|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5533 |
| Enzyme 1 Name |
Arginase-1 |
| Enzyme 1 Synonyms |
- Liver-type arginase
- Type I 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 |
34734.7 |
| Enzyme 1 Theoretical pI |
7.25 |
| Enzyme 1 GO Classification |
| Function |
- arginase activity
- binding
- catalytic activity
- cation binding
- 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
- 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
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
- ion binding
- metal ion binding
|
| Process |
- arginine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glutamine family amino acid metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in arginase activity |
| 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 [RN:R00551]
|
| 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
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
- Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F, Christianson DW: Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response. Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13058-63. Epub 2005 Sep 2. [PubMed
]
- Di Costanzo L, Moulin M, Haertlein M, Meilleur F, Christianson DW: Expression, purification, assay, and crystal structure of perdeuterated human arginase I. Arch Biochem Biophys. 2007 Sep 1;465(1):82-9. Epub 2007 May 21. [PubMed
]
- Di Costanzo L, Pique ME, Christianson DW: Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster. J Am Chem Soc. 2007 May 23;129(20):6388-9. Epub 2007 May 1. [PubMed
]
- Zakharian TY, Di Costanzo L, Christianson DW: Synthesis of (2S)-2-amino-7,8-epoxyoctanoic acid and structure of its metal-bridging complex with human arginase I. Org Biomol Chem. 2008 Sep 21;6(18):3240-3. Epub 2008 Aug 6. [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 |
| Enzyme 2 Synonyms |
- Kidney-type arginase
- Non-hepatic arginase
- Type II arginase
|
| Enzyme 2 Gene Name |
ARG2 |
| Enzyme 2 Protein Sequence |
>Arginase-2, mitochondrial
MSLRGSLSRLLQTRVHSILKKSVHSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSS
LGCHLKDFGDLSFTPVPKDDLYNNLIVNPRSVGLANQELAEVVSRAVSDGYSCVTLGGDH
SLAIGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVSFLLRELQDKVPQLPG
FSWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDIDRLGIQKVMERTFDLLIG
KRQRPIHLSFDIDAFDPTLAPATGTPVVGGLTYREGMYIAEEIHNTGLLSALDLVEVNPQ
LATSEEEAKTTANLAVDVIASSFGQTREGGHIVYDQLPTPSSPDESENQARVRI
|
| Enzyme 2 Number of Residues |
354 |
| Enzyme 2 Molecular Weight |
38577.5 |
| Enzyme 2 Theoretical pI |
6.45 |
| Enzyme 2 GO Classification |
| Function |
- arginase activity
- binding
- catalytic activity
- cation binding
- 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
- 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
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
- ion binding
- metal ion binding
|
| Process |
