Weight 76714.8
Enzyme 51 Theoretical pI 6.86
Enzyme 51 GO Classification
Function
  • ATP binding
  • GMP synthase (glutamine-hydrolyzing) activity
  • GMP synthase (glutamine-hydrolyzing) activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleoside binding
  • purine nucleoside binding
Process
  • GMP biosynthetic process
  • biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • glutamine family amino acid metabolic process
  • glutamine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside monophosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside monophosphate biosynthetic process
Component
Enzyme 51 General Function Involved in catalytic activity
Enzyme 51 Specific Function Not Available
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions Not Available
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • None
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 158256440 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID A8K639 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name A8K639_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >2082 bp
ATGGCTCTGTGCAACGGAGACTCCAAGCTGGAGAATGCTGGAGGAGACCTTAAGGATGGC
CACCACCACTATGAAGGAGCTGTTGTCATTCTGGATGCTGGTGCTCAGTACGGGAAAGTC
ATAGACCGAAGAGTGAGGGAACTGTTCGTGCAGTCTGAAATTTTCCCCTTGGAAACACCA
GCATTTGCTATAAAGGAACAAGGATTCCGTGCTATTATCATCTCTGGAGGACCTAATTCT
GTGTATGCTGAAGATGCTCCCTGGTTTGATCCAGCAATATTCACTATTGGCAAGCCTGTT
CTTGGAATTTGCTATGGTATGCAGATGATGAATAAGGTATTTGGAGGTACTGTGCACAAA
AAAAGTGTCAGAGAAGATGGAGTTTTCAACATTAGTGTGGATAATACATGTTCATTATTC
AGGGGCCTTCAGAAGGAAGAAGTTGTTTTGCTTACACATGGAGATAGTGTAGACAAAGTA
GCTGATGGATTCAAGGTTGTGGCACGTTCTGGAAACATAGTAGCAGGCATAGCAAATGAA
TCTAAAAAGTTATATGGAGCACAGTTCCACCCTGAAGTTGGCCTTACAGAAAATGGAAAA
GTAATACTGAAGAATTTCCTTTATGATATAGCTGGATGCAGTGGAACCTTCACCGTGCAG
AACAGAGAACTTGAGTGTATTCGAGAGATCAAAGAGAGAGTAGGCACGTCAAAAGTTTTG
GTTTTACTCAGTGGTGGAGTAGACTCAACAGTTTGTACAGCTTTGCTAAATCGTGCTTTG
AACCAAGAACAAGTCATTGCTGTGCACATTGATAATGGCTTTATGAGAAAACGAGAAAGC
CAGTCTGTTGAAGAGGCCCTCAAAAAGCTTGGAATTCAGGTCAAAGTGATAAATGCTGCT
CATTCTTTCTACAATGGAACAACAACCCTACCAATATCAGATGAAGATAGAACCCCACGG
AAAAGAATTAGCAAAACGTTAAATATGACCACAAGTCCTGAAGAGAAAAGAAAAATCATT
GGGGATACTTTTGTTAAGATTGCCAATGAAGTAATTGGAGAAATGAACTTGAAACCAGAG
GAGGTTTTCCTTGCCCAAGGTACTTTACGGCCTGATCTAATTGAAAGTGCATCCCTTGTT
GCAAGTGGCAAAGCTGAACTCATCAAAACCCATCACAATGACACAGAGCTCATCAGAAAG
TTGAGAGAGGAGGGAAAAGTAATAGAACCTCTGAAAGATTTTCATAAAGATGAAGTGAGA
ATTTTGGGCAGAGAACTTGGACTTCCAGAAGAGTTAGTTTCCAGGCATCCATTTCCAGGT
CCTGGCCTGGCAATCAGAGTAATATGTGCTGAAGAACCTTATATTTGTAAGGACTTTCCT
GAAACCAACAATATTTTGAAAATAGTAGCTGATTTTTCTGCAAGTGTTAAAAAGCCACAT
ACCCTATTACAGAGAGTCAAAGCCTGCACAACAGAAGAGGATCAGGAGAAGCTGATGCAA
ATTACCAGTCTGCATTCACTGAATGCCTTCTTGCTGCCAATTAAAACTGTAGGTGTGCAG
GGTGACTGTCGTTCCTACAGTTACGTGTGTGGAATCTCCAGTAAAGATGAACCTGACTGG
GAATCACTTATTTTTCTGGCTAGGCTTATACCTCGCATGTGTCACAACGTTAACAGAGTT
GTTTATATATTTGGCCCACCAGTTAAAGAACCTCCTACAGATGTTACTCCCACTTTCTTG
ACAACAGGGGTGCTCAGTACTTTACGCCAAGCTGATTTTGAGGCCCATAACATTCTCAGG
GAGTCTGGGTATGCTGGGAAAATCAGCCAGATGCCGGTGATTTTGACACCATTACATTTT
GATCGGGACCCACTTCAAAAGCAGCCTTCATGCCAGAGATCTGTGGTTATTCGAACCTTT
ATTACTAGTGACTTCATGACTGGTATACCTGCAACACCTGGCAATGAGATCCCTGTAGAG
GTGGTATTAAAGATGGTCACTGAGATTAAGAAGATTCCTGGTATTTCTCGAATTATGTAT
GACTTAACATCAAAGCCCCCAGGAACTACTGAGTGGGAGTAA
Enzyme 51 GenBank Gene ID AK291504 Link Image
Enzyme 51 GeneCard ID GMPS Link Image
Enzyme 51 GenAtlas ID GMPS Link Image
Enzyme 51 HGNC ID HGNC:4378 Link Image
Enzyme 51 Chromosome Location 3
Enzyme 51 Locus 3q24
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References
  1. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 13040
Enzyme 52 Name Glutamine synthetase
Enzyme 52 Synonyms Not Available
Enzyme 52 Gene Name PIG59
Enzyme 52 Protein Sequence >Glutamine synthetase
MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEW
NFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRI
MDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHY
RACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDP
KPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRL
TGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCL
LNETGDEPFQYKN
Enzyme 52 Number of Residues 373
Enzyme 52 Molecular Weight 42064.1
Enzyme 52 Theoretical pI 6.88
Enzyme 52 GO Classification
Function
  • acid-ammonia (or amide) ligase activity
  • acid-ammonia (or amide) ligase activity
  • ammonia ligase activity
  • catalytic activity
  • glutamate-ammonia ligase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glutamine biosynthetic process
  • glutamine family amino acid metabolic process
  • glutamine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
Component
Enzyme 52 General Function Involved in glutamate-ammonia ligase activity
Enzyme 52 Specific Function ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions
  • ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine [RN:R00253]
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 193783746 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID A8YXX4 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name A8YXX4_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >1122 bp
ATGACCACCTCAGCAAGTTCCCACTTAAATAAAGGCATCAAGCAGGTGTACATGTCCCTG
CCTCAGGGTGAGAAAGTCCAGGCCATGTATATCTGGATCGATGGTACTGGAGAAGGACTG
CGCTGCAAGACCCGGACCCTGGACAGTGAGCCCAAGTGTGTGGAAGAGTTGCCTGAGTGG
AATTTCGATGGCTCCAGTACTTTACAGTCTGAGGGTTCCAACAGTGACATGTATCTCGTG
CCTGCTGCCATGTTTCGGGACCCCTTCCGTAAGGACCCTAACAAGCTGGTGTTATGTGAA
GTTTTCAAGTACAATCGAAGGCCTGCAGAGACCAATTTGAGGCACACCTGTAAACGGATA
ATGGACATGGTGAGCAACCAGCACCCCTGGTTTGGCATGGAGCAGGAGTATACCCTCATG
GGGACAGATGGGCACCCCTTTGGTTGGCCTTCCAACGGCTTCCCAGGGCCCCAGGGTCCA
TATTACTGTGGTGTGGGAGCAGACAGAGCCTATGGCAGGGACATCGTGGAGGCCCATTAC
CGGGCCTGCTTGTATGCTGGAGTCAAGATTGCGGGGACTAATGCCGAGGTCATGCCTGCC
CAGTGGGAATTTCAGATTGGACCTTGTGAAGGAATCAGCATGGGAGATCATCTCTGGGTG
GCCCGTTTCATCTTGCATCGTGTGTGTGAAGACTTTGGAGTGATAGCAACCTTTGATCCT
AAGCCCATTCCTGGGAACTGGAATGGTGCAGGCTGCCATACCAACTTCAGCACCAAGGCC
ATGCGGGAGGAGAATGGTCTGAAGTACATCGAGGAGGCCATTGAGAAACTAAGCAAGCGG
CACCAGTACCACATCCGTGCCTATGATCCCAAGGGAGGCCTGGACAATGCCCGACGTCTA
ACTGGATTCCATGAAACCTCCAACATCAACGACTTTTCTGCTGGTGTAGCCAATCGTAGC
GCCAGCATACGCATTCCCCGGACTGTTGGCCAGGAGAAGAAGGGTTACTTTGAAGATCGT
CGCCCCTCTGCCAACTGCGACCCCTTTTCGGTGACAGAAGCCCTCATCCGCACGTGTCTT
CTCAATGAAACCGGCGATGAGCCCTTCCAGTACAAAAATTAA
Enzyme 52 GenBank Gene ID AK122784 Link Image
Enzyme 52 GeneCard ID PIG59 Link Image
Enzyme 52 GenAtlas ID PIG59 Link Image
Enzyme 52 HGNC ID HGNC:4341 Link Image
Enzyme 52 Chromosome Location Not Available
Enzyme 52 Locus Not Available
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 13041
Enzyme 53 Name Probable glutamyl-tRNA synthetase, mitochondrial
Enzyme 53 Synonyms
  1. Glutamate--tRNA ligase
  2. GluRS
Enzyme 53 Gene Name EARS2
Enzyme 53 Protein Sequence >Probable glutamyl-tRNA synthetase, mitochondrial
MAALLRRLLQRERPSAASGRPVGRREANLGTDAGVAVRVRFAPSPTGFLHLGGLRTALYN
YIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRGGPAGPYQQSQR
LELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLA
KDPKPAIRFRLEQVVPAFQDLVYGWNRHEVASVEGDPVIMKSDGFPTYHLACVVDDHHMG
ISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLSKRQGDVFLEHFAAD
GFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQ
RLVSNESQRRQLVGKLQVLVEEAFGCQLQNRDVLNPVYVERILLLRQGHICRLQDLVSPV
YSYLWTRPAVGRAQLDAISEKVDVIAKRVLGLLERSSMSLTQDMLNGELKKLSEGLEGTK
YSNVMKLLRMALSGQQQGPPVAEMMLALGPKEVRERIQKVVSS
Enzyme 53 Number of Residues 523
Enzyme 53 Molecular Weight 58688.1
Enzyme 53 Theoretical pI 8.98
Enzyme 53 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • aminoacyl-tRNA ligase activity
  • binding
  • catalytic activity
  • glutamate-tRNA ligase activity
  • ligase activity
  • ligase activity, forming aminoacyl-tRNA and related compounds
  • ligase activity, forming carbon-oxygen bonds
  • nucleoside binding
  • nucleotide binding
  • purine nucleoside binding
Process
  • RNA metabolic process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • cellular macromolecule metabolic process
  • glutamyl-tRNA aminoacylation
  • 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 53 General Function Involved in nucleotide binding
Enzyme 53 Specific Function Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction:glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu)
Enzyme 53 Pathways
Enzyme 53 Reactions
  • ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu [RN:R05578]
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein 134288884 Link Image
Enzyme 53 UniProtKB/Swiss-Prot ID Q5JPH6 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name SYEM_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >1572 bp
ATGGCGGCGCTCCTGAGGAGACTGCTGCAGCGCGAGAGGCCTTCGGCGGCCTCTGGCCGC
CCCGTAGGACGGCGCGAGGCCAACCTGGGCACTGATGCCGGGGTTGCGGTGCGAGTGCGG
TTCGCTCCCAGCCCCACAGGCTTCTTGCACCTGGGTGGCCTCCGCACTGCCTTGTACAAC
TACATCTTTGCTAAGAAGTACCAGGGGAGCTTCATCCTGAGGCTAGAGGACACAGATCAG
ACTCGCGTTGTGCCTGGGGCAGCGGAGAATATTGAGGACATGCTGGAGTGGGCAGGCATC
CCGCCTGATGAGAGCCCCCGCCGGGGCGGTCCTGCTGGGCCCTACCAGCAATCTCAGCGG
TTGGAGCTGTATGCCCAGGCCACAGAAGCGCTGCTGAAGACCGGAGCTGCTTACCCCTGT
