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Human Metabolome Database Version 2.5

 

Showing metabocard for Urea (HMDB00294)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-01-20 11:11:52
Accession Number HMDB00294
Secondary Accession Numbers Not Available
Common Name Urea
Description Urea is a highly soluble organic compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids. Urea is formed in a cyclic pathway known simply as the urea cycle. In this cycle, amino groups donated by ammonia and L-aspartate are converted to urea. Urea is essentially a waste product; it has no physiological function. It is dissolved in blood (in humans in a concentration of 2.5 - 7.5 mmol/liter) and excreted by the kidney in the urine. In addition, a small amount of urea is excreted (along with sodium chloride and water) in human sweat.
Synonyms
  1. Carbonyl diamine
  2. Ureacin-40 Creme
  3. Hyanit
  4. Carmol
  5. Superprill
  6. Bubber shet
  7. Uremol 20 Cream 20%
  8. Simply botanical sensations healing hands
  9. Onychomal
  10. Pylori-chek breath test
  11. Dermal therapy-finger care
  12. Urederm Cream 10%
  13. Dermaflex Crm 10%
  14. Carbonyldiamide
  15. Urisec Lotion 12%
  16. Pastaron
  17. Urea-13C
  18. Ureophil
  19. Carbamimidic acid
  20. Caswell No. 902
  21. Urea perhydrate
  22. Urea
  23. Isourea
  24. Urepeal
  25. Pseudourea
  26. Ureaphil
  27. Urea solution
  28. Dermal therapy-heel care
  29. Dermaflex 20 Urea Cream 20%
  30. Uremol 10 Cream 10%
  31. Polyurea
  32. Keratinamin
  33. Aquacare HP
  34. Optigen 1200
  35. Urea homopolymer
  36. Mocovina [czech]
  37. URE
  38. Pastaron 20 soft
  39. Eucerin Lotion 10% D'uree
  40. Carbaderm
  41. Carbamex 330mgms
  42. Helicosol
  43. Calmurid HC
  44. Keratinamin kowa
  45. Bromisovalum
  46. Panafil
  47. Ultra Mide 25
  48. Murine ear wax removal system/murine ear drops
  49. Aqua care
  50. Carbamide resin
  51. Urepearl
  52. Urevert
  53. Elaqua XX
  54. Carbamimic acid
  55. ARF
  56. Breathtek ubt for h-pylori
  57. Uree 20 Cream
  58. Urepeal l
  59. Pastaron (TN)
  60. Dermal therapy-hand elbow and knee cream
  61. Pastaron 20
  62. Ureacin-20
  63. Pastaron soft
  64. B-I-k
  65. U-cort
  66. Carmol HC
  67. Urea (JP15/USP)
  68. Urisec 22% Crm
  69. Pastaron 10
  70. Nutraplus
  71. Urea ammonium nitrate solution
  72. Calmurid
  73. Alphadrate
  74. Carmol 40
  75. Carbamide
  76. Lotion
  77. Harnstoff [german]
  78. Varioform II
  79. Mocovina
  80. Carbonyl diamide
  81. Carbonyldiamine
  82. Supercel 3000
  83. Rubinol ST 010
  84. Harnstoff
  85. Uremol 10 Lotion 10%
  86. Aqua care HP
  87. Ultra mide
  88. Ureacin-10 lotion
  89. Prespersion 75 urea
  90. beta-I-k
Chemical IUPAC Name Urea
Chemical Formula CH4N2O
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Ketones and Aldehydes
Class
  • Amino Ketones
Sub Class
  • Miscellaneous amino ketones
Family
  • Mammalian Metabolite
Species
  • urea
Biofunction
  • Component of Arginine and proline metabolism
Application
Source
  • Endogenous
Average Molecular Weight 60.055
Monoisotopic Molecular Weight 60.032364
Isomeric SMILES NC(N)=O
Canonical SMILES NC(N)=O
KEGG Compound ID C00086 Link Image
BioCyc ID UREA Link Image
BiGG ID 33799 Link Image
Wikipedia Link Urea Link Image
NuGOwiki Link HMDB00294 Link Image
Metagene Link HMDB00294 Link Image
METLIN ID 6 Link Image
PubChem Compound 1176 Link Image
PubChem Substance 841412 Link Image
ChEBI ID 16199 Link Image
CAS Registry Number 57-13-6
InChI Identifier InChI=1/CH4N2O/c2-1(3)4/h(H4,2,3,4)
Synthesis Reference Leuthardt, F.; Glasson, B. Biological synthesis of urea. Verhandl. Ver. schweiz. Physiol. (1942), 21 25-7.
Melting Point (Experimental) 132 oC
Experimental Water Solubility 545.0 mg/mL [YALKOWSKY,SH (1989)] Source: PhysProp
Predicted Water Solubility 412.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -2.11 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -1.78 [Predicted by ALOGPS]; -1.7 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1BV3 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum

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 Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
  • Cellular Cytoplasm
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Kidney
Liver
Skin
Concentrations (Normal)
Biofluid Blood
Value 6500.0 (4000.0-9000.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Klassen P, Furst P, Schulz C, Mazariegos M, Solomons NW: Plasma free amino acid concentrations in healthy Guatemalan adults and in patients with classic dengue. Am J Clin Nutr. 2001 Mar;73(3):647-52. [PubMed Link Image]
Biofluid Blood
Value 4530.0 (2590.0 - 6470.0) uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 90. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 4010.0 +/- 920.0 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 90. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 3600.0 (2680.0 - 4780.0) uM
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 90. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 5210.0 (4310.0 - 6780.0) uM
Age Children:1-13 yrs old
Sex N/A
Patient information Normal
Comments Children (1-6 years)
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 90. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Cellular Cytoplasm
Value 3860 (1900 - 5820) uM
Age Adult:>18 yrs old
Sex Male
Patient information Erythrocytes
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 90. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Cellular Cytoplasm
