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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Glutamine (HMDB00641)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2011-06-15 12:49:00
Accession Number HMDB00641
Secondary Accession Numbers Not Available
Common Name L-Glutamine
Description Glutamine (Gln) is one of the 20 amino acids encoded by the standard genetic code. Its side chain is an amide; it is formed by replacing a side-chain hydroxyl of glutamic acid with an amine functional group. glutamine is found in foods high in proteins, such as fish, red meat, beans, and dairy products. glutamine is a supplement that is used in weightlifting, bodybuilding, endurance and other sports, as well as by those who suffer from muscular cramps or pain particularly elderly people. The main use of glutamine within the diet of either group is as a means of replenishing the body's stores of amino acids that have been used during exercise or everyday activities. Studies which are looking into problems with excessive consumption of glutamine thus far have proved inconclusive. However, normal supplementation is healthy mainly because glutamine is supposed to be supplemented after prolonged periods of exercise (for example, a workout or exercise in which amino acids are required for use) and replenishes amino acid stores; this being the main reason glutamine is recommended during fasting or for people who suffer from physical trauma, immune deficiencies, or cancer. There is a significant body of evidence that links glutamine-enriched diets with intestinal effects; aiding maintenance of gut barrier function, intestinal cell proliferation and differentiation, as well as generally reducing septic morbidity and the symptoms of Irritable Bowel Syndrome. The reason for such "cleansing" properties is thought to stem from the fact that the intestinal extraction rate of glutamine is higher than that for other amino acids, and is therefore thought to be the most viable option when attempting to alleviate conditions relating to the gastrointestinal tract. These conditions were discovered after comparing plasma concentration within the gut between glutamine-enriched and non glutamine-enriched diets. However, even though glutamine is thought to have "cleansing" properties and effects, it is unknown to what extent glutamine has clinical benefits, due to the varied concentrations of glutamine in varieties of food. It is also known that glutamine has various effects in reducing healing time after operations. Hospital waiting times after abdominal surgery are reduced by providing parenteral nutrition regimens containing amounts of glutamine to patients. Clinical trials have revealed that patients on supplementation regimes containing glutamine have improved nitrogen balances, generation of cysteinyl-leukotrienes from polymorphonuclear neutrophil granulocytes and improved lymphocyte recovery and intestinal permeability (in postoperative patients) - in comparison to those who had no glutamine within their dietary regime; all without any side-effects. (http://en.wikipedia.org/wiki/glutamine)
Synonyms
  1. (2S)-2,5-diamino-5-oxopentanoic acid
  2. (2S)-2-amino-4-carbamoylbutanoic acid
  3. (S)-2,5-Diamino-5-oxopentanoic acid
  4. 2-Aminoglutaramic acid
  5. Cebrogen
  6. Glavamin
  7. Glumin
  8. Glutamic acid 5-amide
  9. Glutamic acid amide
  10. Glutamine
  11. L-(+)-glutamine
  12. L-2-Aminoglutaramic acid
  13. L-2-Aminoglutaramidic acid
  14. L-Glutamic acid 5-amide
  15. L-Glutaminsaeure-5-amid
  16. L-glutamic acid gamma-amide
  17. L-glutamid
  18. L-glutamide
  19. L-glutamin
  20. L-glutamine
  21. Levoglutamid
  22. Levoglutamida
  23. Levoglutamide
  24. Levoglutamidum
  25. Levoglutamina
  26. Polyglutamine
  27. Stimulina
  28. gamma-glutamine
  29. (2S)-2,5-diamino-5-oxopentanoate
  30. (2S)-2-amino-4-carbamoylbutanoate
  31. (S)-2,5-Diamino-5-oxopentanoate
Chemical IUPAC Name (2S)-2-amino-4-carbamoyl-butanoic acid
Chemical Formula C5H10N2O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • primary carboxylic acid amide
  • alpha-aminoacid
Biofunction
  • Essential amino acid
  • Energy source
  • Non-essential amino acid
  • RNA component
  • Component of Alanine and aspartate metabolism
  • Component of Aminoacyl-tRNA biosynthesis
  • Component of Aminosugars metabolism
  • Component of D-Glutamine and D-glutamate metabolism
  • Component of Glutamate metabolism
  • Component of Nitrogen metabolism
  • Component of Peptidoglycan biosynthesis
  • Component of Purine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 146.145
Monoisotopic Molecular Weight 146.069138
Isomeric SMILES N[C@@H](CCC(N)=O)C(O)=O
Canonical SMILES NC(CCC(N)=O)C(O)=O
KEGG Compound ID C00064 Link Image
BioCyc ID GLN Link Image
BiGG ID 33714 Link Image
Wikipedia Link L-Glutamine Link Image
NuGOwiki Link HMDB00641 Link Image
Metagene Link HMDB00641 Link Image
METLIN ID 5614 Link Image
PubChem Compound 5961 Link Image
PubChem Substance 10527678 Link Image
ChEBI ID 18050 Link Image
CAS Registry Number 56-85-9
InChI Identifier InChI=1/C5H10N2O3/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H2,7,8)(H,9,10)/t3-/m0/s1
Synthesis Reference Jiao, Qingcai; Qian, Shaosong; Chen, Ran; Wu, Xiaoyan. Synthesis of L-glutamine. Faming Zhuanli Shenqing Gongkai Shuomingshu (2005), 7 pp.
Melting Point (Experimental) 185 oC
Experimental Water Solubility 41.3 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)]; 41.3 mg/mL at 25 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 97.799995 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -3.64 [CHMELIK,J ET AL. (1991)] Source: PhysProp
Predicted LogP/Hydrophobicity -3.32 [Predicted by ALOGPS]; -4.1 [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 1CT9 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)
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
Adipose Tissue
Fibroblasts
Gut
Intestine
Kidney
Muscle
Myelin
Neuron
Pancreas
Placenta
Skeletal Muscle
Spleen
Stratum Corneum
Testes
Concentrations (Normal)
Biofluid Blood
Value 586.0 (502.0-670.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
Biofluid Blood
Value 591.0 +/- 66.0 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 645.0 +/- 64.0 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 578.0 +/- 85.0 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 905.0 +/- 250.0 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 600.0 +/- 70.0 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 490.6 +/- 84.3 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Grant SL, Shulman Y, Tibbo P, Hampson DR, Baker GB: Determination of d-serine and related neuroactive amino acids in human plasma by high-performance liquid chromatography with fluorimetric detection. J Chromatogr B Analyt Technol Biomed Life Sci. 2006 Dec 5;844(2):278-82. Epub 2006 Aug 4. [PubMed Link Image]
Biofluid CSF
Value 444.0 +/- 84.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 627.0 (482.0-772.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Subramanian A, Gupta A, Saxena S, Gupta A, Kumar R, Nigam A, Kumar R, Mandal SK, Roy R: Proton MR CSF analysis and a new software as predictors for the differentiation of meningitis in children. NMR Biomed. 2005 Jun;18(4):213-25. [PubMed Link Image]
Biofluid CSF
Value 570.0 +/- 240.0 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Commodari F, Arnold DL, Sanctuary BC, Shoubridge EA: 1H NMR characterization of normal human cerebrospinal fluid and the detection of methylmalonic acid in a vitamin B12 deficient patient. NMR Biomed. 1991 Aug;4(4):192-200. [PubMed Link Image]
Biofluid CSF
Value 623.6 +/- 71.6 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 518.0 +/- 81.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
Biofluid CSF
Value 425.0 +/- 70.5 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
Biofluid CSF
Value 432 +/- 204 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 363.3 +/- 97.6 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Mandal, R. et al. (in preparation)
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 118.96 +/- 89.94 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 36.8 (14.5-59.2) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value 20.0 (9.0-33.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Gatti R, Gioia MG: Liquid chromatographic fluorescence determination of amino acids in plasma and urine after derivatization with phanquinone. Biomed Chromatogr. 2008 Feb;22(2):207-13. [PubMed Link Image]
Biofluid Urine
Value 33.98 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Shaykhutdinov RA, MacInnis GD, Dowlatabadi R, Weljie AM, Vogel HJ. Quantitative analysis of metabolite concentrations in human urine samples using 13C{1H} NMR spectroscopy. Metabolomics. 2009
Concentrations (Abnormal)
Biofluid Blood
Value 476.0 (455.0-498.0) 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 495.0 (477.0-513.0) 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 611.0 (591.0-630.0) 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 650.0 +/- 98.0 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 673.0 +/- 96.0 uM
Age Adult:>18 yrs old
Sex Female
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 228.34 +/- 12.00 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 542.5 (376.0-709.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Carbamoyl Phosphate Synthetase Deficiency
Comments Not Available
References
Biofluid Blood
Value 900.0 (700.0-1100.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Carbamoyl Phosphate Synthetase Deficiency
Comments Not Available
References
Biofluid CSF
Value 254.0 (152.0-356.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Redjems-Bennani N, Jeandel C, Lefebvre E, Blain H, Vidailhet M, Gueant JL: Abnormal substrate levels that depend upon mitochondrial function in cerebrospinal fluid from Alzheimer patients. Gerontology. 1998;44(5):300-4. [PubMed Link Image]
Biofluid CSF
Value 1875.3 +/- 285.8 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 1061.0 +/- 230.2 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 1146.6 +/- 10.6 uM
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid CSF
Value 902 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Scholl-Burgi S, Haberlandt E, Gotwald T, Albrecht U, Baumgartner Sigl S, Rauchenzauner M, Rostasy K, Karall D: Stroke-like episodes in propionic acidemia caused by central focal metabolic decompensation. Neuropediatrics. 2009 Apr;40(2):76-81. Epub 2009 Oct 6. [PubMed Link Image]
Biofluid Urine
Value 1.17 +/- 0.49 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Associated Disorders
Condition References
Alzheimer's disease
Carbamoyl Phosphate Synthetase Deficiency
Epilepsy
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Leukemia
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Schizophrenia
  • 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]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Amino Sugar Metabolism SMP00045 Link Image map00520 Link Image
Ammonia Recycling SMP00009 Link Image map00910 Link Image
Glutamate Metabolism SMP00072 Link Image map00250 Link Image
Phenylacetate Metabolism SMP00126 Link Image map00360 Link Image
Purine Metabolism SMP00050 Link Image map00230 Link Image
Pyrimidine Metabolism SMP00046 Link Image map00240 Link Image
Transcription/Translation SMP00019 Link Image
Urea Cycle SMP00059 Link Image map00330 Link Image
General References
  1. Szebenyi G, Morfini GA, Babcock A, Gould M, Selkoe K, Stenoien DL, Young M, Faber PW, MacDonald ME, McPhaul MJ, Brady ST: Neuropathogenic forms of huntingtin and androgen receptor inhibit fast axonal transport. Neuron. 2003 Sep 25;40(1):41-52. [PubMed Link Image]
  2. Wada A, Yoshida R, Oda K, Fukuba E, Uchida N, Kitagaki H: Acute encephalopathy associated with intravenous immunoglobulin therapy. AJNR Am J Neuroradiol. 2005 Oct;26(9):2311-5. [PubMed Link Image]
  3. Pennisi P, Gavrilova O, Setser-Portas J, Jou W, Santopietro S, Clemmons D, Yakar S, LeRoith D: Recombinant human insulin-like growth factor-I treatment inhibits gluconeogenesis in a transgenic mouse model of type 2 diabetes mellitus. Endocrinology. 2006 Jun;147(6):2619-30. Epub 2006 Mar 2. [PubMed Link Image]
  4. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
  5. 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. Subramanian A, Gupta A, Saxena S, Gupta A, Kumar R, Nigam A, Kumar R, Mandal SK, Roy R: Proton MR CSF analysis and a new software as predictors for the differentiation of meningitis in children. NMR Biomed. 2005 Jun;18(4):213-25. [PubMed Link Image]
  8. Redjems-Bennani N, Jeandel C, Lefebvre E, Blain H, Vidailhet M, Gueant JL: Abnormal substrate levels that depend upon mitochondrial function in cerebrospinal fluid from Alzheimer patients. Gerontology. 1998;44(5):300-4. [PubMed Link Image]
  9. Avila J, Barbaro B, Gangemi A, Romagnoli T, Kuechle J, Hansen M, Shapiro J, Testa G, Sankary H, Benedetti E, Lakey J, Oberholzer J: Intra-ductal glutamine administration reduces oxidative injury during human pancreatic islet isolation. Am J Transplant. 2005 Dec;5(12):2830-7. [PubMed Link Image]
  10. Cooper AJ: Ammonia metabolism in normal and portacaval-shunted rats. Adv Exp Med Biol. 1990;272:23-46. [PubMed Link Image]
  11. Melis GC, Boelens PG, van der Sijp JR, Popovici T, De Bandt JP, Cynober L, van Leeuwen PA: The feeding route (enteral or parenteral) affects the plasma response of the dipetide Ala-Gln and the amino acids glutamine, citrulline and arginine, with the administration of Ala-Gln in preoperative patients. Br J Nutr. 2005 Jul;94(1):19-26. [PubMed Link Image]
  12. Choudry HA, Pan M, Karinch AM, Souba WW: Branched-chain amino acid-enriched nutritional support in surgical and cancer patients. J Nutr. 2006 Jan;136(1 Suppl):314S-8S. [PubMed Link Image]
  13. Commodari F, Arnold DL, Sanctuary BC, Shoubridge EA: 1H NMR characterization of normal human cerebrospinal fluid and the detection of methylmalonic acid in a vitamin B12 deficient patient. NMR Biomed. 1991 Aug;4(4):192-200. [PubMed Link Image]
  14. 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]
  15. 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]
  16. Coeffier M, Miralles-Barrachina O, Le Pessot F, Lalaude O, Daveau M, Lavoinne A, Lerebours E, Dechelotte P: Influence of glutamine on cytokine production by human gut in vitro. Cytokine. 2001 Feb 7;13(3):148-54. [PubMed Link Image]
  17. 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]
  18. 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]
  19. van der Hulst RR, von Meyenfeldt MF, Deutz NE, Soeters PB: Glutamine extraction by the gut is reduced in depleted [corrected] patients with gastrointestinal cancer. Ann Surg. 1997 Jan;225(1):112-21. [PubMed Link Image]
  20. Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 2
  2. Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 1
  3. Amidophosphoribosyltransferase
  4. Kynurenine--oxoglutarate transaminase 1
  5. Glutaminyl-tRNA synthetase
  6. Asparagine synthetase [glutamine-hydrolyzing]
  7. GMP synthase [glutamine-hydrolyzing]
  8. Protein-glutamine gamma-glutamyltransferase E
  9. Protein-glutamine gamma-glutamyltransferase 2
  10. Glutamine synthetase
  11. Coagulation factor XIII A chain
  12. Glutaminase liver isoform, mitochondrial
  13. CTP synthase 1
  14. Protein-glutamine gamma-glutamyltransferase 5
  15. Glutaminase kidney isoform, mitochondrial
  16. Protein-glutamine gamma-glutamyltransferase K
  17. Protein-glutamine gamma-glutamyltransferase 6
  18. Phosphoribosylformylglycinamidine synthase
  19. Probable glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial
  20. Neutral amino acid transporter B(0)
  21. Large neutral amino acids transporter small subunit 2
  22. Glutaminase 2 (Liver, mitochondrial), isoform CRA_b
  23. Sodium-coupled neutral amino acid transporter 3
  24. Glutamine-dependent NAD(+) synthetase
  25. CAD protein
  26. CTP synthase 2
  27. Phosphoribosyl pyrophosphate amidotransferase, isoform CRA_b
  28. Guanine monphosphate synthetase, isoform CRA_b
  29. Glutamine synthetase
  30. Putative uncharacterized protein GFPT1
  31. cDNA FLJ75059, highly similar to Homo sapiens phosphoribosylformylglycinamidine synthase (FGAR amidotransferase) (PFAS), mRNA
  32. Cysteine conjugate-beta lyase
  33. cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
  34. Glutamyl-tRNA(Gln) amidotransferase subunit A homolog
Enzyme 1 [top]
Enzyme 1 ID 5446
Enzyme 1 Name Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 2
Enzyme 1 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 1 Gene Name GFPT2
Enzyme 1 Protein Sequence >Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 2
MCGIFAYMNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNHEVKERHIQLVKKR
GKVKALDEELYKQDSMDLKVEFETHFGIAHTRWATHGVPSAVNSHPQRSDKGNEFVVIHN
GIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRETEDITFSTLVERVIQQLEG
AFALVFKSVHYPGEAVATRRGSPLLIGVRSKYKLSTEQIPILYRTCTLENVKNICKTRMK
RLDSSACLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSAS
DDPSRAIQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDH
LKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFF
ISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVASTKAYT
SQFISLVMFGLMMSEDRISLQNRRQEIIRGLRSLPELIKEVLSLEEKIHDLALELYTQRS
LLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCF
AKCQNALQQVTARQGRPIILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFH
LAVLRGYDVDFPRNLAKSVTVE
Enzyme 1 Number of Residues 682
Enzyme 1 Molecular Weight 76929.9
Enzyme 1 Theoretical pI 7.40
Enzyme 1 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 1 General Function Involved in metabolic process
Enzyme 1 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 1 Pathways
Enzyme 1 Reactions
  • L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate [RN:R00768]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID O94808 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GFPT2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID AB016789 Link Image
Enzyme 1 GeneCard ID GFPT2 Link Image
Enzyme 1 GenAtlas ID GFPT2 Link Image
Enzyme 1 HGNC ID HGNC:4242 Link Image
Enzyme 1 Chromosome Location 5
Enzyme 1 Locus 5q34-q35
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5448
Enzyme 2 Name Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 1
Enzyme 2 Synonyms
  1. D-fructose-6-phosphate amidotransferase 1
  2. Glutamine:fructose 6 phosphate amidotransferase 1
  3. GFAT 1
  4. GFAT1
  5. Hexosephosphate aminotransferase 1
Enzyme 2 Gene Name GFPT1
Enzyme 2 Protein Sequence >Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 1
MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWEANACKIQLI
KKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIV
IHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDNRESQDTSFTTLVERVIQQ
LEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEHKLSTDHIPILYRTARTQIGSKFTRW
GSQGERGKDKKGSCNLSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVA
AVVDGRLSIHRIKRTAGDHPGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRG
RVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELAS
DFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGV
HINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLS
MDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLAL
VDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSVD
CLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE
Enzyme 2 Number of Residues 699
Enzyme 2 Molecular Weight 78805.8
Enzyme 2 Theoretical pI 7.11
Enzyme 2 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 2 General Function Involved in metabolic process
Enzyme 2 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 2 Pathways
Enzyme 2 Reactions
  • L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate [RN:R00768]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 205277386 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q06210 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name GFPT1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID Not Available
Enzyme 2 GeneCard ID GFPT1 Link Image
Enzyme 2 GenAtlas ID GFPT1 Link Image
Enzyme 2 HGNC ID HGNC:4241 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2p13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. McKnight GL, Mudri SL, Mathewes SL, Traxinger RR, Marshall S, Sheppard PO, O'Hara PJ: Molecular cloning, cDNA sequence, and bacterial expression of human glutamine:fructose-6-phosphate amidotransferase. J Biol Chem. 1992 Dec 15;267(35):25208-12. [PubMed Link Image]
  2. 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]
  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. DeHaven JE, Robinson KA, Nelson BA, Buse MG: A novel variant of glutamine: fructose-6-phosphate amidotransferase-1 (GFAT1) mRNA is selectively expressed in striated muscle. Diabetes. 2001 Nov;50(11):2419-24. [PubMed Link Image]
  5. 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]
  6. 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]
  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. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [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. 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]
  11. 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]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5567
Enzyme 3 Name Amidophosphoribosyltransferase
Enzyme 3 Synonyms
  1. ATase
  2. Glutamine phosphoribosylpyrophosphate amidotransferase
  3. GPAT
Enzyme 3 Gene Name PPAT
Enzyme 3 Protein Sequence >Amidophosphoribosyltransferase
MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPT
FKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVA
HNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEA
PTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFL
SIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVY
TVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQP
NMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASP
PIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKE
KKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW
Enzyme 3 Number of Residues 517
Enzyme 3 Molecular Weight 57398.5
Enzyme 3 Theoretical pI 6.74
Enzyme 3 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 3 General Function Involved in amidophosphoribosyltransferase activity
Enzyme 3 Specific Function 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H(2)O
Enzyme 3 Pathways
Enzyme 3 Reactions
  • 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O [RN:R01072]
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 Q06203 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PUR1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1554 bp
ATGGAGCTGGAGGAGTTGGGGATCCGAGAGGAATGTGGCGTGTTCGGGTGCATCGCCTCA
GGAGAGTGGCCCACGCAGCTGGATGTACCGCATGTGATCACTCTGGGACTCGTGGGGCTG
CAGCACCGGGGTCAGGAGAGTGCTGGTATTGTGACTAGTGATGGGAGTTCGGTGCCAACA
TTCAAATCACACAAGGGAATGGGTCTTGTAAATCACGTCTTTACTGAAGACAATTTGAAA
AAATTATATGTTTCAAATCTTGGAATTGGACACACCAGGTATGCCACCACAGGAAAATGT
GAACTAGAAAATTGTCAGCCCTTCGTTGTTGAAACACTTCATGGGAAGATAGCTGTGGCA
CATAATGGCGAATTGGTAAATGCTGCTCGATTAAGGAAAAAGCTTCTGCGTCATGGTATT
GGTCTGTCTACAAGTTCTGATAGTGAAATGATTACCCAGTTACTGGCGTATACCCCTCCT
CAGGAACAAGATGACACCCCAGACTGGGTAGCCAGGATTAAAAACTTGATGAAGGAAGCA
CCCACAGCATACTCCCTGCTTATAATGCACAGAGATGTTATTTATGCAGTACGAGATCCT
TATGGAAATCGTCCCTTATGCATTGGTCGTCTTATTCCAGTGTCTGATATAAATGACAAA
GAGAAAAAAACATCAGAAACAGAAGGATGGGTGGTGTCTTCAGAATCTTGTAGCTTCTTA
TCTATTGGTGCAAGATATTACCGTGAAGTCTTGCCTGGAGAAATTGTGGAAATATCCAGA
CACAATGTCCAAACTCTTGATATTATATCAAGGTCTGAAGGAAACCCAGTGGCTTTTTGT
ATCTTTGAATATGTTTATTTTGCAAGACCAGACAGTATGTTCGAAGACCAAATGGTTTAT
ACAGTAAGATACCGTTGTGGCCAGCAGCTAGCGATTGAAGCACCTGTGGATGCAGATTTG
GTTAGCACTGTTCCAGAATCTGCTACGCCTGCTGCTCTTGCTTACGCAGGAAAGTGTGGA
CTTCCATATGTGGAGGTGCTGTGTAAAAACCGGTATGTAGGGAGAACCTTCATTCAGCCA
AACATGAGGTTAAGACAACTTGGTGTTGCAAAAAAATTTGGAGTATTGTCAGACAACTTT
AAAGGCAAAAGAATTGTTCTTGTAGATGATTCAATTGTCAGAGGCAATACCATCTCACCT
ATAATAAAACTGCTCAAAGAATCTGGTGCAAAAGAGGTACACATTCGAGTAGCTTCACCA
CCAATTAAATATCCATGCTTCATGGGAATAAACATTCCTACAAAAGAAGAGCTCATTGCC
AATAAACCAGAATTTGATCACCTTGCAGAATATCTAGGAGCAAACAGTGTTGTGTATCTG
TCAGTAGAAGGACTGGTTTCATCTGTACAAGAAGGGATAAAGTTTAAAAAACAGAAAGAG
AAAAAGCACGATATTATGATCCAAGAAAATGGAAATGGTCTGGAATGTTTTGAAAAGAGT
GGTCATTGTACAGCTTGTCTCACTGGAAAATATCCTGTAGAATTAGAATGGTAG
Enzyme 3 GenBank Gene ID D13757 Link Image
Enzyme 3 GeneCard ID PPAT Link Image
Enzyme 3 GenAtlas ID PPAT Link Image
Enzyme 3 HGNC ID HGNC:9238 Link Image
Enzyme 3 Chromosome Location 4
Enzyme 3 Locus 4q12
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Iwahana H, Oka J, Mizusawa N, Kudo E, Ii S, Yoshimoto K, Holmes EW, Itakura M: Molecular cloning of human amidophosphoribosyltransferase. Biochem Biophys Res Commun. 1993 Jan 15;190(1):192-200. [PubMed Link Image]
  2. Brayton KA, Chen Z, Zhou G, Nagy PL, Gavalas A, Trent JM, Deaven LL, Dixon JE, Zalkin H: Two genes for de novo purine nucleotide synthesis on human chromosome 4 are closely linked and divergently transcribed. J Biol Chem. 1994 Feb 18;269(7):5313-21. [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. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5703
Enzyme 4 Name Kynurenine--oxoglutarate transaminase 1
Enzyme 4 Synonyms
  1. Cysteine-S-conjugate beta-lyase
  2. Glutamine transaminase K
  3. GTK
  4. Glutamine--phenylpyruvate transaminase
  5. Kynurenine aminotransferase I
  6. KATI
  7. Kynurenine--oxoglutarate transaminase I
Enzyme 4 Gene Name CCBL1
Enzyme 4 Protein Sequence >Kynurenine--oxoglutarate transaminase 1
MAKQLQARRLDGIDYNPWVEFVKLASEHDVVNLGQGFPDFPPPDFAVEAFQHAVSGDFML
NQYTKTFGYPPLTKILASFFGELLGQEIDPLRNVLVTVGGYGALFTAFQALVDEGDEVII
IEPFFDCYEPMTMMAGGRPVFVSLKPGPIQNGELGSSSNWQLDPMELAGKFTSRTKALVL
NTPNNPLGKVFSREELELVASLCQQHDVVCITDEVYQWMVYDGHQHISIASLPGMWERTL
TIGSAGKTFSATGWKVGWVLGPDHIMKHLRTVHQNSVFHCPTQSQAAVAESFEREQLLFR
QPSSYFVQFPQAMQRCRDHMIRSLQSVGLKPIIPQGSYFLITDISDFKRKMPDLPGAVDE
PYDRRFVKWMIKNKGLVAIPVSIFYSVPHQKHFDHYIRFCFVKDEATLQAMDEKLRKWKV
EL
Enzyme 4 Number of Residues 422
Enzyme 4 Molecular Weight 47874.8
Enzyme 4 Theoretical pI 6.45
Enzyme 4 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 4 General Function Involved in 1-aminocyclopropane-1-carboxylate synthase activity
Enzyme 4 Specific Function Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta- elimination of S-conjugates and Se-conjugates of L- (seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond
Enzyme 4 Pathways
Enzyme 4 Reactions
  • RS-CH2-CH(NH3+)COO- = RSH + NH3 + pyruvate [RN:R03528]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 758591 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q16773 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name KAT1_HUMAN Link Image
Enzyme 4 PDB ID 1W7N Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1269 bp
ATGGCCAAACAGCTGCAGGCCCGAAGGCTAGACGGGATCGACTACAACCCCTGGGTGGAG
TTTGTGAAACTGGCCAGTGAGCATGACGTCGTGAACTTGGGCCAGGGCTTCCCGGATTTC
CCACCACCAGACTTTGCCGTGGAAGCCTTTCAGCACGCTGTCAGTGGAGACTTCATGCTT
AACCAGTACACCAAGACATTTGGTTACCCACCACTGACGAAGATCCTGGCAAGTTTCTTT
GGGGAGCTGCTGGGTCAGGAGATAGACCCGCTCAGGAATGTGCTGGTGACTGTTGGTGGC
TATGGGGCCCTGTTCACAGCCTTCCAGGCCCTGGTGGACGAAGGAGACGAGGTCATCATC
ATCGAACCCTTTTTTGACTGCTACGAGCCCATGACAATGATGGCAGGGGGTCGTCCTGTG
TTTGTGTCCCTGAAGCCGGGTCCCATCCAGAATGGAGAACTGGGTTCCAGCAGCAACTGG
CAGCTGGACCCCATGGAGCTGGCCGGCAAATTCACATCACGCACCAAAGCCCTGGTCCTC
AACACCCCCAACAACCCCCTGGGCAAGGTGTTCTCCAGGGAAGAGCTGGAGCTGGTGGCC
AGCCTTTGCCAGCAGCATGACGTGGTGTGTATCACTGATGAAGTCTACCAGTGGATGGTC
TACGACGGGCACCAGCACATCAGCATTGCCAGCCTCCCTGGCATGTGGGAACGGACCCTG
ACCATCGGCAGCGCCGGCAAGACCTTCAGCGCCACTGGCTGGAAGGTGGGCTGGGTCCTG
GGTCCAGATCACATCATGAAGCACCTGCGGACCGTGCACCAGAACTCCGTCTTCCACTGC
CCCACGCAGAGCCAGGCTGCAGTAGCCGAGAGCTTTGAACGGGAGCAGCTGCTCTTCCGC
CAACCCAGCAGCTACTTTGTGCAGTTCCCGCAGGCCATGCAGCGCTGCCGTGACCACATG
ATACGTAGCCTACAGTCAGTGGGCCTGAAGCCCATCATCCCTCAGGGCAGCTACTTCCTC
ATCACAGACATCTCAGACTTCAAGAGGAAGATGCCTGACTTGCCTGGAGCTGTGGATGAG
CCCTATGACAGACGCTTCGTCAAGTGGATGATCAAGAACAAGGGCTTGGTGGCCATCCCT
GTCTCCATCTTCTATAGTGTGCCACATCAGAAGCACTTTGACCACTATATCCGCTTCTGT
TTTGTGAAGGATGAAGCCACGCTCCAGGCCATGGACGAGAAGCTGCGGAAGTGGAAGGTG
GAACTCTAG
Enzyme 4 GenBank Gene ID X82224 Link Image
Enzyme 4 GeneCard ID CCBL1 Link Image
Enzyme 4 GenAtlas ID CCBL1 Link Image
Enzyme 4 HGNC ID HGNC:1564 Link Image
Enzyme 4 Chromosome Location 9
Enzyme 4 Locus 9q34.11
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Perry S, Harries H, Scholfield C, Lock T, King L, Gibson G, Goldfarb P: Molecular cloning and expression of a cDNA for human kidney cysteine conjugate beta-lyase. FEBS Lett. 1995 Mar 6;360(3):277-80. [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. Rossi F, Han Q, Li J, Li J, Rizzi M: Crystal structure of human kynurenine aminotransferase I. J Biol Chem. 2004 Nov 26;279(48):50214-20. Epub 2004 Sep 10. [PubMed Link Image]
  5. Han Q, Robinson H, Cai T, Tagle DA, Li J: Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K. J Med Chem. 2009 May 14;52(9):2786-93. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5852
Enzyme 5 Name Glutaminyl-tRNA synthetase
Enzyme 5 Synonyms
  1. Glutamine--tRNA ligase
  2. GlnRS
Enzyme 5 Gene Name QARS
Enzyme 5 Protein Sequence >Glutaminyl-tRNA synthetase
MAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGSTIDKATGILLYGLA
SRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPE
QIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPK
LEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKT
PGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFL
RFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQ
RGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYRV
KYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPV
QWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVG
VTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADET
KGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVES
LEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLASL
HVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV
Enzyme 5 Number of Residues 775
Enzyme 5 Molecular Weight 87798.0
Enzyme 5 Theoretical pI 7.16
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • aminoacyl-tRNA ligase activity
  • binding
  • catalytic activity
  • glutamine-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
  • glutaminyl-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 5 General Function Involved in nucleotide binding
Enzyme 5 Specific Function ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln)
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln [RN:R03652]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 558586 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P47897 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name SYQ_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2328 bp
ATGGCGGCTCTAGACTCCCTGTCGCTCTTCACTAGCCTCGGCCTGAGCGAGCAGAAGGCC
CGCGAGACGCTCAAGAACTCGGCTCTGAGCGCGCAGCTGCGCGAGGCCGCTACTCAGGCT
CAGCAGACCCTGGGTTCCACCATTGACAAAGCTACCGGGATCCTGTTATATGGCTTGGCC
TCCCGACTCAGGGATACCCGGCGTCTCTCCTTCCTTGTAAGCTACATAGCCAGTAAGAAG
ATCCACACTGAGCCCCAGCTAAGCGCTGCCCTTGAGTATGTGCGGAGTCACCCCTTGGAC
CCCATCGACACTGTGGACTTCGAGCGGGAATGTGGCGTGGGTGTCATTGTGACCCCAGAG
CAGATTGAGGAGGCTGTGGAGGCTGCTATTAACAGGCACCGGCCCCAGCTCCTGGTGGAA
CGTTACCATTTCAACATGGGGCTGCTGATGGGAGAGGCTCGGGCTGTGCTGAAGTGGGCA
GATGGCAAAATGATCAAGAATGAAGTGGACATGCAGGTCCTCCACCTTCTGGGCCCCAAG
TTGGAGGCTGATCTGGAGAAGAAGTTCAAGGTGGCAAAAGCTCGGCTAGAAGAAACAGAC
CGGAGGACGGCAAAGGATGTGGTGGAGAATGGCGAGACTGCTGACCAGACCCTGTCTCTG
ATGGAGCAGCTCCGGGGGGAGGCCCTTAAGTTCCACAAGCCTGGTGAGAACTACAAGACC
CCAGGCTATGTGGTCACTCCACACACCATGAATCTACTAAAGCAGCACCTGGAGATTACT
GGTGGGCAGGTACGTACCCGGTTCCCGCCAGAACCCAATGGAATCCTGCATATTGGACAT
GCCAAAGCCATCAATTTCAACTTTGGCTATGCCAAGGCCAACAATGGCATCTGTTTTCTG
CGTTTTGATGACACCAACCCTGAGAAGGAGGAAGCAAAGTTCTTCACGGCCATCTGTGAC
ATGGTAGCCTGGCTAGGCTACACACCTTACAAAGTCACATATGCGTCTGACTATTTTGAC
CAGCTATATGCGTGGGCTGTGGAGCTCATCCGCAGGGGTCTGGCTTATGTGTGCCACCAG
CGAGGAGAGGAGCTCAAAGGCCATAATACTCTGCCTTCACCCTGGAGAGACCGTCCCATG
GAGGAGTCACTGCTGCTCTTTGAGGCAATGCGCAAGGGCAAGTTTTCAGAGGGCGAGGCC
ACACTACGGATGAAGCTGGTGATGGAGGATGGCAAGATGGACCCTGTAGCCTATCGAGTC
AAGTATACACCACACCACCGCACAGGGGACAAATGGTGCATCTATCCCACCTACGACTAC
ACACACTGCCTCTGTGACTCCATCGAGCACATCACTCACTCACTCTGCACCAAGGAATTC
CAGGCCCGACGCTCTTCCTACTTCTGGCTTTGCAATGCACTGGACGTCTATTGCCCTGTG
CAGTGGGAGTATGGCCGCCTCAACCTGCACTATGCTGTTGTCTCTAAGAGGAAGATCCTC
CAGCTTGTAGCAACTGGTGCTGTGCGGGACTGGGATGACCCACGGCTCTTTACACTCACG
GCCCTGCGACGGCGGGGCTTCCCACCTGAGGCCATCAACAACTTCTGTGCCCGGGTGGGA
GTGACTGTGGCACAAACCACAATGGAGCCACATCTTCTAGAAGCCTGTGTGCGTGATGTG
CTGAATGACACAGCCCCACGAGCCATGGCTGTGCTGGAGTCACTACGGGTCATCATCACC
AACTTTCCTGCTGCCAAGTCCTTGGACATCCAGGTGCCCAACTTCCCAGCTGATGAGACC
AAAGGCTTCCATCAGGTTCCCTTTGCACCCATTGTCTTCATTGAGAGGACTGACTTCAAG
GAGGAGCCAGAGCCAGGATTTAAGCGCCTGGCTTGGGGCCAGCCTGTGGGCCTGAGGCAT
ACAGGCTACGTCATTGAGCTGCAGCATGTTGTCAAGGGCCCCAGTGGTTGTGTAGAGAGT
CTGGAGGTGACCTGCAGACGGGCAGATGCTGGAGAGAAGCCAAAGGCCTTTATTCACTGG
GTGTCACAGCCTTTGATGTGTGAGGTTCGCCTCTATGAGCGACTATTCCAGCACAAGAAC
CCTGAAGATCCTACTGAGGTGCCTGGTGGATTTTTAAGTGACCTGAACCTGGCATCACTA
CACGTGGTGGATGCAGCATTAGTGGACTGCTCTGTGGCCCTGGCAAAACCCTTCGACAAG
TTCCAGTTTGAGCGTCTTGGATATTTCTCCGTGGATCCAGACAGCCATCAGGGAAAGCTT
GTCTTTAACCGAACTGTCACACTGAAGGAAGACCCAGGAAAGGTGTGA
Enzyme 5 GenBank Gene ID X76013 Link Image
Enzyme 5 GeneCard ID QARS Link Image
Enzyme 5 GenAtlas ID QARS Link Image
Enzyme 5 HGNC ID HGNC:9751 Link Image
Enzyme 5 Chromosome Location 3
Enzyme 5 Locus 3p21.31
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Lamour V, Quevillon S, Diriong S, N'Guyen VC, Lipinski M, Mirande M: Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer. Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8670-4. [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. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5855