TTCTGCTCACCCCAGCGGCTGGAGCTCCTGAAGAAGGAGGCCTTGCGGAACCACCAGACG
CCCCGGTATGACAATCGGTGCAGGAACATGAGCCAGGAGCAGGTGGCCCAGAAGCTGGCC
AAGGACCCCAAGCCTGCGATCCGCTTCCGCCTGGAGCAGGTGGTGCCAGCCTTCCAGGAC
CTGGTCTATGGCTGGAATAGGCATGAAGTGGCCAGCGTGGAGGGAGACCCAGTCATCATG
AAGAGCGACGGCTTCCCCACATACCACCTGGCCTGCGTGGTGGACGACCACCACATGGGC
ATCAGCCACGTGCTGCGAGGCTCTGAGTGGCTCGTCTCCACTGCCAAGCACCTGCTCCTC
TACCAGGCCCTGGGCTGGCAGCCACCCCACTTCGCCCACCTGCCCCTGCTCCTCAACAGG
GATGGCAGCAAGCTCTCCAAGAGGCAAGGGGACGTTTTCCTGGAGCACTTTGCTGCTGAT
GGCTTCCTGCCCGATTCCTTGTTGGACATCATCACCAACTGTGGCTCAGGTTTTGCAGAG
AACCAAATGGGCAGGACCCTGCCGGAGCTGATCACACAGTTCAACCTGACACAGGTCACC
TGTCACTCAGCCCTGCTGGACCTGGAGAAGCTCCCAGAATTCAACAGACTGCACCTCCAG
CGGCTGGTGAGCAATGAGAGCCAGAGGCGCCAGCTGGTGGGGAAGCTGCAGGTCCTTGTG
GAGGAGGCCTTTGGTTGCCAGCTGCAAAACAGGGATGTCCTCAACCCAGTCTACGTGGAG
AGGATCCTCCTGCTGAGACAGGGTCACATTTGCCGCCTGCAGGACTTGGTGTCCCCAGTA
TACTCTTACCTGTGGACTCGCCCTGCAGTAGGTCGAGCACAGCTGGACGCCATCTCGGAG
AAGGTGGATGTGATTGCCAAGCGTGTGCTGGGGCTTCTAGAAAGATCTAGTATGAGCTTA
ACTCAGGATATGCTGAATGGAGAACTGAAGAAGCTATCAGAAGGTCTGGAAGGCACCAAG
TACAGTAATGTGATGAAACTCCTTCGGATGGCCCTCAGTGGACAGCAGCAAGGACCTCCT
GTAGCTGAGATGATGTTGGCCTTGGGACCAAAGGAAGTACGGGAACGGATCCAGAAGGTG
GTTTCCAGCTAG
Enzyme 53 GenBank Gene ID NM_001083614.1 Link Image
Enzyme 53 GeneCard ID EARS2 Link Image
Enzyme 53 GenAtlas ID EARS2 Link Image
Enzyme 53 HGNC ID HGNC:29419 Link Image
Enzyme 53 Chromosome Location 1
Enzyme 53 Locus 16p12.2
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. 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]
  3. Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed Link Image]
  4. 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]
  5. 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 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 13053
Enzyme 54 Name Phosphoserine aminotransferase 1
Enzyme 54 Synonyms
  1. Phosphoserine aminotransferase 1, isoform CRA_a
Enzyme 54 Gene Name PSAT1
Enzyme 54 Protein Sequence >Phosphoserine aminotransferase 1
MDAPRQVVNFGPGPAKLPHSVLLEIQKELLDYKGVGISVLEMSHRSSDFAKIINNTENLV
RELLAVPDNYKVIFLQGGGCGQFSAVPLNLIGLKAGRCADYVVTGAWSAKAAEEAKKFGT
INIVHPKLGSYTKIPDPSTWNLNPDASYVYYCANETVHGVEFDFIPDVKGAVLVCDMSSN
FLSKPVDVSKFGVIFAGAQKNVGSAGVTVVIVRDDLLGFALRECPSVLEYKVQAGNSSLY
NTPPCFSIYVMGLVLEWIKNNGGAAAMEKLSSIKSQTIYEIIDNSQGFYVSVGGIRASLY
NAVTIEDVQKLAAFMKKFLEMHQL
Enzyme 54 Number of Residues 324
Enzyme 54 Molecular Weight 35189
Enzyme 54 Theoretical pI 6.66
Enzyme 54 GO Classification
Function
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • L-serine biosynthesis
  • L-serine metabolism
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
  • serine family amino acid metabolism
Component
Enzyme 54 General Function Coenzyme transport and metabolism
Enzyme 54 Specific Function Not Available
Enzyme 54 Pathways Not Available
Enzyme 54 Reactions Not Available
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein Not Available
Enzyme 54 UniProtKB/Swiss-Prot ID Q5T7G5 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name Q5T7G5_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence Not Available
Enzyme 54 GenBank Gene ID AL353594 Link Image
Enzyme 54 GeneCard ID Q5T7G5 Link Image
Enzyme 54 GenAtlas ID PSAT1 Link Image
Enzyme 54 HGNC ID HGNC:19129 Link Image
Enzyme 54 Chromosome Location Not Available
Enzyme 54 Locus Not Available
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References Not Available
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 13067
Enzyme 55 Name Aminoadipate-semialdehyde synthase
Enzyme 55 Synonyms
  1. SubName: Aminoadipate-semialdehyde synthase, isoform CRA_a
Enzyme 55 Gene Name AASS
Enzyme 55 Protein Sequence >Aminoadipate-semialdehyde synthase
MLQVHRTGLGRLGVSLSKGLHHKAVLAVRREDVNAWERRAPLAPKHIKGITNLGYKVLIQ
PSNRRAIHDKDYVKAGGILQEDISEACLILGVKRPPEEKLMSRKTYAFFSHTIKAQEANM
GLLDEILKQEIRLIDYEKMVDHRGVRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFM
HIGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQAIFNELPC
EYVEPHELKEVSQTGDLRKVYGTVLSRHHHLVRKTDAVYDPAEYDKHPERYISRFNTDIA
PYTTCLINGIYWEQNTPRLLTRQDAQSLLAPGKFSPAGVEGCPALPHKLVAICDISADTG
GSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAQLPIEATECFGDMLY
PYVEEMILSDATQPLESQNFSPVVRDAVITSNGTLPDKYKYIQTLRESRERAQSLSMGTR
RKVLVLGSGYISEPVLEYLSRDGNIEITVGSDMKNQIEQLGKKYNINPVSMDICKQEEKL
GFLVAKQDLVISLLPYVLHPLVAKACITNKVNMVTASYITPALKELEKSVEDAGITIIGE
LGLDPGLDHMLAMETIDKAKEVGATIESYISYCGGLPAPEHSNNPLRYKFSWSPVGVLMN
VMQSATYLLDGKVVNVAGGISFLDAVTSMDFFPGLNLEGYPNRDSTKYAEIYGISSAHTL
LRGTLRYKGYMKALNGFVKLGLINREALPAFRPEANPLTWKQLLCDLVGISPSSEHDVLK
EAVLKKLGGDNTQLEAAEWLGLLGDEQVPQAESILDALSKHLVMKLSYGPEEKDMIVMRD
SFGIRHPSGHLEHKTIDLVAYGDINGFSAMAKTVGLPTAMAAKMLLDGEIGAKGLMGPFS
KEIYGPILERIKAEGIIYTTQSTIKP
Enzyme 55 Number of Residues 926
Enzyme 55 Molecular Weight 102130.9
Enzyme 55 Theoretical pI 6.62
Enzyme 55 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 55 General Function Involved in oxidoreductase activity
Enzyme 55 Specific Function Not Available
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions Not Available
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • None
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 13027640 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID A4D0W4 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name A4D0W4_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >2781 bp
ATGCTGCAAGTACATAGGACTGGACTGGGCAGGCTGGGGGTCAGCCTCTCCAAGGGTCTT
CACCACAAAGCTGTGTTGGCCGTCCGGAGGGAGGATGTGAACGCCTGGGAGAGAAGGGCC
CCGCTAGCTCCCAAGCACATCAAAGGCATCACCAATCTGGGATACAAGGTCTTGATACAG
CCTTCGAATCGGCGGGCCATTCATGATAAGGACTATGTCAAAGCTGGTGGCATTCTTCAG
GAGGATATTTCTGAAGCTTGTCTAATTTTAGGAGTTAAAAGACCTCCAGAGGAAAAATTA
ATGTCCAGGAAGACTTATGCATTTTTCTCCCACACAATAAAAGCTCAGGAGGCCAATATG
GGCTTGTTGGATGAGATTCTAAAACAGGAAATTCGCCTTATTGATTATGAGAAAATGGTG
GATCATAGAGGAGTACGGGTAGTGGCATTTGGACAGTGGGCTGGTGTGGCAGGAATGATC
AACATTTTACATGGAATGGGTTTAAGGCTCCTTGCTTTGGGACATCACACACCTTTTATG
CACATTGGCATGGCTCATAACTACAGGAATAGCAGTCAGGCTGTGCAAGCTGTCCGTGAT
GCTGGCTATGAAATATCTTTGGGTTTGATGCCTAAGTCAATAGGACCCTTAACATTTGTG
TTCACAGGAACTGGTAATGTTTCTAAGGGAGCCCAAGCAATCTTTAATGAGCTACCTTGT
GAATATGTGGAGCCCCATGAATTAAAAGAAGTTTCCCAAACTGGAGACCTCAGAAAAGTG
TATGGGACGGTGTTAAGTCGTCATCATCATCTTGTCAGGAAAACAGATGCTGTGTATGAT
CCTGCAGAGTATGACAAACATCCGGAGCGCTACATAAGTCGTTTTAATACTGATATTGCA
CCCTATACAACTTGCTTAATTAATGGAATCTACTGGGAACAAAACACTCCTCGCCTCCTA
ACCCGCCAAGATGCTCAGAGTCTCCTGGCTCCGGGCAAGTTCTCACCTGCTGGTGTGGAA
GGCTGCCCTGCATTACCACACAAACTCGTGGCAATATGTGACATTTCAGCTGACACAGGA
GGGTCTATAGAGTTTATGACTGAGTGTACAACAATAGAGCATCCCTTTTGCATGTATGAT
GCAGACCAGCATATTATTCATGACAGTGTTGAAGGCTCGGGGATCCTGATGTGTTCCATT
GACAATTTGCCGGCACAGCTCCCAATTGAAGCTACAGAATGCTTTGGAGACATGCTTTAC
CCTTATGTTGAAGAAATGATATTATCAGACGCGACACAGCCTCTTGAAAGTCAGAATTTT
TCTCCTGTGGTGAGAGATGCAGTGATTACATCCAACGGTACATTACCTGATAAATATAAA
TATATCCAGACACTCCGGGAGAGCAGGGAACGTGCTCAGTCACTTTCAATGGGCACCAGG
AGAAAGGTTTTGGTTCTTGGATCTGGCTACATATCTGAGCCTGTATTAGAATATTTATCA
AGAGATGGCAATATAGAAATAACAGTAGGATCTGACATGAAGAATCAAATTGAACAGTTA
GGCAAGAAATATAATATTAATCCTGTTAGCATGGACATTTGTAAACAAGAAGAGAAGCTG
GGCTTCTTGGTGGCAAAACAGGATCTTGTCATCAGCTTGTTGCCTTATGTATTGCACCCT
CTTGTGGCCAAGGCCTGCATCACAAACAAAGTTAACATGGTCACTGCAAGCTACATCACA
CCAGCACTAAAAGAATTGGAAAAGAGTGTGGAAGATGCTGGCATCACAATCATTGGTGAA
TTGGGATTGGACCCTGGTCTGGATCACATGTTAGCAATGGAAACAATAGATAAAGCCAAG
GAAGTGGGAGCCACGATTGAATCATATATTTCCTACTGTGGTGGGCTTCCAGCCCCTGAA
CATTCAAACAATCCATTGAGATATAAATTTAGCTGGAGTCCAGTGGGAGTTTTGATGAAT
GTAATGCAGTCTGCCACCTATCTGCTCGATGGAAAGGTTGTGAATGTTGCAGGAGGCATC
TCCTTTCTTGATGCCGTTACGTCCATGGATTTTTTTCCAGGATTAAATTTGGAAGGCTAT
CCTAACAGAGACAGTACGAAATATGCTGAGATTTATGGCATTTCTTCTGCTCACACTTTG
TTGCGGGGGACACTGAGATATAAGGGATATATGAAAGCTTTGAATGGATTTGTAAAATTA
GGTCTTATAAACAGAGAAGCGCTTCCTGCCTTTAGACCTGAGGCCAACCCTCTCACCTGG
AAACAACTCCTCTGTGACCTAGTTGGGATTTCACCCTCCTCTGAGCATGATGTGTTGAAG
GAAGCTGTTCTTAAGAAACTAGGAGGAGACAATACCCAGTTGGAGGCTGCTGAATGGTTG
GGCTTACTTGGGGATGAACAAGTTCCTCAGGCAGAGTCCATTCTGGATGCCCTCTCCAAG
CATTTGGTCATGAAGCTTTCCTATGGTCCTGAAGAAAAAGATATGATTGTGATGAGAGAC
AGCTTTGGAATCAGACATCCTTCTGGACATTTAGAACATAAAACGATTGATCTTGTGGCT
TATGGGGACATCAATGGCTTTTCAGCCATGGCTAAAACCGTGGGGTTACCCACCGCCATG
GCAGCCAAAATGTTGCTTGATGGTGAAATTGGAGCCAAAGGCCTAATGGGGCCCTTTTCA
AAGGAGATCTATGGACCAATATTGGAGCGAATTAAAGCAGAAGGCATTATATATACTACA
CAGAGTACAATTAAACCATAA
Enzyme 55 GenBank Gene ID NM_005763.3 Link Image
Enzyme 55 GeneCard ID AASS Link Image
Enzyme 55 GenAtlas ID AASS Link Image
Enzyme 55 HGNC ID HGNC:17366 Link Image
Enzyme 55 Chromosome Location 7
Enzyme 55 Locus 7q31.3
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  2. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 13123
Enzyme 56 Name cDNA, FLJ96771, Homo sapiens ornithine decarboxylase-like protein (ODC-p), mRNA (Arginine decarboxylase, isoform CRA_d)
Enzyme 56 Synonyms Not Available
Enzyme 56 Gene Name ADC
Enzyme 56 Protein Sequence >cDNA, FLJ96771, Homo sapiens ornithine decarboxylase-like protein (ODC-p)
MAGYLSESDFVMVEEGFSTRDLLKELTLGASQATTDEVAAFFVADLGAIVRKHFCFLKCL
PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQ
IKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRH
LLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFP
GTEGAKVRFEEIASVINSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLD
QPGREEENGSTSKTIVYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWGPA
VDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWGTQACHITYAMSRVAWEALRR
QLMAAEQEDDVEGVCKPLSCGWEITDTLCVGPVFTPASIM
Enzyme 56 Number of Residues 460
Enzyme 56 Molecular Weight 49980
Enzyme 56 Theoretical pI Not Available
Enzyme 56 GO Classification Not Available
Enzyme 56 General Function Not Available
Enzyme 56 Specific Function Not Available
Enzyme 56 Pathways Not Available
Enzyme 56 Reactions Not Available
Enzyme 56 Pfam Domain Function Not Available
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein Not Available
Enzyme 56 UniProtKB/Swiss-Prot ID B2RDU5 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name B2RDU5_HUMAN Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence Not Available
Enzyme 56 GenBank Gene ID Not Available
Enzyme 56 GeneCard ID B2RDU5 Link Image
Enzyme 56 GenAtlas ID Not Available
Enzyme 56 HGNC ID Not Available
Enzyme 56 Chromosome Location Not Available
Enzyme 56 Locus Not Available
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 General References Not Available
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 13124
Enzyme 57 Name cDNA, FLJ95223, Homo sapiens N-acetylglutamate synthase (NAGS), mRNA
Enzyme 57 Synonyms Not Available
Enzyme 57 Gene Name Not Available
Enzyme 57 Protein Sequence >cDNA, FLJ95223, Homo sapiens N-acetylglutamate synthase (NAGS)
MATALMAVVLRAAAVAPRLRGRGGTGGARRLSCGARRRAARGTSPGRRLSTAWSQPQPPP
EEYAGADDVSQSPVAEEPSWVPSPRPPVPHESPEPPSGRSLVQRDIQAFLNQCGASPGEA
RHWLTQFQTCHHSADKPFAVIEVDEEVLKCQQGVSSLAFALAFLQRMDMKPLVVLGLPAP
TAPSGCLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVS
VETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLR
DSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVITAASTLLTE
LFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLASLRPRLHSIYV
SEGYNAAAILTMEPVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNP
INPWYFKHSDGSFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSFHKPASDPGS
Enzyme 57 Number of Residues 534
Enzyme 57 Molecular Weight 58156
Enzyme 57 Theoretical pI Not Available
Enzyme 57 GO Classification Not Available
Enzyme 57 General Function Not Available
Enzyme 57 Specific Function Not Available
Enzyme 57 Pathways Not Available
Enzyme 57 Reactions Not Available
Enzyme 57 Pfam Domain Function Not Available
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • None
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein Not Available
Enzyme 57 UniProtKB/Swiss-Prot ID B2RAZ9 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name B2RAZ9_HUMAN Link Image
Enzyme 57 PDB ID Not Available
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence Not Available
Enzyme 57 GenBank Gene ID Not Available
Enzyme 57 GeneCard ID B2RAZ9 Link Image
Enzyme 57 GenAtlas ID Not Available
Enzyme 57 HGNC ID Not Available
Enzyme 57 Chromosome Location Not Available
Enzyme 57 Locus Not Available
Enzyme 57 SNPs Not Available
Enzyme 57 General References Not Available
Enzyme 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 15189
Enzyme 58 Name GGT7 protein
Enzyme 58 Synonyms Not Available
Enzyme 58 Gene Name GGT7
Enzyme 58 Protein Sequence >GGT7 protein
MAAENEASQESALGAYSPVDYMSITSFPRLPEDEPAPAAPLRGRKDEDAFLGDPDTDPDS
FLKSARLQRLPSSSSEMGSQDGSPLRETRKDPFSAAAAECSCRQDGLTVIVTACLTFATG
VTVALVMQIYFGDPQIFQQGAVVTDAARCTSLGIEVLSKQGSSVDAAVAAALCLGIVAPH
SSGLGGGGVMLVHDIRRNESHLIDFRESAPGALREETLQRSWETKPGLLVGVPGMVKGLH
EAHQLYGRLPWSQVLAFAAAVAQDGFNVTHDLARALAEQLPPNMSERFRETFLPSGRPPL
PGSLLHRPDLAEVLDVLGTSGPAAFYAGGNLTLEMVAEAQHAGGVITEEDFSNYSALVEK
PVCGVYRGHLVLSPPPPHTGPALISALNILEGFNLTSLVSREQALHWVAETLKIALALAS
RLGDPVYDSTITESMDDMLSKVEAAYLRGHINDSQAAPAPLLPVYELDGAPTAAQVLIMG
PDDFIVAMVSSLNQPFGSGLITPSGILLNSQMLDFSWPNRTANHSAPSLENSVQPGKRPL
SFLLPTVVRPAEGLCGTYLALGANGAARGLSGLTQVLLNVLTLNRNLSDSLA
Enzyme 58 Number of Residues 592
Enzyme 58 Molecular Weight 62565.3
Enzyme 58 Theoretical pI 4.64
Enzyme 58 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
Component
Enzyme 58 General Function Involved in gamma-glutamyltransferase activity
Enzyme 58 Specific Function Not Available
Enzyme 58 Pathways Not Available
Enzyme 58 Reactions Not Available
Enzyme 58 Pfam Domain Function
Enzyme 58 Signals
  • None
Enzyme 58 Transmembrane Regions
  • None
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein 118600847 Link Image
Enzyme 58 UniProtKB/Swiss-Prot ID A0PJJ9 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name A0PJJ9_HUMAN Link Image
Enzyme 58 PDB ID Not Available
Enzyme 58 Cellular Location Not Available
Enzyme 58 Gene Sequence >1777 bp
ATGGCGGCGGAGAACGAGGCCAGCCAGGAGAGCGCCCTGGGCGCCTACTCGCCAGTGGAC
TACATGAGCATCACCAGCTTCCCGCGGCTGCCCGAGGACGAGCCGGCGCCCGCGGCCCCG
CTGAGGGGCCGCAAGGACGAGGACGCCTTTCTGGGAGACCCCGACACCGACCCGGACTCC
TTCCTGAAGTCTGCACGGCTGCAGCGGCTGCCATCGTCGTCGTCGGAGATGGGCAGCCAA
GACGGGTCGCCGCTACGCGAGACGCGCAAAGACCCGTTCTCCGCCGCAGCGGCCGAGTGC
TCCTGCCGCCAGGATGGGCTCACGGTCATCGTCACGGCCTGTCTCACCTTCGCTACCGGT
GTCACCGTGGCGCTGGTCATGCAGATCTACTTCGGGGACCCCCAGATCTTCCAGCAGGGT
GCCGTGGTGACCGATGCTGCCCGCTGCACTTCACTGGGCATCGAGGTGCTCAGTAAACAG
GGATCTTCTGTGGACGCAGCGGTGGCAGCAGCCTTGTGTTTGGGTATCGTGGCTCCACAC
AGTTCTGGCCTGGGCGGTGGGGGCGTGATGCTGGTACATGACATCCGACGAAATGAGAGC
CACCTAATTGATTTCCGGGAGTCCGCACCAGGGGCCCTCAGGGAAGAGACCCTGCAAAGA
TCCTGGGAGACCAAGCCTGGGCTCTTGGTGGGGGTTCCCGGAATGGTGAAAGGGCTACAT
GAAGCTCACCAGCTCTATGGCAGGCTGCCATGGTCCCAAGTCCTGGCCTTTGCAGCAGCT
GTGGCCCAAGATGGCTTCAACGTGACTCATGATCTAGCCCGTGCCCTGGCTGAACAGCTG
CCACCCAACATGTCCGAGCGCTTCCGGGAGACGTTCCTGCCATCGGGCCGCCCGCCACTA
CCTGGCTCGTTGCTGCATCGGCCCGACCTGGCTGAGGTGCTGGATGTACTTGGCACCTCC
GGCCCGGCTGCCTTCTACGCAGGTGGCAACCTCACACTGGAGATGGTGGCCGAGGCTCAG
CACGCAGGGGGTGTCATAACCGAAGAGGACTTCAGCAATTACAGCGCCCTTGTGGAGAAG
CCTGTGTGTGGCGTGTACAGAGGCCACCTGGTTCTTAGTCCCCCACCTCCGCACACGGGC
CCTGCCCTCATCAGTGCTCTCAACATCCTGGAGGGCTTCAATCTCACCAGCCTGGTATCC
CGAGAACAGGCTCTTCACTGGGTGGCAGAGACCCTGAAGATTGCATTAGCCCTGGCCAGC
AGACTGGGAGATCCCGTCTATGATTCTACCATCACTGAGAGCATGGATGACATGCTCAGC
AAGGTGGAGGCCGCCTACCTCCGGGGCCATATCAATGACTCCCAGGCAGCCCCTGCCCCA
CTCCTGCCTGTCTATGAACTAGACGGAGCTCCCACGGCTGCCCAGGTGCTGATCATGGGA
CCTGATGACTTCATTGTGGCCATGGTTAGCTCCCTGAACCAGCCCTTTGGCAGCGGCCTT
ATCACCCCCTCGGGGATCCTGCTCAACAGCCAGATGCTGGACTTCTCCTGGCCCAACCGG
ACAGCTAACCACTCTGCACCCAGCCTGGAGAATTCAGTGCAGCCAGGGAAGCGGCCACTC
TCTTTCCTGCTGCCCACAGTGGTCCGACCCGCGGAGGGGCTCTGTGGAACCTACCTCGCT
CTGGGGGCCAATGGAGCTGCGCGGGGCCTCAGCGGCCTGACACAGGTTCTGCTGAATGTC
CTGACCTTGAACCGGAACCTGAGTGACAGCCTGGCCC
Enzyme 58 GenBank Gene ID BC033745 Link Image
Enzyme 58 GeneCard ID GGT7 Link Image
Enzyme 58 GenAtlas ID GGT7 Link Image
Enzyme 58 HGNC ID HGNC:4259 Link Image
Enzyme 58 Chromosome Location 2
Enzyme 58 Locus 20q11.22
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 15190
Enzyme 59 Name Gamma-glutamyltransferase 5
Enzyme 59 Synonyms Not Available
Enzyme 59 Gene Name GGT5
Enzyme 59 Protein Sequence >Gamma-glutamyltransferase 5
MARGYGATVSLVLLGLGLALAVIVLAVVLSRHQAPCGPQAFAHAAVAADSKVCSDIGRAI
LQQQGSPVDATIAALVCTSVVNPQSMGLGGGVIFTIYNVTTGKVEVINARETVPASHAPS
LLDQCAQALPLGTGAQWIGVPGELRGYAEAHRRHGRLPWAQLFQPTIALLRGGHVVAPVL
SRFLHNSILRPSLQASTLRQLFFNGTEPLRPQDPLPWPALATTLETVATEGVEVFYTGRL
GQMLVEDIAKEGSQLTLQDLAKFQPEVVDALEVPLGDYTLYSPPPPAGGAILSFILNVLR
GFNFSTESMARPEGRVNVYHHLVETLKFAKGQRWRLGDPRSHPKLQNASRDLLGETLAQL
IRQQIDGRGDHQLSHYSLAEAWGHGTGTSHVSVLGEDGSAVAATSTINTPFGAMVYSPRT
GIILNNELLDLCERCPRGSGTTPSPAVSGDRVGGAPGRCWPPVPGERSPSSMVPSILINK
AQGSKLVIGGAGGELIISAVAQAIMSKLWLGFDLRAAIAAPILHVNSKGCVEYEPNFSQE
VQRGLQDRGQNQTQRPFFLNVVQAVSQEGACVYAVSDLRKSGEAAGY
Enzyme 59 Number of Residues 587
Enzyme 59 Molecular Weight 62331.8
Enzyme 59 Theoretical pI 7.59
Enzyme 59 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
Component
Enzyme 59 General Function Involved in gamma-glutamyltransferase activity
Enzyme 59 Specific Function Not Available
Enzyme 59 Pathways Not Available
Enzyme 59 Reactions Not Available
Enzyme 59 Pfam Domain Function
Enzyme 59 Signals
  • None
Enzyme 59 Transmembrane Regions
  • None
Enzyme 59 Essentiality Not Available
Enzyme 59 GenBank ID Protein 49256405 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID Q6GMP0 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name Q6GMP0_HUMAN Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence >1764 bp
ATGGCCCGGGGCTACGGGGCCACGGTCAGCCTAGTCCTGCTGGGTCTGGGGCTGGCGCTG
GCTGTCATTGTGCTGGCTGTGGTCCTCTCTCGACACCAGGCCCCATGTGGCCCCCAGGCC
TTTGCCCACGCTGCTGTTGCCGCCGACTCCAAGGTCTGCTCGGATATTGGACGAGCCATC
CTCCAGCAGCAGGGCTCACCCGTGGATGCCACCATCGCGGCTCTGGTCTGCACCAGCGTC
GTCAACCCTCAGAGCATGGGCCTGGGCGGAGGGGTCATCTTCACCATCTACAATGTGACA
ACAGGGAAGGTGGAGGTCATCAATGCCCGGGAGACGGTGCCGGCCAGCCACGCCCCGAGC
CTGCTGGACCAGTGTGCACAGGCTCTGCCACTGGGCACAGGGGCCCAGTGGATCGGGGTG
CCCGGGGAGCTCCGTGGCTATGCCGAGGCCCACCGCCGCCATGGCCGCCTGCCCTGGGCG
CAGCTGTTCCAGCCCACCATCGCGCTGCTCCGAGGGGGGCATGTGGTGGCCCCTGTCCTC
AGCCGTTTCCTGCACAACAGCATCCTGCGGCCTTCCTTGCAGGCGTCAACCCTGCGCCAG
CTCTTCTTCAACGGGACAGAACCCCTGAGGCCTCAGGACCCACTCCCATGGCCTGCACTG