Value 2960 +/- 1000 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 90. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 4160.0 (2300.0-6060.0) 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 3820.0 (0.0-7640.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Lewis MJ, Morrissey JA, Flegel MD, Jeroncic K, Xiong Y, Cheng D, Eisner R, Gautam B, Tzur D, Sawhney S, Bamforth F, Greiner R, Li L: The human cerebrospinal fluid metabolome. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Aug 15;871(2):164-173. Epub 2008 May 8. [PubMed Link Image]
Biofluid Urine
Value 29.6 (6.579-52.6) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value 22566.0 +/- 4407.0 umol/mmol creatinine
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 Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 171680 +/- 8032 uM
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 3500.0 +/- 1500.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Cirrhosis
Comments Not Available
References
  • Marescau B, De Deyn PP, Holvoet J, Possemiers I, Nagels G, Saxena V, Mahler C: Guanidino compounds in serum and urine of cirrhotic patients. Metabolism. 1995 May;44(5):584-8. [PubMed Link Image]
Biofluid CSF
Value 1800.0 (1500.0-2100.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Tuberculous meningitis
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 2150.0 (1850.0-2450.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Meningitis
Comments Bacterial
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]
Associated Disorders
Condition References
Cirrhosis
  • Marescau B, De Deyn PP, Holvoet J, Possemiers I, Nagels G, Saxena V, Mahler C: Guanidino compounds in serum and urine of cirrhotic patients. Metabolism. 1995 May;44(5):584-8. [PubMed Link Image]
Meningitis
  • 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]
Tuberculous meningitis
  • 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]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Arginine and Proline Metabolism SMP00020 Link Image map00330 Link Image
Urea Cycle SMP00059 Link Image map00330 Link Image
General References
  1. Georges J: Determination of ammonia and urea in urine and of urea in blood by use of an ammonia-selective electrode. Clin Chem. 1979 Nov;25(11):1888-90. [PubMed Link Image]
  2. Vaidya VS, Bonventre JV: Mechanistic biomarkers for cytotoxic acute kidney injury. Expert Opin Drug Metab Toxicol. 2006 Oct;2(5):697-713. [PubMed Link Image]
  3. 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]
  4. Deja M, Hildebrandt B, Ahlers O, Riess H, Wust P, Gerlach H, Kerner T: Goal-directed therapy of cardiac preload in induced whole-body hyperthermia. Chest. 2005 Aug;128(2):580-6. [PubMed Link Image]
  5. Nandan RK, Sivapathasundharam B, Sivakumar G: Oral manifestations and analysis of salivary and blood urea levels of patients under going haemo dialysis and kidney transplant. Indian J Dent Res. 2005 Jul-Sep;16(3):77-82. [PubMed Link Image]
  6. Zocco MA, Di Campli C, Gaspari R, Candelli M, Nista EC, Zileri Dal Verme L, Di Gioacchino G, Santoliquido A, Flore R, Tondi P, Proietti R, Pola P, Gasbarrini G, Gasbarrini A: Improvement of mitochondrial function evaluated by ketoisocaproic acid breath test in patients with HCV infection undergoing albumin dialysis. Transplant Proc. 2005 Jul-Aug;37(6):2554-6. [PubMed Link Image]
  7. Kohnle M, Pietruck F, Kribben A, Philipp T, Heemann U, Witzke O: Ezetimibe for the treatment of uncontrolled hypercholesterolemia in patients with high-dose statin therapy after renal transplantation. Am J Transplant. 2006 Jan;6(1):205-8. [PubMed Link Image]
  8. Malyszko J, Malyszko J, Wolczynski S, Mysliwiec M: Adiponectin, leptin and thyroid hormones in patients with chronic renal failure and on renal replacement therapy: are they related? Nephrol Dial Transplant. 2006 Jan;21(1):145-52. Epub 2005 Sep 2. [PubMed Link Image]
  9. Miller TR, Anderson RJ, Linas SL, Henrich WL, Berns AS, Gabow PA, Schrier RW: Urinary diagnostic indices in acute renal failure: a prospective study. Ann Intern Med. 1978 Jul;89(1):47-50. [PubMed Link Image]
  10. Final report of the safety assessment of Urea. Int J Toxicol. 2005;24 Suppl 3:1-56. [PubMed Link Image]
  11. Klassen P, Furst P, Schulz C, Mazariegos M, Solomons NW: Plasma free amino acid concentrations in healthy Guatemalan adults and in patients with classic dengue. Am J Clin Nutr. 2001 Mar;73(3):647-52. [PubMed Link Image]
  12. Miles L, Heubi JE, Bove KE: Hepatocyte glycogen accumulation in patients undergoing dietary management of urea cycle defects mimics storage disease. J Pediatr Gastroenterol Nutr. 2005 Apr;40(4):471-6. [PubMed Link Image]
  13. Hobbs JR: Monitoring myelomatosis. Arch Intern Med. 1975 Jan;135(1):125-30. [PubMed Link Image]
  14. Racz I, Soos G, Jakab E: [Water content of the skin following salicylic acid and urea treatment] Hautarzt. 1989;40 Suppl 9:61-2. [PubMed Link Image]
  15. Younes H, Alphonse JC, Deteix R: [Role of dietary fibers in the nutritional management of chronic renal failure] Nephrologie. 2004;25(7):283-5. [PubMed Link Image]
  16. Roszczenko A, Galazyn-Sidorczuk M, Brzoska MM, Moniuszko-Jakoniuk J, Zwierz K: [Select parameters of renal function in smokers in correlation with the exposure to cadmium] Przegl Lek. 2004;61(4):348-50. [PubMed Link Image]
  17. Gowda GA, Somashekar BS, Ijare OB, Sharma A, Kapoor VK, Khetrapal CL: One-step analysis of major bile components in human bile using 1H NMR spectroscopy. Lipids. 2006 Jun;41(6):577-89. [PubMed Link Image]
  18. Kurekci AE, Atay AA, Sarici SU, Yesilkaya E, Senses Z, Okutan V, Ozcan O: Is there a relationship between childhood Helicobacter pylori infection and iron deficiency anemia? J Trop Pediatr. 2005 Jun;51(3):166-9. Epub 2005 Apr 26. [PubMed Link Image]
