| 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 |
- Carbonyl diamine
- Ureacin-40 Creme
- Hyanit
- Carmol
- Superprill
- Bubber shet
- Uremol 20 Cream 20%
- Simply botanical sensations healing hands
- Onychomal
- Pylori-chek breath test
- Dermal therapy-finger care
- Urederm Cream 10%
- Dermaflex Crm 10%
- Carbonyldiamide
- Urisec Lotion 12%
- Pastaron
- Urea-13C
- Ureophil
- Carbamimidic acid
- Caswell No. 902
- Urea perhydrate
- Urea
- Isourea
- Urepeal
- Pseudourea
- Ureaphil
- Urea solution
- Dermal therapy-heel care
- Dermaflex 20 Urea Cream 20%
- Uremol 10 Cream 10%
- Polyurea
- Keratinamin
- Aquacare HP
- Optigen 1200
- Urea homopolymer
- Mocovina [czech]
- URE
- Pastaron 20 soft
- Eucerin Lotion 10% D'uree
- Carbaderm
- Carbamex 330mgms
- Helicosol
- Calmurid HC
- Keratinamin kowa
- Bromisovalum
- Panafil
- Ultra Mide 25
- Murine ear wax removal system/murine ear drops
- Aqua care
- Carbamide resin
- Urepearl
- Urevert
- Elaqua XX
- Carbamimic acid
- ARF
- Breathtek ubt for h-pylori
- Uree 20 Cream
- Urepeal l
- Pastaron (TN)
- Dermal therapy-hand elbow and knee cream
- Pastaron 20
- Ureacin-20
- Pastaron soft
- B-I-k
- U-cort
- Carmol HC
- Urea (JP15/USP)
- Urisec 22% Crm
- Pastaron 10
- Nutraplus
- Urea ammonium nitrate solution
- Calmurid
- Alphadrate
- Carmol 40
- Carbamide
- Lotion
- Harnstoff [german]
- Varioform II
- Mocovina
- Carbonyl diamide
- Carbonyldiamine
- Supercel 3000
- Rubinol ST 010
- Harnstoff
- Uremol 10 Lotion 10%
- Aqua care HP
- Ultra mide
- Ureacin-10 lotion
- Prespersion 75 urea
- beta-I-k
|
| Chemical IUPAC Name |
Urea |
| Chemical Formula |
CH4N2O |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
|
| Class |
|
| Sub Class |
- Miscellaneous amino ketones
|
| Family |
|
| Species |
|
| Biofunction |
- Component of Arginine and proline metabolism
|
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
60.055 |
| Monoisotopic Molecular Weight |
60.032364 |
| Isomeric SMILES |
NC(N)=O |
| Canonical SMILES |
NC(N)=O |
| KEGG Compound ID |
C00086  |
| BioCyc ID |
UREA  |
| BiGG ID |
33799  |
| Wikipedia Link |
Urea  |
| NuGOwiki Link |
HMDB00294  |
| Metagene Link |
HMDB00294  |
| METLIN ID |
6  |
| PubChem Compound |
1176  |
| PubChem Substance |
841412  |
| ChEBI ID |
16199  |
| 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  |
| Experimental PDB File |
Show |
| Experimental PDB Structure |
|
| Experimental 1H NMR Spectrum |
Download Spectrum
Show Experimental Conditions  |
| Experimental 13C NMR Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Experimental 13C HSQC Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
|
| 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
]
|
| 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
]
|
| 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 |
|
| 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
]
|
| 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
]
|
| 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
]
|
|
| 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
]
|
| 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
]
|
| 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
]
|
|
| OMIM ID |
Not Available |
| Pathways |
|
| General References |
- 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
]
- Vaidya VS, Bonventre JV: Mechanistic biomarkers for cytotoxic acute kidney injury. Expert Opin Drug Metab Toxicol. 2006 Oct;2(5):697-713. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Final report of the safety assessment of Urea. Int J Toxicol. 2005;24 Suppl 3:1-56. [PubMed
]
- 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
]
- 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
]
- Hobbs JR: Monitoring myelomatosis. Arch Intern Med. 1975 Jan;135(1):125-30. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Wikipedia

|
| Metabolic Enzymes |
- Arginase-1
- Arginase-2, mitochondrial precursor
- Urea transporter, kidney
- Agmatinase, mitochondrial precursor
- Urea transporter, erythrocyte
- G-protein coupled receptor family C group 6 member A precursor
- Probable allantoicase
- cDNA, FLJ92843, Homo sapiens arginase, type II (ARG2), nuclear gene encodingmitochondrial protein, mRNA (Arginase, type II, isoform CRA_a)
- cDNA FLJ60951, highly similar to Probable allantoicase (Allantoicase, isoform CRA_a)
- HERV-K_5q33.3 provirus ancestral Pro protein
- Urea transporter JK glycoprotein
- Blood group Kidd urea transporter
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5533 |
| Enzyme 1 Name |
Arginase-1 |
| Enzyme 1 Synonyms |
- Type I arginase
- 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 |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 1 Reactions |
- L-arginine + H2O = L-ornithine + urea
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
178995  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P05089  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ARGI1_HUMAN  |
| 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  |
| Enzyme 1 GeneCard ID |
ARG1  |
| Enzyme 1 GenAtlas ID |
ARG1  |
| Enzyme 1 HGNC ID |
HGNC:663  |
| Enzyme 1 Chromosome Location |
6 |
| Enzyme 1 Locus |
6q23 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6323 |
| Enzyme 2 Name |
Arginase-2, mitochondrial precursor |
| Enzyme 2 Synonyms |
- Arginase II
- Non- hepatic arginase
- 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 |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 2 Reactions |
- L-arginine + H2O = L-ornithine + urea
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
1694633  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P78540  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ARGI2_HUMAN  |
| Enzyme 2 PDB ID |
1PQ3  |
| 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  |
| Enzyme 2 GeneCard ID |
ARG2  |
| Enzyme 2 GenAtlas ID |
ARG2  |
| Enzyme 2 HGNC ID |
HGNC:664  |
| Enzyme 2 Chromosome Location |
14 |
| Enzyme 2 Locus |