GCCACCACCCTGGAGACCGTGGCCACAGAGGGCGTGGAGGTCTTCTACACGGGGAGGCTG
GGCCAGATGCTGGTGGAGGACATTGCCAAGGAAGGGAGCCAGCTGACGCTGCAGGACCTG
GCCAAGTTCCAGCCCGAGGTGGTGGATGCCCTGGAGGTGCCCCTGGGGGACTATACCCTG
TACTCACCACCGCCGCCTGCAGGGGGTGCCATTCTCAGCTTTATCCTCAACGTGCTAAGA
GGGTTCAACTTCTCAACAGAGTCTATGGCCAGGCCTGAAGGGAGGGTGAACGTGTACCAC
CACCTTGTAGAGACGCTCAAGTTTGCCAAGGGGCAGAGGTGGAGGCTGGGGGACCCTCGA
AGCCACCCGAAGCTCCAGAATGCCTCCCGGGACCTGCTGGGGGAGACCCTGGCCCAGCTC
ATCCGCCAACAGATCGATGGCCGGGGGGACCACCAGCTCAGCCACTACAGCTTGGCCGAG
GCCTGGGGCCACGGGACAGGCACGTCCCATGTGTCTGTGCTGGGGGAGGATGGCAGCGCC
GTGGCTGCCACCAGCACCATCAACACACCCTTTGGAGCGATGGTGTATTCACCACGGACA
GGCATCATCCTCAACAACGAGCTCCTGGACTTATGCGAGCGATGCCCCCGGGGTTCCGGC
ACCACCCCCTCACCTGCAGTGAGTGGAGACAGGGTGGGTGGAGCTCCCGGAAGGTGCTGG
CCCCCAGTTCCAGGCGAGCGTTCCCCATCCTCCATGGTGCCCTCCATCTTGATCAACAAA
GCCCAGGGGTCGAAGCTAGTGATTGGCGGGGCTGGCGGGGAGCTCATCATCTCTGCTGTG
GCCCAGGCCATCATGAGCAAGCTGTGGCTTGGCTTTGACCTGAGAGCGGCCATTGCAGCC
CCCATCCTGCATGTCAACAGCAAGGGCTGTGTGGAGTACGAGCCCAACTTCAGCCAGGAG
GTGCAGAGGGGACTCCAAGACCGTGGCCAGAACCAGACCCAGAGGCCCTTCTTCCTGAAC
GTGGTCCAGGCTGTGTCCCAGGAGGGGGCCTGTGTGTACGCCGTCTCGGACCTGAGGAAG
AGTGGGGAGGCCGCAGGCTACTAA
Enzyme 59 GenBank Gene ID BC073999 Link Image
Enzyme 59 GeneCard ID GGT5 Link Image
Enzyme 59 GenAtlas ID GGT5 Link Image
Enzyme 59 HGNC ID HGNC:4260 Link Image
Enzyme 59 Chromosome Location 2
Enzyme 59 Locus 22q11.23
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 15222
Enzyme 60 Name Putative uncharacterized protein GFPT1
Enzyme 60 Synonyms Not Available
Enzyme 60 Gene Name GFPT1
Enzyme 60 Protein Sequence >Putative uncharacterized protein GFPT1
MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWEANACKIQLI
KKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIV
IHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDNRESQDTSFTTLVERVIQQ
LEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEHKLSTDHIPILYRTGKDKKGSCNLSR
VDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGD
HPGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHI
KEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFL
SQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTS
QFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSV
LIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYA
KCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHL
AVLRGYDVDFPRNLAKSVTVE
Enzyme 60 Number of Residues 681
Enzyme 60 Molecular Weight 76760
Enzyme 60 Theoretical pI 6.84
Enzyme 60 GO Classification
Function
  • binding
  • carbohydrate binding
  • catalytic activity
  • glutamine-fructose-6-phosphate transaminase (isomerizing) activity
  • sugar binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • carbohydrate biosynthesis
  • carbohydrate metabolism
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 60 General Function Cell wall/membrane/envelope biogenesis
Enzyme 60 Specific Function Not Available
Enzyme 60 Pathways Not Available
Enzyme 60 Reactions Not Available
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • None
Enzyme 60 Transmembrane Regions
  • None
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein 62822278 Link Image
Enzyme 60 UniProtKB/Swiss-Prot ID Q53QE6 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name Q53QE6_HUMAN Link Image
Enzyme 60 PDB ID Not Available
Enzyme 60 Cellular Location Not Available
Enzyme 60 Gene Sequence >2046 bp
ATGTGTGGTATATTTGCTTACTTAAACTACCATGTTCCTCGAACGAGACGAGAAATCCTG
GAGACCCTAATCAAAGGCCTTCAGAGACTGGAGTACAGAGGATATGATTCTGCTGGTGTG
GGATTTGATGGAGGCAATGATAAAGATTGGGAAGCCAATGCCTGCAAAATCCAGCTTATT
AAGAAGAAAGGAAAAGTTAAGGCACTGGATGAAGAAGTTCACAAGCAACAAGATATGGAT
TTGGATATAGAATTTGATGTACACCTTGGAATAGCTCATACCCGTTGGGCAACACATGGA
GAACCCAGTCCTGTCAATAGCCACCCCCAGCGCTCTGATAAAAATAATGAATTTATCGTT
ATTCACAATGGAATCATCACCAACTACAAAGACTTGAAAAAGTTTTTGGAAAGCAAAGGC
TATGACTTCGAATCTGAAACAGACACAGAGACAATTGCCAAGCTCGTTAAGTATATGTAT
GACAATCGGGAAAGTCAAGATACCAGCTTTACTACCTTGGTGGAGAGAGTTATCCAACAA
TTGGAAGGTGCTTTTGCACTTGTGTTTAAAAGTGTTCATTTTCCCGGGCAAGCAGTTGGC
ACAAGGCGAGGTAGCCCTCTGTTGATTGGTGTACGGAGTGAACATAAACTTTCTACTGAT
CACATTCCTATACTCTACAGAACAGGCAAAGACAAGAAAGGAAGCTGCAATCTCTCTCGT
GTGGACAGCACAACCTGCCTTTTCCCGGTGGAAGAAAAAGCAGTGGAGTATTACTTTGCT
TCTGATGCAAGTGCTGTCATAGAACACACCAATCGCGTCATCTTTCTGGAAGATGATGAT
GTTGCAGCAGTAGTGGATGGACGTCTTTCTATCCATCGAATTAAACGAACTGCAGGAGAT
CACCCCGGACGAGCTGTGCAAACACTCCAGATGGAACTCCAGCAGATCATGAAGGGCAAC
TTCAGTTCATTTATGCAGAAGGAAATATTTGAGCAGCCAGAGTCTGTCGTGAACACAATG
AGAGGAAGAGTCAACTTTGATGACTATACTGTGAATTTGGGTGGTTTGAAGGATCACATA
AAGGAGATCCAGAGATGCCGGCGTTTGATTCTTATTGCTTGTGGAACAAGTTACCATGCT
GGTGTAGCAACACGTCAAGTTCTTGAGGAGCTGACTGAGTTGCCTGTGATGGTGGAACTA
GCAAGTGACTTCCTGGACAGAAACACACCAGTCTTTCGAGATGATGTTTGCTTTTTCCTT
AGTCAATCAGGTGAGACAGCAGATACTTTGATGGGTCTTCGTTACTGTAAGGAGAGAGGA
GCTTTAACTGTGGGGATCACAAACACAGTTGGCAGTTCCATATCACGGGAGACAGATTGT
GGAGTTCATATTAATGCTGGTCCTGAGATTGGTGTGGCCAGTACAAAGGCTTATACCAGC
CAGTTTGTATCCCTTGTGATGTTTGCCCTTATGATGTGTGATGATCGGATCTCCATGCAA
GAAAGACGCAAAGAGATCATGCTTGGATTGAAACGGCTGCCTGATTTGATTAAGGAAGTA
CTGAGCATGGATGACGAAATTCAGAAACTAGCAACAGAACTTTATCATCAGAAGTCAGTT
CTGATAATGGGACGAGGCTATCATTATGCTACTTGTCTTGAAGGGGCACTGAAAATCAAA
GAAATTACTTATATGCACTCTGAAGGCATCCTTGCTGGTGAATTGAAACATGGCCCTCTG
GCTTTGGTGGATAAATTGATGCCTGTGATCATGATCATCATGAGAGATCACACTTATGCC
AAGTGTCAGAATGCTCTTCAGCAAGTGGTTGCTCGGCAGGGGCGGCCTGTGGTAATTTGT
GATAAGGAGGATACTGAGACCATTAAGAACACAAAAAGAACGATCAAGGTGCCCCACTCA
GTGGACTGCTTGCAGGGCATTCTCAGCGTGATCCCTTTACAGTTGCTGGCTTTCCACCTT
GCTGTGCTGAGAGGCTATGATGTTGATTTCCCACGGAATCTTGCCAAATCTGTGACTGTA
GAGTGA
Enzyme 60 GenBank Gene ID AC114772 Link Image
Enzyme 60 GeneCard ID Q53QE6 Link Image
Enzyme 60 GenAtlas ID GFPT1 Link Image
Enzyme 60 HGNC ID HGNC:4241 Link Image
Enzyme 60 Chromosome Location Not Available
Enzyme 60 Locus Not Available
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 General References Not Available
Enzyme 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 15223
Enzyme 61 Name cDNA FLJ75059, highly similar to Homo sapiens phosphoribosylformylglycinamidine synthase (FGAR amidotransferase) (PFAS), mRNA
Enzyme 61 Synonyms Not Available
Enzyme 61 Gene Name Not Available
Enzyme 61 Protein Sequence >cDNA FLJ75059, highly similar to Homo sapiens phosphoribosylformylglycinamidine synthase (FGAR amidotransferase) (PFAS), mRNA
MSPVLHFYVRPSGHEGAAPGHTRRKLQGKLPELQGVETELCYNVNWTAEALPSAEETKKL
MWLFGCPLLLDDVARESWLLPGSNDLLLEVGPRLNFSTPTSTNIVSVCRATGLGPVDRVE
TTRRYRLSFAHPPSAEVEAIALATLHDRMTEQHFPHPIQSFSPESMPEPLNGPINILGEG
RLALEKANQELGLALDSWDLDFYTKRFQELQRNPSTVEAFDLAQSNSEHSRHWFFKGQLH
VDGQKLVHSLFESIMSTQESSNPNNVLKFCDNSSAIQGKEVRFLRPEDPTRPSRFQQQQG
LRHVVFTAETHNFPTGVCPFSGATTGTGGRIRDVQCTGRGAHVVAGTAGYCFGNLHIPGY
NLPWEDPSFQYPGNFARPLEVAIEASNGASDYGNKFGEPVLAGFARSLGLQLPDGQRREW
IKPIMFSGGIGSMEADHISKEAPEPGMEVVKVGGPVYRIGVGGGAASSVQVQGDNTSDLD
FGAVQRGDPEMEQKMNRVIRACVEAPKGNPICSLHDQGAGGNGNVLKELSDPAGAIIYTS
RFQLGDPTLNALEIWGAEYQESNALLLRSPNRDFLTHVSARERCPACFVGTITGDRRIVL
VDDRECPVRRNGQGDAPPTPLPTPVDLELGWVLGKMPRKEFFLQRKPPMLQPLALPPGLS
VHQALERVLRLPAVASKRYLTNKVDRSVGGLVAQQQCVGPLQTPLADVAVVALSHEELIG
AATALGEQPVKSLLDPKVAARLAVAEALTNLVFALVTDLRDVKCSGNWMWAAKLPGEGAA
LADACEAMVAVMAALGVAVDGGKDSLSMAARVGTETVRAPGSLVISAYAVCPDITATVTP
DLKHPEGRGHLLYVALSPGQHRLGGTALAQCFSQLGEHPPDLDLPENLVRAFSITQGLLK
DRLLCSGHDVSDGGLVTCLLEMAFAGNCGLQVDVPVPRVDVLSVLFAEEPGLVLEVQEPD
LAQVLKRYRDAGLHCLELGHTGEAGPHAMVRVSVNGAVVLEEPVGELRALWEETSFQLDR
LQAEPRCVAEEERGLRERMGPSYCLPPTFPKASVPREPGGPSPRVAILREEGSNGDREMA
DAFHLAGFEVWDVTMQDLCSGAIGLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFHPRAG
AELRRFRKRPDTFSLGVCNGCQLLALLGWVGGDPNEDAAEMGPDSQPARPGLLLHHNLSG
RYESRWASVRVGPGPALMLRGMEGAVLPVWSAHGEGYVAFSSPELQAQIEARGLAPLHWA
DDDGNPTEQYPLNPNGSPGGVAGICSCDGRHLAVMPHPERAVRPWQWAWRPPPFDTLTTS
PWLQLFINARNWTLEGSC
Enzyme 61 Number of Residues 1338
Enzyme 61 Molecular Weight 144642.1
Enzyme 61 Theoretical pI 5.60
Enzyme 61 GO Classification
Function
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • phosphoribosylformylglycinamidine synthase activity
Process
  • 'de novo' IMP biosynthetic process
  • IMP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside monophosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside monophosphate biosynthetic process
Component
Enzyme 61 General Function Involved in catalytic activity
Enzyme 61 Specific Function Not Available
Enzyme 61 Pathways Not Available
Enzyme 61 Reactions Not Available
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • None
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein 158259069 Link Image
Enzyme 61 UniProtKB/Swiss-Prot ID A8K9T9 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name A8K9T9_HUMAN Link Image
Enzyme 61 PDB ID Not Available
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence >4017 bp
ATGTCCCCAGTCCTTCACTTCTATGTTCGTCCCTCTGGCCATGAGGGGGCAGCCCCTGGA
CACACTCGGAGGAAACTGCAAGGGAAACTGCCAGAGCTGCAGGGCGTCGAGACTGAACTG
TGCTACAACGTGAACTGGACAGCTGAGGCCCTCCCCAGTGCTGAGGAGACAAAGAAGCTG
ATGTGGCTGTTTGGTTGCCCCTTACTGCTGGATGATGTTGCTCGGGAGTCCTGGCTCCTT
CCTGGCTCCAATGACCTGCTGCTGGAGGTCGGGCCCAGGCTGAACTTCTCCACCCCAACA
TCCACCAACATCGTGTCAGTGTGCCGCGCCACTGGGCTGGGGCCTGTGGATCGTGTGGAG
ACCACCCGGCGCTACCGGCTCTCGTTTGCCCACCCCCCGTCAGCTGAGGTGGAAGCCATT