  19. Fostel J, Boneva R, Lloyd A: Exploration of the gene expression correlates of chronic unexplained fatigue using factor analysis. Pharmacogenomics. 2006 Apr;7(3):441-54. [PubMed Link Image]
  20. Wikipedia Link Image
Metabolic Enzymes
  1. Arginase-1
  2. Arginase-2, mitochondrial precursor
  3. Urea transporter, kidney
  4. Agmatinase, mitochondrial precursor
  5. Urea transporter, erythrocyte
  6. G-protein coupled receptor family C group 6 member A precursor
  7. Probable allantoicase
  8. cDNA, FLJ92843, Homo sapiens arginase, type II (ARG2), nuclear gene encodingmitochondrial protein, mRNA (Arginase, type II, isoform CRA_a)
  9. cDNA FLJ60951, highly similar to Probable allantoicase (Allantoicase, isoform CRA_a)
  10. HERV-K_5q33.3 provirus ancestral Pro protein
  11. Urea transporter JK glycoprotein
  12. Blood group Kidd urea transporter
Enzyme 1 [top]
Enzyme 1 ID 5533
Enzyme 1 Name Arginase-1
Enzyme 1 Synonyms
  1. Type I arginase
  2. Liver-type arginase
Enzyme 1 Gene Name ARG1
Enzyme 1 Protein Sequence >Arginase-1
MSAKSRTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPN
DSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGV
IWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVPGFSWVTPCISAKDIVYIGLR
DVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSF
TPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAIT
LACFGLAREGNHKPIDYLNPPK
Enzyme 1 Number of Residues 322
Enzyme 1 Molecular Weight 34735
Enzyme 1 Theoretical pI 7.25
Enzyme 1 GO Classification
Function
  • arginase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
Process
  • arginine catabolism
  • arginine metabolism
  • metabolism
  • physiological process
  • urea cycle intermediate metabolism
Component
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function L-arginine + H(2)O = L-ornithine + urea
Enzyme 1 Pathways
Enzyme 1 Reactions
  • L-arginine + H2O = L-ornithine + urea
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 178995 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P05089 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ARGI1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >969 bp
ATGAGCGCCAAGTCCAGAACCATAGGGATTATTGGAGCTCCTTTCTCAAAGGGACAGCCA
CGAGGAGGGGTGGAAGAAGGCCCTACAGTATTGAGAAAGGCTGGTCTGCTTGAGAAACTT
AAAGAACAAGAGTGTGATGTGAAGGATTATGGGGACCTGCCCTTTGCTGACATCCCTAAT
GACAGTCCCTTTCAAATTGTGAAGAATCCAAGGTCTGTGGGAAAAGCAAGCGAGCAGCTG
GCTGGCAAGGTGGCACAAGTCAAGAAGAACGGAAGAATCAGCCTGGTGCTGGGCGGAGAC
CACAGTTTGGCAATTGGAAGCATCTCTGGCCATGCCAGGGTCCACCCTGATCTTGGAGTC
ATCTGGGTGGATGCTCACACTGATATCAACACTCCACTGACAACCACAAGTGGAAACTTG
CATGGACAACCTGTATCTTTCCTCCTGAAGGAACTAAAAGGAAAGATTCCCGATGTGCCA
GGATTCTCCTGGGTGACTCCCTGTATATCTGCCAAGGATATTGTGTATATTGGCTTGAGA
GACGTGGACCCTGGGGAACACTACATTTTGAAAACTCTAGGCATTAAATACTTTTCAATG
ACTGAAGTGGACAGACTAGGAATTGGCAAGGTGATGGAAGAAACACTCAGCTATCTACTA
GGAAGAAAGAAAAGGCCAATTCATCTAAGTTTTGATGTTGACGGACTGGACCCATCTTTC
ACACCAGCTACTGGCACACCAGTCGTGGGAGGTCTGACATACAGAGAAGGTCTCTACATC
ACAGAAGAAATCTACAAAACAGGGCTACTCTCAGGATTAGATATAATGGAAGTGAACCCA
TCCCTGGGGAAGACACCAGAAGAAGTAACTCGAACAGTGAACACAGCAGTTGCAATAACC
TTGGCTTGTTTCGGACTTGCTCGGGAGGGTAATCACAAGCCTATTGACTACCTTAACCCA
CCTAAGTAA
Enzyme 1 GenBank Gene ID M14502 Link Image
Enzyme 1 GeneCard ID ARG1 Link Image
Enzyme 1 GenAtlas ID ARG1 Link Image
Enzyme 1 HGNC ID HGNC:663 Link Image
Enzyme 1 Chromosome Location 6
Enzyme 1 Locus 6q23
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Haraguchi Y, Takiguchi M, Amaya Y, Kawamoto S, Matsuda I, Mori M: Molecular cloning and nucleotide sequence of cDNA for human liver arginase. Proc Natl Acad Sci U S A. 1987 Jan;84(2):412-5. [PubMed Link Image]
  2. Takiguchi M, Haraguchi Y, Mori M: Human liver-type arginase gene: structure of the gene and analysis of the promoter region. Nucleic Acids Res. 1988 Sep 26;16(18):8789-802. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Ikemoto M, Tabata M, Miyake T, Kono T, Mori M, Totani M, Murachi T: Expression of human liver arginase in Escherichia coli. Purification and properties of the product. Biochem J. 1990 Sep 15;270(3):697-703. [PubMed Link Image]
  5. Uchino T, Haraguchi Y, Aparicio JM, Mizutani N, Higashikawa M, Naitoh H, Mori M, Matsuda I: Three novel mutations in the liver-type arginase gene in three unrelated Japanese patients with argininemia. Am J Hum Genet. 1992 Dec;51(6):1406-12. [PubMed Link Image]
  6. Grody WW, Klein D, Dodson AE, Kern RM, Wissmann PB, Goodman BK, Bassand P, Marescau B, Kang SS, Leonard JV, et al.: Molecular genetic study of human arginase deficiency. Am J Hum Genet. 1992 Jun;50(6):1281-90. [PubMed Link Image]
  7. Uchino T, Snyderman SE, Lambert M, Qureshi IA, Shapira SK, Sansaricq C, Smit LM, Jakobs C, Matsuda I: Molecular basis of phenotypic variation in patients with argininemia. Hum Genet. 1995 Sep;96(3):255-60. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6323
Enzyme 2 Name Arginase-2, mitochondrial precursor
Enzyme 2 Synonyms
  1. Arginase II
  2. Non- hepatic arginase
  3. Kidney-type arginase
Enzyme 2 Gene Name ARG2
Enzyme 2 Protein Sequence >Arginase-2, mitochondrial precursor
MSLRGSLSRLLQTRVHSILKKSVHSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSS
LGCHLKDFGDLSFTPVPKDDLYNNLIVNPRSVGLANQELAEVVSRAVSDGYSCVTLGGDH
SLAIGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVSFLLRELQDKVPQLPG
FSWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDIDRLGIQKVMERTFDLLIG
KRQRPIHLSFDIDAFDPTLAPATGTPVVGGLTYREGMYIAEEIHNTGLLSALDLVEVNPQ
LATSEEEAKTTANLAVDVIASSFGQTREGGHIVYDQLPTPSSPDESENQARVRI
Enzyme 2 Number of Residues 354
Enzyme 2 Molecular Weight 38578
Enzyme 2 Theoretical pI 6.45
Enzyme 2 GO Classification
Function
  • arginase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
Process