- arginine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glutamine family amino acid metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in arginase activity |
| 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 [RN:R00551]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
189065548  |
| 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 |
AK312484  |
| Enzyme 2 GeneCard ID |
ARG2  |
| Enzyme 2 GenAtlas ID |
ARG2  |
| Enzyme 2 HGNC ID |
HGNC:664  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
14q24.1 |
| 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
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Cama E, Colleluori DM, Emig FA, Shin H, Kim SW, Kim NN, Traish AM, Ash DE, Christianson DW: Human arginase II: crystal structure and physiological role in male and female sexual arousal. Biochemistry. 2003 Jul 22;42(28):8445-51. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
8017 |
| Enzyme 3 Name |
Urea transporter 2 |
| Enzyme 3 Synonyms |
- Solute carrier family 14 member 2
- Urea transporter, kidney
|
| Enzyme 3 Gene Name |
SLC14A2 |
| Enzyme 3 Protein Sequence |
>Urea transporter 2
MSDPHSSPLLPEPLSSRYKLYEAEFTSPSWPSTSPDTHPALPLLEMPEEKDLRSSNEDSH
IVKIEKLNERSKRKDDGVAHRDSAGQRCICLSKAVGYLTGDMKEYRIWLKDKHLALQFID
WVLRGTAQVMFINNPLSGLIIFIGLLIQNPWWTITGGLGTVVSTLTALALGQDRSAIASG
LHGYNGMLVGLLMAVFSEKLDYYWWLLFPVTFTAMSCPVLSSALNSIFSKWDLPVFTLPF
NIAVTLYLAATGHYNLFFPTTLVEPVSSVPNITWTEMEMPLLLQAIPVGVGQVYGCDNPW
TGGVFLVALFISSPLICLHAAIGSIVGLLAALSVATPFETIYTGLWSYNCVLSCIAIGGM
FYALTWQTHLLALICALFCAYMEAAISNIMSVVGVPPGTWAFCLATIIFLLLTTNNPAIF
RLPLSKVTYPEANRIYYLTVKSGEEEKAPSGGGGEHPPTAGPKVEEGSEAVLSKHRSVFH
IEWSSIRRRSKVFGKGEHQERQNKDPFPYRYRKPTVELLDLDTMEESSEIKVETNISKTS
WIRSSMAASGKRVSKALSYITGEMKECGEGLKDKSPVFQFFDWVLRGTSQVMFVNNPLSG
ILIILGLFIQNPWWAISGCLGTIMSTLTALILSQDKSAIAAGFHGYNGVLVGLLMAVFSD
KGDYYWWLLLPVIIMSMSCPILSSALGTIFSKWDLPVFTLPFNITVTLYLAATGHYNLFF
PTTLLQPASAMPNITWSEVQVPLLLRAIPVGIGQVYGCDNPWTGGIFLIALFISSPLICL
HAAIGSTMGMLAALTIATPFDSIYFGLCGFNSTLACIAIGGMFYVITWQTHLLAIACALF
AAYLGAALANMLSVFGLPPCTWPFCLSALTFLLLTTNNPAIYKLPLSKVTYPEANRIYYL
SQERNRRASIITKYQAYDVS
|
| Enzyme 3 Number of Residues |
920 |
| Enzyme 3 Molecular Weight |
101208.0 |
| Enzyme 3 Theoretical pI |
6.94 |
| Enzyme 3 GO Classification |
| Function |
- amide transmembrane transporter activity
- substrate-specific transmembrane transporter activity
- transmembrane transporter activity
- transporter activity
- urea transmembrane transporter activity
|
| Process |
- amide transport
- establishment of localization
- transport
- urea transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 3 General Function |
Involved in urea transmembrane transporter activity |
| Enzyme 3 Specific Function |
Specialized low-affinity vasopressin-regulated urea transporter. Mediates rapid transepithelial urea transport across the inner medullary collecting duct and plays a major role in the urinary concentrating mechanism |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
- 151-170
176-196
204-224
233-253
272-291
302-322