GCTCTGGCTACCCTGCACGACCGGATGACAGAGCAGCACTTCCCCCATCCCATCCAGAGT
TTCTCCCCTGAGAGCATGCCGGAACCCCTCAATGGCCCTATCAATATACTGGGTGAGGGC
CGGCTTGCGCTGGAGAAGGCCAACCAGGAGCTTGGTCTGGCTTTAGACTCTTGGGACCTA
GACTTCTACACCAAGCGCTTCCAGGAGCTACAGCGGAACCCGAGCACTGTGGAGGCCTTT
GACTTGGCGCAGTCCAATAGCGAGCACAGCCGACACTGGTTCTTCAAGGGCCAGCTCCAC
GTGGATGGGCAGAAGCTGGTGCACTCACTGTTTGAGTCCATCATGAGCACCCAGGAATCC
TCGAACCCCAACAACGTCCTCAAATTCTGTGATAACAGCAGTGCAATCCAGGGAAAGGAA
GTCCGATTCCTACGGCCTGAGGACCCCACACGGCCAAGCCGCTTCCAGCAACAGCAAGGG
CTGAGACATGTTGTCTTCACAGCAGAGACTCACAACTTTCCCACAGGAGTATGCCCCTTT
AGTGGTGCAACCACTGGCACAGGGGGCCGGATTCGAGATGTCCAGTGCACAGGCCGCGGG
GCCCACGTGGTGGCTGGCACTGCCGGCTATTGCTTTGGAAATCTGCATATTCCAGGTTAC
AATCTGCCCTGGGAGGATCCAAGCTTCCAGTATCCTGGGAATTTTGCCCGGCCCCTGGAG
GTTGCCATTGAAGCCAGTAATGGAGCTTCTGACTATGGCAACAAGTTTGGGGAACCAGTG
CTGGCTGGCTTCGCCCGCTCCTTGGGCCTCCAGCTCCCAGACGGCCAGCGGCGTGAGTGG
ATCAAGCCCATCATGTTTAGTGGGGGCATTGGGTCCATGGAAGCTGACCACATAAGCAAG
GAGGCCCCAGAGCCAGGCATGGAAGTTGTAAAGGTTGGAGGTCCCGTCTACAGGATTGGA
GTTGGAGGTGGAGCTGCTTCATCTGTGCAGGTGCAGGGAGATAACACCAGTGACCTGGAC
TTTGGGGCTGTGCAGCGAGGAGACCCGGAGATGGAACAGAAGATGAACCGTGTGATCAGG
GCTTGTGTGGAGGCCCCCAAGGGAAACCCCATCTGCAGCCTTCATGATCAGGGCGCTGGT
GGCAATGGCAATGTCCTAAAAGAGCTGAGTGACCCAGCTGGAGCCATCATTTACACCAGC
CGCTTCCAGCTTGGGGACCCAACCCTGAATGCCCTGGAAATCTGGGGGGCTGAGTACCAG
GAATCAAATGCTCTTCTGCTGAGGTCCCCCAACCGGGACTTCCTGACTCATGTCAGTGCC
CGTGAACGTTGCCCGGCTTGCTTCGTGGGCACCATCACTGGAGACCGGAGAATAGTGCTG
GTGGACGATCGGGAGTGTCCTGTCAGAAGAAATGGCCAGGGGGATGCCCCCCCGACACCC
CTGCCAACCCCTGTGGACCTGGAGCTCGGATGGGTGCTGGGCAAGATGCCTCGGAAGGAG
TTCTTCCTGCAGAGGAAGCCCCCCATGCTGCAGCCTCTGGCCTTGCCCCCAGGGCTGAGC
GTGCACCAGGCTCTGGAGAGGGTTCTGAGGCTGCCCGCCGTGGCCAGCAAGCGCTACCTC
ACCAATAAGGTGGACCGCTCTGTGGGAGGCCTGGTGGCCCAGCAGCAGTGCGTGGGGCCC
CTGCAAACTCCTCTGGCAGATGTAGCGGTTGTGGCACTGAGCCATGAGGAGCTCATAGGG
GCTGCCACAGCCTTGGGAGAACAGCCAGTCAAGAGCCTGCTGGACCCAAAAGTCGCCGCC
CGGCTGGCCGTGGCCGAAGCCCTCACCAACCTGGTGTTTGCTCTGGTCACTGACCTCCGG
GATGTGAAGTGTAGCGGGAACTGGATGTGGGCAGCCAAGCTCCCAGGGGAGGGCGCAGCT
TTGGCGGATGCCTGTGAGGCTATGGTGGCAGTGATGGCAGCCCTGGGTGTGGCAGTGGAT
GGTGGCAAGGACTCCCTCAGCATGGCTGCTCGGGTTGGCACTGAGACCGTGCGGGCTCCT
GGGTCACTGGTCATCTCAGCCTATGCCGTCTGCCCAGACATCACAGCCACTGTGACCCCA
GACCTCAAGCATCCTGAAGGGAGAGGCCATCTGCTCTATGTGGCTCTGAGCCCTGGGCAG
CACCGGCTCGGGGGCACAGCTCTGGCCCAGTGCTTCTCCCAGCTTGGGGAACACCCTCCA
GACCTGGACCTTCCTGAGAACTTGGTGCGGGCCTTCAGCATCACTCAGGGGCTGCTGAAA
GACCGCCTCCTCTGCTCAGGCCACGATGTCAGTGACGGAGGCCTCGTCACATGCCTGCTG
GAGATGGCCTTTGCTGGAAATTGCGGGCTACAGGTGGATGTGCCTGTCCCCAGGGTTGAT
GTCCTGTCTGTGCTGTTCGCTGAGGAGCCAGGCCTCGTGCTGGAGGTGCAGGAGCCAGAC
CTGGCCCAGGTGCTGAAGCGTTACCGGGATGCTGGCCTCCATTGCCTGGAGCTGGGCCAC
ACAGGCGAGGCCGGGCCCCACGCCATGGTCCGGGTGTCAGTGAACGGGGCTGTGGTTCTG
GAGGAGCCTGTTGGGGAGCTGCGAGCCCTCTGGGAGGAGACGAGTTTCCAGCTGGACCGG
CTACAGGCAGAGCCTCGCTGTGTGGCAGAGGAGGAACGGGGCCTGAGGGAGCGGATGGGG
CCCAGCTATTGCCTGCCCCCCACCTTTCCCAAAGCCTCCGTGCCCCGTGAGCCTGGTGGT
CCCAGCCCCCGAGTCGCCATCTTGCGAGAGGAGGGCAGTAATGGAGACCGGGAGATGGCC
GATGCCTTCCACTTAGCTGGGTTTGAGGTATGGGACGTGACCATGCAGGACCTCTGCTCT
GGGGCAATTGGGCTGGACACTTTCCGTGGCGTGGCCTTCGTGGGCGGCTTCAGCTATGCA
GATGTCCTGGGCTCTGCCAAAGGGTGGGCAGCTGCTGTGACCTTTCATCCCAGGGCTGGG
GCTGAGCTGAGGCGCTTCCGGAAGCGGCCAGACACCTTCAGCCTGGGCGTGTGTAATGGC
TGTCAACTGCTGGCTCTGCTCGGCTGGGTGGGAGGCGACCCCAATGAGGATGCTGCAGAG
ATGGGCCCTGACTCCCAGCCAGCCCGGCCAGGCCTTCTGCTACACCACAACCTGTCTGGG
CGCTACGAGTCTCGCTGGGCCAGCGTGCGTGTGGGGCCTGGGCCAGCCCTGATGCTGCGA
GGGATGGAGGGCGCCGTGCTGCCCGTGTGGAGTGCGCACGGGGAAGGTTACGTAGCATTT
TCTTCTCCGGAACTCCAAGCTCAGATTGAGGCCAGGGGCTTGGCTCCACTGCACTGGGCT
GATGATGACGGGAACCCCACAGAGCAGTACCCTCTGAATCCCAATGGGTCCCCAGGGGGC
GTGGCTGGCATCTGCTCCTGTGATGGCCGCCACCTGGCTGTCATGCCTCACCCTGAGCGG
GCCGTTAGGCCTTGGCAGTGGGCATGGCGACCCCCTCCATTTGATACTCTGACCACCTCC
CCCTGGCTCCAGCTCTTTATCAATGCCCGAAACTGGACCCTGGAAGGGAGCTGCTGA
Enzyme 61 GenBank Gene ID AK292804 Link Image
Enzyme 61 GeneCard ID Not Available
Enzyme 61 GenAtlas ID Not Available
Enzyme 61 HGNC ID HGNC:8863 Link Image
Enzyme 61 Chromosome Location Not Available
Enzyme 61 Locus Not Available
Enzyme 61 SNPs Not Available
Enzyme 61 General References Not Available
Enzyme 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 16424
Enzyme 62 Name cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial)
Enzyme 62 Synonyms Not Available
Enzyme 62 Gene Name BCAT2
Enzyme 62 Protein Sequence >cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial)
MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKT
FTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRP
WLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSL
GVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLV
QQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQS
LLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIP
TMENGPELILRFQKELKEIQYGIRAHEWMFPV
Enzyme 62 Number of Residues 392
Enzyme 62 Molecular Weight 44288
Enzyme 62 Theoretical pI 8.82
Enzyme 62 GO Classification
Function
  • branched-chain-amino-acid transaminase activity
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • branched chain family amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
Enzyme 62 General Function Amino acid transport and metabolism
Enzyme 62 Specific Function Not Available
Enzyme 62 Pathways Not Available
Enzyme 62 Reactions Not Available
Enzyme 62 Pfam Domain Function
Enzyme 62 Signals
  • None
Enzyme 62 Transmembrane Regions
  • None
Enzyme 62 Essentiality Not Available
Enzyme 62 GenBank ID Protein Not Available
Enzyme 62 UniProtKB/Swiss-Prot ID B2RB87 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name B2RB87_HUMAN Link Image
Enzyme 62 PDB ID 1KTA Link Image
Enzyme 62 PDB File Show
Enzyme 62 3D Structure
Enzyme 62 Cellular Location Not Available
Enzyme 62 Gene Sequence Not Available
Enzyme 62 GenBank Gene ID AK314548 Link Image
Enzyme 62 GeneCard ID B2RB87 Link Image
Enzyme 62 GenAtlas ID Not Available
Enzyme 62 HGNC ID Not Available
Enzyme 62 Chromosome Location 19
Enzyme 62 Locus 19q13
Enzyme 62 SNPs SNPJam Report Link Image
Enzyme 62 General References Not Available
Enzyme 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 16463
Enzyme 63 Name cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
Enzyme 63 Synonyms
  1. SubName: cDNA FLJ43358 fis, clone NT2RP7014005, highly similar to CTP synthase 2 (EC 6.3.4.2)
  2. SubName: CTP synthase II, isoform CRA_a
Enzyme 63 Gene Name CTPS2
Enzyme 63 Protein Sequence >cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFV
LNDGGEVDLDLGNYERFLDINLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDA
VQEWVMNQAKVPVDGNKEEPQICVIELGGTIGDIEGMPFVEAFRQFQFKAKRENFCNIHV
SLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ
VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSASNLLFKWRNMADRYERLQKICS
IALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEKITETEDPVKFHEAWQK
LCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCLGMQLAVIEFARNCLNLKDAD
STEFRPNAPVPLVIDMPEHNPGNLGGTMRLGIRRTVFKTENSILRKLYGDVPFIEERHRH
RFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPY
LGLLLAATGNLNAYLQQGCKLSSSDRYSDASDDSFSEPRIAELEIS
Enzyme 63 Number of Residues 586
Enzyme 63 Molecular Weight 65678
Enzyme 63 Theoretical pI 6.91
Enzyme 63 GO Classification
Function
  • CTP synthase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • pyrimidine nucleotide biosynthesis
  • pyrimidine nucleotide metabolism
Component
Enzyme 63 General Function Nucleotide transport and metabolism
Enzyme 63 Specific Function Not Available
Enzyme 63 Pathways Not Available
Enzyme 63 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571] ALL_REAC R00571
  • (other) R00573
Enzyme 63 Pfam Domain Function
Enzyme 63 Signals
  • None
Enzyme 63 Transmembrane Regions
  • None
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein Not Available
Enzyme 63 UniProtKB/Swiss-Prot ID B3KWM2 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name B3KWM2_HUMAN Link Image
Enzyme 63 PDB ID Not Available
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence Not Available
Enzyme 63 GenBank Gene ID AK125332 Link Image
Enzyme 63 GeneCard ID B3KWM2 Link Image
Enzyme 63 GenAtlas ID Not Available
Enzyme 63 HGNC ID Not Available
Enzyme 63 Chromosome Location Not Available
Enzyme 63 Locus Not Available
Enzyme 63 SNPs SNPJam Report Link Image
Enzyme 63 General References Not Available
Enzyme 63 Metabolite References Not Available
Enzyme 64 [top]
Enzyme 64 ID 16502
Enzyme 64 Name cDNA, FLJ93078, Homo sapiens glutamic-oxaloacetic transaminase 1, soluble(aspartate aminotransferase 1) (GOT1), mRNA (Glutamic-oxaloacetic transaminase 1, soluble (Aspartate aminotransferase 1), isoform CRA_b)
Enzyme 64 Synonyms Not Available
Enzyme 64 Gene Name GOT1
Enzyme 64 Protein Sequence >cDNA, FLJ93078, Homo sapiens glutamic-oxaloacetic transaminase 1, soluble(aspartate aminotransferase 1) (GOT1), mRNA (Glutamic-oxaloacetic transaminase 1, soluble (Aspartate aminotransferase 1), isoform CRA_b)
MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQK
IANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFL
ARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLEN
APEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWA
IRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPP
AQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGM
FSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ
Enzyme 64 Number of Residues 413
Enzyme 64 Molecular Weight 46248
Enzyme 64 Theoretical pI 7.01
Enzyme 64 GO Classification
Function
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • biosynthesis
  • cellular metabolism
  • metabolism
  • physiological process
Component
Enzyme 64 General Function Amino acid transport and metabolism
Enzyme 64 Specific Function Not Available
Enzyme 64 Pathways Not Available
Enzyme 64 Reactions Not Available
Enzyme 64 Pfam Domain Function
Enzyme 64 Signals
  • None
Enzyme 64 Transmembrane Regions
  • None
Enzyme 64 Essentiality Not Available
Enzyme 64 GenBank ID Protein Not Available
Enzyme 64 UniProtKB/Swiss-Prot ID B2R6R7 Link Image
Enzyme 64 UniProtKB/Swiss-Prot Entry Name B2R6R7_HUMAN Link Image
Enzyme 64 PDB ID 1AJS Link Image
Enzyme 64 PDB File Show
Enzyme 64 3D Structure
Enzyme 64 Cellular Location Not Available
Enzyme 64 Gene Sequence Not Available
Enzyme 64 GenBank Gene ID AK312684 Link Image
Enzyme 64 GeneCard ID B2R6R7 Link Image
Enzyme 64 GenAtlas ID Not Available
Enzyme 64 HGNC ID Not Available
Enzyme 64 Chromosome Location 10
Enzyme 64 Locus 10q24.1-q25.1
Enzyme 64 SNPs SNPJam Report Link Image
Enzyme 64 General References Not Available
Enzyme 64 Metabolite References Not Available
Enzyme 65 [top]
Enzyme 65 ID 16503
Enzyme 65 Name cDNA, FLJ93913, Homo sapiens tyrosine aminotransferase (TAT), nuclear gene encodingmitochondrial protein, mRNA (Tyrosine aminotransferase, isoform CRA_a)
Enzyme 65 Synonyms Not Available
Enzyme 65 Gene Name TAT
Enzyme 65 Protein Sequence >cDNA, FLJ93913, Homo sapiens tyrosine aminotransferase (TAT), nuclear gene encodingmitochondrial protein, mRNA (Tyrosine aminotransferase, isoform CRA_a)
MDPYMIQMSSKGNLPSILDVHVNVGGRSSVPGKMKGRKARWSVRPSDMAKKTFNPIRAIV
DNMKVKPNPNKTMISLSIGDPTVFGNLPTDPEVTQAMKDALDSGKYNGYAPSIGFLSSRE
EIASYYHCPEAPLEAKDVILTSGCSQAIDLCLAVLANPGQNILVPRPGFSLYKTLAESMG
IEVKLYNLLPEKSWEIDLKQLEYLIDEKTACLIVNNPSNPCGSVFSKRHLQKILAVAARQ
CVPILADEIYGDMVFSDCKYEPLATLSTDVPILSCGGLAKRWLVPGWRLGWILIHDRRDI
FGNEIRDGLVKLSQRILGPCTIVQGALKSILCRTPGEFYHNTLSFLKSNADLCYGALAAI
PGLRPVRPSGAMYLMVGIEMEHFPEFENDVEFTERLVAEQSVHCLPATCFEYPNFIRVVI
TVPEVMMLEACSRIQEFCEQHYHCAEGSQEECDK
Enzyme 65 Number of Residues 454
Enzyme 65 Molecular Weight 50400
Enzyme 65 Theoretical pI 6.24
Enzyme 65 GO Classification
Function
  • 1-aminocyclopropane-1-carboxylate synthase activity
  • binding
  • carbon-sulfur lyase activity
  • catalytic activity
  • lyase activity
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
  • tyrosine transaminase activity
  • vitamin binding
Process
  • amino acid and derivative metabolism
  • amino acid catabolism
  • amino acid metabolism
  • aromatic amino acid family catabolism
  • aromatic amino acid family metabolism
  • biosynthesis
  • cellular metabolism
  • metabolism
  • physiological process
Component
Enzyme 65 General Function Amino acid transport and metabolism
Enzyme 65 Specific Function Not Available
Enzyme 65 Pathways Not Available
Enzyme 65 Reactions Not Available
Enzyme 65 Pfam Domain Function
Enzyme 65 Signals
  • None
Enzyme 65 Transmembrane Regions
  • None
Enzyme 65 Essentiality Not Available
Enzyme 65 GenBank ID Protein Not Available
Enzyme 65 UniProtKB/Swiss-Prot ID B2R8I1 Link Image
Enzyme 65 UniProtKB/Swiss-Prot Entry Name B2R8I1_HUMAN Link Image
Enzyme 65 PDB ID Not Available
Enzyme 65 Cellular Location Not Available
Enzyme 65 Gene Sequence Not Available
Enzyme 65 GenBank Gene ID AK313380 Link Image
Enzyme 65 GeneCard ID B2R8I1 Link Image
Enzyme 65 GenAtlas ID Not Available
Enzyme 65 HGNC ID Not Available
Enzyme 65 Chromosome Location 16
Enzyme 65 Locus 16q22.1
Enzyme 65 SNPs SNPJam Report Link Image
Enzyme 65 General References Not Available
Enzyme 65 Metabolite References Not Available
Enzyme 66 [top]
Enzyme 66 ID 16913
Enzyme 66 Name Aspartyl aminopeptidase
Enzyme 66 Synonyms Not Available
Enzyme 66 Gene Name DNPEP
Enzyme 66 Protein Sequence >Aspartyl aminopeptidase
MQVAMNGKARKEAVQTAAKELLKFVNRSPSPFHAVAECRNRLLQAGFSELKETEKWNIKP
ESKYFMTRNSSTIIAFAVGGQYVPGNGFSLIGAHTDSPCLRVKRRSRRSQVGFQQVGVET
YGGGIWSTWFDRDLTLAGRVIVKCPTSGRLEQQLVHVERPILRIPHLAIHLQRNINENFG
PNTEMHLVPILATAIQEELEKGTPEPGPLNAVDERHHSVLMSLLCAHLGLSPKDIVEMEL
CLADTQPAVLGGAYDEFIFAPRLDNLHSCFCALQALIDSCAGPGSLATEPHVRMVTLYDN
EEVGSESAQGAQSLLTELVLRRISASCQHPTAFEEAIPKSFMISADMAHAVHPNYLDKHE
ENHRPLFHKGPVIKVNSKQRYASNAVSEALIREVANKVKVPLQDLMVRNDTPCGTTIGPI
LASRLGLRVLDLGSPQLAMHSIREMACTTGVLQTLTLFKGFFELFPSLSHNLLVD
Enzyme 66 Number of Residues 475
Enzyme 66 Molecular Weight 52427.9
Enzyme 66 Theoretical pI 7.44
Enzyme 66 GO Classification
Function
  • aminopeptidase activity
  • binding
  • catalytic activity
  • cation binding
  • exopeptidase activity
  • hydrolase activity
  • ion binding
  • metal ion binding
  • peptidase activity
  • peptidase activity, acting on L-amino acid peptides
  • transition metal ion binding
  • zinc ion binding
Process
  • macromolecule metabolic process
  • metabolic process
  • protein metabolic process
  • proteolysis
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • organelle
  • vacuole
Enzyme 66 General Function Involved in aminopeptidase activity
Enzyme 66 Specific Function Likely to play an important role in intracellular protein and peptide metabolism
Enzyme 66 Pathways Not Available
Enzyme 66 Reactions
  • Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate
Enzyme 66 Pfam Domain Function
Enzyme 66 Signals
  • None
Enzyme 66 Transmembrane Regions
  • None
Enzyme 66 Essentiality Not Available
Enzyme 66 GenBank ID Protein Not Available
Enzyme 66 UniProtKB/Swiss-Prot ID Q9ULA0 Link Image
Enzyme 66 UniProtKB/Swiss-Prot Entry Name DNPEP_HUMAN Link Image
Enzyme 66 PDB ID Not Available
Enzyme 66 Cellular Location Not Available
Enzyme 66 Gene Sequence >1428 bp
ATGCAGGTGGCCATGAACGGTAAGGCCCGCAAAGAGGCGGTGCAGACTGCGGCTAAGGAA
CTCCTCAAGTTCGTGAACCGGAGTCCCTCTCCTTTCCATGCTGTGGCTGAATGCCGCAAC
CGCCTTCTCCAGGCTGGCTTCAGTGAACTCAAGGAGACTGAGAAATGGAATATTAAGCCC
GAGAGCAAGTACTTCATGACCAGGAACTCCTCCACCATCATAGCTTTTGCTGTAGGGGGC
CAGTACGTTCCTGGCAATGGCTTCAGCCTCATCGGGGCCCACACGGACAGCCCCTGCCTC
CGGGTGAAACGTCGGTCTCGCCGCAGCCAGGTGGGCTTCCAGCAAGTCGGTGTGGAGACC
TATGGTGGTGGGATCTGGAGCACCTGGTTTGACCGTGACCTGACTCTGGCTGGACGCGTC
ATTGTCAAGTGCCCTACCTCAGGTCGGCTGGAGCAGCAGCTGGTGCACGTGGAGCGGCCC
ATTCTTCGCATCCCACACCTGGCCATCCATCTGCAGCGAAATATCAACGAGAACTTTGGG
CCCAACACAGAGATGCATCTAGTCCCCATTCTTGCCACAGCCATCCAGGAGGAGCTGGAG
AAGGGGACTCCTGAGCCAGGGCCTCTCAATGCTGTGGATGAGCGGCACCATTCGGTCCTC
ATGTCCCTGCTCTGTGCCCATCTGGGGCTGAGCCCCAAGGACATAGTGGAGATGGAGCTC
TGCCTTGCAGACACCCAGCCTGCGGTCTTGGGTGGTGCCTATGATGAGTTCATCTTTGCT
CCTCGGCTGGACAATCTGCACAGCTGCTTCTGTGCCCTGCAGGCCTTGATAGATTCCTGT
GCAGGCCCTGGCTCCCTGGCCACAGAGCCTCACGTGCGCATGGTCACACTCTATGACAAC
GAAGAGGTGGGGTCTGAGAGTGCACAGGGAGCACAGTCACTGCTGACAGAGCTGGTGCTG
CGGCGGATCTCAGCCTCGTGCCAGCACCCGACAGCCTTCGAGGAAGCCATACCCAAGTCC
TTCATGATCAGCGCAGACATGGCCCATGCTGTGCATCCCAACTACCTGGACAAGCATGAG
GAGAACCACCGGCCTTTATTCCACAAGGGCCCCGTGATCAAGGTGAACAGCAAGCAACGC
TATGCTTCAAACGCGGTGTCAGAGGCCCTGATCCGAGAGGTGGCCAACAAAGTCAAGGTC
CCCCTGCAGGATCTCATGGTCCGGAATGACACCCCCTGTGGAACCACCATTGGACCTATC
TTGGCTTCTCGGCTGGGGCTGCGGGTGCTGGATTTAGGCAGCCCCCAACTGGCCATGCAC
TCTATCCGGGAGATGGCCTGCACCACAGGAGTCCTCCAGACCCTCACCCTCTTCAAGGGC
TTCTTTGAGCTGTTCCCTTCTCTAAGCCATAATCTCTTAGTGGATTGA
Enzyme 66 GenBank Gene ID AF005050 Link Image
Enzyme 66 GeneCard ID DNPEP Link Image
Enzyme 66 GenAtlas ID DNPEP Link Image
Enzyme 66 HGNC ID HGNC:2981 Link Image
Enzyme 66 Chromosome Location 2
Enzyme 66 Locus 2q35
Enzyme 66 SNPs SNPJam Report Link Image
Enzyme 66 General References
  1. Wilk S, Wilk E, Magnusson RP: Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidase. J Biol Chem. 1998 Jun 26;273(26):15961-70. [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. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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 66 Metabolite References Not Available
Enzyme 67 [top]
Enzyme 67 ID 17151
Enzyme 67 Name Metabotropic glutamate receptor 8
Enzyme 67 Synonyms
  1. mGluR8
Enzyme 67 Gene Name GRM8
Enzyme 67 Protein Sequence >Metabotropic glutamate receptor 8
MVCEGKRSASCPCFFLLTAKFYWILTMMQRTHSQEYAHSIRVDGDIILGGLFPVHAKGER
GVPCGELKKEKGIHRLEAMLYAIDQINKDPDLLSNITLGVRILDTCSRDTYALEQSLTFV
QALIEKDASDVKCANGDPPIFTKPDKISGVIGAAASSVSIMVANILRLFKIPQISYASTA
PELSDNTRYDFFSRVVPPDSYQAQAMVDIVTALGWNYVSTLASEGNYGESGVEAFTQISR
EIGGVCIAQSQKIPREPRPGEFEKIIKRLLETPNARAVIMFANEDDIRRILEAAKKLNQS
GHFLWIGSDSWGSKIAPVYQQEEIAEGAVTILPKRASIDGFDRYFRSRTLANNRRNVWFA
EFWEENFGCKLGSHGKRNSHIKKCTGLERIARDSSYEQEGKVQFVIDAVYSMAYALHNMH
KDLCPGYIGLCPRMSTIDGKELLGYIRAVNFNGSAGTPVTFNENGDAPGRYDIFQYQITN
KSTEYKVIGHWTNQLHLKVEDMQWAHREHTHPASVCSLPCKPGERKKTVKGVPCCWHCER
CEGYNYQVDELSCELCPLDQRPNMNRTGCQLIPIIKLEWHSPWAVVPVFVAILGIIATTF
VIVTFVRYNDTPIVRASGRELSYVLLTGIFLCYSITFLMIAAPDTIICSFRRVFLGLGMC
FSYAALLTKTNRIHRIFEQGKKSVTAPKFISPASQLVITFSLISVQLLGVFVWFVVDPPH