  • arginine catabolism
  • arginine metabolism
  • metabolism
  • physiological process
  • urea cycle intermediate metabolism
Component
Enzyme 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to NO synthase. Since NO synthase is found in the penile corpus cavernosum smooth muscle, the clitoral corpus cavernosum and the vagina, arginase II plays a role in both male and female sexual arousal. It is therefore a potential target for the treatment of male and female sexual arousal disorders
Enzyme 2 Pathways
Enzyme 2 Reactions
  • L-arginine + H2O = L-ornithine + urea
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 1694633 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P78540 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ARGI2_HUMAN Link Image
Enzyme 2 PDB ID 1PQ3 Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1065 bp
ATGTCCCTAAGGGGCAGCCTCTCGCGTCTCCTCCAGACGCGAGTGCATTCCATCCTGAAG
AAATCCGTCCACTCCGTGGCTGTGATAGGAGCCCCGTTCTCACAAGGGCAGAAAAGAAAA
GGAGTGGAGCATGGTCCCGCTGCCATAAGAGAAGCTGGCTTGATGAAAAGGCTCTCCAGT
TTGGGCTGCCACCTAAAAGACTTTGGAGATTTGAGTTTTACTCCAGTCCCCAAAGATGAT
CTCTACAACAACCTGATAGTGAATCCACGCTCAGTGGGTCTTGCCAACCAGGAACTGGCT
GAGGTGGTTAGCAGAGCTGTGTCAGATGGCTACAGCTGTGTCACACTGGGAGGAGACCAC
AGCCTGGCAATCGGTACCATTAGTGGCCATGCCCGACACTGCCCAGACCTTTGTGTTGTC
TGGGTTGATGCCCATGCTGACATCAACACACCCCTTACCACTTCATCAGGAAATCTCCAT
GGACAGCCAGTTTCATTTCTCCTCAGAGAACTACAGGATAAGGTACCACAACTCCCAGGA
TTTTCCTGGATCAAACCTTGTATCTCTTCTGCAAGTATTGTGTATATTGGTCTGAGAGAC
GTGGACCCTCCTGAACATTTTATTTTAAAGAACTATGATATCCAGTATTTTTCCATGAGA
GATATTGATCGACTTGGTATCCAGAAGGTCATGGAACGAACATTTGATCTGCTGATTGGC
AAGAGACAAAGACCAATCCATTTGAGTTTTGATATTGATGCATTTGACCCTACACTGGCT
CCAGCCACAGGAACTCCTGTTGTCGGGGGACTAACCTATCGAGAAGGCATGTATATTGCT
GAGGAAATACACAATACAGGGTTGCTATCAGCACTGGATCTTGTTGAAGTCAATCCTCAG
TTGGCCACCTCAGAGGAAGAGGCGAAGACTACAGCTAACCTGGCAGTAGATGTGATTGCT
TCAAGCTTTGGTCAGACAAGAGAAGGAGGGCATATTGTCTATGACCAACTTCCTACTCCC
AGTTCACCAGATGAATCAGAAAATCAAGCACGTGTGAGAATTTAG
Enzyme 2 GenBank Gene ID D86724 Link Image
Enzyme 2 GeneCard ID ARG2 Link Image
Enzyme 2 GenAtlas ID ARG2 Link Image
Enzyme 2 HGNC ID HGNC:664 Link Image
Enzyme 2 Chromosome Location 14
Enzyme 2 Locus 14q24.1-q24.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Gotoh T, Sonoki T, Nagasaki A, Terada K, Takiguchi M, Mori M: Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase II) and comparison of its induction with nitric oxide synthase in a murine macrophage-like cell line. FEBS Lett. 1996 Oct 21;395(2-3):119-22. [PubMed Link Image]
  2. Vockley JG, Jenkinson CP, Shukla H, Kern RM, Grody WW, Cederbaum SD: Cloning and characterization of the human type II arginase gene. Genomics. 1996 Dec 1;38(2):118-23. [PubMed Link Image]
  3. Morris SM Jr, Bhamidipati D, Kepka-Lenhart D: Human type II arginase: sequence analysis and tissue-specific expression. Gene. 1997 Jul 9;193(2):157-61. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 8017
Enzyme 3 Name Urea transporter, kidney
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name SLC14A2
Enzyme 3 Protein Sequence >Urea transporter, kidney
MEESSEIKVETNISKTSWIRSSMAASGKRVSKALSYITGEMKECGEGLKDKSPVFQFFDW
VLRGTSQVMFVNNPLSGILIILGLFIQNPWWAISGCLGTIMSTLTALILSQDKSAIAAGF
HGYNGVLVGLLMAVFSDKGDYYWWLLLPVIIMSMSCPILSSALGTIFSKWDLPVFTLPFN
ITVTLYLAATGHYNLFFPTTLLQPASAMPNITWSEVQVPLLLRAIPVGIGQVYGCDNPWT
GGIFLIALFISSPLICLHAAIGSTMGMLAALTIATPFDSIYFGLCGFNSTLACIAIGGMF
YVITWQTHLLAIACALFAAYLGAALANMLSVFGLPPCTWPFCLSALTFLLLTTNNPAIYK
LPLSKVTYPEANRIYYLSQERNRRASIITKYQAYDVS
Enzyme 3 Number of Residues 397
Enzyme 3 Molecular Weight 43396
Enzyme 3 Theoretical pI 7.87
Enzyme 3 GO Classification
Function
  • amine transporter activity
  • transporter activity
  • urea transporter activity
Process
  • amine transport
  • cellular physiological process
  • physiological process
  • transport
  • urea transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Specialized low-affinity urea transporter. Mediates urea transport in kidney
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 68-85 92-109 115-135 143-163 172-192 239-257 264-280 287-303 309-329 331-351
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1483516 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q15849 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name UT2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1194 bp
ATGGAGGAGAGCTCTGAGATAAAAGTGGAAACAAACATTTCCAAGACATCCTGGATTCGG
AGTTCCATGGCTGCCAGTGGGAAAAGGGTCAGCAAAGCCCTCAGCTACATCACAGGAGAG
ATGAAGGAGTGTGGAGAGGGACTTAAAGACAAGTCCCCAGTGTTCCAGTTCTTTGACTGG
GTCCTCCGAGGCACATCTCAAGTGATGTTTGTGAACAACCCCCTCAGCGGCATCCTCATC
ATCCTCGGCCTCTTCATCCAGAACCCCTGGTGGGCGATCTCAGGCTGCCTGGGTACCATC
ATGTCCACCTTGACAGCCCTCATCCTGAGTCAGGACAAGTCGGCCATCGCTGCAGGATTT
CACGGCTACAATGGGGTGCTGGTGGGGCTGCTGATGGCCGTGTTCTCAGACAAAGGTGAC
TACTACTGGTGGCTGTTGCTACCCGTCATCATCATGTCCATGTCTTGCCCCATCCTCTCC
AGTGCCCTGGGTACCATCTTCAGCAAGTGGGACCTCCCAGTCTTCACACTGCCCTTCAAT
ATCACTGTGACTTTGTACCTGGCAGCCACAGGCCACTACAACCTTTTCTTCCCCACAACG
CTGCTGCAGCCTGCATCCGCCATGCCCAACATCACCTGGTCAGAGGTCCAAGTGCCCTTG
CTTTTGAGAGCCATCCCCGTTGGAATTGGCCAAGTGTACGGCTGTGATAACCCCTGGACT
GGAGGCATCTTCCTCATAGCTCTGTTCATATCCTCACCTCTCATTTGCTTGCATGCAGCA
ATTGGATCCACCATGGGGATGCTAGCAGCACTCACTATTGCGACGCCCTTTGACTCCATC
TACTTCGGCCTGTGTGGCTTCAACAGCACCCTCGCATGCATAGCGATAGGAGGCATGTTC
TACGTCATCACCTGGCAGACGCACCTCCTCGCCATCGCCTGCGCACTGTTTGCTGCCTAC
CTGGGTGCTGCCCTGGCTAACATGTTATCTGTGTTTGGATTGCCGCCCTGCACTTGGCCC
TTCTGTCTCTCAGCTCTCACCTTCCTGCTCCTGACGACCAATAACCCCGCCATCTACAAG
CTCCCGCTCAGCAAAGTCACCTACCCAGAGGCCAACCGCATCTACTACCTGTCCCAGGAG
AGAAACAGAAGGGCATCAATCATAACAAAGTATCAAGCCTACGATGTCTCCTAA
Enzyme 3 GenBank Gene ID X96969 Link Image
Enzyme 3 GeneCard ID SLC14A2 Link Image
Enzyme 3 GenAtlas ID SLC14A2 Link Image
Enzyme 3 HGNC ID HGNC:10919 Link Image