Enzyme 6 Name Asparagine synthetase [glutamine-hydrolyzing]
Enzyme 6 Synonyms
  1. Cell cycle control protein TS11
  2. Glutamine-dependent asparagine synthetase
Enzyme 6 Gene Name ASNS
Enzyme 6 Protein Sequence >Asparagine synthetase [glutamine-hydrolyzing]
MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQ
PIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGV
FAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPF
LPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFN
NAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAAR
KVADHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVV
IFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPF
LDHRFSSYYLSLPPEMRIPKNGIEKHLLRETFEDSNLIPKEILWRPKEAFSDGITSVKNS
WFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLSHYWMPK
WINATDPSARTLTHYKSAVKA
Enzyme 6 Number of Residues 561
Enzyme 6 Molecular Weight 64369.4
Enzyme 6 Theoretical pI 6.85
Enzyme 6 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 6 General Function Involved in asparagine synthase (glutamine-hydrolyzing) activity
Enzyme 6 Specific Function ATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate
Enzyme 6 Pathways
Enzyme 6 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 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 179100 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P08243 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ASNS_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 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 6 GenBank Gene ID M27396 Link Image
Enzyme 6 GeneCard ID ASNS Link Image
Enzyme 6 GenAtlas ID ASNS Link Image
Enzyme 6 HGNC ID HGNC:753 Link Image
Enzyme 6 Chromosome Location 7
Enzyme 6 Locus 7q21.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5864
Enzyme 7 Name GMP synthase [glutamine-hydrolyzing]
Enzyme 7 Synonyms
  1. GMP synthetase
  2. Glutamine amidotransferase
Enzyme 7 Gene Name GMPS
Enzyme 7 Protein Sequence >GMP synthase [glutamine-hydrolyzing]
MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETP
AFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHK
KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANE
SKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAA
HSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPE
EVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVR
ILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPH
TLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDW
ESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVE
VVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
Enzyme 7 Number of Residues 693
Enzyme 7 Molecular Weight 76714.8
Enzyme 7 Theoretical pI 6.86
Enzyme 7 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 7 General Function Involved in catalytic activity
Enzyme 7 Specific Function Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate [RN:R01231]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID P49915 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name GUAA_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 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 7 GenBank Gene ID U10860 Link Image
Enzyme 7 GeneCard ID GMPS Link Image
Enzyme 7 GenAtlas ID GMPS Link Image
Enzyme 7 HGNC ID HGNC:4378 Link Image
Enzyme 7 Chromosome Location 3
Enzyme 7 Locus 3q24
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Hirst M, Haliday E, Nakamura J, Lou L: Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA. J Biol Chem. 1994 Sep 23;269(38):23830-7. [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. Pegram LD, Megonigal MD, Lange BJ, Nowell PC, Rowley JD, Rappaport EF, Felix CA: t(3;11) translocation in treatment-related acute myeloid leukemia fuses MLL with the GMPS (GUANOSINE 5' MONOPHOSPHATE SYNTHETASE) gene. Blood. 2000 Dec 15;96(13):4360-2. [PubMed Link Image]
  4. 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]
  5. 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]
  6. 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]
  7. 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 5938
Enzyme 8 Name Protein-glutamine gamma-glutamyltransferase E
Enzyme 8 Synonyms
  1. Transglutaminase E
  2. TG(E)
  3. TGE
  4. TGase E
  5. Transglutaminase-3
  6. TGase-3
  7. Protein-glutamine gamma-glutamyltransferase E 50 kDa non-catalytic chain
  8. Protein-glutamine gamma-glutamyltransferase E 27 kDa catalytic chain
Enzyme 8 Gene Name TGM3
Enzyme 8 Protein Sequence >Protein-glutamine gamma-glutamyltransferase E
MAALGVQSINWQTAFNRQAHHTDKFSSQELILRRGQNFQVLMIMNKGLGSNERLEFIVST
GPYPSESAMTKAVFPLSNGSSGGWSAVLQASNGNTLTISISSPASAPIGRYTMALQIFSQ
GGISSVKLGTFILLFNPWLNVDSVFMGNHAEREEYVQEDAGIIFVGSTNRIGMIGWNFGQ
FEEDILSICLSILDRSLNFRRDAATDVASRNDPKYVGRVLSAMINSNDDNGVLAGNWSGT
YTGGRDPRSWNGSVEILKNWKKSGFSPVRYGQCWVFAGTLNTALRSLGIPSRVITNFNSA
HDTDRNLSVDVYYDPMGNPLDKGSDSVWNFHVWNEGWFVRSDLGPSYGGWQVLDATPQER
SQGVFQCGPASVIGVREGDVQLNFDMPFIFAEVNADRITWLYDNTTGKQWKNSVNSHTIG
RYISTKAVGSNARMDVTDKYKYPEGSDQERQVFQKALGKLKPNTPFAATSSMGLETEEQE
PSIIGKLKVAGMLAVGKEVNLVLLLKNLSRDTKTVTVNMTAWTIIYNGTLVHEVWKDSAT
MSLDPEEEAEHPIKISYAQYEKYLKSDNMIRITAVCKVPDESEVVVERDIILDNPTLTLE
VLNEARVRKPVNVQMLFSNPLDEPVRDCVLMVEGSGLLLGNLKIDVPTLGPKEGSRVRFD
ILPSRSGTKQLLADFSCNKFPAIKAMLSIDVAE
Enzyme 8 Number of Residues 693
Enzyme 8 Molecular Weight 76631.3
Enzyme 8 Theoretical pI 5.60
Enzyme 8 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
Enzyme 8 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 8 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. It is responsible for the later stages of cell envelope formation in the epidermis and the hair follicle
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 [RN:R03983]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 307504 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q08188 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name TGM3_HUMAN Link Image
Enzyme 8 PDB ID 1SGX Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >2082 bp
ATGGCTGCTCTAGGAGTCCAGAGTATCAACTGGCAGAAGGCCTTCAACCGACAAGCGCAT
CACACAGACAAGTTCTCCAGCCAGGAGCTCATCTTGCGGAGAGGCCAAAACTTCCAGGTC
TTAATGATCATGAACAAAGGCCTTGGCTCTAACGAAAGACTGGAGTTCATTGACACCACA
GGGCCTTACCCCTCAGAGTCGGCCATGACGAAGGCTGTGTTTCCACTCTCCAATGGCAGT
AGTGGTGGCTGGAGTGCGGTGCTTCAGGCCAGCAATGGCAATACTCTGACTATCAGCATC
TCCAGTCCTGCCAGCGCACCCATAGGACGGTACACAATGGCCCTCCAGATCTTCTCCCAG
GGCGGCATCTCCTCTGTGAAACTTGGGACGTTCATACTGCTTTTTAACCCCTGGCTGAAT
GTGGATAGCGTCTTTATGGGTAACCATGCTGAGAGAGAAGAGTATGTTCAGGAAGATGCC
GGCATCATCTTTGTGGGAAGCACAAACCGAATTGGCATGATTGGCTGGAACTTTGGACAG
TTTGAAGAAGACATTCTCAGCATCTGCCTCTCAATCTTGGATAGGAGTCTGAATTTCCGC
CGTGACGCTGCTACTGATGTGGCCAGCAGAAATGACCCCAAATACGTTGGCCGGGTGCTG
AGTGCCATGATCAATAGCAATGATGACAATGGTGTGCTTGCTGGGAATTGGAGCGGCACT
TACACCGGTGGCCGGGACCCAAGGAGCTGGGACGGCAGCGTGGAGATCCTCAAAAATTGG
AAAAAATCTGGCTTCAGCCCAGTCCGATATGGCCAGTGCTGGGTCTTTGCTGGGACCCTC
AACACAGCGCTGCGGTCTTTGGGGATTCCTTCCCGGGTGATCACCAACTTCAACTCAGCT
CATGACACAGACCGAAATCTCAGTGTGGATGTGTACTACGACCCCATGGGAAACCCCCTG
GACAAGGGTAGTGATAGCGTATGGAATTTCCATGTCTGGAATGAAGGCTGGTTTGTGAGG
TCTGACCTGGGCCCCCCGTACGGTGGATGGCAGGTGTTGGATGCTACCCCGCAGGAAAGA
AGCCAAGGGGTGTTCCAGTGCGGCCCCGCTTCGGTCATTGGTGTTCGAGAGGGTGATGTG
CAGCTGAACTTCGACATGCCCTTTATCTTCGCGGAGGTTAATGCCGACCGCATCACCTGG
CTGTACGACAACACCACTGGCAAACAGTGGAAGAATTCCGTGAACAGTCACACCATTGGC
AGGTACATCAGCACCAAGGCGGTGGGCAGCAATGCTCGCATGGACGTCACGGACAAGTAC
AAGTACCCAGAAGGCTCTGACCAGGAAAGACAAGTGTTCCAAAAGGCTTTGGGGAAACTT
AAACCCAACACGCCATTTGCCGCGACGTCTTCGATGGGTTTGGAAACAGAGGAACAGGAG
CCCAGCATCATCGGGAAGCTGAAGGTCGCTGGCATGCTGGCAGTAGGCAAAGAAGTCAAC
CTGGTCCTACTGCTCAAAAACCTGAGCAGGGATACGAAGACAGTGACAGTGAACATGACA
GCCTGGACCATCATCTACAACGGCACGCTTGTACATGAAGTGTGGAAGGACTCTGCCACA
ATGTCCCTGGACCCTGAGGAAGAGGCAGAACATCCCATAAAGATCTCGTACGCTCAGTAT
GAGAGGTACCTGAAGTCAGACAACATGATCCGGATCACAGCGGTGTGCAAGGTCCCAGAT
GAGTCTGAGGTGGTGGTGGAGCGGGACATCATCCTGGACAACCCCACCTTGACCCTGGAG
GTGCTGAACGAGGCTCGTGTGCGGAAGCCTGTGAACGTGCAGATGCTCTTCTCCAATCCA
CTGGATGAGCCGGTGAGGGACTGCGTGCTGATGGTGGAGGGAAGCGGCCTGCTGTTGGGT
AACCTGAAGATCGACGTGCCGACCCTAGGGCCCAAGGAGCGGTCCCGGGTCCGTTTTGAT
ATCCTGCCCTCCCGGAGTGGCACCAAGCAACTGCTCGCCGACTTCTCCTGCAACAAGTTC
CCTGCAATCAAGGCCATGTTGTCCATCGACGTAGCCGAATGA
Enzyme 8 GenBank Gene ID L10386 Link Image
Enzyme 8 GeneCard ID TGM3 Link Image
Enzyme 8 GenAtlas ID TGM3 Link Image
Enzyme 8 HGNC ID HGNC:11779 Link Image
Enzyme 8 Chromosome Location 2
Enzyme 8 Locus 20q11.2
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Kim IG, Gorman JJ, Park SC, Chung SI, Steinert PM: The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse. J Biol Chem. 1993 Jun 15;268(17):12682-90. [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. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5940
Enzyme 9 Name Protein-glutamine gamma-glutamyltransferase 2
Enzyme 9 Synonyms
  1. Tissue transglutaminase
  2. Transglutaminase C
  3. TG(C)
  4. TGC
  5. TGase C
  6. Transglutaminase H
  7. TGase H
  8. Transglutaminase-2
  9. TGase-2
Enzyme 9 Gene Name TGM2
Enzyme 9 Protein Sequence >Protein-glutamine gamma-glutamyltransferase 2
MAEELVLERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEGRNYEASVDSLTFS
VVTGPAPSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTTPANAPIGLYRLSLE
ASTGYQGSSFVLGHFILLFNAWCPADAVYLDSEEERQEYVLTQQGFIYQGSAKFIKNIPW
NFGQFEDGILDICLILLDVNPKFLKNAGRDCSRRSSPVYVGRVVSGMVNCNDDQGVLLGR
WDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTN
YNSAHDQNSNLLIEYFRNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQALDPT
PQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAEVNADVVDWIQQDDGSVHKSINRSL
IVGLKISTKSVGRDEREDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMRIRVG
QSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSYNGILGPECGTKYLLNLNLEPFSEK
SVPLCILYEKYRDCLTESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGEPKQK
RKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTVEIPDPVEAGEEVKVRMDLLPLHMG
LHKLVVNFESDKLKAVKGFRNVIIGPA
Enzyme 9 Number of Residues 687
Enzyme 9 Molecular Weight 77328.2
Enzyme 9 Theoretical pI 4.86
Enzyme 9 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
Enzyme 9 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 9 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 [RN:R03983]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 158256860 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P21980 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name TGM2_HUMAN Link Image
Enzyme 9 PDB ID 1KV3 Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >2064 bp
ATGGCCGAGGAGCTGGTCTTAGAGAGGTGTGATCTGGAGCTGGAGACCAATGGCCGAGAC
CACCACACGGCCGACCTGTGCCGGGAGAAGCTGGTGGTGCGACGGGGCCAGCCCTTCTGG
CTGACCCTGCACTTTGAGGGCCGCAACTACGAGGCCAGTGTAGACAGTCTCACCTTCAGT
GTCGTGACCGGCCCAGCCCCTAGCCAGGAGGCCGGGACCAAGGCCCGTTTTCCACTAAGA
GATGCTGTGGAGGAGGGTGACTGGACAGCCACCGTGGTGGACCAGCAAGACTGCACCCTC
TCGCTGCAGCTCACCACCCCGGCCAACGCCCCCATCGGCCTGTATCGCCTCAGCCTGGAG
GCCTCCACTGGCTACCAGGGATCCAGCTTTGTGCTGGGCCACTTCATTTTGCTCTTCAAC
GCCTGGTGCCCAGCGGATGCTGTGTACCTGGACTCGGAAGAGGAGCGGCAGGAGTATGTC
CTCACCCAGCAGGGCTTTATCTACCAGGGCTCGGCCAAGTTCATCAAGAACATACCTTGG
AATTTTGGGCAGTTTGAAGATGGGATCCTAGACATCTGCCTGATCCTTCTAGATGTCAAC
CCCAAGTTCCTGAAGAACGCCGGCCGTGACTGCTCCCGCCGCAGCAGCCCCGTCTACGTG
GGCCGGGTGGTGAGTGGCATGGTCAACTGCAACGATGACCAGGGTGTGCTGCTGGGACGC
TGGGACAACAACTACGGGGACGGCGTCAGCCCCATGTCCTGGATCGGCAGCGTGGACATC
CTGCGGCGCTGGAAGAACCACGGCTGCCAGCGCGTCAAGTATGGCCAGTGCTGGGTCTTC
GCCGCCGTGGCCTGCACAGTGCTGAGGTGCCTGGGCATCCCTACCCGCGTCGTGACCAAC
TACAACTCGGCCCATGACCAGAACAGCAACCTTCTCATCGAGTACTTCCGCAATGAGTTT
GGGGAGATCCAGGGTGACAAGAGCGAGATGATCTGGAACTTCCACTGCTGGGTGGAGTCG
TGGATGACCAGGCCGGACCTGCAGCCGGGGTACGAGGGCTGGCAGGCCCTGGACCCAACG
CCCCAGGAGAAGAGCGAAGGGACGTACTGCTGTGGCCCAGTTCCAGTTCGTGCCATCAAG
GAGGGCGACCTGAGCACCAAGTACGATGCGCCCTTTGTCTTTGCGGAGGTCAATGCCGAC
GTGGTAGACTGGATCCAGCAGGACGATGGGTCTGTGCACAAATCCATCAACCGTTCCCTG
ATCGTTGGGCTGAAGATCAGCACTAAGAGCGTGGGCCGAGACGAGCGGGAGGATATCACC
CACACCTACAAATACCCAGAGGGGTCCTCAGAGGAGAGGGAGGCCTTCACAAGGGCGAAC
CACCTGAACAAACTGGCCGAGAAGGAGGAGACAGGGATGGCCATGCGGATCCGTGTGGGC
CAGAGCATGAACATGGGCAGTGACTTTGACGTCTTTGCCCACATCACCAACAACACCGCT
GAGGAGTACGTCTGCCGCCTCCTGCTCTGTGCCCGCACCGTCAGCTACAATGGGATCTTG
GGGCCCGAGTGTGGCACCAAGTACCTGCTCAACCTCAACCTGGAGCCTTTCTCTGAGAAG
AGCGTTCCTCTTTGCATCCTCTATGAGAAATACCGTGACTGCCTTACGGAGTCCAACCTC
ATCAAGGTGCGGGCCCTCCTCGTGGAGCCAGTTATCAACAGCTACCTGCTGGCTGAGAGG
GACCTCTACCTGGAGAATCCAGAAATCAAGATCCGGATCCTTGGGGAGCCCAAGCAGAAA
CGCAAGCTGGTGGCTGAGGTGTCCCTGCAGAACCCGCTCCCTGTGGCCCTGGAAGGCTGC
ACCTTCACTGTGGAGGGGGCCGGCCTGACTGAGGAGCAGAAGACGGTGGAGATCCCAGAC
CCCGTGGAGGCAGGGGAGGAAGTTAAGGTGAGAATGGACCTGCTGCCGCTCCACATGGGC
CTCCACAAGCTGGTGGTGAACTTCGAGAGCGACAAGCTGAAGGCTGTGAAGGGCTTCCGG
AATGTCATCATTGGCCCCGCCTAA
Enzyme 9 GenBank Gene ID AK291714 Link Image
Enzyme 9 GeneCard ID TGM2 Link Image
Enzyme 9 GenAtlas ID TGM2 Link Image
Enzyme 9 HGNC ID HGNC:11778 Link Image
Enzyme 9 Chromosome Location 2
Enzyme 9 Locus 20q12
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Gentile V, Saydak M, Chiocca EA, Akande O, Birckbichler PJ, Lee KN, Stein JP, Davies PJ: Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases. J Biol Chem. 1991 Jan 5;266(1):478-83. [PubMed Link Image]
  2. Fraij BM, Birckbichler PJ, Patterson MK Jr, Lee KN, Gonzales RA: A retinoic acid-inducible mRNA from human erythroleukemia cells encodes a novel tissue transglutaminase homologue. J Biol Chem. 1992 Nov 5;267(31):22616-23. [PubMed Link Image]
  3. Fraij BM, Gonzales RA: A third human tissue transglutaminase homologue as a result of alternative gene transcripts. Biochim Biophys Acta. 1996 Apr 10;1306(1):63-74. [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. 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]
  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. 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. 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. 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]
  10. Pinkas DM, Strop P, Brunger AT, Khosla C: Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol. 2007 Dec;5(12):e327. [PubMed Link Image]
  11. 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]
  12. Porzio O, Massa O, Cunsolo V, Colombo C, Malaponti M, Bertuzzi F, Hansen T, Johansen A, Pedersen O, Meschi F, Terrinoni A, Melino G, Federici M, Decarlo N, Menicagli M, Campani D, Marchetti P, Ferdaoussi M, Froguel P, Federici G, Vaxillaire M, Barbetti F: Missense mutations in the TGM2 gene encoding transglutaminase 2 are found in patients with early-onset type 2 diabetes. Mutation in brief no. 982. Online. Hum Mutat. 2007 Nov;28(11):1150. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5943
Enzyme 10 Name Glutamine synthetase
Enzyme 10 Synonyms
  1. GS
  2. Glutamate decarboxylase
  3. Glutamate--ammonia ligase
Enzyme 10 Gene Name GLUL
Enzyme 10 Protein Sequence >Glutamine synthetase
MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEW
NFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRI
MDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHY
RACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDP
KPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRL
TGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCL
LNETGDEPFQYKN
Enzyme 10 Number of Residues 373
Enzyme 10 Molecular Weight 42064.1
Enzyme 10 Theoretical pI 6.88
Enzyme 10 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 10 General Function Involved in glutamate-ammonia ligase activity
Enzyme 10 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 10 Pathways
Enzyme 10 Reactions
  • ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine [RN:R00253]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 31833 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P15104 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name GLNA_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1122 bp
ATGACCACCTCAGCAAGTTCCCACTTAAATAAAGGCATCAAGCAGGTGTACATGTCCCTG
CCTCAGGGTGAGAAAGTCCAGGCCATGTATATCTGGATCGATGGTACTGGAGAAGGACTG
CGCTGCAAGACCCGGACCCTGGACAGTGAGCCCAAGTGTGTGGAAGAGTTGCCTGAGTGG
AATTTCGATGGCTCCAGTACTTTACAGTCTGAGGGTTCCAACAGTGACATGTATCTCGTG
CCTGCTGCCATGTTTCGGGACCCCTTCCGTAAGGACCCTAACAAGCTGGTGTTATGTGAA
GTTTTCAAGTACAATCGAAGGCCTGCAGAGACCAATTTGAGGCACACCTGTAAACGGATA
ATGGACATGGTGAGCAACCAGCACCCCTGGTTTGGCATGGAGCAGGAGTATACCCTCATG
GGGACAGATGGGCACCCCTTTGGTTGGCCTTCCAACGGCTTCCCAGGGCCCCAGGGTCCA
TATTACTGTGGTGTGGGAGCAGACAGAGCCTATGGCAGGGACATCGTGGAGGCCCATTAC
CGGGCCTGCTTGTATGCTGGAGTCAAGATTGCGGGGACTAATGCCGAGGTCATGCCTGCC
CAGTGGGAATTTCAGATTGGACCTTGTGAAGGAATCAGCATGGGAGATCATCTCTGGGTG
GCCCGTTTCATCTTGCATCGTGTGTGTGAAGACTTTGGAGTGATAGCAACCTTTGATCCT
AAGCCCATTCCTGGGAACTGGAATGGTGCAGGCTGCCATACCAACTTCAGCACCAAGGCC
ATGCGGGAGGAGAATGGTCTGAAGTACATCGAGGAGGCCATTGAGAAACTAAGCAAGCGG
CACCAGTACCACATCCGTGCCTATGATCCCAAGGGAGGCCTGGACAATGCCCGACGTCTA
ACTGGATTCCATGAAACCTCCAACATCAACGACTTTTCTGGTGGTGTAGCCAATCGTAGC
GCCAGCATACGCATTCCCCGGACTGTTGGCCAGGAGAAGAAGGGTTACTTTGAAGATCGT
CGCCCCTCTGCCAACTGCGACCCCTTTTCGGTGACAGAAGCCCTCATCCGCACGTGTCTT
CTCAATGAAACCGGCGATGAGCCCTTCCAGTACAAAAATTAA
Enzyme 10 GenBank Gene ID Y00387 Link Image