IIIDYGEQRTLDPEKARGVLKCDISDLSLICSLGYSILLMVTCTVYAIKTRGVPETFNEA
KPIGFTMYTTCIIWLAFIPIFFGTAQSAEKMYIQTTTLTVSMSLSASVSLGMLYMPKVYI
IIFHPEQNVQKRKRSFKAVVTAATMQSKLIQKGNDRPNGEVKSELCESLETNTSSTKTTY
ISYSNHSI
Enzyme 67 Number of Residues 908
Enzyme 67 Molecular Weight 101739.6
Enzyme 67 Theoretical pI 8.21
Enzyme 67 GO Classification
Function
  • G-protein coupled receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 67 General Function Involved in G-protein coupled receptor activity
Enzyme 67 Specific Function Receptor for glutamate. The activity of this receptor is mediated by a G-protein that inhibits adenylate cyclase activity
Enzyme 67 Pathways Not Available
Enzyme 67 Reactions Not Available
Enzyme 67 Pfam Domain Function
Enzyme 67 Signals
  • 1-33
Enzyme 67 Transmembrane Regions
  • 584-608 621-641 648-668 696-716 747-768 782-803 819-843
Enzyme 67 Essentiality Not Available
Enzyme 67 GenBank ID Protein 2435410 Link Image
Enzyme 67 UniProtKB/Swiss-Prot ID O00222 Link Image
Enzyme 67 UniProtKB/Swiss-Prot Entry Name GRM8_HUMAN Link Image
Enzyme 67 PDB ID Not Available
Enzyme 67 Cellular Location Not Available
Enzyme 67 Gene Sequence >2727 bp
ATGGTATGCGAGGGAAAGCGATCAGCCTCTTGCCCTTGTTTCTTCCTCTTGACCGCCAAG
TTCTACTGGATCCTCACAATGATGCAAAGAACTCACAGCCAGGAGTATGCCCATTCCATA
CGGGTGGATGGGGACATTATTTTGGGGGGTCTCTTCCCTGTCCACGCAAAGGGAGAGAGA
GGGGTGCCTTGTGGGGAGCTGAAGAAGGAAAAGGGGATTCACAGACTGGAGGCCATGCTT
TATGCAATTGACCAGATTAACAAGGACCCTGATCTCCTTTCCAACATCACTCTGGGTGTC
CGCATCCTCGACACGTGCTCTAGGGACACCTATGCTTTGGAGCAGTCACTAACATTCGTG
CAGGCATTAATAGAGAAAGATGCTTCGGATGTGAAGTGTGCTAATGGAGATCCACCCATT
TTCACCAAGCCCGACAAGATTTCTGGCGTCATAGGTGCTGCAGCAAGCTCCGTGTCCATC
ATGGTTGCTAACATTTTAAGACTTTTTAAGATACCTCAAATCAGCTATGCATCCACAGCC
CCAGAGCTAAGTGATAACACCAGGTATGACTTTTTCTCTGCAGTGGTTCCGCCTGACTCC
TACCAAGCCCAAGCCATGGTGGACATCGTGACAGCACTGGGATGGAATTATGTTTCTACA
CTGGCTTCTGAGGGGAACTATGGTGAGAGCGGTGTGGAGGCCTTCACCCAGATCTCGAGG
GAGATTGGTGGTGTTTGCATTGCTCAGTCACAGAAAATCCCACGTGAACCAAGACCTGGA
GAATTTGAAAAAATTATCAAACGCCTGCTGGAAACACCTAATGCTCGAGCAGTGATTATG
TTTGCCAATGAGGATGACATCAGGAGGATATTGGAAGCAGCAAAAAAACTAAACCAAAGT
GGGCATTTTCTCTGGATTGGCTCAGATAGTTGGGGATCCAAAATAGCACCTGTCTATCAG
CAGGAGGAGATTGCAGAAGGGGCTGTGACAATTTTGCCCAAACGAGCATCAATTGATGGA
TTTGATCGATACTTTAGAAGCCGAACTCTTGCCAATAATCGAAGAAATGTGTGGTTTGCA
GAATTCTGGGAGGAGAATTTTGGCTGCAAGTTAGGATCACATGGGAAAAGGAACAGTCAT
ATAAAGAAATGCACAGGGCTGGAGCGAATTGCTCGGGATTCATCTTATGAACAGGAAGGA
AAGGTCCAATTTGTAATTGATGCTGTATATTCCATGGCTTACGCCCTGCACAATATGCAC
AAAGATCTCTGCCCTGGATACATTGGCCTTTGTCCACGAATGAGTACCATTGATGGGAAA
GAGCTACTTGGTTATATTCGGGCTGTAAATTTTAATGGCAGTGCTGGCACTCCTGTCATC
TTTAATGAAAACGGAGATGCTCCTGGACGTTATGATATCTTCCAGTATCAAATAACCAAC
AAAAGCACAGAGTACAAAGTCATCGGCCACTGGACCAATCAGCTTCATCTAAAAGTGGAA
GACATGCAGTGGGCTCATAGAGAACATACTCACCCGGCGTCTGTCTGCAGCCTGCCGTGT
AAGCCAGGGGAGAGGAAGAAAACGGTGAAAGGGGTCCCTTGCTGCTGGCACTGTGAACGC
TGTGAAGGTTACAACTACCAGGTGGATGAGCTGTCCTGTGAACTTTGCCCTCTGGATCAG
AGACCCAACATGAACCGCACAGGCTGCCAGCTTATCCCCATCATCAAGTTGGAGTGGCAT
TCTCCCTGGGCTGTGGTGCCTGTGTTTGTTGCAATATTGGGAATCATCGCCACCACCTTT
GTGATCGTGACCTTTGTCCGCTATAATGACACACCTATCGTGAGGGCTTCAGGACGCGAA
CTTAGTTACGTGCTCCTAACGGGGATTTTTCTCTGTTATTCAATCACGTTTTTAATGATT
GCAGGACCAGATACAATCATATGCTCCTTCCGACGGGTCTTCCTAGGACTTGGCATGTGT
TTCAGCTATGCAGCCCTTCTGACCAAAACAAACCGTATCCACCGAATATTTGAGCAGGGG
AAGAAATCTGTCACAGCGCCCAAGTTCATTAGTCCAGCATCTCAGCTGGTGATCACCTTC
AGCCTCATCTCCGTCCAGCTCCTTGGAGTGTTTGTCTGGTTTGTTGTGGATCCCCCCCAC
ATCATCATTGACTATGGAGAGCAGCGGACACTAGATCCAGAGAAGGCCAGGGGAGTGCTC
AAGTGTGACATTTCTGATCTCTCACTCATTTGTTCACTTGGATACAGTATCCTCTTGATG
GTCACTTGTACTGTTTATGCCATTAAAACGAGAGGTGTCCCAGAGACTTTCAATGAAGCC
AAACCTATTGGATTTACCATGTATACCACCTGCATCATTTGGTTAGCTTTCATCCCCATC
TTTTTTGGTACAGCCCAGTCAGCAGAAAAGATGTACATCCAGACAACAACACTTACTGTC
TCCATGAGTTTAAGTGCTTCAGTATCTCTGGGCATGCTCTATATGCCCAAGGTTTATATT
ATAATTTTTCATCCAGAACAGAATGTTCAAAAACGCAAGAGGAGCTTCAAGGCTGTGGTG
ACAGCTGCCACCATGCAAAGCAAACTGATCCAAAAAGGAAATGACAGACCAAATGGCGAG
GTGAAAAGTGAACTCTGTGAGAGTCTTGAAACCAACACTTCCTCTACCAAGACAACATAT
ATCAGTTACACGAATCATTCAATCTGA
Enzyme 67 GenBank Gene ID U95025 Link Image
Enzyme 67 GeneCard ID GRM8 Link Image
Enzyme 67 GenAtlas ID GRM8 Link Image
Enzyme 67 HGNC ID HGNC:4600 Link Image
Enzyme 67 Chromosome Location 7
Enzyme 67 Locus 7q31.3-q32.1
Enzyme 67 SNPs SNPJam Report Link Image
Enzyme 67 General References
  1. Scherer SW, Soder S, Duvoisin RM, Huizenga JJ, Tsui LC: The human metabotropic glutamate receptor 8 (GRM8) gene: a disproportionately large gene located at 7q31.3-q32.1. Genomics. 1997 Sep 1;44(2):232-6. [PubMed Link Image]
  2. Wu S, Wright RA, Rockey PK, Burgett SG, Arnold JS, Rosteck PR Jr, Johnson BG, Schoepp DD, Belagaje RM: Group III human metabotropic glutamate receptors 4, 7 and 8: molecular cloning, functional expression, and comparison of pharmacological properties in RGT cells. Brain Res Mol Brain Res. 1998 Jan;53(1-2):88-97. [PubMed Link Image]
  3. Malherbe P, Kratzeisen C, Lundstrom K, Richards JG, Faull RL, Mutel V: Cloning and functional expression of alternative spliced variants of the human metabotropic glutamate receptor 8. Brain Res Mol Brain Res. 1999 Apr 20;67(2):201-10. [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]
Enzyme 67 Metabolite References Not Available
Enzyme 68 [top]
Enzyme 68 ID 17152
Enzyme 68 Name Metabotropic glutamate receptor 4
Enzyme 68 Synonyms
  1. mGluR4
Enzyme 68 Gene Name GRM4
Enzyme 68 Protein Sequence >Metabotropic glutamate receptor 4
MPGKRGLGWWWARLPLCLLLSLYGPWMPSSLGKPKGHPHMNSIRIDGDITLGGLFPVHGR
GSEGKPCGELKKEKGIHRLEAMLFALDRINNDPDLLPNITLGARILDTCSRDTHALEQSL
TFVQALIEKDGTEVRCGSGGPPIITKPERVVGVIGASGSSVSIMVANILRLFKIPQISYA
STAPDLSDNSRYDFFSRVVPSDTYQAQAMVDIVRALKWNYVSTVASEGSYGESGVEAFIQ
KSREDGGVCIAQSVKIPREPKAGEFDKIIRRLLETSNARAVIIFANEDDIRRVLEAARRA
NQTGHFFWMGSDSWGSKIAPVLHLEEVAEGAVTILPKRMSVRGFDRYFSSRTLDNNRRNI
WFAEFWEDNFHCKLSRHALKKGSHVKKCTNRERIGQDSAYEQEGKVQFVIDAVYAMGHAL
HAMHRDLCPGRVGLCPRMDPVDGTQLLKYIRNVNFSGIAGNPVTFNENGDAPGRYDIYQY
QLRNDSAEYKVIGSWTDHLHLRIERMHWPGSGQQLPRSICSLPCQPGERKKTVKGMPCCW
HCEPCTGYQYQVDRYTCKTCPYDMRPTENRTGCRPIPIIKLEWGSPWAVLPLFLAVVGIA
ATLFVVITFVRYNDTPIVKASGRELSYVLLAGIFLCYATTFLMIAEPDLGTCSLRRIFLG
LGMSISYAALLTKTNRIYRIFEQGKRSVSAPRFISPASQLAITFSLISLQLLGICVWFVV
DPSHSVVDFQDQRTLDPRFARGVLKCDISDLSLICLLGYSMLLMVTCTVYAIKTRGVPET
FNEAKPIGFTMYTTCIVWLAFIPIFFGTSQSADKLYIQTTTLTVSVSLSASVSLGMLYMP
KVYIILFHPEQNVPKRKRSLKAVVTAATMSNKFTQKGNFRPNGEAKSELCENLEAPALAT
KQTYVTYTNHAI
Enzyme 68 Number of Residues 912
Enzyme 68 Molecular Weight 101866.8
Enzyme 68 Theoretical pI 8.98
Enzyme 68 GO Classification
Function
  • G-protein coupled receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 68 General Function Involved in G-protein coupled receptor activity
Enzyme 68 Specific Function Receptor for glutamate. The activity of this receptor is mediated by a G-protein that inhibits adenylate cyclase activity
Enzyme 68 Pathways Not Available
Enzyme 68 Reactions Not Available
Enzyme 68 Pfam Domain Function
Enzyme 68 Signals
  • 1-32
Enzyme 68 Transmembrane Regions
  • 588-610 625-645 657-675 700-720 751-772 786-808 822-847
Enzyme 68 Essentiality Not Available
Enzyme 68 GenBank ID Protein 1160183 Link Image
Enzyme 68 UniProtKB/Swiss-Prot ID Q14833 Link Image
Enzyme 68 UniProtKB/Swiss-Prot Entry Name GRM4_HUMAN Link Image
Enzyme 68 PDB ID Not Available
Enzyme 68 Cellular Location Not Available
Enzyme 68 Gene Sequence >2739 bp
ATGCCTGGGAAGAGAGGCTTGGGCTGGTGGTGGGCCCGGCTGCCCCTTTGCCTGCTCCTC
AGCCTTTACGGCCCCTGGATGCCTTCCTCCCTGGGAAAGCCCAAAGGCCACCCTCACATG
AATTCCATCCGCATAGATGGGGACATCACACTGGGAGGCCTGTTCCCGGTGCATGGCCGG
GGCTCAGAGGGCAAGCCCTGTGGAGAACTTAAGAAGGAAAAGGGCATCCACCGGCTGGAG
GCCATGCTGTTCGCCCTGGATCGCATCAACAACGACCCGGACCTGCTGCCTAACATCACG
CTGGGCGCCCGCATTCTGGACACCTGCTCCAGGGACACCCATGCCCTCGAGCAGTCGCTG
ACCTTTGTGCAGGCGCTCATCGAGAAGGATGGCACAGAGGTCCGCTGTGGCAGTGGCGGC
CCACCCATCATCACCAAGCCTGAACGTGTGGTGGGTGTCATCGGTGCTTCAGGGAGCTCG
GTCTCCATCATGGTGGCCAACATCCTTCGCCTCTTCAAGATACCCCAGATCAGCTACGCC
TCCACAGCGCCAGACCTGAGTGACAACAGCCGCTACGACTTCTTCTCCCGCGTGGTGCCC
TCGGACACGTACCAGGCCCAGGCCATGGTGGACATCGTCCGTGCCCTCAAGTGGAACTAT
GTGTCCACAGTGGCCTCGGAGGGCAGCTATGGTGAGAGCGGTGTGGAGGCCTTCATCCAG
AAGTCCCGTGAGGACGGGGGCGTGTGCATCGCCCAGTCGGTGAAGATACCACGGGAGCCC
AAGGCAGGCGAGTTCGACAAGATCATCCGCCGCCTCCTGGAGACTTCGAACGCCAGGGCA
GTCATCATCTTTGCCAACGAGGATGACATCAGGCGTGTGCTGGAGGCAGCACGAAGGGCC
AACCAGACAGGCCATTTCTTCTGGATGGGCTCTGACAGCTGGGGCTCCAAGATTGCACCT
GTGCTGCACCTGGAGGAGGTGGCTGAGGGTGCTGTCACGATCCTCCCCAAGAGGATGTCC
GTACGAGGCTTCGACCGCTACTTCTCCAGCCGCACGCTGGACAACAACCGGCGCAACATC
TGGTTTGCCGAGTTCTGGGAGGACAACTTCCACTGCAAGCTGAGCCGCCACGCCCTCAAG
AAGGGCAGCCACGTCAAGAAGTGCACCAACCGTGAGCGAATTGGGCAGGATTCAGCTTAT
GAGCAGGAGGGGAAGGTGCAGTTTGTGATCGATGCCGTGTACGCCATGGGCCACGCGCTG
CACGCCATGCACCGTGACCTGTGTCCCGGCCGCGTGGGGCTCTGCCCGCGCATGGACCCT
GTAGATGGCACCCAGCTGCTTAAGTACATCCGAAACGTCAACTTCTCAGGCATCGCAGGG
AACCCTGTGACCTTCAATGAGAATGGAGATGCGCCTGGGCGCTATGACATCTACCAATAC
CAGCTGCGCAACGATTCTGCCGAGTACAAGGTCATTGGCTCCTGGACTGACCACCTGCAC
CTTAGAATAGAGCGGATGCACTGGCCGGGGAGCGGGCAGCAGCTGCCCCGCTCCATCTGC
AGCCTGCCCTGCCAACCGGGTGAGCGGAAGAAGACAGTGAAGGGCATGCCTTGCTGCTGG
CACTGCGAGCCTTGCACAGGGTACCAGTACCAGGTGGACCGCTACACCTGTAAGACGTGT