Enzyme 3 Chromosome Location 18
Enzyme 3 Locus 18q12.1-q21.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Olives B, Martial S, Mattei MG, Matassi G, Rousselet G, Ripoche P, Cartron JP, Bailly P: Molecular characterization of a new urea transporter in the human kidney. FEBS Lett. 1996 May 20;386(2-3):156-60. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 8199
Enzyme 4 Name Agmatinase, mitochondrial precursor
Enzyme 4 Synonyms
  1. Agmatine ureohydrolase
  2. AUH
Enzyme 4 Gene Name AGMAT
Enzyme 4 Protein Sequence >Agmatinase, mitochondrial precursor
MLRLLASGCARGPGPGVGARPAAGLFHPGRRQSRQASDAPRNQPPSPEFVARPVGVCSMM
RLPVQTSPEGLDAAFIGVPLDTGTSNRPGARFGPRRIREESVMLGTVNPSTGALPFQSLM
VADLGDVNVNLYNLQDSCRRIQEAYEKIVAAGCIPLTLGGDHTITYPILQAMAKKHGPVG
LLHVDAHTDTTDKALGEKLYHGAPFRRCVDEGLLDCKRVVQIGIRGSSTTLDPYRYNRSQ
GFRVVLAEDCWMKSLVPLMGEVRQQMGGKPIYISFDIDALDPAYAPGTGTPEIAGLTPSQ
ALEIIRGCQGLNVMGCDLVEVSPPYDLSGNTALLAANLLFEMLCALPKVTTV
Enzyme 4 Number of Residues 352
Enzyme 4 Molecular Weight 37661
Enzyme 4 Theoretical pI 7.66
Enzyme 4 GO Classification
Function
  • agmatinase activity
  • arginase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
Process
  • amino acid and derivative metabolism
  • amino acid derivative metabolism
  • arginine catabolism
  • arginine metabolism
  • biogenic amine metabolism
  • cellular metabolism
  • metabolism
  • physiological process
  • polyamine biosynthesis
  • polyamine metabolism
  • urea cycle intermediate metabolism
Component
Enzyme 4 General Function Amino acid transport and metabolism
Enzyme 4 Specific Function Agmatine + H(2)O = putrescine + urea
Enzyme 4 Pathways
Enzyme 4 Reactions
  • agmatine + H2O = putrescine + urea
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 18031951 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9BSE5 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SPEB_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1059 bp
ATGCTGAGGCTGCTGGCGTCCGGGTGCGCCCGGGGCCCGGGGCCCGGCGTGGGCGCGCGT
CCTGCCGCAGGGCTCTTTCATCCGGGGCGCCGCCAGAGCCGCCAGGCTTCCGACGCGCCC
CGGAACCAGCCCCCCAGCCCCGAGTTCGTGGCCCGGCCGGTGGGCGTCTGCTCCATGATG
CGCCTGCCGGTGCAGACCTCCCCCGAGGGGCTGGACGCTGCCTTCATCGGGGTGCCCCTG
GATACTGGGACCTCCAACCGGCCTGGGGCGAGATTCGGACCTCGCCGCATCCGGGAAGAA
TCAGTGATGCTTCGGACAGTCAATCCTAGCACGGGGGCCCTCCCCTTCCAGTCCCTCATG
GTTGCAGACCTAGGCGATGTGAATGTCAATCTTTACAACCTTCAGGACAGCTGCCGGCAA
ATTCAAGAGGCCTATGAGAAAATTGTAGCAGCTGGCTGTATTCCTCTGACCTTGGGTGGA
GATCACACAATCACATATCCCATATTGCAAGCGATGGCAAAAAAGCATGGCCCAGTGGGG
CTGCTGCACGTGGATGCGCACACGGACACGACCGACAAGGCCCTAGGAGAGAAGCTCTAC
CACGGGGCGCCCTTCCGCCGGTGTGTGGATGAGGGTCTCCTGGACTGTAAGCGTGTGGTG
CAGATTGGCATCCGGGGCTCTTCCACGACCTTGGATCCCTACAGATACAACCGGAGCCAG
GGCTTCCGGGTAGTCCTGGCTGAAGACTGCTGGATGAAGTCGCTGGTTCCTCTGATGGGG
GAAGTCAGGCAGCAGATGGGAGGCAAACCCATTTATATCAGCTTTGATATTGACGCTCTG
GATCCTGCCTATGCGCCAGGGACAGGGACACCTGAAATTGCTGGTCTCACTCCTAGTCAG
GCTCTGGAGATCATCAGGGGTTGTCAAGGCCTGAACGTGATGGGCTGTGATCTTGTCGAA
GTTTCACCACCGTATGATCTTTCTGGGAACACAGCCCTGCTGGCGGCTAACCTGCTGTTT
GAGATGCTATGTGCTCTCCCCAAAGTGACAACCGTCTGA
Enzyme 4 GenBank Gene ID AY057097 Link Image
Enzyme 4 GeneCard ID AGMAT Link Image
Enzyme 4 GenAtlas ID AGMAT Link Image
Enzyme 4 HGNC ID HGNC:18407 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 1p36.21
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Mistry SK, Burwell TJ, Chambers RM, Rudolph-Owen L, Spaltmann F, Cook WJ, Morris SM Jr: Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus. Am J Physiol Gastrointest Liver Physiol. 2002 Feb;282(2):G375-81. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 8415
Enzyme 5 Name Urea transporter, erythrocyte
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name SLC14A1
Enzyme 5 Protein Sequence >Urea transporter, erythrocyte
MEDSPTMVRVDSPTMVRGENQVSPCQGRRCFPKALGYVTGDMKELANQLKDKPVVLQFID
WILRGISQVVFVNNPVSGILILVGLLVQNPWWALTGWLGTVVSTLMALLLSQDRSLIASG
LYGYNATLVGVLMAVFSDKGDYFWWLLLPVCAMSMTCPIFSSALNSMLSKWDLPVFTLPF
NMALSMYLSATGHYNPFFPAKLVIPITTAPNISWSDLSALELLKSIPVGVGQIYGCDNPW
TGGIFLGAILLSSPLMCLHAAIGSLLGIAAGLSLSAPFEDIYFGLWGFNSSLACIAMGGM
FMALTWQTHLLALGCALFTAYLGVGMANFMAEVGLPACTWPFCLATLLFLIMTTKNSNIY
KMPLSKVTYPEENRIFYLQAKKRMVESPL
Enzyme 5 Number of Residues 389
Enzyme 5 Molecular Weight 42529
Enzyme 5 Theoretical pI 7.19
Enzyme 5 GO Classification
Function
  • amine transporter activity
  • transporter activity
  • urea transporter activity
Process
  • amine transport
  • cellular physiological process
  • physiological process
  • transport
  • urea transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Specialized low-affinity urea transporter. Mediates urea transport in erythrocytes
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 53-73 78-98 116-136 143-163 173-193 243-263 281-301 310-330 333-353
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID Q13336 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name UT1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID L36121 Link Image
Enzyme 5 GeneCard ID SLC14A1 Link Image
Enzyme 5 GenAtlas ID SLC14A1 Link Image
Enzyme 5 HGNC ID HGNC:10918 Link Image
Enzyme 5 Chromosome Location 18
Enzyme 5 Locus 18q11-q12
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Olives B, Neau P, Bailly P, Hediger MA, Rousselet G, Cartron JP, Ripoche P: Cloning and functional expression of a urea transporter from human bone marrow cells. J Biol Chem. 1994 Dec 16;269(50):31649-52. [PubMed Link Image]
  2. Davey S, Beach D: RACH2, a novel human gene that complements a fission yeast cell cycle checkpoint mutation. Mol Biol Cell. 1995 Oct;6(10):1411-21. [PubMed Link Image]
  3. Olives B, Merriman M, Bailly P, Bain S, Barnett A, Todd J, Cartron JP, Merriman T: The molecular basis of the Kidd blood group polymorphism and its lack of association with type 1 diabetes susceptibility. Hum Mol Genet. 1997 Jul;6(7):1017-20. [PubMed Link Image]