14q24.1-q24.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| 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  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q15849  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
UT2_HUMAN  |
| 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  |
| Enzyme 3 GeneCard ID |
SLC14A2  |
| Enzyme 3 GenAtlas ID |
SLC14A2  |
| Enzyme 3 HGNC ID |
HGNC:10919  |
| Enzyme 3 Chromosome Location |
18 |
| Enzyme 3 Locus |
18q12.1-q21.1 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
8199 |
| Enzyme 4 Name |
Agmatinase, mitochondrial precursor |
| Enzyme 4 Synonyms |
- Agmatine ureohydrolase
- 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 |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 4 Reactions |
- agmatine + H2O = putrescine + urea
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
18031951  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9BSE5  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
SPEB_HUMAN  |
| 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  |
| Enzyme 4 GeneCard ID |
AGMAT  |
| Enzyme 4 GenAtlas ID |
AGMAT  |
| Enzyme 4 HGNC ID |
HGNC:18407  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
1p36.21 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- 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
]
|
| 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 |
|
| 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  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
UT1_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
Not Available |
| Enzyme 5 GenBank Gene ID |
L36121  |
| Enzyme 5 GeneCard ID |
SLC14A1  |
| Enzyme 5 GenAtlas ID |
SLC14A1  |
| Enzyme 5 HGNC ID |
HGNC:10918  |
| Enzyme 5 Chromosome Location |
18 |
| Enzyme 5 Locus |
18q11-q12 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- hGPRC6A
- G-protein coupled receptor 33
- 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 |
|
|
| 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 |
|
| 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  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q5T6X5  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
GPC6A_HUMAN  |
| 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  |
| Enzyme 6 GeneCard ID |
Q5T6X5  |
| Enzyme 6 GenAtlas ID |
GPRC6A  |
| Enzyme 6 HGNC ID |
HGNC:18510  |
| Enzyme 6 Chromosome Location |
Not Available |
| Enzyme 6 Locus |
Not Available |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- 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
]
- 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
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
14907 |
| Enzyme 7 Name |
Probable allantoicase |
| Enzyme 7 Synonyms |
- 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 |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
7677260  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q8N6M5  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
ALLC_HUMAN  |
| 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  |
| Enzyme 7 GeneCard ID |
Q8N6M5  |
| Enzyme 7 GenAtlas ID |
ALLC  |
| Enzyme 7 HGNC ID |
HGNC:17377  |
| Enzyme 7 Chromosome Location |
Not Available |
| Enzyme 7 Locus |
Not Available |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
B2R690  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
B2R690_HUMAN  |
| Enzyme 8 PDB ID |
1PQ3  |
| 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  |
| Enzyme 8 GeneCard ID |
B2R690  |
| 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  |
| 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 |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
Not Available |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
B4DY77  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
B4DY77_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
Not Available |
| Enzyme 9 GenBank Gene ID |
AK302299  |
| Enzyme 9 GeneCard ID |
B4DY77  |
| 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  |
| 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 |
- HERV-K10 Pro protein
- HERV-K107 Pro protein
- Protease
- Proteinase
- 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 |
|
|
| 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 |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
Not Available |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P10265  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
VPK10_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
Not Available |
| Enzyme 10 GenBank Gene ID |
M14123  |
| Enzyme 10 GeneCard ID |
P10265  |
| 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 |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
Not Available |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q8WXW8  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
Q8WXW8_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
Not Available |
| Enzyme 11 GenBank Gene ID |
AF328890  |
| Enzyme 11 GeneCard ID |
Q8WXW8  |
| Enzyme 11 GenAtlas ID |
JK  |
| Enzyme 11 HGNC ID |
HGNC:10918  |
| Enzyme 11 Chromosome Location |
18 |
| Enzyme 11 Locus |
18q11-q12 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- 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
]
|
| 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 |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
Not Available |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q71UV7  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
Q71UV7_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
Not Available |
| Enzyme 12 GenBank Gene ID |
AF046026  |
| Enzyme 12 GeneCard ID |
Q71UV7  |
| Enzyme 12 GenAtlas ID |
HUT11  |
| Enzyme 12 HGNC ID |
HGNC:10918  |
| Enzyme 12 Chromosome Location |
Not Available |
| Enzyme 12 Locus |
Not Available |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- 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
]
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| Enzyme 12 Metabolite References |
Not Available |