CCCTATGACATGCGGCCCACAGAGAACCGCACGGGCTGCCGGCCCATCCCCATCATCAAG
CTTGAGTGGGGCTCGCCCTGGGCCGTGCTGCCCCTCTTCCTGGCCGTGGTGGGCATCGCT
GCCACGTTGTTCGTGGTGATCACCTTTGTGCGCTACAACGACACGCCCATCGTCAAGGCC
TCGGGCCGTGAACTGAGCTACGTGCTGCTGGCAGGCATCTTCCTGTGCTATGCCACCACC
TTCCTCATGATCGCTGAGCCCGACCTTGGCACCTGCTCGCTGCGCCGAATCTTCCTGGGA
CTAGGGATGAGCATCAGCTATGCAGCCCTGCTCACCAAGACCAACCGCATCTACCGCATC
TTCGAGCAGGGCAAGCGCTCGGTCAGTGCCCCACGCTTCATCAGCCCCGCCTCACAGCTG
GCCATCACCTTCAGCCTCATCTCGCTGCAGCTGCTGGGCATCTGTGTGTGGTTTGTGGTG
GACCCCTCCCACTCGGTGGTGGACTTCCAGGACCAGCGGACACTCGACCCCCGCTTCGCC
AGGGGTGTGCTCAAGTGTGACATCTCGGACCTGTCGCTCATCTGCCTGCTGGGCTACAGC
ATGCTGCTCATGGTCACGTGCACCGTGTATGCCATCAAGACACGCGGCGTGCCCGAGACC
TTCAATGAGGCCAAGCCCATTGGCTTCACCATGTACACCACTTGCATCGTCTGGCTGGCC
TTCATCCCCATCTTCTTTGGCACCTCGCAGTCGGCCGACAAGCTGTACATCCAGACGACG
ACGCTGACGGTCTCGGTGAGTCTGAGCGCCTCGGTGTCCCTGGGAATGCTCTACATGCCC
AAAGTCTACATCATCCTCTTCCACCCGGAGCAGAACGTGCCCAAGCGCAAGCGCAGCCTC
AAAGCCGTCGTTACGGCGGCCACCATGTCCAACAAGTTCACGCAGAAGGGCAACTTCCGG
CCCAACGGAGAGGCCAAGTCTGAGCTCTGCGAGAACCTTGAGGCCCCAGCGCTGGCCACC
AAACAGACTTACGTCACTTACACCAACCATGCAATCTAG
Enzyme 68 GenBank Gene ID X80818 Link Image
Enzyme 68 GeneCard ID GRM4 Link Image
Enzyme 68 GenAtlas ID GRM4 Link Image
Enzyme 68 HGNC ID HGNC:4596 Link Image
Enzyme 68 Chromosome Location 6
Enzyme 68 Locus 6p21.3
Enzyme 68 SNPs SNPJam Report Link Image
Enzyme 68 General References
  1. Makoff A, Lelchuk R, Oxer M, Harrington K, Emson P: Molecular characterization and localization of human metabotropic glutamate receptor type 4. Brain Res Mol Brain Res. 1996 Apr;37(1-2):239-48. [PubMed Link Image]
  2. Wu S, Wright RA, Rockey PK, Burgett SG, Arnold JS, Rosteck PR Jr, Johnson BG, Schoepp DD, Belagaje RM: Group III human metabotropic glutamate receptors 4, 7 and 8: molecular cloning, functional expression, and comparison of pharmacological properties in RGT cells. Brain Res Mol Brain Res. 1998 Jan;53(1-2):88-97. [PubMed Link Image]
  3. Flor PJ, Lukic S, Ruegg D, Leonhardt T, Knopfel T, Kuhn R: Molecular cloning, functional expression and pharmacological characterization of the human metabotropic glutamate receptor type 4. Neuropharmacology. 1995 Feb;34(2):149-55. [PubMed Link Image]
  4. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  5. Ohtsuki T, Toru M, Arinami T: Mutation screening of the metabotropic glutamate receptor mGluR4 (GRM4) gene in patients with schizophrenia. Psychiatr Genet. 2001 Jun;11(2):79-83. [PubMed Link Image]
Enzyme 68 Metabolite References Not Available
Enzyme 69 [top]
Enzyme 69 ID 17153
Enzyme 69 Name Metabotropic glutamate receptor 7
Enzyme 69 Synonyms
  1. mGluR7
Enzyme 69 Gene Name GRM7
Enzyme 69 Protein Sequence >Metabotropic glutamate receptor 7
MVQLRKLLRVLTLMKFPCCVLEVLLCALAAAARGQEMYAPHSIRIEGDVTLGGLFPVHAK
GPSGVPCGDIKRENGIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSL
TFVQALIQKDTSDVRCTNGEPPVFVKPEKVVGVIGASGSSVSIMVANILRLFQIPQISYA
STAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFTQ
ISKEAGGLCIAQSVRIPQERKDRTIDFDRIIKQLLDTPNSRAVVIFANDEDIKQILAAAK
RADQVGHFLWVGSDSWGSKINPLHQHEDIAEGAITIQPKRATVEGFDAYFTSRTLENNRR
NVWFAEYWEENFNCKLTISGSKKEDTDRKCTGQERIGKDSNYEQEGKVQFVIDAVYAMAH
ALHHMNKDLCADYRGVCPEMEQAGGKKLLKYIRNVNFNGSAGTPVMFNKNGDAPGRYDIF
QYQTTNTSNPGYRLIGQWTDELQLNIEDMQWGKGVREIPASVCTLPCKPGQRKKTQKGTP
CCWTCEPCDGYQYQFDEMTCQHCPYDQRPNENRTGCQDIPIIKLEWHSPWAVIPVFLAML
GIIATIFVMATFIRYNDTPIVRASGRELSYVLLTGIFLCYIITFLMIAKPDVAVCSFRRV
FLGLGMCISYAALLTKTNRIYRIFEQGKKSVTAPRLISPTSQLAITSSLISVQLLGVFIW
FGVDPPNIIIDYDEHKTMNPEQARGVLKCDITDLQIICSLGYSILLMVTCTVYAIKTRGV
PENFNEAKPIGFTMYTTCIVWLAFIPIFFGTAQSAEKLYIQTTTLTISMNLSASVALGML
YMPKVYIIIFHPELNVQKRKRSFKAVVTAATMSSRLSHKPSDRPNGEAKTELCENVDPNS
PAAKKKYVSYNNLVI
Enzyme 69 Number of Residues 915
Enzyme 69 Molecular Weight 102250.1
Enzyme 69 Theoretical pI 7.94
Enzyme 69 GO Classification
Function
  • G-protein coupled receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 69 General Function Involved in G-protein coupled receptor activity
Enzyme 69 Specific Function Receptor for glutamate. The activity of this receptor is mediated by a G-protein that inhibits adenylate cyclase activity
Enzyme 69 Pathways Not Available
Enzyme 69 Reactions Not Available
Enzyme 69 Pfam Domain Function
Enzyme 69 Signals
  • 1-34
Enzyme 69 Transmembrane Regions
  • 591-615 628-648 655-675 703-723 754-775 789-810 826-850
Enzyme 69 Essentiality Not Available
Enzyme 69 GenBank ID Protein 1370111 Link Image
Enzyme 69 UniProtKB/Swiss-Prot ID Q14831 Link Image
Enzyme 69 UniProtKB/Swiss-Prot Entry Name GRM7_HUMAN Link Image
Enzyme 69 PDB ID Not Available
Enzyme 69 Cellular Location Not Available
Enzyme 69 Gene Sequence >2748 bp
ATGGTCCAGCTGAGGAAGCTGCTCCGCGTCCTGACTTTGATGAAGTTCCCCTGCTGCGTG
CTGGAGGTGCTCCTGTGCGCGCTGGCGGCGGCGGCGCGCGGCCAGGAGATGTACGCCCCG
CACTCAATCCGGATCGAGGGGGACGTCACCCTCGGGGGGCTGTTCCCCGTGCACGCCAAG
GGTCCCAGCGGAGTGCCCTGCGGCGACATCAAGAGGGAAAACGGGATCCACAGGCTGGAA
GCGATGCTCTACGCCCTGGACCAGATCAACAGTGATCCCAACCTACTGCCCAACGTGACG
CTGGGCGCGCGGATCCTGGACACTTGTTCCAGGGACACTTACGCGCTCGAACAGTCGCTT
ACTTTCGTCCAGGCGCTCATCCAGAAGGACACCTCCGACGTGCGCTGCACCAACGGCGAA
CCGCCGGTTTTCGTCAAGCCGGAGAAAGTAGTTGGAGTGATTGGGGCTTCGGGGAGTTCG
GTCTCCATCATGGTAGCCAACATCCTGAGGCTCTTCCAGATCCCCCAGATTAGTTATGCA
TCAACGGCACCCGAGCTAAGTGATGACCGGCGCTATGACTTCTTCTCTCGCGTGGTGCCA
CCCGATTCCTTCCAAGCCCAGGCCATGGTAGACATTGTAAAGGCCCTAGGCTGGAATTAT
GTGTCTACCCTCGCATCGGAAGGAAGTTATGGAGAGAAAGGTGTGGAGTCCTTCACGCAG
ATTTCCAAAGAGGCAGGTGGACTCTGCATTGCCCAGTCCGTGAGAATCCCCCAGGAACGC
AAAGACAGGACCATTGACTTTGATAGAATTATCAAACAGCTCCTGGACACCCCCAACTCC
AGGGCCGTCGTGATTTTTGCCAACGATGAGGATATAAAGCAGATCCTTGCAGCAGCCAAA
AGAGCTGACCAAGTTGGCCATTTTCTTTGGGTGGGATCAGACAGCTGGGGATCCAAAATA
AACCCACTGCACCAGCATGAAGATATCGCAGAAGGGGCCATCACCATTCAGCCCAAGCGA
GCCACGGTGGAAGGGTTTGATGCCTACTTTACGTCCCGTACACTTGAAAACAACAGAAGA
AATGTATGGTTTGCCGAATACTGGGAGGAAAACTTCAACTGCAAGTTGACGATTAGTGGG
TCAAAAAAAGAAGACACAGATCGCAAATGCACAGGACAGGAGAGAATTGGAAAAGATTCC
AACTATGAGCAGGAGGGTAAAGTCCAGTTCGTGATTGACGCAGTCTATGCTATGGCTCAC
GCCCTTCACCACATGAACAAGGATCTCTGTGCTGACTACCGGGGTGTCTGCCCAGAGATG
GAGCAAGCTGGAGGCAAGAAGTTGCTGAAGTATATACGCAATGTTAATTTCAATGGTAGT
GCTGGCACTCCAGTGATGTTTAACAAGAACGGGGATGCACCTGGGCGTTATGACATCTTT
CAGTACCAGACCACAAACACCAGCAACCCGGGTTACCGTCTGATCGGGCAGTGGACAGAC
GAACTTCAGCTCAATATAGAAGACATGCAGTGGGGTAAAGGAGTCCGAGAGATACCCGCC
TCAGTGTGCACACTACCATGTAAGCCAGGACAGAGAAAGAAGACACAGAAAGGAACTCCT
TGCTGTTGGACCTGTGAGCCTTGCGATGGTTACCAGTACCAGTTTGATGAGATGACATGC
CAGCATTGCCCCTATGACCAGAGGCCCAATGAAAATCGAACCGGATGCCAGGATATTCCC
ATCATCAAACTGGAGTGGCACTCCCCCTGGGCTGTGATTCCTGTCTTCCTGGCAATGTTG
GGGATCATTGCCACCATCTTTGTCATGGCCACTTTCATCCGCTACAATGACACGCCCATT
GTCCGGGCATCTGGGCGGGAACTCAGCTATGTTCTTTTGACGGGCATCTTTCTTTGCTAC
ATCATCACTTTCCTGATGATTGCCAAACCAGATGTGGCAGTGTGTTCTTTCCGGCGAGTT
TTCTTGGGCTTGGGTATGTGCATCAGTTATGCAGCCCTCTTGACGAAAACAAATCGGATT
TATCGCATATTTGAGCAGGGCAAGAAATCAGTAACAGCTCCCAGACTCATAAGCCCAACA
TCACAACTGGCAATCACTTCCAGTTTAATATCAGTTCAGCTTCTAGGGGTGTTCATTTGG
TTTGGTGTTGATCCACCCAACATCATCATAGACTACGATGAACACAAGACAATGAACCCT
GAGCAAGCCAGAGGGGTTCTCAAGTGTGACATTACAGATCTCCAAATCATTTGCTCCTTG
GGATATAGCATTCTTCTCATGGTCACATGTACTGTGTATGCCATCAAGACTCGGGGTGTA
CCCGAGAATTTTAACGAAGCCAAGCCCATTGGATTCACTATGTACACGACATGTATAGTA
TGGCTTGCCTTCATTCCAATTTTTTTTGGCACCGCTCAATCAGCGGAAAAGCTCTACATA
CAAACTACCACGCTTACAATCTCCATGAACCTAAGTGCATCAGTGGCGCTGGGGATGCTA
TACATGCCGAAAGTGTACATCATCATTTTCCACCCTGAACTCAATGTCCAGAAACGGAAG
CGAAGCTTCAAGGCGGTAGTCACAGCAGCCACCATGTCATCGAGGCTGTCACACAAACCC
AGTGACAGACCCAACGGTGAGGCAAAGACCGAGCTCTGTGAAAACGTAGACCCAAACAGC
CCTGCTGCAAAAAAGAAGTATGTCAGTTATAATAACCTGGTTATCTAA
Enzyme 69 GenBank Gene ID X94552 Link Image
Enzyme 69 GeneCard ID GRM7 Link Image
Enzyme 69 GenAtlas ID GRM7 Link Image
Enzyme 69 HGNC ID HGNC:4599 Link Image
Enzyme 69 Chromosome Location 3
Enzyme 69 Locus 3p26.1-p25.1
Enzyme 69 SNPs SNPJam Report Link Image
Enzyme 69 General References
  1. Makoff A, Pilling C, Harrington K, Emson P: Human metabotropic glutamate receptor type 7: molecular cloning and mRNA distribution in the CNS. Brain Res Mol Brain Res. 1996 Aug;40(1):165-70. [PubMed Link Image]
  2. Flor PJ, Van Der Putten H, Ruegg D, Lukic S, Leonhardt T, Bence M, Sansig G, Knopfel T, Kuhn R: A novel splice variant of a metabotropic glutamate receptor, human mGluR7b. Neuropharmacology. 1997 Feb;36(2):153-9. [PubMed Link Image]
  3. Wu S, Wright RA, Rockey PK, Burgett SG, Arnold JS, Rosteck PR Jr, Johnson BG, Schoepp DD, Belagaje RM: Group III human metabotropic glutamate receptors 4, 7 and 8: molecular cloning, functional expression, and comparison of pharmacological properties in RGT cells. Brain Res Mol Brain Res. 1998 Jan;53(1-2):88-97. [PubMed Link Image]
  4. Schulz HL, Stohr H, Weber BH: Characterization of three novel isoforms of the metabotrobic glutamate receptor 7 (GRM7). Neurosci Lett. 2002 Jun 21;326(1):37-40. [PubMed Link Image]
  5. Bolonna AA, Kerwin RW, Munro J, Arranz MJ, Makoff AJ: Polymorphisms in the genes for mGluR types 7 and 8: association studies with schizophrenia. Schizophr Res. 2001 Jan 15;47(1):99-103. [PubMed Link Image]
Enzyme 69 Metabolite References Not Available