  4. Sidoux-Walter F, Lucien N, Olives B, Gobin R, Rousselet G, Kamsteeg EJ, Ripoche P, Deen PM, Cartron JP, Bailly P: At physiological expression levels the Kidd blood group/urea transporter protein is not a water channel. J Biol Chem. 1999 Oct 15;274(42):30228-35. [PubMed Link Image]
  5. Sidoux-Walter F, Lucien N, Nissinen R, Sistonen P, Henry S, Moulds J, Cartron JP, Bailly P: Molecular heterogeneity of the Jk(null) phenotype: expression analysis of the Jk(S291P) mutation found in Finns. Blood. 2000 Aug 15;96(4):1566-73. [PubMed Link Image]
  6. Irshaid NM, Henry SM, Olsson ML: Genomic characterization of the kidd blood group gene:different molecular basis of the Jk(a-b-) phenotype in Polynesians and Finns. Transfusion. 2000 Jan;40(1):69-74. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 13424
Enzyme 6 Name G-protein coupled receptor family C group 6 member A precursor
Enzyme 6 Synonyms
  1. hGPRC6A
  2. G-protein coupled receptor 33
  3. hGPCR33
Enzyme 6 Gene Name GPRC6A
Enzyme 6 Protein Sequence >G-protein coupled receptor family C group 6 member A precursor
MAFLIILITCFVIILATSQPCQTPDDFVAATSPGHIIIGGLFAIHEKMLSSEDSPRRPQI
QECVGFEISVFLQTLAMIHSIEMINNSTLLPGVKLGYEIYDTCTEVTVAMAATLRFLSKF
NCSRETVEFKCDYSSYMPRVKAVIGSGYSEITMAVSRMLNLQLMPQVGYESTAEILSDKI
RFPSFLRTVPSDFHQIKAMAHLIQKSGWNWIGIITTDDDYGRLALNTFIIQAEANNVCIA
FKEVLPAFLSDNTIEVRINRTLKKIILEAQVNVIVVFLRQFHVFDLFNKAIEMNINKMWI
ASDNWSTATKITTIPNVKKIGKVVGFAFRRGNISSFHSFLQNLHLLPSDSHKLLHEYAMH
LSACAYVKDTDLSQCIFNHSQRTLAYKANKAIERNFVMRNDFLWDYAEPGLIHSIQLAVF
ALGYAIRDLCQARDCQNPNAFQPWELLGVLKNVTFTDGWNSFHFDAHGDLNTGYDVVLWK
EINGHMTVTKMAEYDLQNDVFIIPDQETKNEFRNLKQIQSKCSKECSPGQMKKTTRSQHI
CCYECQNCPENHYTNQTDMPHCLLCNNKTHWAPVRSTMCFEKEVEYLNWNDSLAILLLIL
SLLGIIFVLVVGIIFTRNLNTPVVKSSGGLRVCYVILLCHFLNFASTSFFIGEPQDFTCK
TRQTMFGVSFTLCISCILTKSLKILLAFSFDPKLQKFLKCLYRPILIIFTCTGIQVVICT
LWLIFAAPTVEVNVSLPRVIILECEEGSILAFGTMLGYIAILAFICFIFAFKGKYENYNE
AKFITFGMLIYFIAWITFIPIYATTFGKYVPAVEIIVILISNYGILYCTFIPKCYVIICK
QEINTKSAFLKMIYSYSSHSVSSIALSPASLDSMSGNVTMTNPSSSGKSATWQKSKDLQA
QAFAHICRENATSVSKTLPRKRMSSI
Enzyme 6 Number of Residues 926
Enzyme 6 Molecular Weight 104754
Enzyme 6 Theoretical pI 8.00
Enzyme 6 GO Classification
Function
  • G-protein coupled receptor activity
  • metabotropic glutamate, GABA-B-like receptor activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
Component
  • cell
  • membrane
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Receptor that is activated by both amino acids and extracellular concentration of calcium ions. The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. Senses changes in the extracellular concentration of calcium ions, suggesting that it may mediate extracellular calcium-sensing responses in osteoblasts. Osteocalin, stimulates its activity in presence of calcium. Has a lower affinity for calcium than CASR. Also acts as a receptor for amino acids, with a preference for basic amino acids such as L-Lys, L-Arg and L-ornithine. Its affinity for amino acids suggests that it may act as a regulatory component of the urea cycle
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-18
Enzyme 6 Transmembrane Regions
  • 595-615 632-652 670-690 705-725 749-769 783-803 811-831
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 42398178 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q5T6X5 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name GPC6A_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >2781 bp
ATGGCATTCTTAATTATACTAATTACCTGCTTTGTGATTATTCTTGCTACTTCACAGCCT
TGCCAGACCCCTGATGACTTTGTGGCTGCCACTTCTCCGGGACATATCATAATTGGAGGT
TTGTTTGCTATTCATGAAAAAATGTTGTCCTCAGAAGACTCTCCCAGACGACCACAAATC
CAGGAGTGTGTTGGCTTTGAAATATCAGTTTTTCTTCAAACTCTTGCCATGATACACAGC
ATTGAGATGATCAACAATTCAACACTCTTATCTGGAGTCAAACTGGGGTATGAAATCTAT
GACACTTGTACAGAAGTCACAGTGGCAATGGCAGCCACTCTGAGGTTTCTTTCTAAATTC
AACTGCTCCAGAGAAACTGTGGAGTTTAAGTGTGACTATTCCAGCTACATGCCAAGAGTT
AAGGCTGTCATAGGTTCTGGGTACTCAGAAATAACTATGGCTGTCTCCAGGATGTTGAAT
TTACAGCTCATGCCACAGGTGGGTTATGAATCAACTGCAGAAATCCTGAGTGACAAAATT
CGCTTTCCTTCATTTTTACGGACTGTGCCCAGTGACTTCCATCAAATTAAAGCAATGGCT
CACCTGATTCAGAAATCTGGTTGGAACTGGATTGGCATCATAACCACAGATGATGACTAT
GGACGATTGGCTCTTAACACTTTTATAATTCAGGCTGAAGCAAATAACGTGTGCATAGCC
TTCAAAGAGGTTCTTCCAGCCTTTCTTTCAGATAATACCATTGAAGTCAGAATCAATCGG
ACACTGAAGAAAATCATTTTAGAAGCCCAGGTTAATGTCATTGTGGTATTTCTGAGGCAA
TTTCATGTTTTTGATCTCTTCAATAAAGCCATTGAAATGAATATAAATAAGATGTGGATT
GCTAGTGATAATTGGTCAACTGCCACCAAGATTACCACCATTCCTAATGTTAAAAAGATT
GGCAAAGTTGTAGGGTTTGCCTTTAGAAGAGGGAATATATCCTCTTTCCATTCCTTTCTT
CAAAATCTGCACTTGCTTCCCAGTGACAGTCACAAACTCTTACATGAATATGCCATGCAT
TTATCTGCCTGCGCATATGTCAAGGACACTGATTTGAGTCAATGCATATTCAATCATTCT
CAAAGGACTTTGGCCTACAAGGCTAACAAGGCTATAGAAAGGAACTTCGTCATGAGAAAT
GACTTCCTCTGGGACTATGCTGAGCCAGGACTCATTCATAGTATTCAGCTTGCAGTGTTT
GCCCTTGGTTATGCCATTCGGGATCTGTGTCAAGCTCGTGACTGTCAGAACCCCAACGCC
TTTCAACCATGGGAGTTACTTGGTGTGCTAAAAAATGTGACATTCACTGATGGATGGAAT
TCATTTCATTTTGATGCTCATGGGGATTTAAATACTGGATATGATGTTGTGCTCTGGAAG
GAGATCAATGGACACATGACTGTCACTAAGATGGCAGAATATGACCTACAGAATGATGTC
TTCATCATCCCAGATCAGGAAACAAAAAATGAGTTCAGGAATCTTAAGCAAATTCAATCT
AAATGCTCCAAGGAATGCAGTCCTGGGCAAATGAAGAAAACTACAAGAAGTCAACACATC
TGTTGCTATGAATGTCAGAACTGTCCTGAAAATCATTACACTAATCAGACAGATATGCCT
CATTGCCTTTTATGCAACAACAAAACTCACTGGGCCCCTGTTAGGAGCACTATGTGCTTT
GAAAAGGAAGTGGAATATCTCAACTGGAATGACTCCTTGGCCATCCTACTCCTGATTCTC
TCCCTACTGGGAATCATATTTGTTCTGGTTGTTGGCATAATATTTACAAGAAACCTGAAC
ACACCTGTTGTGAAATCATCCGGGGGATTAAGAGTCTGCTATGTGATCCTTCTCTGTCAT
TTCCTCAATTTTGCCAGCACGAGCTTTTTCATTGGAGAACCACAAGACTTCACATGTAAA
ACCAGGCAGACAATGTTTGGAGTGAGCTTTACTCTTTGCATCTCCTGCATTTTGACGAAG
TCTCTGAAAATTTTGCTAGCCTTCAGCTTTGATCCCAAATTACAGAAATTTCTGAAGTGC