Enzyme 10 GeneCard ID GLUL Link Image
Enzyme 10 GenAtlas ID GLUL Link Image
Enzyme 10 HGNC ID HGNC:4341 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 1q31
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5945
Enzyme 11 Name Coagulation factor XIII A chain
Enzyme 11 Synonyms
  1. Coagulation factor XIIIa
  2. Protein-glutamine gamma-glutamyltransferase A chain
  3. Transglutaminase A chain
Enzyme 11 Gene Name F13A1
Enzyme 11 Protein Sequence >Coagulation factor XIII A chain
MSETSRTAFGGRRAVPPNNSNAAEDDLPTVELQGVVPRGVNLQEFLNVTSVHLFKERWDT
NKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPV
PIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETD
TYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCL
YVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDIL
LEYRSSENPVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGN
VNSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAIKH
GHVCFQFDAPFVFAEVNSDLIYITAKKDGTHVVENVDATHIGKLIVTKQIGGDGMMDITD
TYKFQEGQEEERLALETALMYGAKKPLNTEGVMKSRSNVDMDFEVENAVLGKDFKLSITF
RNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLIQAGEYMGQLL
EQASLHFFVTARINETRDVLAKQKSTVLTIPEIIIKVRGTQVVGSDMTVTVQFTNPLKET
LRNVWVHLDGPGVTRPMKKMFREIRPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYG
ELDVQIQRRPSM
Enzyme 11 Number of Residues 732
Enzyme 11 Molecular Weight 83266.8
Enzyme 11 Theoretical pI 5.95
Enzyme 11 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
Enzyme 11 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 11 Specific Function Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl- epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 [RN:R03983]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 119395709 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P00488 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name F13A_HUMAN Link Image
Enzyme 11 PDB ID 1FIE Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >2199 bp
ATGTCAGAAACTTCCAGGACCGCCTTTGGAGGCAGAAGAGCAGTTCCACCCAATAACTCT
AATGCAGCGGAAGATGACCTGCCCACAGTGGAGCTTCAGGGCGTGGTGCCCCGGGGCGTC
AACCTGCAAGAGTTTCTTAATGTCACGAGCGTTCACCTGTTCAAGGAGAGATGGGACACT
AACAAGGTGGACCACCACACTGACAAGTATGAAAACAACAAGCTGATTGTCCGCAGAGGG
CAGTCTTTCTATGTGCAGATTGACTTCAGTCGTCCATATGACCCCAGAAGGGATCTCTTC
AGGGTGGAATACGTCATTGGTCGCTACCCACAGGAGAACAAGGGAACCTACATCCCAGTG
CCTATAGTCTCAGAGTTACAAAGTGGAAAGTGGGGGGCCAAGATTGTCATGAGAGAGGAC
AGGTCTGTGCGGCTGTCCATCCAGTCTTCCCCCAAATGTATTGTGGGGAAATTCCGCATG
TATGTTGCTGTCTGGACTCCCTATGGCGTACTTCGAACCAGTCGAAACCCAGAAACAGAC
ACGTACATTCTCTTCAATCCTTGGTGTGAAGATGATGCTGTGTATCTGGACAATGAGAAA
GAAAGAGAAGAGTATGTCCTGAATGACATCGGGGTAATTTTTTATGGAGAGGTCAATGAC
ATCAAGACCAGAAGCTGGAGCTATGGTCAGTTTGAAGATGGCATCCTGGACACTTGCCTG
TATGTGATGGACAGAGCACAAATGGACCTCTCTGGAAGAGGGAATCCCATCAAAGTCAGC
CGTGTGGGGTCTGCAATGGTGAATGCCAAAGATGACGAAGGTGTCCTCGTTGGATCCTGG
GACAATATCTATGCCTATGGCGTCCCCCCATCGGCCTGGACTGGAAGCGTTGACATTCTA
TTGGAATACCGGAGCTCTGAGAATCCAGTCCGGTATGGCCAATGCTGGGTTTTTGCTGGT
GTCTTTAACACATTTTTACGATGCCTTGGAATACCAGCAAGAATTGTTACCAATTATTTC
TCTGCCCATGATAATGATGCCAATTTGCAAATGGACATCTTCCTGGAAGAAGATGGGAAC
GTGAATTCCAAACTCACCAAGGATTCAGTGTGGAACTACCACTGCTGGAATGAAGCATGG
ATGACAAGGCCTGACCTTCCTGTTGGATTTGGAGGCTGGCAAGCTGTGGACAGCACCCCC
CAGGAAAATAGCGATGGCATGTATCGGTGTGGCCCCGCCTCGGTTCAAGCCATCAAGCAC
GGCCATGTCTGCTTCCAATTTGATGCACCTTTTGTTTTTGCAGAGGTCAACAGCGACCTC
ATTTACATTACAGCTAAGAAAGATGGCACTCATGTGGTGGAAAATGTGGATGCCACCCAC
ATTGGGAAATTAATTGTGACCAAACAAATTGGAGGAGATGGCATGATGGATATTACTGAT
ACTTACAAATTCCAAGAAGGTCAAGAAGAAGAGAGATTGGCCCTAGAAACTGCCCTGATG
TACGGAGCTAAAAAGCCCCTCAACACAGAAGGTGTCATGAAATCAAGGTCCAACGTTGAC
ATGGACTTTGAAGTGGAAAATGCTGTGCTGGGAAAAGACTTCAAGCTCTCCATCACCTTC
CGGAACAACAGCCACAACCGTTACACCATCACAGCTTATCTCTCAGCCAACATCACCTTC
TACACCGGGGTCCCGAAGGCAGAATTCAAGAAGGAGACGTTCGACGTGACGCTGGAGCCC
TTGTCCTTCAAGAAAGAGGCGGTGCTGATCCAAGCCGGCGAGTACATGGGTCAGCTGCTG
GAACAAGCGTCCCTGCACTTCTTTGTCACAGCTCGCATCAATGAGACCAGGGATGTTCTG
GCCAAGCAAAAGTCCACCGTGCTAACCATCCCTGAGATCATCATCAAGGTCCGTGGCACT
CAGGTAGTTGGTTCTGACATGACTGTGACAGTTGAGTTTACCAATCCTTTAAAAGAAACC
CTGCGAAATGTCTGGGTACACCTGGATGGTCCTGGAGTAACAAGACCAATGAAGAAGATG
TTCCGTGAAATCCGGCCCAACTCCACCGTGCAGTGGGAAGAAGTGTGCCGGCCCTGGGTC
TCTGGGCATCGGAAGCTGATAGCCAGCATGAGCAGTGACTCCCTGAGACATGTGTATGGC
GAGCTGGACGTGCAGATTCAAAGACGACCTTCCATGTGA
Enzyme 11 GenBank Gene ID NM_000129.3 Link Image
Enzyme 11 GeneCard ID F13A1 Link Image
Enzyme 11 GenAtlas ID F13A1 Link Image
Enzyme 11 HGNC ID HGNC:3531 Link Image
Enzyme 11 Chromosome Location 6
Enzyme 11 Locus 6p25.3-p24.3
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Ichinose A, Hendrickson LE, Fujikawa K, Davie EW: Amino acid sequence of the a subunit of human factor XIII. Biochemistry. 1986 Nov 4;25(22):6900-6. [PubMed Link Image]
  2. Grundmann U, Amann E, Zettlmeissl G, Kupper HA: Characterization of cDNA coding for human factor XIIIa. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8024-8. [PubMed Link Image]
  3. Ichinose A, Davie EW: Characterization of the gene for the a subunit of human factor XIII (plasma transglutaminase), a blood coagulation factor. Proc Natl Acad Sci U S A. 1988 Aug;85(16):5829-33. [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. 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. Takahashi N, Takahashi Y, Putnam FW: Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8019-23. [PubMed Link Image]
  7. Takagi T, Doolittle RF: Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin. Biochemistry. 1974 Feb 12;13(4):750-6. [PubMed Link Image]
  8. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  9. Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC: Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7296-300. [PubMed Link Image]
  10. Yee VC, Pedersen LC, Bishop PD, Stenkamp RE, Teller DC: Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII. Thromb Res. 1995 Jun 1;78(5):389-97. [PubMed Link Image]
  11. Weiss MS, Metzner HJ, Hilgenfeld R: Two non-proline cis peptide bonds may be important for factor XIII function. FEBS Lett. 1998 Feb 27;423(3):291-6. [PubMed Link Image]
  12. Fox BA, Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC: Identification of the calcium binding site and a novel ytterbium site in blood coagulation factor XIII by x-ray crystallography. J Biol Chem. 1999 Feb 19;274(8):4917-23. [PubMed Link Image]
  13. Suzuki K, Iwata M, Ito S, Matsui K, Uchida A, Mizoi Y: Molecular basis for subtypic differences of the "a" subunit of coagulation factor XIII with description of the genesis of the subtypes. Hum Genet. 1994 Aug;94(2):129-35. [PubMed Link Image]
  14. Board P, Coggan M, Miloszewski K: Identification of a point mutation in factor XIII A subunit deficiency. Blood. 1992 Aug 15;80(4):937-41. [PubMed Link Image]
  15. Kangsadalampai S, Board PG: The Val34Leu polymorphism in the A subunit of coagulation factor XIII contributes to the large normal range in activity and demonstrates that the activation peptide plays a role in catalytic activity. Blood. 1998 Oct 15;92(8):2766-70. [PubMed Link Image]
  16. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5948
Enzyme 12 Name Glutaminase liver isoform, mitochondrial
Enzyme 12 Synonyms
  1. GLS
  2. L-glutaminase
  3. L-glutamine amidohydrolase
Enzyme 12 Gene Name GLS2
Enzyme 12 Protein Sequence >Glutaminase liver isoform, mitochondrial
MRSMKALQKALSRAGSHCGRGGWGHPSRSPLLGGGVRHHLSEAAAQGRETPHSHQPQHQD
HDSSESGMLSRLGDLLFYTIAEGQERIPIHKFTTALKATGLQTSDPRLRDCMSEMHRVVQ
ESSSGGLLDRDLFRKCVSSNIVLLTQAFRKKFVIPDFEEFTGHVDRIFEDVKELTGGKVA
AYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHK
FVGKEPSGLRYNKLSLNEEGIPHNPMVNAGAIVVSSLIKMDCNKAEKFDFVLQYLNKMAG
NEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMMAALDLYFQLCSVEVTCESG
SVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGA
ILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFHNYDNLRHCARKLDPRREGA
EIRNKTVVNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIE
ACKVNPFAKDRWGNIPLDDAVQFNHLEVVKLLQDYQDSYTLSETQAEAAAEALSKENLES
MV
Enzyme 12 Number of Residues 602
Enzyme 12 Molecular Weight 66322.2
Enzyme 12 Theoretical pI 7.32
Enzyme 12 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 12 General Function Involved in glutaminase activity
Enzyme 12 Specific Function Plays an important role in the regulation of glutamine catabolism
Enzyme 12 Pathways
Enzyme 12 Reactions
  • L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 6650606 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9UI32 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name GLSL_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1809 bp
ATGCGCTCCATGAAGGCTCTGCAGAAGGCCCTGAGCCGGGCTGGCAGTCACTGCGGGCGA
GGAGGCTGGGGTCACCCGAGCCGGAGCCCCCTCCTTGGCGGGGGCGTCCGGCACCACCTC
AGTGAGGCCGCGGCGCAGGGCAGAGAGACGCCACACAGCCACCAGCCGCAGCACCAGGAT
CATGATTCATCAGAAAGTGGCATGCTGTCCCGCCTGGGTGATTTGCTCTTTTACACTATT
GCTGAAGGACAGGAACGAACCCCTATCCACAAGTTCACCACTGCACTAAAGGCCACTGGA
CTGCAGACATCAGATCCTCGGCTCCGAGACTGCATGAGCGAGATGCACCGCGTGGTCCAA
GAGTCCAGTAGTGGTGGCCTCTTGGACCGAGATCTCTTCCGAAAGTGTGTGAGCAGCAGC
ATTGTGCTCCTGACCCAGGCATTCCGAAAGAAGTTTGTCATTCCTGATTTTGAGGAGTTC
ACGGGCCATGTGGATCGCATCTTTGAGGATGTCAAAGAGCTCACTGGAGGCAAAGTGGCA
GCCTACATCCCTCAGCTGGCCAAGTCAAACCCAGACCTGTGGGGTGTCTCCCTGTGCACT
GTGGATGGTCAACGGCACTCTGTGGGCCACACAAAGATCCCCTTCTGCCTGCAGTCCTGT
GTGAAGCCCCTCACCTATGCCATCTCCATAAGCACCCTAGGCACTGACTACGTGCACAAG
TTTGTGGGCAAAGAGCCAAGTGGCCTGCGCTACAACAAGCTCTCCCTCGATGAGGAAGGA
ATCCCCCATAACCCCATGGTCAATGCTGGTGCCATTGTTGTCAGCTCCCTGATCAAGATG
GACTGTAACAAAGCAGAGAAGTTTGATTTTGTGTTGCAGTATCTCAACAAAATGGCTGGG
AATGAATACATGGGTTTCAGCAATGCCACATTCCAGTCAGAGAAGGAAACAGGGGATCGG
AATTATGCCATCGGCTATTATCACGAGGAAAAGAAGTGCTTTCCTAAGGGGGTGGACATG
ATGGCTGCCCTTGATCTCTACTTCCAGCTGTGTTCTGTGGAGGTCACTTGTGAATCAGGC
AGTGTCATGGCAGCCACCCTCGCCAACGGTGGGATTTGCCCCATCACAGGCGAGAGTGTG
CTGAGTGCTGAAGCAGTGCGCAACACCCTCAGCCTCATGCATTCCTGCGGCATGTATGAC
TTCTCTGGCCAGTTTGCCTTCCACGTGGGCCTGCCAGCCAAGTCAGCTGTATCAGGAGCC
ATCCTCCTGGTGGTACCCAATGTCATGGGAATGATGTGCCTGTCACCCCCATTGGACAAG
CTGGGGAACAGCCATAGGGGGACCAGCTTCTGCCAGAAGTTGGTGTCTCTCTTCAATTTC
CACAACTATGACAACCTGAGGCACTGTGCTCGGAAGTTAGACCCACGGCGTGAAGGGGCA
GAAATTCGGAACAAGACTGTGGTCAACCTGTTATTTGCTGCCTATAGTGGCGATGTCTCA
GCTCTTCGAAGGTTTGCCTTGTCAGCCATGGATATGGAACAGAAAGACTATGACTCGCGC
ACAGCTCTGCATGTTGCTGCAGCTGAAGGACACATCGAAGTTGTTAAATTCCTGATCGAG
GCTTGCAAAGTGAATCCTTTTGCCAAGGACAGGTGGGGCAACATTCCCCTGGATGATGCT
GTGCAGTTCAACCATCTGGAGGTGGTCAAACTGCTTCAAGATTACCAGGACTCCTACACA
CTCTCTGAAACTCAGGCTGAGGCAGCAGCTGAGGCCCTGTCCAAAGAGAACTTAGAAAGC
ATGGTATGA
Enzyme 12 GenBank Gene ID AF110330 Link Image
Enzyme 12 GeneCard ID GLS2 Link Image
Enzyme 12 GenAtlas ID GLS2 Link Image
Enzyme 12 HGNC ID HGNC:29570 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 12q13
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Gomez-Fabre PM, Aledo JC, Del Castillo-Olivares A, Alonso FJ, Nunez De Castro I, Campos JA, Marquez J: Molecular cloning, sequencing and expression studies of the human breast cancer cell glutaminase. Biochem J. 2000 Jan 15;345 Pt 2:365-75. [PubMed Link Image]
  2. Olalla L, Aledo JC, Bannenberg G, Marquez J: The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins. FEBS Lett. 2001 Jan 19;488(3):116-22. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5949
Enzyme 13 Name CTP synthase 1
Enzyme 13 Synonyms
  1. CTP synthetase 1
  2. UTP--ammonia ligase 1
Enzyme 13 Gene Name CTPS
Enzyme 13 Protein Sequence >CTP synthase 1
MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFV
LDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDA
IQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHV
SLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ
VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCS
IALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQK
LCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDAN
STEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRH
RFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPY
FGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD
Enzyme 13 Number of Residues 591
Enzyme 13 Molecular Weight 66689.9
Enzyme 13 Theoretical pI 6.42
Enzyme 13 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 13 General Function Involved in CTP synthase activity
Enzyme 13 Specific Function Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen
Enzyme 13 Pathways
Enzyme 13 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 30293 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P17812 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name PYRG1_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 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 13 GenBank Gene ID X52142 Link Image
Enzyme 13 GeneCard ID CTPS Link Image
Enzyme 13 GenAtlas ID CTPS Link Image
Enzyme 13 HGNC ID HGNC:2519 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 1p34.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5952
Enzyme 14 Name Protein-glutamine gamma-glutamyltransferase 5
Enzyme 14 Synonyms
  1. Transglutaminase X
  2. TG(X)
  3. TGX
  4. TGase X
  5. Transglutaminase-5
  6. TGase-5
Enzyme 14 Gene Name TGM5
Enzyme 14 Protein Sequence >Protein-glutamine gamma-glutamyltransferase 5
MAQGLEVALTDLQSSRNNVRHHTEEITVDHLLVRRGQAFNLTLYFRNRSFQPGLDNIIFV
VETGPLPDLALGTRAVFSLARHHSPSPWIAWLETNGATSTEVSLCAPPTAAVGRYLLKIH
IDSFQGSVTAYQLGEFILLFNPWCPEDAVYLDSEPQRQEYVMNDYGFIYQGSKNWIRPCP
WNYGQFEDKIIDICLKLLDKSLHFQTDPATDCALRGSPVYVSRVVCAMINSNDDNGVLNG
NWSENYTDGANPAEWTGSVAILKQWNATGCQPVRYGQCWVFAAVMCTVMRCLGIPTRVIT
NFDSGHDTDGNLIIDEYYDNTGRILGNKKKDTIWNFHVWNECWMARKDLPPAYGGWQVLD
ATPQEMSNGVYCCGPASVRAIKEGEVDLNYDTPFVFSMVNADCMSWLVQGGKEQKLHQDT
SSVGNFISTKSIQSDERDDITENYKYEEGSLQERQVFLKALQKLKARSFHGSQRGAELQP
SRPTSLSQDSPRSLHTPSLRPSDVVQVSLKFKLLDPPNMGQDICFVLLALNMSSQFKDLK
VNLSAQSLLHDGSPLSPFWQDTAFITLSPKEAKTYPCKISYSQYSQYLSTDKLIRISALG
EEKSSPEKILVNKIITLSYPSITINVLGAAVVNQPLSIQVIFSNPLSEQVEDCVLTVEGS
GLFKKQQKVFLGVLKPQHQASIILETVPFKSGQRQIQANMRSNKFKDIKGYRNVYVDFAL
Enzyme 14 Number of Residues 720
Enzyme 14 Molecular Weight 80777.1
Enzyme 14 Theoretical pI 6.39
Enzyme 14 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
Enzyme 14 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 14 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Contributes to the formation of the cornified cell envelope of keratinocytes
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 [RN:R03983]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 2895530 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O43548 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name TGM5_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >2163 bp
ATGGCCCAAGGGCTAGAAGTGGCCCTCACAGACCTCCAGAGCTCCAGAAATAATGTGCGG
CACCACACGGAGGAGATCACTGTGGACCACCTGCTTGTTCGCCGGGGCCAGGCCTTCAAC
CTCACCCTGTACTTCAGGAACCGGAGCTTCCAGCCAGGCCTGGACAACATCATCTTCGTG
GTTGAAACTGGACCGCTGTCAGACCTGGCCTTGGGGACTCGGGCTGTGTTCAGCCTGGCA
CGCCATCACAGCCCCAGCCCCTGGATTGCCTGGCTGGAGACCAATGGGGCCACCTCCACA
GAGGTGAGCTTGTGCGCTCCTCCCACGGCGGCCGTGGGTCGGTACCTCTTGAAAATCCAC
ATCGACTCCTTCCAGGGGTCTGTGACGGCCTACCAGCTAGGGGAGTTCATCCTGCTTTTC
AATCCCTGGTGCCCAGAGGATGCTGTCTACTTGGACAGTGAACCCCAGAGGCAGGAGTAT
GTCATGAATGATTATGGCTTCATCTACCAAGGCAGCAAGAACTGGATCCGCCCATGTCCC
TGGAACTATGGACAGTTTGAAGACAAAATCATAGACATCTGCCTGAAGCTGCTAGACAAG
AGCCTGCACTTCCAGACTGACCCAGCCACAGACTGTGCTCTGCGGGGAAGCCCCGTCTAC
GTCAGCAGAGTGGTGTGTGCCATGATCAACAGCAATGATGATAATGGGGTGCTCAATGGA
AACTGGAGTGAGAATTACACAGACGGCGCCAACCCTGCGGAGTGGACGGGCAGCGTGGCC
ATCCTGAAGCAGTGGAACGCCACAGGCTGCCAGCCCGTGCGCTACGGGCAATGCTGGGTC
TTTGCTGCCGTCATGTGCACAGTGATGAGGTGTCTGGGGATCCCTACCCGTGTGATCACC
AACTTCGACTCTGGCCACGATACAGATGGAAACCTGATCATAGATGAGTATTATGACAAC
ACAGGCAGGATTTTGGGGAATAAGAAGAAGGATACTATCTGGAACTTCCATGTCTGGAAT
GAGTGCTGGATGGCCCGGAAGGATCTGCCCCCTGCATATGGAGGCTGGCAGGTGCTGGAC
GCCACACCTCAGGAGATGAGCAACGGCGTCTACTGCTGTGGCCCTGCCTCTGTCAGAGCC
ATCAAAGAAGGAGAAGTGGACCTGAACTATGACACGCCCTTTGTGTTTTCGATGGTGAAT
GCTGACTGCATGTCCTGGCTCGTCCAGGGAGGGAAGGAGCAGAAGCTTCACCAGGACACG
AGTTCTGTTGGCAATTTTATCAGCACAAAGAGCATCCAGAGTGACGAGCGGGATGACATC
ACAGAGAACTACAAGTATGAAGAAGGATCCCTCCAGGAGAGGCAGGTGTTTCTGAAGGCT
CTGCAGAAGCTGAAGGCTAGAAGCTTCCATGGCTCCCAAAGAGGAGCAGAGTTGCAACCT
TCCAGGCCCACATCACTGAGCCAGGACAGCCCTCGGAGCCTGCATACACCTTCCCTTCGA
CCCAGTGATGTGGTGCAAGTCTCCCTGAAATTCAAGCTGCTCGACCCGCCCAACATGGGC
CAGGATATATGCTTTGTCCTGCTGGCCCTCAACATGTCCTCCCAGTTCAAGGACCTCAAA
GTGAACCTGAGTGCCCAGTCTCTGCTGCACGATGGCAGCCCCCTGTCCCCATTCTGGCAG
GACACAGCGTTCATCACACTCTCTCCTAAAGAAGCAAAGACCTACCCCTGCAAAATCTCC
TATTCCCAGTACAGCCAGTACCTGTCAACAGACAAGCTGATCCGCATCAGTGCCCTGGGT
GAAGAGAAAAGCAGTCCTGAGAAAATCCTGGTGAACAAGATCATCACCTTATCTTATCCA
AGCATCACGATTAATGTTCTAGGAGCAGCCGTTGTGAACCAGCCACTCTCCATACAGGTG
ATATTTTCAAACCCCCTCTCGGAGCAGGTTGAGGACTGTGTGCTGACTGTGGAAGGAAGT
GGCCTCTTCAAGAAACAGCAGAAAGTCTTCCTTGGAGTCCTCAAACCCCAACACCAAGCA
AGCATCATTCTGGAGACCGTCCCCTTCAAGAGTGGACAAAGGCAGATCCAAGCTAATATG
AGAAGCAACAAGTTTAAGGACATTAAGGGTTACAGGAATGTTTATGTAGACTTTGCATTA
TAA
Enzyme 14 GenBank Gene ID AF035960 Link Image
Enzyme 14 GeneCard ID TGM5 Link Image
Enzyme 14 GenAtlas ID TGM5 Link Image
Enzyme 14 HGNC ID HGNC:11781 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 15q15.2