346-366
370-390
392-412
600-620
638-658
666-686
695-715
764-784
803-823
832-852
854-874
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
157694503  |
| 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 |
>2763 bp
ATGTCTGACCCCCACAGCAGTCCTCTCCTGCCAGAGCCACTTTCCAGCAGATACAAACTC
TACGAGGCAGAGTTTACCAGCCCGAGCTGGCCCTCGACATCCCCGGATACTCACCCAGCT
CTGCCCCTCCTGGAAATGCCTGAAGAAAAGGATCTCCGGTCTTCCAATGAAGACAGTCAC
ATTGTGAAGATCGAAAAGCTCAATGAAAGGAGTAAAAGGAAAGACGACGGGGTGGCCCAT
CGGGACTCAGCAGGCCAAAGGTGCATCTGCCTCTCCAAAGCAGTGGGCTACCTCACGGGC
GACATGAAGGAGTACAGGATCTGGCTGAAAGACAAGCACCTTGCCCTCCAGTTCATAGAC
TGGGTCCTGAGAGGGACCGCTCAGGTGATGTTCATCAACAATCCTCTCAGCGGCCTCATC
ATCTTCATAGGGCTGCTGATCCAGAATCCCTGGTGGACAATCACTGGGGGCCTGGGGACA
GTGGTCTCGACCTTAACAGCTCTCGCCTTGGGCCAAGACAGGTCTGCCATTGCCTCAGGA
CTCCATGGGTACAACGGGATGCTGGTGGGACTGCTGATGGCCGTGTTCTCGGAGAAGTTA
GACTACTACTGGTGGCTTCTGTTTCCTGTGACCTTCACAGCCATGTCCTGCCCAGTTCTT
TCTAGTGCCTTGAATTCCATCTTCAGCAAGTGGGACCTCCCGGTCTTCACTCTGCCCTTC
AACATTGCAGTCACCTTGTACCTTGCAGCCACAGGCCACTACAACCTCTTCTTCCCCACA
ACACTGGTAGAGCCTGTGTCTTCAGTGCCCAATATCACCTGGACAGAGATGGAAATGCCC
CTGCTGTTACAAGCCATCCCTGTTGGGGTCGGCCAGGTGTATGGCTGTGACAATCCCTGG
ACAGGCGGCGTGTTCCTGGTGGCTCTGTTCATCTCCTCGCCACTCATCTGCTTGCATGCA
GCCATTGGCTCAATCGTGGGGCTGCTAGCAGCCCTGTCAGTGGCCACACCCTTCGAGACC
ATCTACACAGGCCTCTGGAGCTACAACTGCGTCCTCTCCTGCATCGCCATCGGAGGCATG
TTCTATGCCCTCACCTGGCAGACTCACCTGCTGGCCCTCATCTGTGCCCTGTTCTGTGCA
TACATGGAAGCAGCCATCTCCAACATCATGTCAGTGGTGGGCGTGCCACCAGGCACCTGG
GCCTTCTGCCTTGCCACCATCATCTTCCTGCTCCTGACGACAAACAACCCAGCCATCTTC
AGACTCCCACTCAGCAAAGTCACCTACCCCGAGGCCAACCGCATCTACTACCTGACAGTG
AAAAGCGGTGAAGAAGAGAAGGCCCCCAGCGGAGGCGGTGGGGAGCATCCACCCACAGCA
GGCCCAAAGGTGGAGGAGGGCTCGGAGGCTGTGCTCTCCAAGCACAGGAGTGTATTTCAC
ATCGAGTGGTCATCCATTCGGAGGAGGAGCAAAGTGTTTGGAAAAGGCGAACACCAGGAA
AGACAAAACAAAGACCCATTTCCCTATCGATACCGGAAGCCCACAGTCGAGCTGCTTGAT
CTGGACACCATGGAGGAGAGCTCTGAGATAAAAGTGGAAACAAACATTTCCAAGACATCC
TGGATTCGGAGTTCCATGGCTGCCAGTGGGAAAAGGGTCAGCAAAGCCCTCAGCTACATC
ACAGGAGAGATGAAGGAGTGTGGAGAGGGACTTAAAGACAAGTCCCCAGTGTTCCAGTTC
TTTGACTGGGTCCTCCGAGGCACATCTCAAGTGATGTTTGTGAACAACCCCCTCAGCGGC
ATCCTCATCATCCTCGGCCTCTTCATCCAGAACCCCTGGTGGGCGATCTCAGGCTGCCTG
GGTACCATCATGTCCACCTTGACAGCCCTCATCCTGAGTCAGGACAAGTCGGCCATCGCT
GCAGGATTTCACGGCTACAATGGGGTGCTGGTGGGGCTGCTGATGGCCGTGTTCTCAGAC
AAAGGTGACTACTACTGGTGGCTGTTGCTACCCGTCATCATCATGTCCATGTCTTGCCCC
ATCCTCTCCAGTGCCCTGGGTACCATCTTCAGCAAGTGGGACCTCCCAGTCTTCACACTG
CCCTTCAATATCACTGTGACTTTGTACCTGGCAGCCACGGGCCACTACAACCTTTTCTTC
CCCACAACGCTGCTGCAGCCTGCATCCGCCATGCCCAACATCACCTGGTCAGAGGTCCAA
GTGCCCTTGCTTTTGAGAGCCATCCCCGTTGGAATTGGCCAAGTGTACGGCTGTGATAAC
CCCTGGACTGGAGGCATCTTCCTCATAGCTCTGTTCATATCCTCACCTCTCATTTGCTTG
CATGCAGCAATTGGATCCACCATGGGGATGCTAGCAGCACTCACTATTGCGACGCCCTTT
GACTCCATCTACTTCGGCCTGTGTGGCTTCAACAGCACCCTCGCATGCATAGCGATAGGA
GGCATGTTCTACGTCATCACCTGGCAGACGCACCTCCTCGCCATCGCCTGCGCACTGTTT
GCTGCCTACCTGGGTGCTGCCCTGGCTAACATGTTATCTGTGTTTGGATTGCCGCCCTGC
ACTTGGCCCTTCTGTCTCTCAGCTCTCACCTTCCTGCTCCTGACGACCAATAACCCCGCC