CTCTATAGACCGATCCTTATTATCTTCACTTGCACGGGCATCCAGGTTGTCATTTGCACA
CTCTGGCTAATCTTTGCAGCACCTACTGTAGAGGTGAATGTCTCCTTGCCCAGAGTCATC
ATCCTGGAGTGTGAGGAGGGATCCATACTTGCATTTGGCACCATGCTGGGCTACATTGCC
ATCCTGGCCTTCATTTGCTTCATATTTGCTTTCAAAGGCAAATATGAGAATTACAATGAA
GCCAAATTCATTACATTTGGCATGCTCATTTACTTCATAGCTTGGATCACATTCATCCCT
ATCTATGCTACCACATTTGGCAAATATGTACCAGCTGTGGAGATTATTGTCATATTAATA
TCTAACTATGGAATCCTGTATTGCACATTCATCCCCAAATGCTATGTTATTATTTGTAAG
CAAGAGATTAACACAAAGTCTGCCTTTCTCAAGATGATCTACAGTTATTCTTCCCATAGT
GTGAGCAGCATTGCCCTGAGTCCTGCTTCACTGGACTCCATGAGCGGCAATGTCACAATG
ACCAATCCCAGCTCTAGTGGCAAGTCTGCAACCTGGCAGAAAAGCAAAGATCTTCAGGCA
CAAGCATTTGCACACATATGCAGGGAAAATGCCACAAGTGTATCTAAAACTTTGCCTCGA
AAAAGAATGTCAAGTATATGA
Enzyme 6 GenBank Gene ID AY435125 Link Image
Enzyme 6 GeneCard ID Q5T6X5 Link Image
Enzyme 6 GenAtlas ID GPRC6A Link Image
Enzyme 6 HGNC ID HGNC:18510 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. 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]
  2. Takeda S, Kadowaki S, Haga T, Takaesu H, Mitaku S: Identification of G protein-coupled receptor genes from the human genome sequence. FEBS Lett. 2002 Jun 5;520(1-3):97-101. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 14907
Enzyme 7 Name Probable allantoicase
Enzyme 7 Synonyms
  1. Allantoate amidinohydrolase
Enzyme 7 Gene Name ALLC
Enzyme 7 Protein Sequence >Probable allantoicase
MADAPKEGRLTRFLDFTQLMDMASESVGGKILFATDDFFAPAENLIKSDSPCFKEHEYTE
FGKWMDGWETRRKRIPGHDWCVLRLGIQGVIRGFDVDVSYFTGDYAPRVSIQAANLEEDK
LPEIPERGIRTGAAATPEEFEAIAELKSDDWSYLVPMTELKPGNPASGHNYFLVNSQQRW
THIRLNIFPDGGIARLRVFGTGQKDWTATDPKEPADLVAIAFGGVCVGFSNAKFGHPNNI
IGVGGAKSMADGWETARRLDRPPILENDENGILLVPGCEWAVFRLAHPGVITRIEIDTKY
FEGNAPDSCKVDGCILTTQEEEAVIRQKWILPAHKWKPLLPVTKLSPNQSHLFDSLTLEL
QDVITHARLTIVPDGGVSRLRLRGFPSSICLLRPREKPMLKFSVSFKANP
Enzyme 7 Number of Residues 410
Enzyme 7 Molecular Weight 45763
Enzyme 7 Theoretical pI 6.07
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function The function of this enzyme is unclear as allantoicase activity is not known to exist in mammals
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 7677260 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q8N6M5 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name ALLC_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >486 bp
ATGGCGGATGGTTGGGAAACTGCAAGAAGGCTGGACCGGCCACCAATATTAGAAAATGAT
GAGAATGGCATTCTCTTGGTTCCGGGTTGTGAATGGGCAGTTTTCCGATTGGCACATCCT
GGAGTAATAACTCGAATTGAAATTGACACAAAATATTTTGAAGGCAATGCTCCTGACAGC
TGTAAAGTGGATGGGTGCATCCTGACAACTCAGGAAGAAGCCGTGATCAGGCAAAAGTGG
ATTCTCCCGGCCCACAAGTGGAAACCACTGCTTCCAGTGACCAAGTTGTCTCCCAACCAA
AGTCATCTGTTCGATAGCCTGACCCTAGAGCTCCAAGATGTCATCACTCACGCCAGGCTC
ACCATCGTCCCCGACGGGGGAGTGAGCCGCCTTCGGCTCCGGGGCTTCCCCAGCTCCATC
TGCCTCCTGAGGCCCCGGGAGAAGCCCATGTTGAAGTTCTCGGTGAGCTTCAAAGCAAAC
CCTTAA
Enzyme 7 GenBank Gene ID AF215924 Link Image
Enzyme 7 GeneCard ID Q8N6M5 Link Image
Enzyme 7 GenAtlas ID ALLC Link Image
Enzyme 7 HGNC ID HGNC:17377 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Vigetti D, Monetti C, Acquati F, Taramelli R, Bernardini G: Human allantoicase gene: cDNA cloning, genomic organization and chromosome localization. Gene. 2000 Oct 3;256(1-2):253-60. [PubMed Link Image]
  2. Vigetti D, Monetti C, Prati M, Gornati R, Bernardini G: Genomic organization and chromosome localization of the murine and human allantoicase gene. Gene. 2002 May 1;289(1-2):13-7. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 16516
Enzyme 8 Name cDNA, FLJ92843, Homo sapiens arginase, type II (ARG2), nuclear gene encodingmitochondrial protein, mRNA (Arginase, type II, isoform CRA_a)
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name ARG2
Enzyme 8 Protein Sequence >cDNA, FLJ92843, Homo sapiens arginase, type II (ARG2), nuclear gene encodingmitochondrial protein, mRNA (Arginase, type II, isoform CRA_a)
MSLRGSLSRLLQTRVHSILKKSVHSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSS
LGCHLKDFGDLSFTPVPKDDLYNNLIVNPRSVGLANQELAEVVSRAVSDGYSCVTLGGDH
SLAIGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVSFLLRELQDKVPQLPG
FSWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDIDRLGIQKVMERTFDLLIG
KRQRPIHLSFDIDAFDPTLAPATGTPVVGGLTYREGMYIAEEIHNTGLLSALDLVEVNPQ
LATSEEEAKTTANLAVDVIASSFGQTREGGHIVYDQLPTPSSPDESENQARVRI
Enzyme 8 Number of Residues 354
Enzyme 8 Molecular Weight 38578
Enzyme 8 Theoretical pI 6.45
Enzyme 8 GO Classification
Function
  • arginase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
Process
  • arginine catabolism
  • arginine metabolism
  • metabolism
  • physiological process
  • urea cycle intermediate metabolism
Component
Enzyme 8 General Function Amino acid transport and metabolism
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID B2R690 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name B2R690_HUMAN Link Image
Enzyme 8 PDB ID 1PQ3 Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AK312484 Link Image
Enzyme 8 GeneCard ID B2R690 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location 14
Enzyme 8 Locus 14q24.1-q24.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 16548
Enzyme 9 Name cDNA FLJ60951, highly similar to Probable allantoicase (Allantoicase, isoform CRA_a)
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name ALLC
Enzyme 9 Protein Sequence >cDNA FLJ60951, highly similar to Probable allantoicase (Allantoicase, isoform CRA_a)
MDMASESVGGKILFATDDFFAPAENLIKSDSPCFKEHEYTEFGKWMDGWETRRKRIPGHD
WCVLRLGIQGVIRGFDVDVSYFTGDYAPRVSIQAANLEEDKLPEIPERGTRTGAAATPEE
FEAIAELKSDDWSYLVPMTELKPGNPASGHNYFLVNSQQRWTHIRLNIFPDGGIARLRVF
GTGQKDWTATDPKEPADLVAIAFGGVCVGFSNAKFGHPNNIIGVGGAKSMADGWETARRL
DRPPILENDENGILLVPGCEWAVFRLAHPGVITRIEIDTKYFEGNAPDSCKVDGCILTTQ
EEEAVIRQKWILPAHKWKPLLPVTKLSPNQSHLFDSLTLELQDVITHARLTIVPDGGVSR