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Aeschlimann D, Koeller MK, Allen-Hoffmann BL, Mosher DF: Isolation of a cDNA encoding a novel member of the transglutaminase gene family from human keratinocytes. Detection and identification of transglutaminase gene products based on reverse transcription-polymerase chain reaction with degenerate primers. J Biol Chem. 1998 Feb 6;273(6):3452-60. [PubMed Link Image]
  2. Grenard P, Bates MK, Aeschlimann D: Evolution of transglutaminase genes: identification of a transglutaminase gene cluster on human chromosome 15q15. Structure of the gene encoding transglutaminase X and a novel gene family member, transglutaminase Z. J Biol Chem. 2001 Aug 31;276(35):33066-78. Epub 2001 Jun 4. [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. Rufini A, Vilbois F, Paradisi A, Oddi S, Tartaglione R, Leta A, Bagetta G, Guerrieri P, Finazzi-Agro' A, Melino G, Candi E: Transglutaminase 5 is acetylated at the N-terminal end. Amino Acids. 2004 Jul;26(4):425-30. Epub 2004 Jun 17. [PubMed Link Image]
  5. Cassidy AJ, van Steensel MA, Steijlen PM, van Geel M, van der Velden J, Morley SM, Terrinoni A, Melino G, Candi E, McLean WH: A homozygous missense mutation in TGM5 abolishes epidermal transglutaminase 5 activity and causes acral peeling skin syndrome. Am J Hum Genet. 2005 Dec;77(6):909-17. Epub 2005 Oct 11. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5953
Enzyme 15 Name Glutaminase kidney isoform, mitochondrial
Enzyme 15 Synonyms
  1. GLS
  2. K-glutaminase
  3. L-glutamine amidohydrolase
Enzyme 15 Gene Name GLS
Enzyme 15 Protein Sequence >Glutaminase kidney isoform, mitochondrial
MMRLRGSGMLRDLLLRSPAGVSATLRRAQPLVTLCRRPRGGGRPAAGPAAAARLHPWWGG
GGWPAEPLARGLSSSPSEILQELGKGSTHPQPGVSPPAAPAAPGPKDGPGETDAFGNSEG
KELVASGENKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMD
MLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKK
QSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDL
GTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQ
FLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSI
EVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPA
KSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKL
DPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVE
VVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQT
VHKNLDGLL
Enzyme 15 Number of Residues 669
Enzyme 15 Molecular Weight 73460.6
Enzyme 15 Theoretical pI 7.82
Enzyme 15 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 15 General Function Involved in glutaminase activity
Enzyme 15 Specific Function Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine
Enzyme 15 Pathways
Enzyme 15 Reactions
  • L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 156104878 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID O94925 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name GLSK_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 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 15 GenBank Gene ID NM_014905.3 Link Image
Enzyme 15 GeneCard ID GLS Link Image
Enzyme 15 GenAtlas ID GLS Link Image
Enzyme 15 HGNC ID HGNC:4331 Link Image
Enzyme 15 Chromosome Location 2
Enzyme 15 Locus 2q32-q34
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5955
Enzyme 16 Name Protein-glutamine gamma-glutamyltransferase K
Enzyme 16 Synonyms
  1. Epidermal TGase
  2. Transglutaminase K
  3. TG(K)
  4. TGK
  5. TGase K
  6. Transglutaminase-1
  7. TGase-1
Enzyme 16 Gene Name TGM1
Enzyme 16 Protein Sequence >Protein-glutamine gamma-glutamyltransferase K
MMDGPRSDVGRWGGNPLQPPTTPSPEPEPEPDGRSRRGGGRSFWARCCGCCSCRNAADDD
WGPEPSDSRGRGSSSGTRRPGSRGSDSRRPVSRGSGVNAAGDGTIREGMLVVNGVDLLSS
RSDQNRREHHTDEYEYDELIVRRGQPFHMLLLLSRTYESSDRITLELLIGNNPEVGKGTH
VIIPVGKGGSGGWKAQVVKASGQNLNLRVHTSPNAIIGKFQFTVRTQSDAGEFQLPFDPR
NEIYILFNPWCPEDIVYVDHEDWRQEYVLNESGRIYYGTEAQIGERTWNYGQFDHGVLDA
CLYILDRRGMPYGGRGDPVNVSRVISAMVNSLDDNGVLIGNWSGDYSRGTNPSAWVGSVE
ILLSYLRTGYSVPYGQCWVFAGVTTTVLRCLGLATRTVTNFNSAHDTDTSLTMDIYFDEN
MKPLEHLNHDSVWNFHVWNDCWMKRPDLPSGFDGWQVVDATPQETSSGIFCCGPCSVESI
KNGLVYMKYDTPFIFAEVNSDKVYWQRQDDGSFKIVYVEEKAIGTLIVTKAISSNMREDI
TYLYKHPEGSDAERKAVETAAAHGSKPNVYANRGSAEDVAMQVEAQDAVMGQDLMVSVML
INHSSSRRTVKLHLYLSVTFYTGVSGTIFKETKKEVELAPGASDRVTMPVAYKEYRPHLV
DQGAMLLNVSGHVKESGQVLAKQHTFRLRTPDLSLTLLGAAVVGQECEVQIVFKNPLPVT
LTNVVFRLEGSGLQRPKILNVGDIGGNETVTLRQSFVPVRPGPRQLIASLDSPQLSQVHG
VIQVDVAPAPGDGGFFSDAGGDSHLGETIPMASRGGA
Enzyme 16 Number of Residues 817
Enzyme 16 Molecular Weight 89786.1
Enzyme 16 Theoretical pI 5.92
Enzyme 16 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
Enzyme 16 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 16 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross- linking epidermal proteins during formation of the stratum corneum
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 [RN:R03983]
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 P22735 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name TGM1_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >2454 bp
ATGATGGATGGGCCACGTTCCGATGTGGGCCGTTGGGGTGGCAACCCCTTGCAGCCCCCT
ACCACGCCATCTCCAGAGCCAGAGCCAGAGCCAGACGGACGCTCTCGCAGAGGAGGAGGC
CGTTCCTTCTGGGCTCGCTGCTGTGGCTGCTGTTCATGCCGAAATGCGGCAGATGACGAC
TGGGGACCTGAACCCTCTGACTCCAGGGGTCGAGGGTCCAGCTCTGGCACTCGAAGACCT
GGCTCCCGGGGCTCAGACTCCCGCCGGCCTGTATCCCGGGGCAGCGGTGTCAATGCAGCT
GGAGATGGCACCATCCGAGAGGGCATGCTAGTAGTGAACGGTGTGGACTTGCTGAGCTCG
CGCTCGGACCAGAACCGCCGAGAGCACCACACAGACGAGTATGAGTACGACGAGCTGATA
GTGCGCCGCGGGCAGCCTTTCCATATGCTCCTCCTCCTGTCCCGGACCTATGAATCCTCT
GATCGCATCACCCTTGAGTTACTCATCGGAAACAACCCCGAGGTGGGCAAGGGCACGCAC
GTGATCATCCCAGTGGGCAAGGGGGGCAGTGGAGGCTGGAAAGCCCAGGTGGTCAAGGCC
AGTGGGCAGAATCTGAACCTGCGGGTCCACACTTCCCCCAACGCCATCATCGGCAAGTTT
CAGTTCACAGTCCGCACACAATCAGACGCTGGGGAGTTCCAGTTGCCCTTTGACCCCCGC
AATGAGATCTACATCCTCTTCAACCCCTGGTGCCCAGAGGACATTGTGTACGTGGACCAT
GAGGATTGGCGGCAGGAGTATGTTCTTAATGAGTCTGGGAGAATTTACTACGGGACCGAA
GCACAGATTGGTGAGCGGACCTGGAACTACGGCCAGTTTGACCACGGGGTGCTGGATGCC
TGCTTATACATCCTGGACCGGCGGGGGATGCCATATGGAGGCCGTGGAGACCCAGTCAAT
GTCTCCCGGGTCATCTCTGCCATGGTGAACTCCCTGGATGACAATGGAGTCCTGATTGGG
AACTGGTCTGGTGATTACTCCCGAGGCACCAACCCATCAGCGTGGGTGGGCAGCGTGGAG
ATCCTGCTTAGCTACCTACGCACGGGATATTCCGTCCCCTATGGCCAGTGCTGGGTCTTT
GCTGGAGTGACCACCACAGTGCTGCGCTGCCTGGGTCTGGCCACCCGTACTGTCACCAAC
TTCAACTCCGCCCACGACACAGACACATCCCTTACCATGGACATCTACTTCGACGAGAAC
ATGAAGCCCCTGGAGCACCTGAACCATGATTCTGTCTGGAACTTCCATGTGTGGAACGAC
TGCTGGATGAAGAGGCCGGATCTGCCCTCGGGCTTTGATGGGTGGCAGGTGGTGGATGCC
ACACCCCAAGAGACTAGCAGTGGCATCTTCTGCTGCGGCCCCTGCTCTGTGGAGTCCATC
AAGAATGGCCTGGTCTACATGAAGTACGACACGCCTTTCATTTTTGCTGAGGTGAATAGT
GACAAGGTGTACTGGCAGCGGCAGGATGATGGCAGCTTCAAGATTGTTTATGTGGAGGAG
AAGGCCATCGGCACACTCATTGTCACAAAGGCCATCAGCTCCAACATGCGGGAGGACATC
ACCTACCTCTATAAGCACCCAGAAGGCTCAGACGCAGAGCGGAAGGCAGTAGAGACAGCA
GCAGCCCACGGCAGCAAACCCAATGTGTATGCCAACCGGGGCTCAGCGGAGGATGTGGCC
ATGCAGGTGGAGGCACAGGACGCGGTGATGGGGCAGGATCTGATGGTCTCTGTGATGCTG
ATCAATCACAGCAGCAGCCGCCGCACAGTGAAACTGCACCTCTACCTCTCAGTCACTTTC
TATACTGGTGTCAGTGGTACCATCTTCAAGGAGACCAAGAAGGAAGTGGAGCTGGCACCA
GGGGCCTCGGACCGTGTGACCATGCCAGTGGCCTACAAGGAATACCGGCCCCATCTTGTG
GACCAGGGGGCCATGCTGCTCAATGTCTCAGGCCACGTCAAGGAGAGCGGGCAGGTGCTG
GCCAAGCAGCACACCTTCCGTCTGCGCACCCCAGACCTCTCCCTCACGTTACTGGGAGCA
GCAGTGGTTGGCCAGGAGTGTGAAGTACAGATTGTCTTCAAGAACCCCCTTCCCGTCACC
CTCACCAATGTCGTCTTCCGGCTCGAAGGCTCTGGGTTACAGAGGCCCAAGATCCTCAAC
GTTGGGGACATTGGAGGCAATGAAACAGTGACACTGCGCCAGTCGTTTGTGCCTGTGCGA
CCAGGCCCCCGCCAGCTCATTGCCAGCTTGGACAGCCCACAGCTCTCCCAGGTGCACGGT
GTCATCCAGGTGGATGTGGCCCCAGCCCCTGGGGATGGGGGCTTCTTCTCAGACGCTGGA
GGTGACAGTCACTTAGGAGAGACCATCCCTATGGCATCTCGAGGTGGAGCTTAG
Enzyme 16 GenBank Gene ID M55183 Link Image
Enzyme 16 GeneCard ID TGM1 Link Image
Enzyme 16 GenAtlas ID TGM1 Link Image
Enzyme 16 HGNC ID HGNC:11777 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 14q11.2
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Phillips MA, Stewart BE, Qin Q, Chakravarty R, Floyd EE, Jetten AM, Rice RH: Primary structure of keratinocyte transglutaminase. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9333-7. [PubMed Link Image]
  2. Yamanishi K, Liew FM, Konishi K, Yasuno H, Doi H, Hirano J, Fukushima S: Molecular cloning of human epidermal transglutaminase cDNA from keratinocytes in culture. Biochem Biophys Res Commun. 1991 Mar 29;175(3):906-13. [PubMed Link Image]
  3. Kim HC, Idler WW, Kim IG, Han JH, Chung SI, Steinert PM: The complete amino acid sequence of the human transglutaminase K enzyme deduced from the nucleic acid sequences of cDNA clones. J Biol Chem. 1991 Jan 5;266(1):536-9. [PubMed Link Image]
  4. Phillips MA, Stewart BE, Rice RH: Genomic structure of keratinocyte transglutaminase. Recruitment of new exon for modified function. J Biol Chem. 1992 Feb 5;267(4):2282-6. [PubMed Link Image]
  5. Kim IG, McBride OW, Wang M, Kim SY, Idler WW, Steinert PM: Structure and organization of the human transglutaminase 1 gene. J Biol Chem. 1992 Apr 15;267(11):7710-7. [PubMed Link Image]
  6. Yamanishi K, Inazawa J, Liew FM, Nonomura K, Ariyama T, Yasuno H, Abe T, Doi H, Hirano J, Fukushima S: Structure of the gene for human transglutaminase 1. J Biol Chem. 1992 Sep 5;267(25):17858-63. [PubMed Link Image]
  7. Polakowska RR, Eickbush T, Falciano V, Razvi F, Goldsmith LA: Organization and evolution of the human epidermal keratinocyte transglutaminase I gene. Proc Natl Acad Sci U S A. 1992 May 15;89(10):4476-80. [PubMed Link Image]
  8. 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]
  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. Polakowska R, Herting E, Goldsmith LA: Isolation of cDNA for human epidermal type I transglutaminase. J Invest Dermatol. 1991 Feb;96(2):285-8. [PubMed Link Image]
  11. Schroeder WT, Thacher SM, Stewart-Galetka S, Annarella M, Chema D, Siciliano MJ, Davies PJ, Tang HY, Sowa BA, Duvic M: Type I keratinocyte transglutaminase: expression in human skin and psoriasis. J Invest Dermatol. 1992 Jul;99(1):27-34. [PubMed Link Image]
  12. Herman ML, Farasat S, Steinbach PJ, Wei MH, Toure O, Fleckman P, Blake P, Bale SJ, Toro JR: Transglutaminase-1 gene mutations in autosomal recessive congenital ichthyosis: summary of mutations (including 23 novel) and modeling of TGase-1. Hum Mutat. 2009 Apr;30(4):537-47. [PubMed Link Image]
  13. Huber M, Rettler I, Bernasconi K, Frenk E, Lavrijsen SP, Ponec M, Bon A, Lautenschlager S, Schorderet DF, Hohl D: Mutations of keratinocyte transglutaminase in lamellar ichthyosis. Science. 1995 Jan 27;267(5197):525-8. [PubMed Link Image]
  14. Russell LJ, DiGiovanna JJ, Rogers GR, Steinert PM, Hashem N, Compton JG, Bale SJ: Mutations in the gene for transglutaminase 1 in autosomal recessive lamellar ichthyosis. Nat Genet. 1995 Mar;9(3):279-83. [PubMed Link Image]
  15. Laiho E, Ignatius J, Mikkola H, Yee VC, Teller DC, Niemi KM, Saarialho-Kere U, Kere J, Palotie A: Transglutaminase 1 mutations in autosomal recessive congenital ichthyosis: private and recurrent mutations in an isolated population. Am J Hum Genet. 1997 Sep;61(3):529-38. [PubMed Link Image]
  16. Akiyama M, Takizawa Y, Kokaji T, Shimizu H: Novel mutations of TGM1 in a child with congenital ichthyosiform erythroderma. Br J Dermatol. 2001 Feb;144(2):401-7. [PubMed Link Image]
  17. Yang JM, Ahn KS, Cho MO, Yoneda K, Lee CH, Lee JH, Lee ES, Candi E, Melino G, Ahvazi B, Steinert PM: Novel mutations of the transglutaminase 1 gene in lamellar ichthyosis. J Invest Dermatol. 2001 Aug;117(2):214-8. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5964
Enzyme 17 Name Protein-glutamine gamma-glutamyltransferase 6
Enzyme 17 Synonyms
  1. Transglutaminase Y
  2. TGase Y
  3. Transglutaminase-3-like
  4. TGase-3-like
  5. Transglutaminase-6
  6. TGase-6
Enzyme 17 Gene Name TGM6
Enzyme 17 Protein Sequence >Protein-glutamine gamma-glutamyltransferase 6
MAGIRVTKVDWQRSRNGAAHHTQEYPCPELVVRRGQSFSLTLELSRALDCEEILIFTMET
GPRASEALHTKAVFQTSELERGEGWTAAREAQMEKTLTVSLASPPSAVIGRYLLSIRLSS
HRKHSNRRLGEFVLLFNPWCAEDDVFLASEEERQEYVLSDSGIIFRGVEKHIRAQGWNYG
QFEEDILNICLSILDRSPGHQNNPATDVSCRHNPIYVTRVISAMVNSNNDRGVVQGQWQG
KYGGGTSPLHWRGSVAILQKWLKGRYKPVKYGQCWVFAGVLCTVLRCLGIATRVVSNFNS
AHDTDQNLSVDKYVDSFGRTLEDLTEDSMWNFHVWNESWFARQDLGPSYNGWQVLDATPQ
EESEGVFRCGPASVTAIREGDVHLAHDGPFVFAEVNADYITWLWHEDESRERVYSNTKKI
GRCISTKAVGSDSRVDITDLYKYPEGSRKERQVYSKAVNRLFGVEASGRRIWIRRAGGRC
LWRDDLLEPATKPSIAGKFKVLEPPMLGHDLRLALCLANLTSRAQRVRVNLSGATILYTR
KPVAEILHESHAVRLGPQEEKRIPITISYSKYKEDLTEDKKILLAAMCLVTKGEKLLVEK
DITLEDFITIKVLGPAMVGVAVTVEVTVVNPLIERVKDCALMVEGSGLLQEQLSIDVPTL
EPQERASVQFDITPSKSGPRQLQVDLVSPHFPDIKGFVIVHVATAK
Enzyme 17 Number of Residues 706
Enzyme 17 Molecular Weight 79311.7
Enzyme 17 Theoretical pI 7.26
Enzyme 17 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
Enzyme 17 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 17 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 [RN:R03983]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 33331030 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID O95932 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name TGM3L_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >2121 bp
ATGGCAGGGATCAGAGTCACCAAGGTGGACTGGCAGCGGTCGAGGAATGGCGCTGCCCAC
CACACCCAGGAGTACCCCTGCCCTGAGCTGGTGGTTCGCAGGGGCCAGTCGTTCAGCCTC
ACGCTGGAGCTGAGCAGAGCCCTGGACTGTGAGGAGATCCTCATCTTCACGGTGGAGACA
GGACCCCGGGCTTCTGAGGCCCTCCACACCAAAGCTGTGTTCCAGACATCGGAGCTGGAG
CGGGGTGAGGGCTGGACAGCAGCAAGGGAGGCTCAGATGGAGAAAACTCTGACCGTCAGT
CTCGCCAGCCCTCCCAGTGCTGTCATTGGCCGCTACCTGCTGAGCATCAGGCTTTCCTCT
CACCGCAAACACAGCAACCGGAGGCTGGGCGAGTTTGTTCTCCTTTTCAACCCATGGTGT
GCAGAGGACGATGTGTTTCTGGCCTCAGAGGAGGAGAGACAGGAGTACGTGCTCAGCGAC
AGCGGCATCATCTTCCGAGGCGTGGAGAAGCACATACGAGCCCAGGGCTGGAACTACGGG
CAGTTTGAGGAGGACATCCTGAACATCTGCCTCTCCATCCTGGATCGAAGCCCCGGTCAC
CAAAACAACCCAGCCACCGACGTGTCCTGCCGCCACAACCCCATCTACGTCACCAGGGTC
ATCAGTGCCATGGTGAACAGCAACAACGACCGAGGTGTGGTGCAAGGACAGTGGCAGGGC
AAGTACGGCGGCGGCACCAGCCCGCTGCACTGGCGCGGCAGCGTGGCCATTCTGCAGAAG
TGGCTCAAGGGCAGGTACAAGCCAGTCAAGTACGGCCAGTGCTGGGTCTTCGCCGGAGTC
CTGTGCACAGTCCTCAGGTGCTTGGGGATAGCCACACGGGTCGTGTCCAACTTCAACTCA
GCCCACGACACAGACCAGAACCTGAGTGTGGACAAATACGTGGACTCCTTCGGGCGGACC
CTGGAGGACCTGACAGAAGACAGCATGTGGAATTTCCATGTCTGGAATGAGAGCTGGTTT
GCCCGGCAGGACCTAGGCCCCTCTTACAATGGCTGGCAGGTTCTGGATGCCACCCCCCAG
GAGGAGAGTGAAGGTGTGTTCCGGTGCGGCCCAGCCTCAGTCACCGCCATCCGCGAGGGT
GATGTGCACCTGGCTCACGATGGCCCCTTCGTGTTTGCGGAGGTCAACGCCGACTACATC
ACCTGGCTGTGGCACGAGGATGAGAGCCGGGAGCGTGTATACTCAAACACGAAGAAGATT
GGGAGATGCATCAGCACCAAGGCGGTGGGCAGTGACTCCCGCGTGGACATCACTGACCTC
TACAAGTATCCGGAAGGGTCCCGGAAAGAGAGGCAGGTGTACAGCAAGGCGGTGAACAGG
CTGTTCGGCGTGGAAGCCTCTGGAAGGAGAATCTGGATCCGCAGGGCTGGGGGTCGCTGT
CTCTGGCGTGACGACCTCCTGGAGCCTGCCACCAAGCCCAGCATCGCTGGCAAGTTCAAG
GTGCTAGAGCCTCCCATGCTGGGCCACGACCTGAGACTGGCCCTGTGCTTGGCCAACCTC
ACCTCCCGGGCCCAGCGGGTGAGGGTCAACCTGAGCGGTGCCACCATCCTCTATACCCGC
AAGCCAGTGGCAGAGATCCTGCATGAATCCCACGCCGTGAGGCTGGGGCCGCAAGAAGAG
AAGAGAATCCCAATTACAATATCTTACTCTAAGTATAAAGAAGACCTGACAGAGGACAAG
AAGATCCTGTTGGCTGCCATGTGCCTTGTCACCAAAGGAGAGAAGCTTCTGGTGGAGAAG
GACATTACTCTAGAGGACTTCATCACCATCAAGGTTCTGGGCCCAGCCATGGTGGGAGTG
GCAGTTACAGTGGAAGTGACAGTAGTCAACCCCCTCATAGAGAGAGTGAAGGACTGTGCG
CTGATGGTGGAGGGCAGCGGCCTTCTCCAGGAACAGCTCAGCATCGACGTGCCTACCCTG
GAGCCTCAGGAGAGGGCCTCAGTCCAGTTTGACATCACCCCCTCCAAAAGTGGCCCAAGG
CAGCTGCAGGTGGACCTTGTAAGCCCTCACTTCCCGGACATCAAGGGCTTTGTGATCGTC
CATGTGGCCACTGCCAAGTGA
Enzyme 17 GenBank Gene ID AF540969 Link Image
Enzyme 17 GeneCard ID TGM6 Link Image
Enzyme 17 GenAtlas ID TGM6 Link Image
Enzyme 17 HGNC ID HGNC:16255 Link Image
Enzyme 17 Chromosome Location 2
Enzyme 17 Locus 20p13
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. 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]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6134
Enzyme 18 Name Phosphoribosylformylglycinamidine synthase
Enzyme 18 Synonyms
  1. FGAM synthase
  2. FGAMS
  3. Formylglycinamide ribotide amidotransferase
  4. FGARAT
  5. Formylglycinamide ribotide synthetase
Enzyme 18 Gene Name PFAS
Enzyme 18 Protein Sequence >Phosphoribosylformylglycinamidine synthase
MSPVLHFYVRPSGHEGAASGHTRRKLQGKLPELQGVETELCYNVNWTAEALPSAEETKKL
MWLFGCPLLLDDVARESWLLPGSNDLLLEVGPRLNFSTPTSTNIVSVCRATGLGPVDRVE
TTRRYRLSFAHPPSAEVEAIALATLHDRMTEQHFPHPIQSFSPESMPEPLNGPINILGEG
RLALEKANQELGLALDSWDLDFYTKRFQELQRNPSTVEAFDLAQSNSEHSRHWFFKGQLH
VDGQKLVHSLFESIMSTQESSNPNNVLKFCDNSSAIQGKEVRFLRPEDPTRPSRFQQQQG
LRHVVFTAETHNFPTGVCPFSGATTGTGGRIRDVQCTGRGAHVVAGTAGYCFGNLHIPGY
NLPWEDPSFQYPGNFARPLEVAIEASNGASDYGNKFGEPVLAGFARSLGLQLPDGQRREW
IKPIMFSGGIGSMEADHISKEAPEPGMEVVKVGGPVYRIGVGGGAASSVQVQGDNTSDLD
FGAVQRGDPEMEQKMNRVIRACVEAPKGNPICSLHDQGAGGNGNVLKELSDPAGAIIYTS
RFQLGDPTLNALEIWGAEYQESNALLLRSPNRDFLTHVSARERCPACFVGTITGDRRIVL
VDDRECPVRRNGQGDAPPTPLPTPVDLELEWVLGKMPRKEFFLQRKPPMLQPLALPPGLS
VHQALERVLRLPAVASKRYLTNKVDRSVGGLVAQQQCVGPLQTPLADVAVVALSHEELIG
AATALGEQPVKSLLDPKVAARLAVAEALTNLVFALVTDLRDVKCSGNWMWAAKLPGEGAA
LADACEAMVAVMAALGVAVDGGKDSLSMAARVGTETVRAPGSLVISAYAVCPDITATVTP
DLKHPEGRGHLLYVALSPGQHRLGGTALAQCFSQLGEHPPDLDLPENLVRAFSITQGLLK
DRLLCSGHDVSDGGLVTCLLEMAFAGNCGLQVDVPVPRVDVLSVLFAEEPGLVLEVQEPD
LAQVLKRYRDAGLHCLELGHTGEAGPHAMVRVSVNGAVVLEEPVGELRALWEETSFQLDR