ATCTACAAGCTCCCGCTCAGCAAAGTCACCTACCCAGAGGCCAACCGCATCTACTACCTG
TCCCAGGAGAGAAACAGAAGGGCATCAATCATAACAAAGTATCAGGCCTACGATGTCTCC
TAA
|
| Enzyme 3 GenBank Gene ID |
NM_007163.3  |
| Enzyme 3 GeneCard ID |
SLC14A2  |
| Enzyme 3 GenAtlas ID |
SLC14A2  |
| Enzyme 3 HGNC ID |
HGNC:10919  |
| Enzyme 3 Chromosome Location |
1 |
| 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
]
- Bagnasco SM, Peng T, Janech MG, Karakashian A, Sands JM: Cloning and characterization of the human urea transporter UT-A1 and mapping of the human Slc14a2 gene. Am J Physiol Renal Physiol. 2001 Sep;281(3):F400-6. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Nusbaum C, Zody MC, Borowsky ML, Kamal M, Kodira CD, Taylor TD, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Abouelleil A, Allen NR, Anderson S, Bloom T, Bugalter B, Butler J, Cook A, DeCaprio D, Engels R, Garber M, Gnirke A, Hafez N, Hall JL, Norman CH, Itoh T, Jaffe DB, Kuroki Y, Lehoczky J, Lui A, Macdonald P, Mauceli E, Mikkelsen TS, Naylor JW, Nicol R, Nguyen C, Noguchi H, O'Leary SB, O'Neill K, Piqani B, Smith CL, Talamas JA, Topham K, Totoki Y, Toyoda A, Wain HM, Young SK, Zeng Q, Zimmer AR, Fujiyama A, Hattori M, Birren BW, Sakaki Y, Lander ES: DNA sequence and analysis of human chromosome 18. Nature. 2005 Sep 22;437(7058):551-5. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Mistry AC, Mallick R, Frohlich O, Klein JD, Rehm A, Chen G, Sands JM: The UT-A1 urea transporter interacts with snapin, a SNARE-associated protein. J Biol Chem. 2007 Oct 12;282(41):30097-106. Epub 2007 Aug 16. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
8199 |
| Enzyme 4 Name |
Agmatinase, mitochondrial |
| Enzyme 4 Synonyms |
- Agmatine ureohydrolase
- AUH
|
| Enzyme 4 Gene Name |
AGMAT |
| Enzyme 4 Protein Sequence |
>Agmatinase, mitochondrial
MLRLLASGCARGPGPGVGARPAAGLFHPGRRQSRQASDAPRNQPPSPEFVARPVGVCSMM
RLPVQTSPEGLDAAFIGVPLDTGTSNRPGARFGPRRIREESVMLGTVNPSTGALPFQSLM
VADLGDVNVNLYNLQDSCRRIQEAYEKIVAAGCIPLTLGGDHTITYPILQAMAKKHGPVG
LLHVDAHTDTTDKALGEKLYHGAPFRRCVDEGLLDCKRVVQIGIRGSSTTLDPYRYNRSQ
GFRVVLAEDCWMKSLVPLMGEVRQQMGGKPIYISFDIDALDPAYAPGTGTPEIAGLTPSQ
ALEIIRGCQGLNVMGCDLVEVSPPYDLSGNTALLAANLLFEMLCALPKVTTV
|
| Enzyme 4 Number of Residues |
352 |
| Enzyme 4 Molecular Weight |
37660.1 |
| Enzyme 4 Theoretical pI |
7.66 |
| Enzyme 4 GO Classification |
| Function |
- agmatinase activity
- binding
- catalytic activity
- cation binding
- 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
- 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
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
- ion binding
- metal ion binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- metabolic process
- polyamine biosynthetic process
- polyamine metabolic process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in agmatinase activity |
| 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 [RN:R01157]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
10440052  |