LRLRGFPSSICLLRPREKPMLKFSVSFKANP
Enzyme 9 Number of Residues 391
Enzyme 9 Molecular Weight 43559
Enzyme 9 Theoretical pI 6.07
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID B4DY77 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name B4DY77_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID AK302299 Link Image
Enzyme 9 GeneCard ID B4DY77 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 16961
Enzyme 10 Name HERV-K_5q33.3 provirus ancestral Pro protein
Enzyme 10 Synonyms
  1. HERV-K10 Pro protein
  2. HERV-K107 Pro protein
  3. Protease
  4. Proteinase
  5. PR
Enzyme 10 Gene Name Not Available
Enzyme 10 Protein Sequence >HERV-K_5q33.3 provirus ancestral Pro protein
WASQVSENRPVCKAIIQGKQFEGLVDTGADVSIIALNQWPKNWPKQKAVTGLVGIGTASE
VYQSMEILHCLGPDNQESTVQPMITSIPLNLWGRDLLQQWGAEITMPAPLYSPTSQKIMT
KMGYIPGKGLGKNEDGIKVPVEAKINQEREGIGYPF
Enzyme 10 Number of Residues 156
Enzyme 10 Molecular Weight 17108
Enzyme 10 Theoretical pI 5.90
Enzyme 10 GO Classification
Function
  • aspartic-type endopeptidase activity
  • binding
  • catalytic activity
  • endopeptidase activity
  • hydrolase activity
  • nucleic acid binding
  • peptidase activity
Process
  • cellular protein metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
  • proteolysis
Component
  • cell
  • intracellular
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Retroviral proteases have roles in processing of the primary translation products and the maturation of the viral particle. Endogenous Pro proteins may have kept, lost or modified their original function during evolution. This endogenous protein has retained most of the characteristics of retroviral proteases
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
Enzyme 10 UniProtKB/Swiss-Prot ID P10265 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name VPK10_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID M14123 Link Image
Enzyme 10 GeneCard ID P10265 Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs Not Available
Enzyme 10 General References
  1. Ono M, Yasunaga T, Miyata T, Ushikubo H: Nucleotide sequence of human endogenous retrovirus genome related to the mouse mammary tumor virus genome. J Virol. 1986 Nov;60(2):589-98. [PubMed Link Image]
  2. Barbulescu M, Turner G, Seaman MI, Deinard AS, Kidd KK, Lenz J: Many human endogenous retrovirus K (HERV-K) proviruses are unique to humans. Curr Biol. 1999 Aug 26;9(16):861-8. [PubMed Link Image]
  3. Schommer S, Sauter M, Krausslich HG, Best B, Mueller-Lantzsch N: Characterization of the human endogenous retrovirus K proteinase. J Gen Virol. 1996 Feb;77 ( Pt 2 ):375-9. [PubMed Link Image]
  4. Towler EM, Gulnik SV, Bhat TN, Xie D, Gustschina E, Sumpter TR, Robertson N, Jones C, Sauter M, Mueller-Lantzsch N, Debouck C, Erickson JW: Functional characterization of the protease of human endogenous retrovirus, K10: can it complement HIV-1 protease? Biochemistry. 1998 Dec 8;37(49):17137-44. [PubMed Link Image]
  5. Kuhelj R, Rizzo CJ, Chang CH, Jadhav PK, Towler EM, Korant BD: Inhibition of human endogenous retrovirus-K10 protease in cell-free and cell-based assays. J Biol Chem. 2001 May 18;276(20):16674-82. Epub 2001 Feb 21. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 17165
Enzyme 11 Name Urea transporter JK glycoprotein
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name JK
Enzyme 11 Protein Sequence >Urea transporter JK glycoprotein
PIFSSALNSMLSKWDLPVFTLPFNMALSMYLSATGH
Enzyme 11 Number of Residues 36
Enzyme 11 Molecular Weight 3989
Enzyme 11 Theoretical pI 7.54
Enzyme 11 GO Classification
Function
  • amine transporter activity
  • transporter activity
  • urea transporter activity
Process
  • amine transport
  • cellular physiological process
  • physiological process
  • transport
  • urea transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID Q8WXW8 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name Q8WXW8_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AF328890 Link Image
Enzyme 11 GeneCard ID Q8WXW8 Link Image
Enzyme 11 GenAtlas ID JK Link Image
Enzyme 11 HGNC ID HGNC:10918 Link Image
Enzyme 11 Chromosome Location 18
Enzyme 11 Locus 18q11-q12
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Irshaid NM, Eicher NI, Hustinx H, Poole J, Olsson ML: Novel alleles at the JK blood group locus explain the absence of the erythrocyte urea transporter in European families. Br J Haematol. 2002 Feb;116(2):445-53. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 17166
Enzyme 12 Name Blood group Kidd urea transporter
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name HUT11
Enzyme 12 Protein Sequence >Blood group Kidd urea transporter
IYGCDNPWTGGIFLGAILLSSPLMCLHAAIGSLLGIAAGLSLSAPFEDIYFGLW
Enzyme 12 Number of Residues 54
Enzyme 12 Molecular Weight 5628
Enzyme 12 Theoretical pI 3.88
Enzyme 12 GO Classification
Function
  • amine transporter activity
  • transporter activity
  • urea transporter activity
Process
  • amine transport
  • cellular physiological process
  • physiological process
  • transport
  • urea transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID Q71UV7 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name Q71UV7_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID AF046026 Link Image
Enzyme 12 GeneCard ID Q71UV7 Link Image
Enzyme 12 GenAtlas ID HUT11 Link Image
Enzyme 12 HGNC ID HGNC:10918 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Irshaid NM, Thuresson B, Olsson ML: Genomic typing of the Kidd blood group locus by a single-tube allele-specific primer PCR technique. Br J Haematol. 1998 Sep;102(4):1010-4. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available