LQAEPRCVAEEERGLRERMGPSYCLPPTFPKASVPREPGGPSPRVAILREEGSNGDREMA
DAFHLAGFEVWDVTMQDLCSGAIGLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFHPRAG
AELRRFRKRPDTFSLGVCNGCQLLALLGWVGGDPNEDAAEMGPDSQPARPGLLLRHNLSG
RYESRWASVRVGPGPALMLRGMEGAVLPVWSAHGEGYVAFSSPELQAQIEARGLAPLHWA
DDDGNPTEQYPLNPNGSPGGVAGICSCDGRHLAVMPHPERAVRPWQWAWRPPPFDTLTTS
PWLQLFINARNWTLEGSC
Enzyme 18 Number of Residues 1338
Enzyme 18 Molecular Weight 144723.1
Enzyme 18 Theoretical pI 5.55
Enzyme 18 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 18 General Function Involved in catalytic activity
Enzyme 18 Specific Function ATP + N(2)-formyl-N(1)-(5-phospho-D- ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2- (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate
Enzyme 18 Pathways
Enzyme 18 Reactions
  • ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate [RN:R04463]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 148922280 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID O15067 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PUR4_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >4017 bp
ATGTCCCCAGTCCTTCACTTCTATGTTCGTCCCTCTGGCCATGAGGGGGCAGCCTCTGGA
CACACTCGGAGGAAACTGCAAGGGAAACTGCCAGAGCTGCAGGGCGTCGAGACTGAACTG
TGCTACAACGTGAACTGGACAGCTGAGGCCCTCCCCAGTGCTGAGGAGACAAAGAAGCTG
ATGTGGCTGTTTGGTTGCCCCTTACTGCTGGATGATGTTGCTCGGGAGTCCTGGCTCCTT
CCTGGCTCCAATGACCTGCTGCTGGAGGTCGGGCCCAGGCTGAACTTCTCCACCCCAACA
TCCACCAACATCGTGTCAGTGTGCCGCGCCACTGGGCTGGGGCCTGTGGATCGTGTGGAG
ACCACCCGGCGCTACCGGCTCTCGTTTGCCCACCCCCCGTCAGCTGAGGTGGAAGCCATT
GCTCTGGCTACCCTGCACGACCGGATGACAGAGCAGCACTTCCCCCATCCCATCCAGAGT
TTCTCCCCTGAGAGCATGCCGGAACCCCTCAATGGCCCTATCAATATACTGGGTGAGGGC
CGGCTTGCGCTGGAGAAGGCCAACCAGGAGCTTGGTCTGGCTTTAGACTCTTGGGACCTA
GACTTCTACACCAAGCGCTTCCAGGAGCTACAGCGGAACCCGAGCACTGTGGAGGCCTTT
GACTTGGCGCAGTCCAATAGCGAGCACAGCCGACACTGGTTCTTCAAGGGCCAGCTCCAC
GTGGATGGGCAGAAGCTGGTGCACTCACTGTTTGAGTCCATCATGAGCACCCAGGAATCC
TCGAACCCCAACAACGTCCTCAAATTCTGTGATAACAGCAGTGCAATCCAGGGAAAGGAA
GTCCGATTCCTACGGCCTGAGGACCCCACACGGCCAAGCCGCTTCCAGCAACAGCAAGGG
CTGAGACATGTTGTCTTCACAGCAGAGACTCACAACTTTCCCACAGGAGTATGCCCCTTT
AGTGGTGCAACCACTGGCACAGGGGGCCGGATTCGAGATGTCCAGTGCACAGGCCGCGGG
GCCCACGTGGTGGCTGGCACTGCCGGCTATTGCTTTGGAAATCTGCATATTCCAGGTTAC
AATCTGCCCTGGGAGGATCTAAGCTTCCAGTATCCTGGGAATTTTGCCCGGCCCCTGGAG
GTTGCCATTGAAGCCAGTAATGGAGCTTCTGACTATGGCAACAAGTTTGGGGAACCAGTG
CTGGCTGGCTTCGCCCGCTCCTTGGGCCTCCAGCTCCCAGACGGCCAGCGGCGTGAGTGG
ATCAAGCCCATCATGTTTAGTGGGGGCATTGGGTCCATGGAAGCTGACCACATAAGCAAG
GAGGCCCCAGAGCCAGGCATGGAAGTTGTAAAGGTTGGAGGTCCCGTCTACAGGATTGGA
GTTGGAGGTGGAGCTGCTTCATCTGTGCAGGTGCAGGGAGATAACACCAGTGACCTGGAC
TTTGGGGCTGTGCAGCGAGGAGACCCGGAGATGGAACAGAAGATGAACCGTGTGATCAGG
GCTTGTGTGGAGGCCCCCAAGGGAAACCCCATCTGCAGCCTTCATGATCAGGGCGCTGGT
GGCAATGGCAATGTCCTAAAAGAGCTGAGTGACCCAGCTGGAGCCATCATTTACACCAGC
CGCTTCCAGCTTGGGGACCCAACCCTGAATGCCCTGGAAATCTGGGGGGCTGAGTACCAG
GAATCAAATGCTCTTCTGCTGAGGTCCCCCAACCGGGACTTCCTGACTCATGTCAGTGCC
CGTGAACGTTGCCCGGCTTGCTTCGTGGGCACCATCACTGGAGACCGGAGAATAGTGCTG
GTGGACGATCGGGAGTGTCCTGTCAGAAGAAATGGCCAGGGGGATGCCCCCCCGACACCC
CCGCCAACCCCTGTGGACCTGGAGCTCGAATGGGTGCTGGGCAAGATGCCTCGGAAGGAG
TTCTTCCTGCAGAGGAAGCCCCCCATGCTGCAGCCTCTGGCCTTGCCCCCAGGGCTGAGC
GTGCACCAGGCTCTGGAGAGGGTTCTGAGGCTGCCCGCCGTGGCCAGCAAGCGCTACCTC
ACCAATAAGGTGGACCGCTCCGTGGGAGGCCTGGTGGCCCAGCAGCAGTGCGTGGGGCCC
CTGCAAACTCCTCTGGCAGATGTAGCGGTTGTGGCACTGAGCCATGAGGAGCTCATAGGG
GCTGCCACAGCCTTGGGAGAACAGCCAGTCAAGAGCCTGCTGGACCCAAAAGTCGCCGCC
CGGCTGGCCGTGGCCGAAGCCCTCACCAACCTGGTGTTTGCTCTGGTCACTGACCTCCGG
GATGTGAAGTGTAGCGGGAACTGGATGTGGGCAGCCAAGCTCCCAGGGGAGGGCGCAGCT
TTGGCGGATGCCTGTGAGGCTATGGTGGCAGTGATGGCAGCCCTGGGTGTGGCAGTGGAT
GGTGGCAAGGACTCCCTCAGCATGGCTGCTCGGGTTGGCACTGAGACCGTGCGGGCTCCT
GGGTCACTGGTCATCTCAGCCTATGCCGTCTGCCCAGACATCACAGCCACTGTGACCCCA
GACCTCAAGCATCCTGAAGGGAGAGGCCATCTGCTCTATGTGGCTCTGAGCCCTGGGCAG
CACCGGCTCGGGGGCACAGCTCTGGCCCAGTGCTTCTCCCAGCTTGGGGAACACCCTCCA
GACCTGGACCTTCCTGAGAACTTGGTGCGGGCCTTCAGCATCACTCAGGGGCTGCTGAAA
GACCGCCTCCTCTGCTCAGGCCACGATGTCAGTGACGGAGGCCTCGTCACATGCCTGCTG
GAGATGGCCTTTGCTGGAAATTGCGGGCTACAGGTGGATGTGCCTGTCCCCAGGGTTGAT
GTCCTGTCTGTGCTGTTCGCTGAGGAGCCAGGCCTCGTGCTGGAGGTGCAGGAGCCAGAC
CTGGCCCAGGTGCTGAAGCGTTACCGGGATGCTGGCCTCCATTGCCTGGAGCTGGGCCAC
ACAGGCGAGGCCGGGCCCCACGCCATGGTCCGGGTGTCAGTGAACGGGGCTGTGGTTCTG
GAGGAGCCTGTTGGGGAGCTGCGAGCCCTCTGGGAGGAGACGAGTTTCCAGCTGGACCGG
CTACAGGCAGAGCCTCGCTGTGTGGCAGAGGAGGAACGGGGCCTGAGGGAGCGGATGGGG
CCCAGCTATTGCCTGCCCCCCACCTTTCCCAAAGCCTCCGTGCCCCGTGAGCCTGGTGGT
CCCAGCCCCCGAGTCGCCATCTTGCGAGAGGAGGGCAGTAATGGAGACCGGGAGATGGCC
GATGCCTTCCACTTAGCTGGGTTTGAGGTATGGGACGTGACCATGCAGGACCTCTGCTCT
GGGGCAATTGGGCTGGACACTTTCCGTGGCGTGGCCTTCGTGGGCGGCTTCAGCTATGCA
GATGTCCTGGGCTCTGCCAAAGGGTGGGCAGCTGCTGTGACCTTTCATCCCAGGGCTGGG
GCTGAGCTGAGGCGCTTCCGGAAGCGGCCAGACACCTTCAGCCTGGGCGTGTGTAATGGC
TGTCAACTGCTGGCTCTGCTCGGCTGGGTGGGAGGCGACCCCAATGAGGATGCTGCAGAG
ATGGGCCCTGACTCCCAGCCAGCCCGGCCAGGCCTTCTGCTACGCCACAACCTGTCTGGG
CGCTACGAGTCTCGCTGGGCCAGCGTGCGTGTGGGGCCTGGGCCAGCCCTGATGCTGCGA
GGGATGGAGGGCGCCGTGCTGCCCGTGTGGAGTGCGCACGGGGAAGGTTACGTAGCATTT
TCTTCTCCGGAACTCCAAGCTCAGATTGAGGCCAGGGGCTTGGCTCCACTGCACTGGGCT
GATGATGACGGGAACCCCACAGAGCAGTACCCTCTGAATCCCAATGGGTCCCCAGGGGGC
GTGGCTGGCATCTGCTCCTGTGATGGCCGCCACCTGGCTGTCATGCCTCACCCTGAGCGG
GCCGTTAGGCCTTGGCAGTGGGCATGGCGACCCCCTCCATTTGATACTCTGACCACCTCC
CCCTGGCTCCAGCTCTCTATCAATGCCCGAAACTGGACCCTGGAAGGGAGCTGCTGA
Enzyme 18 GenBank Gene ID BC146768 Link Image
Enzyme 18 GeneCard ID PFAS Link Image
Enzyme 18 GenAtlas ID PFAS Link Image
Enzyme 18 HGNC ID HGNC:8863 Link Image
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 17p13.1
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Patterson D, Bleskan J, Gardiner K, Bowersox J: Human phosphoribosylformylglycineamide amidotransferase (FGARAT): regional mapping, complete coding sequence, isolation of a functional genomic clone, and DNA sequence analysis. Gene. 1999 Nov 1;239(2):381-91. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  3. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [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. 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]
  6. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 7366
Enzyme 19 Name Probable glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial
Enzyme 19 Synonyms
  1. Glu-ADT subunit B
  2. Cytochrome oxidase assembly factor PET112 homolog
Enzyme 19 Gene Name PET112L
Enzyme 19 Protein Sequence >Probable glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial
MAAPMLRWGCRGRRWAFARVDGGSCHRRGAPTGSTSNQIRGESSVAQQPLHTAQKTRKGE
HKWAAVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAV
MTGLALNCHINKKSLFDRKHYFYADLPAGYQITQQRLPIAVNGSLIYGVCAGKKQSQVIP
KTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVVLEPDMSCGEEAATAVRELQ
LILQALGTSQANMAEGQLRVDANISVHHPGEPLGVRTEVKNLNSIRFLAKAIDYEIQRQI
NELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATSLPAGADP
QQVINIDQIRETLPELPSVTREKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIKETRAEPK
KVTSWVLNTFLGYLKQQNLAVSESPVTPSALAELLDLLDSRTISSSAAKQVFEELWKREG
KTPGQIVSEKQLELMQDQGALEQLCHSVMEAHPQVVMDVKNRNPRAINKLIGLVRKATQS
RADPVMIKEILEKKLSL
Enzyme 19 Number of Residues 557
Enzyme 19 Molecular Weight 61863.6
Enzyme 19 Theoretical pI 8.86
Enzyme 19 GO Classification
Function
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • translation
Component
Enzyme 19 General Function Involved in carbon-nitrogen ligase activity, with glutamine as amido-N-donor
Enzyme 19 Specific Function Furnishes a means for formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu- tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho- Glu-tRNA(Gln) (Potential)
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein Not Available
Enzyme 19 UniProtKB/Swiss-Prot ID O75879 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name GATB_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1674 bp
ATGGCGGCGCCCATGCTGCGCTGGGGCTGCCGTGGAAGACGTTGGGCTTTCGCCCGGGTT
GACGGTGGTTCTTGCCACCGAAGAGGGGCTCCGACTGGGTCCACATCCAACCAGATTAGG
GGAGAGAGCTCAGTGGCTCAGCAGCCCCTCCACACGGCCCAGAAGACGAGGAAAGGTGAA
CACAAATGGGCTGCTGTGGTAGGTTTGGAAATTCATGCCCAGATTTCCTCCAACTCTAAA
CTCTTCTCTGGATCTCAAGTTCGCTTTTCAGCACCTCCAAATTCTTTGGTTTCTTTTTTT
GATGCATCTCTACCTGGAACTTTGCCGGTTCTCAACAGGAGGTGTGTAGAAGCGGCGGTG
ATGACAGGCCTGGCTCTGAACTGCCACATAAACAAGAAGTCCTTGTTTGACAGGAAGCAC
TACTTCTATGCAGACCTCCCTGCAGGCTACCAAATTACCCAGCAGAGGCTCCCAATTGCT
GTGAATGGGAGCTTGATATATGGCGTCTGTGCAGGGAAGAAGCAGAGTCAGGTGATCCCC
AAGACGGTGAGGATCAAGCAGATCCAGTTGGAGCAAGACAGTGGCAAAAGCCTCCACGAC
AACCTGAGGTCTCAGACGCTCATTGATTTGAACAGGGCAGGAGTGGGCCTTCTGGAGGTG
GTCCTGGAGCCCGACATGTCCTGTGGAGAAGAGGCGGCAACAGCTGTCAGGGAGCTGCAG
CTGATCCTTCAAGCCCTGGGGACCAGCCAGGCGAACATGGCAGAGGGCCAGTTGAGAGTG
GATGCCAATATATCCGTGCATCACCCTGGGGAGCCTTTGGGCGTTCGAACGGAAGTGAAG
AATCTCAACAGCATCAGGTTCCTGGCCAAAGCCATAGACTATGAAATTCAGAGGCAAATC
AATGAACTTGAGAATGGAGGTGAAATTCTGAACGAAACACGCTCATTTCATCACAAGCTG
GGGTGCACCATGTCAATGAGAGACAAAGAAGGAAAACAGGACTACAGGTTCATGCCAGAA
CCCAACCTGCCTCCCCTGGTGCTCTACGACGCCACATCTCTGCCCGCAGGTGCAGACCCA
CAGCAAGTGATCAATATTGACCAGATTCGGGAGACACTCCCGGAGCTCCCCAGTGTGACC
CGAGAGAAGCTTGTCCAACAGTATGGGATGCTGCTGGAACACAGCTTCACTTTGCTGAAC
GAAGTCGGCCTACTGGAGTTCTTCCAAAATGTGATAAAAGAAACTAGGGCAGAGCCAAAA
AAGGTGACTAGTTGGGTCCTCAACACTTTTCTGGGCTATTTAAAGCAACAGAACCTCGCT
GTCAGTGAGAGTCCTGTCACACCCTCTGCACTCGCTGAGCTTCTTGACCTGCTGGACAGC
AGAACAATTTCTTCATCAGCAGCTAAACAGGTGTTTGAGGAACTGTGGAAGAGGGAAGGC
AAGACTCCAGGGCAGATTGTTTCAGAAAAGCAGCTTGAACTGATGCAGGACCAGGGGGCA
CTGGAGCAGCTCTGCCACTCTGTGATGGAGGCCCATCCTCAAGTGGTAATGGATGTGAAG
AACAGAAACCCCAGAGCTATAAATAAACTGATTGGGTTGGTCCGGAAAGCGACTCAAAGC
CGAGCAGATCCAGTCATGATAAAGGAGATCCTGGAGAAGAAGCTGTCATTGTGA
Enzyme 19 GenBank Gene ID AF026851 Link Image
Enzyme 19 GeneCard ID PET112L Link Image
Enzyme 19 GenAtlas ID PET112L Link Image
Enzyme 19 HGNC ID HGNC:8849 Link Image
Enzyme 19 Chromosome Location 4
Enzyme 19 Locus 4q27-q28
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Petruzzella V, Tiranti V, Fernandez P, Ianna P, Carrozzo R, Zeviani M: Identification and characterization of human cDNAs specific to BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain. Genomics. 1998 Dec 15;54(3):494-504. [PubMed Link Image]
  2. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  3. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 7373
Enzyme 20 Name Neutral amino acid transporter B(0)
Enzyme 20 Synonyms
  1. ATB(0)
  2. Baboon M7 virus receptor
  3. RD114/simian type D retrovirus receptor
  4. Sodium-dependent neutral amino acid transporter type 2
  5. Solute carrier family 1 member 5
Enzyme 20 Gene Name SLC1A5
Enzyme 20 Protein Sequence >Neutral amino acid transporter B(0)
MVADPPRDSKGLAAAEPTANGGLALASIEDQGAAAGGYCGSRDQVRRCLRANLLVLLTVV
AVVAGVALGLGVSGAGGALALGPERLSAFVFPGELLLRLLRMIILPLVVCSLIGGAASLD
PGALGRLGAWALLFFLVTTLLASALGVGLALALQPGAASAAINASVGAAGSAENAPSKEV
LDSFLDLARNIFPSNLVSAAFRSYSTTYEERNITGTRVKVPVGQEVEGMNILGLVVFAIV
FGVALRKLGPEGELLIRFFNSFNEATMVLVSWIMWYAPVGIMFLVAGKIVEMEDVGLLFA
RLGKYILCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGIVTPLATAFGTSSSSATLPLM
MKCVEENNGVAKHISRFILPIGATVNMDGAALFQCVAAVFIAQLSQQSLDFVKIITILVT
ATASSVGAAGIPAGGVLTLAIILEAVNLPVDHISLILAVDWLVDRSCTVLNVEGDALGAG
LLQNYVDRTESRSTEPELIQVKSELPLDPLPVPTEEGNPLLKHYRGPAGDATVASEKESV
M
Enzyme 20 Number of Residues 541
Enzyme 20 Molecular Weight 56597.6
Enzyme 20 Theoretical pI 5.14
Enzyme 20 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 20 General Function Involved in sodium:dicarboxylate symporter activity
Enzyme 20 Specific Function Has a broad substrate specificity, a preference for zwitterionic amino acids, and a sodium-dependence. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated amino acids, anionic amino acids, and cationic amino acids. Act as a cell surface receptor for feline endogenous virus RD114, baboon M7 endogenous virus and type D simian retroviruses
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 53-73 99-119 133-153 225-245 266-286 306-326 336-356 377-397 399-419 426-446
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 4191556 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q15758 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name AAAT_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1626 bp
ATGGTGGCCGATCCTCCTCGAGACTCCAAGGGGCTCGCAGCGGCGGAGCCCACCGCCAAC
GGGGGCCTGGCGCTGGCCTCCATCGAGGACCAAGGCGCGGCAGCAGGCGGCTACTGCGGT
TCCCGGGACCAGGTGCGCCGCTGCCTTCGAGCCAACCTGCTTGTGCTGCTGACAGTGGTG
GCCGTGGTGGCCGGCGTGGCGCTGGGACTGGGGGTGTCGGGGGCCGGGGGTGCGCTGGCG
TTGGGCCCGGAGCGCTTGAGCGCCTTCGTCTTCCCGGGCGAGCTGCTGCTGCGTCTGCTG
CGGATGATCATCTTGCCGCTGGTGGTGTGCAGCTTGATAGGCGGCGCCGCCAGCCTGGAC
CCCGGCGCGCTCGGCCGTCTGGGCGCCTGGGCGCTGCTCTTTTTCCTGGTCACCACGCTG
CTGGCGTCGGCGCTCGGAGTGGGCTTGGCGCTGGCTCTGCAGCCGGGCGCCGCCTCCGCC
GCCATCAACGCCTCCGTGGGAGCCGCGGGCAGTGCCGAAAATGCCCCCAGCAAGGAGGTG
CTCGATTCGTTCCTGGATCTTGCGAGAAATATCTTCCCTTCCAACCTGGTGTCAGCAGCC
TTTCGCTCATACTCTACCACCTATGAAGAGAGGAATATCACCGGAACCAGGGTGAAGGTG
CCCGTGGGGCAGGAGGTGGAGGGGATGAACATCCTGGGCTTGGTAGTGTTTGCCATCGTC
TTTGGTGTGGCGCTGCGGAAGCTGGGGCCTGAAGGGGAGCTGCTTATCCGCTTCTTCAAC
TCCTTCAATGAGGCCACCATGGTTCTGGTCTCCTGGATCATGTGGTACGCCCCTGTGGGC
ATCATGTTCCTGGTGGCTGGCAAGATCGTGGAGATGGAGGATGTGGGTTTACTCTTTGCC
CGCCTTGGCAAGTACATTCTGTGCTGCCTGCTGGGTCACGCCATCCATGGGCTCCTGGTA
CTGCCCCTCATCTACTTCCTCTTCACCCGCAAAAACCCCTACCGCTTCCTGTGGGGCATC
GTGACGCCGCTGGCCACTGCCTTTGGGACCTCTTCCAGTTCCGCCACGCTGCCGCTGATG
ATGAAGTGCGTGGAGGAGAATAATGGCGTGGCCAAGCACATCAGCCGTTTCATCCTGCCC
ATCGGCGCCACCGTCAACATGGACGGTGCCGCGCTCTTCCAGTGCGTGGCCGCAGTGTTC
ATTGCACAGCTCAGCCAGCAGTCCTTGGACTTCGTAAAGATCATCACCATCCTGGTCACG
GCCACAGCGTCCAGCGTGGGGGCAGCGGGCATCCCTGCTGGAGGTGTCCTCACTCTGGCC
ATCATCCTCGAAGCAGTCAACCTCCCGGTCGACCATGTCTCCTTGATCCTGGCTGTGGGC
TGGCTAGCCGACCGGTCCTGTACCGTCCTCAATGTAGAAGGTGACGCTCTGGGGGCAGGA
CTCCTCCAAAATTACGTGGACCGTACGGAGTCGAGAAGCACAGAGCCTGAGTTGATACAA
GTGAAGAGTGAGCTGCCCCTGGGTCCGCTGCCAGTCCCCACTGAGGAAGGAAACCCCCTC
CTCAAACACTATCGGGGGCCCGCAGGGGATGCCACGGTCGCCTCTGAGAAGGAATCAGTC
ATGTAA
Enzyme 20 GenBank Gene ID AF102826 Link Image
Enzyme 20 GeneCard ID SLC1A5 Link Image
Enzyme 20 GenAtlas ID SLC1A5 Link Image
Enzyme 20 HGNC ID HGNC:10943 Link Image
Enzyme 20 Chromosome Location 1
Enzyme 20 Locus 19q13.3
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Kekuda R, Prasad PD, Fei YJ, Torres-Zamorano V, Sinha S, Yang-Feng TL, Leibach FH, Ganapathy V: Cloning of the sodium-dependent, broad-scope, neutral amino acid transporter Bo from a human placental choriocarcinoma cell line. J Biol Chem. 1996 Aug 2;271(31):18657-61. [PubMed Link Image]
  2. Rasko JE, Battini JL, Gottschalk RJ, Mazo I, Miller AD: The RD114/simian type D retrovirus receptor is a neutral amino acid transporter. Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2129-34. [PubMed Link Image]
  3. Tailor CS, Nouri A, Zhao Y, Takeuchi Y, Kabat D: A sodium-dependent neutral-amino-acid transporter mediates infections of feline and baboon endogenous retroviruses and simian type D retroviruses. J Virol. 1999 May;73(5):4470-4. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Tailor CS, Marin M, Nouri A, Kavanaugh MP, Kabat D: Truncated forms of the dual function human ASCT2 neutral amino acid transporter/retroviral receptor are translationally initiated at multiple alternative CUG and GUG codons. J Biol Chem. 2001 Jul 20;276(29):27221-30. Epub 2001 May 11. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  11. Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed Link Image]
  12. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 7884
Enzyme 21 Name Large neutral amino acids transporter small subunit 2
Enzyme 21 Synonyms
  1. L-type amino acid transporter 2
  2. hLAT2
  3. Solute carrier family 7 member 8
Enzyme 21 Gene Name SLC7A8
Enzyme 21 Protein Sequence >Large neutral amino acids transporter small subunit 2
MEEGARHRNNTEKKHPGGGESDASPEAGSGGGGVALKKEIGLVSACGIIVGNIIGSGIFV
SPKGVLENAGSVGLALIVWIVTGFITVVGALCYAELGVTIPKSGGDYSYVKDIFGGLAGF
LRLWIAVLVIYPTNQAVIALTFSNYVLQPLFPTCFPPESGLRLLAAICLLLLTWVNCSSV
RWATRVQDIFTAGKLLALALIIIMGIVQICKGEYFWLEPKNAFENFQEPDIGLVALAFLQ
GSFAYGGWNFLNYVTEELVDPYKNLPRAIFISIPLVTFVYVFANVAYVTAMSPQELLASN
AVAVTFGEKLLGVMAWIMPISVALSTFGGVNGSLFTSSRLFFAGAREGHLPSVLAMIHVK
RCTPIPALLFTCISTLLMLVTSDMYTLINYVGFINYLFYGVTVAGQIVLRWKKPDIPRPI
KINLLFPIIYLLFWAFLLVFSLWSEPVVCGIGLAIMLTGVPVYFLGVYWQHKPKCFSDFI
ELLTLVSQKMCVVVYPEVERGSGTEEANEDMEEQQQPMYQPTPTKDKDVAGQPQP
Enzyme 21 Number of Residues 535
Enzyme 21 Molecular Weight 58381.1
Enzyme 21 Theoretical pI 5.75
Enzyme 21 GO Classification
Function
  • active transmembrane transporter activity
  • amine transmembrane transporter activity
  • amino acid transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • amine transport
  • amino acid transport
  • establishment of localization
  • transmembrane transport
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 21 General Function Involved in transport
Enzyme 21 Specific Function Sodium-independent, high-affinity transport of small and large neutral amino acids such as alanine, serine, threonine, cysteine, phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Acts as an amino acid exchanger. Has higher affinity for L-phenylalanine than LAT1 but lower affinity for glutamine and serine. L-alanine is transported at physiological concentrations. Plays a role in basolateral (re)absorption of neutral amino acids. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Plays an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 40-60 72-92 113-133 155-175 189-209 231-251 268-288 310-330 362-382 388-408 424-444 447-467