| 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
CCTGCCGCAGGGCTCTTTCATCCGGGGCGCCGCCAGAGCCGCCAGGCTTCCGATGCGCCC
CGGAACCAGCCCCCCAGCCCCGAGTTCGTGGCCCGGCCGGTGGGCGTCTGCTCCATGATG
CGCCTGCCGGTGCAGACCTCCCCCGAGGGGCTGGACGCTGCCTTCATCGGGGTGCCCCTG
GATACTGGGACCTCCAACCGGCCTGGGGCGAGATTCGGACCTCGCCGCATCCGGGAAGAA
TCAGTGATGCTTCGGACAGTCAATCCTAGCACGGGGGCCCTCCCCTTCCAGTCCCTCATG
GTTGCAGACCTAGGCGATGTGAATGTCAATCTTTACAACCTTCAGGACAGCTGCCGGCGA
ATTCAAGAGGCCTGTGAGAAAATTGTAGCAGCTGGCTGTATTCCTCTGACCTTGGGTGGA
GATCACACAATCACATATCCCATATTGCAAGCGATGGCAAAAAAGCATGGCCCAGTGGGG
CTGCTGCACGTGGATGCGCACACGGACACGACCGACAAGGCCCTAGGAGAGAAGCTCTAC
CACGGGGCGCCCTTCCGCCGGTGTGTGGATGAGGGTCTCCTGGACTGTAAGCGTGTGGTG
CAGATTGGCATCCGGGGCTCTTCCACGACCTTGGATCCCTACAGATACAACCGGAGCCAG
GGCTTCCGGGTAGTCCTGGCTGAAGACTGCTGGATGAAGTCGCTGGTTCCTCTGATGGGG
GAAGTCAGGCAGCAGATGGGAGGCAAACCCATTTATATCAGCTTTGATATTGACGCTCTG
GATCCTGCCTATGCGCCAGGGACAGGGACACCTGAAATTGCTGGTCTCACTCCTAGTCAG
GCTCTGGAGATCATCAGGGGTTGTCAAGGCCTGAACGTGATGGGCTGTGATCTTGTCGAA
GTTTCACCACCGTATGATCTTTCTGGGAACACAGCCCTGCTGGCGGCTAACCTGCTGTTT
GAGATGCTATGTGCTCTCCCCAAAGTGACAACCGTCTGA
|
| Enzyme 4 GenBank Gene ID |
AK027037  |
| 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
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
8415 |
| Enzyme 5 Name |
Urea transporter 1 |
| Enzyme 5 Synonyms |
- Solute carrier family 14 member 1
- Urea transporter, erythrocyte
|
| Enzyme 5 Gene Name |
SLC14A1 |
| Enzyme 5 Protein Sequence |
>Urea transporter 1
MEDSPTMVRVDSPTMVRGENQVSPCQGRRCFPKALGYVTGDMKELANQLKDKPVVLQFID
WILRGISQVVFVNNPVSGILILVGLLVQNPWWALTGWLGTVVSTLMALLLSQDRSLIASG
LYGYNATLVGVLMAVFSDKGDYFWWLLLPVCAMSMTCPIFSSALNSMLSKWDLPVFTLPF
NMALSMYLSATGHYNPFFPAKLVIPITTAPNISWSDLSALELLKSIPVGVGQIYGCDNPW
TGGIFLGAILLSSPLMCLHAAIGSLLGIAAGLSLSAPFEDIYFGLWGFNSSLACIAMGGM
FMALTWQTHLLALGCALFTAYLGVGMANFMAEVGLPACTWPFCLATLLFLIMTTKNSNIY
KMPLSKVTYPEENRIFYLQAKKRMVESPL
|
| Enzyme 5 Number of Residues |
389 |
| Enzyme 5 Molecular Weight |
42527.9 |
| Enzyme 5 Theoretical pI |
7.19 |
| Enzyme 5 GO Classification |
| Function |
- amide transmembrane transporter activity
- substrate-specific transmembrane transporter activity
- transmembrane transporter activity
- transporter activity
- urea transmembrane transporter activity
|
| Process |
- amide transport
- establishment of localization
- transport
- urea transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 5 General Function |
Involved in urea transmembrane transporter activity |
| 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 |
193784782  |
| 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 |
>1170 bp
ATGGAGGACAGCCCCACTATGGTTAGAGTGGACAGCCCCACTATGGTTAGGGGTGAAAAC
CAGGTTTCGCCATGTCAAGGGAGAAGGTGCTTCCCCAAAGCTCTTGGCTATGTCACCGGT
GACATGAAAAAACTTGCCAACCAGCTTAAAGACAAACCCGTGGTGCTCCAGTTCATTGAC
TGGATTCTCCGGGGCATATCCCAAGTGGTGTTCGTCAACAACCCCGTCAGTGGAATCCTG
ATTCTGGTAGGACTTCTTGTTCAGAACCCCTGGTGGGCTCTCACTGGCTGGCTGGGAACA
GTGGTCTCCACTCTGATGGCCCTCTTGCTCAGCCAGGACAGGTCATTAATAGCATCTGGG
CTCTATGGCTACAATGCCACCCTGGTGGGAGTACTCATGGCTGTCTTTTCGGACAAGGGA