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 12597192 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q9UHI5 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name LAT2_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1608 bp
ATGGAAGAAGGAGCCAGGCACCGAAACAACACCGAAAAGAAACACCCAGGTGGGGGCGAG
TCGGACGCCAGCCCCGAGGCTGGTTCCGGAGGGGGCGGAGTAGCCCTGAAGAAAGAGATC
GGATTGGTCAGTGCCTGTGGTATCATCGTAGGGAACATCATCGGCTCTGGAATCTTTGTC
TCGCCAAAGGGAGTGCTGGAGAATGCTGGTTCTGTGGGCCTTGCTCTCATCGTCTGGATT
GTGACGGGCTTCATCACAGTTGTGGGAGCCCTCTGCTATGCTGAACTCGGGGTCACCATC
CCCAAATCTGGAGGTGACTACTCCTATGTCAAGGACATCTTCGGAGGACTGGCTGGGTTC
CTGAGGCTGTGGATTGCTGTGCTGGTGATCTACCCCACCAACCAGGCTGTCATCGCCCTC
ACCTTCTCCAACTACGTGCTGCAGCCGCTCTTCCCCACCTGCTTCCCCCCAGAGTCTGGC
CTTCGGCTCCTGGCTGCCATCTGCTTATTGCTCCTCACATGGGTCAACTGTTCCAGTGTG
CGGTGGGCCACCCGGGTTCAAGACATCTTCACAGCTGGGAAGCTCCTGGCCTTGGCCCTG
ATTATCATCATGGGGATTGTACAGATATGCAAAGGAGAGTACTTCTGGCTGGAGCCAAAG
AATGCATTTGAGAATTTCCAGGAACCTGACATCGGCCTCGTCGCACTGGCTTTCCTTCAG
GGCTCCTTTGCCTATGGAGGCTGGAACTTTCTGAATTACGTGACTGAGGAGCTTGTTGAT
CCCTACAAGAACCTTCCCAGAGCCATCTTCATCTCCATCCCACTGGTCACATTTGTGTAT
GTCTTTGCCAATGTCGCTTATGTCACTGCAATGTCCCCCCAGGAGCTGCTGGCATCCAAC
GCCGTCGCTGTGACTTTTGGAGAGAAGCTCCTAGGAGTCATGGCCTGGATCATGCCCATT
TCTGTTGCCCTGTCCACATTTGGAGGAGTTAATGGGTCTCTCTTCACCTCCTCTCGGCTG
TTCTTCGCTGGAGCCCGAGAGGGCCACCTTCCCAGTGTGTTGGCCATGATCCACGTGAAG
CGCTGCACCCCAATCCCAGCCCTGCTCTTCACATGCATCTCCACCCTGCTGATGCTGGTC
ACCAGCGACATGTACACACTCATCAACTACGTGGGCTTCATCAACTACCTCTTCTATGGG
GTCACGGTTGCTGGACAGATAGTCCTTCGCTGGAAGAAGCCTGATATCCCCCGCCCCATC
AAGATCAACCTGCTGTTCCCCATCATCTACTTGCTGTTCTGGGCCTTCCTGCTGGTCTTC
AGCCTGTGGTCAGAGCCGGTGGTGTGTGGCATTGGCCTGGCCATCATGCTGACAGGAGTG
CCTGTCTATTTCCTGGGTGTTTACTGGCAACACAAGCCCAAGTGTTTCAGTGACTTCATT
GAGCTGCTAACCCTGGTGAGCCAGAAGATGTGTGTGGTCGTGTACCCCGAGGTGGAGCGG
GGCTCAGGGACAGAGGAGGCTAATGAGGACATGGAGGAGCAGCAGCAGCCCATGTACCAA
CCCACTCCCACGAAGGACAAGGACGTGGCGGGGCAGCCCCAGCCCTGA
Enzyme 21 GenBank Gene ID AB037669 Link Image
Enzyme 21 GeneCard ID SLC7A8 Link Image
Enzyme 21 GenAtlas ID SLC7A8 Link Image
Enzyme 21 HGNC ID HGNC:11066 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 14q11.2
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Pineda M, Fernandez E, Torrents D, Estevez R, Lopez C, Camps M, Lloberas J, Zorzano A, Palacin M: Identification of a membrane protein, LAT-2, that Co-expresses with 4F2 heavy chain, an L-type amino acid transport activity with broad specificity for small and large zwitterionic amino acids. J Biol Chem. 1999 Jul 9;274(28):19738-44. [PubMed Link Image]
  2. Rossier G, Meier C, Bauch C, Summa V, Sordat B, Verrey F, Kuhn LC: LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of kidney and intestine. J Biol Chem. 1999 Dec 3;274(49):34948-54. [PubMed Link Image]
  3. Borsani G, Bassi MT, Sperandeo MP, De Grandi A, Buoninconti A, Riboni M, Manzoni M, Incerti B, Pepe A, Andria G, Ballabio A, Sebastio G: SLC7A7, encoding a putative permease-related protein, is mutated in patients with lysinuric protein intolerance. Nat Genet. 1999 Mar;21(3):297-301. [PubMed Link Image]
  4. Park SY, Kim JK, Kim IJ, Choi BK, Jung KY, Lee S, Park KJ, Chairoungdua A, Kanai Y, Endou H, Kim DK: Reabsorption of neutral amino acids mediated by amino acid transporter LAT2 and TAT1 in the basolateral membrane of proximal tubule. Arch Pharm Res. 2005 Apr;28(4):421-32. [PubMed Link Image]
  5. 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]
  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. Broer A, Friedrich B, Wagner CA, Fillon S, Ganapathy V, Lang F, Broer S: Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2 requires different domains. Biochem J. 2001 May 1;355(Pt 3):725-31. [PubMed Link Image]
  8. Simmons-Willis TA, Koh AS, Clarkson TW, Ballatori N: Transport of a neurotoxicant by molecular mimicry: the methylmercury-L-cysteine complex is a substrate for human L-type large neutral amino acid transporter (LAT) 1 and LAT2. Biochem J. 2002 Oct 1;367(Pt 1):239-46. [PubMed Link Image]
  9. Liu X, Charrier L, Gewirtz A, Sitaraman S, Merlin D: CD98 and intracellular adhesion molecule I regulate the activity of amino acid transporter LAT-2 in polarized intestinal epithelia. J Biol Chem. 2003 Jun 27;278(26):23672-7. Epub 2003 Apr 25. [PubMed Link Image]
  10. Gandhi MD, Pal D, Mitra AK: Identification and functional characterization of a Na(+)-independent large neutral amino acid transporter (LAT2) on ARPE-19 cells. Int J Pharm. 2004 May 4;275(1-2):189-200. [PubMed Link Image]
  11. Fraga S, Pinho MJ, Soares-da-Silva P: Expression of LAT1 and LAT2 amino acid transporters in human and rat intestinal epithelial cells. Amino Acids. 2005 Nov;29(3):229-33. Epub 2005 Jul 20. [PubMed Link Image]
  12. Li S, Whorton AR: Identification of stereoselective transporters for S-nitroso-L-cysteine: role of LAT1 and LAT2 in biological activity of S-nitrosothiols. J Biol Chem. 2005 May 20;280(20):20102-10. Epub 2005 Mar 15. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 7918
Enzyme 22 Name Glutaminase 2 (Liver, mitochondrial), isoform CRA_b
Enzyme 22 Synonyms
  1. SubName: L-glutaminase
Enzyme 22 Gene Name GLS2
Enzyme 22 Protein Sequence >Glutaminase 2 (Liver, mitochondrial), isoform CRA_b
MRSMKALQKALSRAGSHCGRGGWGHPSRSPLLGGGVRHHLSEAAAQGRETPHSHQPQHQD
HDSSESGMLSRLGDLLFYTIAEGQERIPIHKFTTALKATGLQTSDPRLRDCMSEMHRVVQ
ESSSGGLLDRDLFRKCVSSNIVLLTQAFRKKFVIPDFEEFTGHVDRIFEDVKELTGGKVA
AYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHK
FVGKEPSGLRYNKLSLNEEGIPHNPMVNAGAIVVSSLIKMDCNKAEKFDFVLQYLNKMAG
NEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMMAALDLYFQLCSVEVTCESG
SVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGA
ILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFHNYDNLRHCARKLDPRREGA
EIRNKTVVNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIE
ACKVNPFAKDRWGNIPLDDAVQFNHLEVVKLLQDYQDSYTLSETQAEAAAEALSKENLES
MV
Enzyme 22 Number of Residues 602
Enzyme 22 Molecular Weight 66322.2
Enzyme 22 Theoretical pI 7.32
Enzyme 22 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 22 General Function Involved in glutaminase activity
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways
Enzyme 22 Reactions
  • L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 29029569 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q8IX91 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name Q8IX91_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 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 22 GenBank Gene ID AF348119 Link Image
Enzyme 22 GeneCard ID GLS2 Link Image
Enzyme 22 GenAtlas ID GLS2 Link Image
Enzyme 22 HGNC ID HGNC:29570 Link Image
Enzyme 22 Chromosome Location 1
Enzyme 22 Locus 12q13
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 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 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 8562
Enzyme 23 Name Sodium-coupled neutral amino acid transporter 3
Enzyme 23 Synonyms
  1. N-system amino acid transporter 1
  2. Na(+)-coupled neutral amino acid transporter 3
  3. Solute carrier family 38 member 3
  4. System N amino acid transporter 1
Enzyme 23 Gene Name SLC38A3
Enzyme 23 Protein Sequence >Sodium-coupled neutral amino acid transporter 3
MEAPLQTEMVELVPNGKHSEGLLPVITPMAGNQRVEDPARSCMEGKSFLQKSPSKEPHFT
DFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKS
SGVVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEE
KTSDWYMNGNYLVILVSVTIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFHVPC
PLPPNFNNTTGNFSHVEIVKEKVQLQVEPEASAFCTPSYFTLNSQTAYTIPIMAFAFVCH
PEVLPIYTELKDPSKKKMQHISNLSIAVMYIMYFLAALFGYLTFYNGVESELLHTYSKVD
PFDVLILCVRVAVLTAVTLTVPIVLFPVRRAIQQMLFPNQEFSWLRHVLIAVGLLTCINL
LVIFAPNILGIFGVIGATSAPFLIFIFPAIFYFRIMPTEKEPARSTPKILALCFAMLGFL
LMTMSLSFIIIDWASGTSRHGGNH
Enzyme 23 Number of Residues 504
Enzyme 23 Molecular Weight 55772.4
Enzyme 23 Theoretical pI 8.01
Enzyme 23 GO Classification Not Available
Enzyme 23 General Function Amino acid transport and metabolism
Enzyme 23 Specific Function Sodium-dependent amino acid/proton antiporter. Mediates electrogenic cotransport of glutamine and sodium ions in exchange for protons. Also recognizes histidine, asparagine and alanine. May mediate amino acid transport in either direction under physiological conditions. May play a role in nitrogen metabolism and synaptic transmission
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 83-103 106-126 144-164 187-207 213-233 324-344 366-386 408-428 431-451 471-491
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 5870893 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q99624 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name S38A3_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1515 bp
ATGGAGGCGCCTTTGCAGACAGAGATGGTGGAGCTGGTGCCCAATGGCAAACACTCAGAG
GGGCTGCTCCCGGTCATCACCCCCATGGCAGGCAACCAGAGGGTCGAGGACCCTGCACGG
AGCTGTATGGAGGGCAAGAGCTTCCTACAGAAAAGTCCCAGCAAGGAGCCACACTTCACT
GACTTCGAGGGGAAGACATCATTCGGGATGTCAGTGTTCAACCTCAGCAATGCCATCATG
GGCAGCGGCATCCTGGGACTCGCCTATGCCATGGCCAATACGGGCATTATCCTTTTCCTG
TTCCTGTTGACAGCTGTCGCCTTGCTCTCCAGCTACTCCATCCACCTGCTACTCAAGTCC
TCAGGGGTCGTGGGCATCCGTGCCTATGAGCAGCTGGGCTACCGTGCCTTTGGGACCCCA
GGAAAGCTGGCAGCAGCCCTGGCCATCACGCTCCAGAACATCGGAGCCATGTCCAGCTAC
CTGTACATCATCAAGTCTGAGCTGCCACTTGTCATACAGACCTTCCTGAACCTGGAGGAG
AAAACCTCGGACTGGTACATGAACGGGAACTACCTGGTAATCCTTGTCTCTGTCACCATC
ATTCTGCCCCTGGCACTGATGCGGCAGCTTGGCTACCTGGGCTACTCCAGCGGCTTCTCT
CTTAGCTGCATGGTGTTCTTCCTAATTGCAGTCATCTACAAAAAGTTCCACGTGCCCTGC
CCACTGCCCCCCAACTTCAACAACACCACAGGCAACTTCAGCCACGTGGAGATCGTGAAG
GAGAAGGTGCAGCTGCAGGTCGAGCCTGAGGCTTCAGCCTTCTGCACTCCCAGCTACTTC
ACGCTCAACTCACAGACAGCATACACCATCCCCATCATGGCCTTCGCCTTCGTCTGCCAC
CCCGAGGTGCTGCCCATCTATACTGAGCTCAAGGACCCCTCCAAGAAGAAGATGCAGCAC
ATCTCCAACCTGTCCATCGCTGTCATGTACATCATGTACTTCCTGGCTGCCCTCTTCGGC
TACCTCACCTTCTACAACGGGGTGGAGTCGGAGCTGCTGCACACCTACAGCAAGGTGGAC
CCGTTTGACGTCCTGATCCTGTGTGTGCGCGTGGCCGTGCTGACAGCAGTCACGCTCACA
GTGCCCATCGTTCTGTTCCCGGTGCGCCGCGCCATCCAGCAGATGCTGTTTCCAAACCAG
GAGTTCAGCTGGCTGCGGCATGTGCTTATTGCCGTTGGCCTGCTCACTTGTATCAACCTG
CTGGTCATCTTTGCCCCCAACATCCTGGGCATCTTTGGGGTCATCGGTGCCACATCTGCC
CCATTCCTCATCTTCATCTTCCCTGCCATCTTCTACTTCCGAATCATGCCCACGGAGAAG
GAGCCTGCAAGATCCACCCCCAAAATCCTGGCCCTGTGTTTTGCTATGCTTGGCTTCTTG
CTGATGACCATGAGCTTGAGCTTCATCATCATTGACTGGGCCTCAGGGACCAGCCGGCAT
GGAGGAAACCACTAG
Enzyme 23 GenBank Gene ID NM_006841.4 Link Image
Enzyme 23 GeneCard ID SLC38A3 Link Image
Enzyme 23 GenAtlas ID SLC38A3 Link Image
Enzyme 23 HGNC ID HGNC:18044 Link Image
Enzyme 23 Chromosome Location 3
Enzyme 23 Locus 3p21.3
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Fei YJ, Sugawara M, Nakanishi T, Huang W, Wang H, Prasad PD, Leibach FH, Ganapathy V: Primary structure, genomic organization, and functional and electrogenic characteristics of human system N 1, a Na+- and H+-coupled glutamine transporter. J Biol Chem. 2000 Aug 4;275(31):23707-17. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Lerman MI, Minna JD: The 630-kb lung cancer homozygous deletion region on human chromosome 3p21.3: identification and evaluation of the resident candidate tumor suppressor genes. The International Lung Cancer Chromosome 3p21.3 Tumor Suppressor Gene Consortium. Cancer Res. 2000 Nov 1;60(21):6116-33. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 8813
Enzyme 24 Name Glutamine-dependent NAD(+) synthetase
Enzyme 24 Synonyms
  1. NAD(+) synthase [glutamine-hydrolyzing]
  2. NAD(+) synthetase
Enzyme 24 Gene Name NADSYN1
Enzyme 24 Protein Sequence >Glutamine-dependent NAD(+) synthetase
MGRKVTVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYES
DTLLHSFQVLAALVESPVTQDIICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANE
GNYRELRWFTPWSRSRHTEEYFLPRMIQDLTKQETVPFGDAVLVTWDTCIGSEICEELWT
PHSPHIDMGLDGVEIITNASGSHQVLRKANTRVDLVTMVTSKNGGIYLLANQKGCDGDRL
YYDGCAMIAMNGSVFAQGSQFSLDDVEVLTATLDLEDVRSYRAEISSRNLAASRASPYPR
VKVDFALSCHEDLLAPISEPIEWKYHSPEEEISLGPACWLWDFLRRSQQAGFLLPLSGGV
DSAATACLIYSMCCQVCEAVRSGNEEVLADVRTIVNQISYTPQDPRDLCGRILTTCYMAS
KNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFSLVTGKSPLFAAHGGSSRENLA
LQNVQARIRMVLAYLFAQLSLWSRGVHGGLLVLGSANVDESLLGYLTKYDCSSADINPIG
GISKTDLRAFVQFCIQRFQLPALQSILLAPATAELEPLADGQVSQTDEEDMGMTYAELSV
YGKLRKVAKMGPYSMFCKLLGMWRHICTPRQVADKVKRFFSKYSMNRHKMTTLTPAYHAE
NYSPEDNRFDLRPFLYNTSWPWQFRCIENQVLQLERAEPQSLDGVD
Enzyme 24 Number of Residues 706
Enzyme 24 Molecular Weight 79283.9
Enzyme 24 Theoretical pI 6.40
Enzyme 24 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 24 General Function Involved in NAD+ synthase (glutamine-hydrolyzing) activity
Enzyme 24 Specific Function ATP + deamido-NAD(+) + L-glutamine + H(2)O = AMP + diphosphate + NAD(+) + L-glutamate
Enzyme 24 Pathways
Enzyme 24 Reactions
  • ATP + deamido-NAD+ + L-glutamine + H2O = AMP + diphosphate + NAD+ + L-glutamate [RN:R00257]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 28849201 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q6IA69 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name NADE_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 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 24 GenBank Gene ID AB091316 Link Image
Enzyme 24 GeneCard ID NADSYN1 Link Image
Enzyme 24 GenAtlas ID NADSYN1 Link Image
Enzyme 24 HGNC ID HGNC:29832 Link Image
Enzyme 24 Chromosome Location 1
Enzyme 24 Locus 11q13.4
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 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 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 8876
Enzyme 25 Name CAD protein
Enzyme 25 Synonyms
  1. Glutamine-dependent carbamoyl-phosphate synthase
  2. Aspartate carbamoyltransferase
  3. Dihydroorotase
Enzyme 25 Gene Name CAD
Enzyme 25 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 25 Number of Residues 2225
Enzyme 25 Molecular Weight 242981.7
Enzyme 25 Theoretical pI 6.42
Enzyme 25 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 25 General Function Involved in hydrolase activity
Enzyme 25 Specific Function This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase)
Enzyme 25 Pathways
Enzyme 25 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 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 1228049 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P27708 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name PYR1_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 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 25 GenBank Gene ID D78586 Link Image
Enzyme 25 GeneCard ID CAD Link Image
Enzyme 25 GenAtlas ID CAD Link Image
Enzyme 25 HGNC ID HGNC:1424 Link Image
Enzyme 25 Chromosome Location 2
Enzyme 25 Locus 2p22-p21
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 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 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 9663
Enzyme 26 Name CTP synthase 2
Enzyme 26 Synonyms
  1. CTP synthetase 2
  2. UTP--ammonia ligase 2
Enzyme 26 Gene Name CTPS2
Enzyme 26 Protein Sequence >CTP synthase 2
MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFV
LNDGGEVDLDLGNYERFLDINLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDA
VQEWVMNQAKVPVDGNKEEPQICVIELGGTIGDIEGMPFVEAFRQFQFKAKRENFCNIHV
SLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ
VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSASNLLFKWRNMADRYERLQKICS
IALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEKITETEDPVKFHEAWQK
LCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCLGMQLAVIEFARNCLNLKDAD
STEFRPNAPVPLVIDMPEHNPGNLGGTMRLGIRRTVFKTENSILRKLYGDVPFIEERHRH
RFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPY
LGLLLAATGNLNAYLQQGCKLSSSDRYSDASDDSFSEPRIAELEIS
Enzyme 26 Number of Residues 586
Enzyme 26 Molecular Weight 65677.0
Enzyme 26 Theoretical pI 6.91
Enzyme 26 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 26 General Function Involved in CTP synthase activity
Enzyme 26 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 26 Pathways
Enzyme 26 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 9651727 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q9NRF8 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name PYRG2_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 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 26 GenBank Gene ID AF226667 Link Image
Enzyme 26 GeneCard ID CTPS2 Link Image
Enzyme 26 GenAtlas ID CTPS2 Link Image
Enzyme 26 HGNC ID HGNC:2520 Link Image
Enzyme 26 Chromosome Location Not Available
Enzyme 26 Locus Not Available
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 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 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 13038
Enzyme 27 Name Phosphoribosyl pyrophosphate amidotransferase, isoform CRA_b
Enzyme 27 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 27 Gene Name PPAT
Enzyme 27 Protein Sequence >Phosphoribosyl pyrophosphate amidotransferase, isoform CRA_b
MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPT
FKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVA
HNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEA
PTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFL
SIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVY
TVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQP
NMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASP
PIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKE
KKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW
Enzyme 27 Number of Residues 517
Enzyme 27 Molecular Weight 57398.5
Enzyme 27 Theoretical pI 6.74
Enzyme 27 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 27 General Function Involved in amidophosphoribosyltransferase activity
Enzyme 27 Specific Function Not Available
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 158255320 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID A8K4H7 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name A8K4H7_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 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 27 GenBank Gene ID AK290942 Link Image
Enzyme 27 GeneCard ID PPAT Link Image
Enzyme 27 GenAtlas ID PPAT Link Image
Enzyme 27 HGNC ID HGNC:9238 Link Image
Enzyme 27 Chromosome Location 4
Enzyme 27 Locus 4q12
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References Not Available
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 13039
Enzyme 28 Name Guanine monphosphate synthetase, isoform CRA_b
Enzyme 28 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 28 Gene Name GMPS
Enzyme 28 Protein Sequence >Guanine monphosphate synthetase, isoform CRA_b
MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETP
AFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHK
KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANE
SKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAA
HSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPE
EVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVR
ILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPH
TLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDW
ESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVE
VVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
Enzyme 28 Number of Residues 693
Enzyme 28 Molecular Weight 76714.8
Enzyme 28 Theoretical pI 6.86
Enzyme 28 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 28 General Function Involved in catalytic activity
Enzyme 28 Specific Function Not Available
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 158256440 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID A8K639 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name A8K639_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 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 28 GenBank Gene ID AK291504 Link Image
Enzyme 28 GeneCard ID GMPS Link Image
Enzyme 28 GenAtlas ID GMPS Link Image
Enzyme 28 HGNC ID HGNC:4378 Link Image
Enzyme 28 Chromosome Location 3
Enzyme 28 Locus 3q24
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 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 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 13040
Enzyme 29 Name Glutamine synthetase
Enzyme 29 Synonyms Not Available
Enzyme 29 Gene Name PIG59
Enzyme 29 Protein Sequence >Glutamine synthetase
MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEW
NFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRI
MDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHY
RACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDP
KPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRL
TGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCL
LNETGDEPFQYKN
Enzyme 29 Number of Residues 373
Enzyme 29 Molecular Weight 42064.1
Enzyme 29 Theoretical pI 6.88
Enzyme 29 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 29 General Function Involved in glutamate-ammonia ligase activity
Enzyme 29 Specific Function ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions
  • ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine [RN:R00253]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 193783746 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID A8YXX4 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name A8YXX4_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1122 bp
ATGACCACCTCAGCAAGTTCCCACTTAAATAAAGGCATCAAGCAGGTGTACATGTCCCTG
CCTCAGGGTGAGAAAGTCCAGGCCATGTATATCTGGATCGATGGTACTGGAGAAGGACTG
CGCTGCAAGACCCGGACCCTGGACAGTGAGCCCAAGTGTGTGGAAGAGTTGCCTGAGTGG
AATTTCGATGGCTCCAGTACTTTACAGTCTGAGGGTTCCAACAGTGACATGTATCTCGTG
CCTGCTGCCATGTTTCGGGACCCCTTCCGTAAGGACCCTAACAAGCTGGTGTTATGTGAA
GTTTTCAAGTACAATCGAAGGCCTGCAGAGACCAATTTGAGGCACACCTGTAAACGGATA
ATGGACATGGTGAGCAACCAGCACCCCTGGTTTGGCATGGAGCAGGAGTATACCCTCATG
GGGACAGATGGGCACCCCTTTGGTTGGCCTTCCAACGGCTTCCCAGGGCCCCAGGGTCCA
TATTACTGTGGTGTGGGAGCAGACAGAGCCTATGGCAGGGACATCGTGGAGGCCCATTAC
CGGGCCTGCTTGTATGCTGGAGTCAAGATTGCGGGGACTAATGCCGAGGTCATGCCTGCC
CAGTGGGAATTTCAGATTGGACCTTGTGAAGGAATCAGCATGGGAGATCATCTCTGGGTG
GCCCGTTTCATCTTGCATCGTGTGTGTGAAGACTTTGGAGTGATAGCAACCTTTGATCCT
AAGCCCATTCCTGGGAACTGGAATGGTGCAGGCTGCCATACCAACTTCAGCACCAAGGCC
ATGCGGGAGGAGAATGGTCTGAAGTACATCGAGGAGGCCATTGAGAAACTAAGCAAGCGG
CACCAGTACCACATCCGTGCCTATGATCCCAAGGGAGGCCTGGACAATGCCCGACGTCTA
ACTGGATTCCATGAAACCTCCAACATCAACGACTTTTCTGCTGGTGTAGCCAATCGTAGC
GCCAGCATACGCATTCCCCGGACTGTTGGCCAGGAGAAGAAGGGTTACTTTGAAGATCGT
CGCCCCTCTGCCAACTGCGACCCCTTTTCGGTGACAGAAGCCCTCATCCGCACGTGTCTT
CTCAATGAAACCGGCGATGAGCCCTTCCAGTACAAAAATTAA
Enzyme 29 GenBank Gene ID AK122784 Link Image
Enzyme 29 GeneCard ID PIG59 Link Image
Enzyme 29 GenAtlas ID PIG59 Link Image
Enzyme 29 HGNC ID HGNC:4341 Link Image
Enzyme 29 Chromosome Location Not Available
Enzyme 29 Locus Not Available
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 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 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 15222
Enzyme 30 Name Putative uncharacterized protein GFPT1
Enzyme 30 Synonyms Not Available
Enzyme 30 Gene Name GFPT1
Enzyme 30 Protein Sequence >Putative uncharacterized protein GFPT1
MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWEANACKIQLI
KKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIV
IHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDNRESQDTSFTTLVERVIQQ
LEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEHKLSTDHIPILYRTGKDKKGSCNLSR
VDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGD
HPGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHI
KEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFL
SQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTS
QFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSV
LIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYA
KCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHL
AVLRGYDVDFPRNLAKSVTVE
Enzyme 30 Number of Residues 681
Enzyme 30 Molecular Weight 76760
Enzyme 30 Theoretical pI 6.84
Enzyme 30 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 30 General Function Cell wall/membrane/envelope biogenesis
Enzyme 30 Specific Function Not Available
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 62822278 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q53QE6 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name Q53QE6_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 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 30 GenBank Gene ID AC114772 Link Image
Enzyme 30 GeneCard ID Q53QE6 Link Image
Enzyme 30 GenAtlas ID GFPT1 Link Image
Enzyme 30 HGNC ID HGNC:4241 Link Image
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References Not Available
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 15223
Enzyme 31 Name cDNA FLJ75059, highly similar to Homo sapiens phosphoribosylformylglycinamidine synthase (FGAR amidotransferase) (PFAS), mRNA
Enzyme 31 Synonyms Not Available
Enzyme 31 Gene Name Not Available
Enzyme 31 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 31 Number of Residues 1338
Enzyme 31 Molecular Weight 144642.1
Enzyme 31 Theoretical pI 5.60
Enzyme 31 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 31 General Function Involved in catalytic activity
Enzyme 31 Specific Function Not Available
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 158259069 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID A8K9T9 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name A8K9T9_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 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 31 GenBank Gene ID AK292804 Link Image
Enzyme 31 GeneCard ID Not Available
Enzyme 31 GenAtlas ID Not Available
Enzyme 31 HGNC ID HGNC:8863 Link Image
Enzyme 31 Chromosome Location Not Available
Enzyme 31 Locus Not Available
Enzyme 31 SNPs Not Available
Enzyme 31 General References Not Available
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 15228
Enzyme 32 Name Cysteine conjugate-beta lyase
Enzyme 32 Synonyms
  1. cytoplasmic (Glutamine transaminase K, kyneurenine aminotransferase), isoform CRA_a
  2. SubName: cDNA FLJ77833, highly similar to H.sapiens glutamine transaminase K
  3. SubName: cDNA, FLJ95217, Homo sapiens cysteine conjugate-beta lyase
  4. cytoplasmic (glutaminetransaminase K, kyneurenine aminotransferase) (CCBL1), mRNA
Enzyme 32 Gene Name CCBL1
Enzyme 32 Protein Sequence >Cysteine conjugate-beta lyase
MAKQLQARRLDGIDYNPWVEFVKLASEHDVVNLGQGFPDFPPPDFAVEAFQHAVSGDFML
NQYTKTFGYPPLTKILASFFGELLGQEIDPLRNVLVTVGGYGALFTAFQALVDEGDEVII
IEPFFDCYEPMTMMAGGRPVFVSLKPGPIQNGELGSSSNWQLDPMELAGKFTSRTKALVL
NTPNNPLGKVFSREELELVASLCQQHDVVCITDEVYQWMVYDGHQHISIASLPGMWERTL
TIGSAGKTFSATGWKVGWVLGPDHIMKHLRTVHQNSVFHCPTQSQAAVAESFEREQLLFR
QPSSYFVQFPQAMQRCRDHMIRSLQSVGLKPIIPQGSYFLITDISDFKRKMPDLPGAVDE
PYDRRFVKWMIKNKGLVAIPVSIFYSVPHQKHFDHYIRFCFVKDEATLQAMDEKLRKWKV
EL
Enzyme 32 Number of Residues 422
Enzyme 32 Molecular Weight 47874.8
Enzyme 32 Theoretical pI 6.45
Enzyme 32 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 32 General Function Involved in 1-aminocyclopropane-1-carboxylate synthase activity
Enzyme 32 Specific Function Not Available
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 158255792 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID A8K563 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name A8K563_HUMAN Link Image
Enzyme 32 PDB ID 1W7N Link Image
Enzyme 32 PDB File Show
Enzyme 32 3D Structure
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >1269 bp
ATGGCCAAACAGCTGCAGGCCCGAAGGCTAGACGGGATCGACTACAACCCCTGGGTGGAG
TTTGTGAAACTGGCCAGTGAGCATGACGTCGTGAACTTGGGCCAGGGCTTCCCGGATTTC
CCACCACCAGACTTTGCCGTGGAAGCCTTTCAGCACGCTGTCAGTGGAGACTTTATGCTT
AACCAGTACACCAAGACATTTGGTTACCCACCACTGACGAAGATCCTGGCAAGTTTCTTT
GGGGAGCTGCTGGGTCAGGAGATAGACCCGCTCAGGAATGTGCTGGTGACTGTTGGTGGC
TATGGGGCCCTGTTCACAGCCTTCCAGGCCCTGGTGGACGAAGGAGACGAGGTCATCATC
ATCGAACCCTTTTTTGACTGCTACGAGCCCATGACAATGATGGCAGGGGGTCGTCCTGTG
TTTGTGTCCCTGAAGCCGGGTCCCATCCAGAATGGAGAACTGGGTTCCAGCAGCAACTGG
CAGCTGGACCCCATGGAGCTGGCCGGCAAATTCACATCACGCACCAAAGCCCTGGTCCTC
AACACCCCCAACAACCCCCTGGGCAAGGTGTTCTCCAGGGAAGAGCTGGAGCTGGTGGCC
AGCCTTTGCCAGCAGCATGACGTGGTGTGTATCACTGATGAAGTCTACCAGTGGATGGTC
TACGACGGGCACCAGCACATCAGCATTGCCAGCCTCCCTGGCATGTGGGAACGGACCCTG
ACCATCGGCAGCGCCGGCAAGACCTTCAGCGCCACTGGCTGGAAGGTGGGCTGGGTCCTG
GGTCCAGATCACATCATGAAGCACCTGCGGACCGTGCACCAGAACTCCGTCTTCCACTGC
CCCACGCAGAGCCAGGCTGCAGTAGCCGAGAGCTTTGAACGGGAGCAGCTGCTCTTCCGC
CAACCCAGCAGCTACTTTGTGCAGTTCCCGCAGGCCATGCAGCGCTGCCGTGACCACATG
ATACGTAGCCTACAGTCAGTGGGCCTGAAGCCCATCATCCCTCAGGGCAGCTACTTCCTC
ATCACAGACATCTCAGACTTCAAGAGGAAGATGCCTGACTTGCCTGGAGCTGTGGATGAG
CCCTATGACAGACGCTTCGTCAAGTGGATGATCAAGAACAAGGGCTTGGTGGCCATCCCT
GTCTCCATCTTCTATAGTGTGCCACATCAGAAGCACTTTGACCACTATATCCGCTTCTGT
TTTGTGAAGGATGAAGCCACGCTCCAGGCCATGGACGAGAAGCTGCGGAAGTGGAAGGTG
GAACTCTAG
Enzyme 32 GenBank Gene ID AK291178 Link Image
Enzyme 32 GeneCard ID CCBL1 Link Image
Enzyme 32 GenAtlas ID CCBL1 Link Image
Enzyme 32 HGNC ID HGNC:1564 Link Image
Enzyme 32 Chromosome Location 9
Enzyme 32 Locus 9q34.11
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References Not Available
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 16463
Enzyme 33 Name cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
Enzyme 33 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 33 Gene Name CTPS2
Enzyme 33 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 33 Number of Residues 586
Enzyme 33 Molecular Weight 65678
Enzyme 33 Theoretical pI 6.91
Enzyme 33 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 33 General Function Nucleotide transport and metabolism
Enzyme 33 Specific Function Not Available
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571] ALL_REAC R00571
  • (other) R00573
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein Not Available
Enzyme 33 UniProtKB/Swiss-Prot ID B3KWM2 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name B3KWM2_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence Not Available
Enzyme 33 GenBank Gene ID AK125332 Link Image
Enzyme 33 GeneCard ID B3KWM2 Link Image
Enzyme 33 GenAtlas ID Not Available
Enzyme 33 HGNC ID Not Available
Enzyme 33 Chromosome Location Not Available
Enzyme 33 Locus Not Available
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References Not Available
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 16912
Enzyme 34 Name Glutamyl-tRNA(Gln) amidotransferase subunit A homolog
Enzyme 34 Synonyms
  1. Glutaminyl-tRNA synthase-like protein 1
Enzyme 34 Gene Name QRSL1
Enzyme 34 Protein Sequence >Glutamyl-tRNA(Gln) amidotransferase subunit A homolog
MLGRSLREVSAALKQGQITPTELCQKCLSLIKKTKFLNAYITVSEEVALKQAEESEKRYK
NGQSLGDLDGIPIAVKDNFSTSGIETTCASNMLKGYIPPYNATVVQKLLDQGALLMGKTN
LDEFAMGSGSTDGVFGPVKNPWSYSKQYREKRKQNPHSENEDSDWLITGGSSGGSAAAVS
AFTCYAALGSDTGGSTRNPAAHCGLVGFKPSYGLVSRHGLIPLVNSMDVPGILTRCVDDA
AIVLGALAGPDPRDSTTVHEPINKPFMLPSLADVSKLCIGIPKEYLVPELSSEVQSLWSK
AADLFESEGAKVIEVSLPHTSYSIVCYHVLCTSEVASNMARFDGLQYGHRCDIDVSTEAM
YAATRREGFNDVVRGRILSGNFFLLKENYENYFVKAQKVRRLIANDFVNAFNSGVDVLLT
PTTLSEAVPYLEFIKEDNRTRSAQDDIFTQAVNMAGLPAVSIPVALSNQGLPIGLQFIGR
AFCDQQLLTVAKWFEKQVQFPVIQLQELMDDCSAVLENEKLASVSLKQ
Enzyme 34 Number of Residues 528
Enzyme 34 Molecular Weight 57459.9
Enzyme 34 Theoretical pI 5.37
Enzyme 34 GO Classification
Function
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • translation
Component
Enzyme 34 General Function Involved in carbon-nitrogen ligase activity, with glutamine as amido-N-donor
Enzyme 34 Specific Function ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 7023375 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q9H0R6 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name QRSL1_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1587 bp
ATGCTGGGCCGGAGCCTCCGAGAAGTTTCTGCGGCACTGAAACAAGGCCAAATTACACCA
ACAGAGCTCTGTCAAAAATGTCTCTCTCTTATCAAGAAGACCAAGTTTCTAAATGCCTAC
ATTACTGTGTCAGAAGAGGTGGCCTTAAAACAAGCTGAAGAATCAGAAAAGAGATATAAG
AATGGACAGTCACTTGGGGATTTAGATGGAATTCCTATTGCAGTAAAAGACAATTTCAGC
ACTTCTGGCATTGAGACAACATGTGCATCAAATATGCTGAAAGGTTATATACCACCTTAT
AATGCTACAGTAGTTCAGAAGTTGTTGGATCAGGGAGCTCTACTAATGGGAAAAACAAAT
TTAGATGAGTTTGCTATGGGATCTGGGAGCACAGATGGTGTATTTGGACCAGTTAAAAAC
CCCTGGAGTTATTCAAAACAATATAGAGAAAAGAGGAAGCAGAATCCCCACAGCGAGAAT
GAAGATTCAGACTGGCTGATAACTGGAGGAAGCTCAGGTGGGAGTGCAGCTGCTGTATCG
GCGTTCACATGCTACGCGGCTTTAGGATCAGATACAGGAGGATCGACCAGAAATCCTGCT
GCCCACTGTGGGCTTGTTGGTTTCAAACCAAGCTATGGCTTAGTTTCCCGTCATGGTCTC
ATTCCCCTGGTGAATTCGATGGATGTGCCAGGAATCTTAACCAGATGTGTGGATGATGCA
GCAATTGTGTTGGGTGCACTGGCCGGACCTGACCCCAGGGACTCTACCACAGTACATGAA
CCTATTAATAAACCATTCATGCTTCCCAGTTTGGCAGATGTGAGCAAACTATGTATAGGA
ATTCCAAAGGAATATCTTGTACCGGAATTATCAAGTGAAGTACAGTCTCTTTGGTCCAAA
GCTGCTGACCTCTTTGAGTCTGAGGGGGCCAAAGTAATTGAAGTATCCCTTCCTCACACC
AGTTATTCAATTGTCTGCTACCATGTATTGTGCACATCAGAAGTGGCATCGAATATGGCA
AGATTTGATGGGCTACAATATGGTCACAGATGTGACATTGATGTGTCCACTGAAGCCATG
TATGCTGCAACCAGACGAGAAGGGTTTAATGATGTGGTGAGAGGAAGAATTCTCTCAGGA
AACTTTTTCTTATTAAAAGAAAACTATGAAAATTATTTTGTCAAAGCACAGAAAGTGAGA
CGCCTCATTGCTAATGACTTTGTAAATGCTTTTAACTCTGGAGTAGATGTCTTGCTAACT
CCCACCACCTTGAGTGAGGCAGTACCATACTTGGAGTTCATCAAAGAGGACAACAGAACC
CGAAGTGCCCAGGATGATATTTTTACACAAGCTGTAAATATGGCAGGATTGCCAGCAGTG
AGTATCCCTGTTGCACTCTCAAACCAAGGGTTGCCAATAGGACTGCAGTTTATTGGACGT
GCGTTTTGTGACCAGCAGCTTCTTACAGTAGCCAAATGGTTTGAAAAACAAGTACAGTTT
CCTGTTATTCAACTTCAAGAACTCATGGATGATTGTTCAGCAGTCCTTGAAAATGAAAAG
TTAGCCTCTGTCTCTCTAAAACAGTAA
Enzyme 34 GenBank Gene ID AK001851 Link Image
Enzyme 34 GeneCard ID QRSL1 Link Image
Enzyme 34 GenAtlas ID QRSL1 Link Image
Enzyme 34 HGNC ID HGNC:21020 Link Image
Enzyme 34 Chromosome Location 6
Enzyme 34 Locus 6q21
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  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]
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Enzyme 34 Metabolite References Not Available