GACTATTTCTGGTGGCTGTTACTCCCTGTATGTGCTATGTCCATGACTTGCCCAATTTTC
TCAAGTGCATTGAATTCCATGCTCAGCAAATGGGACCTCCCCGTCTTCACCCTCCCTTTC
AACATGGCGTTGTCAATGTACCTTTCAGCCACAGGACATTACAATCCGTTCTTTCCAGCC
AAACTGGTCATACCTATAACTACAGCTCCAAATATCTCCTGGTCTGACCTCAGTGCCCTG
GAGTTGTTGAAATCTATACCAGTGGGAGTTGGTCAGATCTATGGCTGTGATAATCCATGG
ACAGGGGGCATTTTCCTGGGAGCCATCCTACTCTCCTCCCCACTCATGTGCCTGCATGCT
GCCATAGGATCATTGCTGGGCATAGCAGCGGGACTCAGTCTTTCAGCCCCATTTGAGGAC
ATCTACTTTGGACTCTGGGGTTTCAACAGCTCTCTGGCCTGCATTGCAATGGGAGGAATG
TTCATGGCGCTCACCTGGCAAACCCACCTCCTGGCTCTTGGCTGTGCCCTGTTCACGGCC
TATCTTGGAGTCGGCATGGCAAACTTTATGGCTGAGGTTGGATTGCCAGCTTGTACCTGG
CCCTTCTGTTTGGCCACGCTATTGTTCCTCATCATGACCACAAAAAATTCCAACATCTAC
AAGATGCCCCTCAGTAAAGTTACTTATCCTGAAGAAAACCGCATCTTCTACCTGCAAGCC
AAGAAAAGAATGGTGGAAAGCCCTTTGTGA
|
| Enzyme 5 GenBank Gene ID |
AK123681  |
| Enzyme 5 GeneCard ID |
SLC14A1  |
| Enzyme 5 GenAtlas ID |
SLC14A1  |
| Enzyme 5 HGNC ID |
HGNC:10918  |
| Enzyme 5 Chromosome Location |
1 |
| 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
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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 |
| Enzyme 6 Synonyms |
- hGPRC6A
- G-protein coupled receptor GPCR33
- hGPCR33
|
| Enzyme 6 Gene Name |
GPRC6A |
| Enzyme 6 Protein Sequence |
>G-protein coupled receptor family C group 6 member A
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 |
104752.2 |
| Enzyme 6 Theoretical pI |
8.00 |
| Enzyme 6 GO Classification |
| Function |
- G-protein coupled receptor activity
- molecular transducer activity
- receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- signaling
- signaling pathway
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 6 General Function |
Involved in G-protein coupled receptor activity |
| 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 |
112807234  |
| 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
ATTGAGATGATCAACAATTCAACACTCTTACCTGGAGTCAAACTGGGGTATGAAATCTAT
GACACTTGTACAGAAGTCACAGTGGCAATGGCAGCCACTCTGAGGTTTCTTTCTAAATTC
AACTGCTCCAGAGAAACTGTGGAGTTTAAGTGTGACTATTCCAGCTACATGCCAAGAGTT
AAGGCTGTCATAGGTTCTGGGTACTCAGAAATAACTATGGCTGTCTCCAGGATGTTGAAT
TTACAGCTCATGCCACAGGTGGGTTATGAATCAACTGCAGAAATCCTGAGTGACAAAATT
CGCTTTCCTTCATTTTTACGGACTGTGCCCAGTGACTTCCATCAAATTAAAGCAATGGCT
CACCTGATTCAGAAATCTGGTTGGAACTGGATTGGCATCATAACCACAGATGATGACTAT
GGACGATTGGCTCTTAACACTTTTATAATTCAGGCTGAAGCAAATAACGTGTGCATAGCC
TTCAAAGAGGTTCTTCCAGCCTTTCTTTCAGATAATACCATTGAAGTCAGAATCAATCGG
ACACTGAAGAAAATCATTTTAGAAGCCCAGGTTAATGTCATTGTGGTATTTCTGAGGCAA
TTCCATGTTTTTGATCTCTTCAATAAAGCCATTGAAATGAATATAAATAAGATGTGGATT
GCTAGTGATAATTGGTCAACTGCCACCAAGATTACCACCATTCCTAATGTTAAAAAGATT
GGCAAAGTTGTAGGGTTTGCCTTTAGAAGAGGGAATATATCCTCTTTCCATTCCTTTCTT
CAAAATCTGCACTTGCTTCCCAGTGACAGTCACAAACTCTTACATGAATATGCCATGCAT
TTATCTGCCTGCGCATATGTCAAGGACACTGATTTGAGTCAATGCATATTCAATCATTCT
CAAAGGACTTTGGCCTACAAGGCTAACAAGGCTATAGAAAGGAACTTCGTCATGAGAAAT
GACTTCCTCTGGGACTATGCTGAGCCAGGACTCATTCATAGTATTCAGCTTGCAGTGTTT
GCCCTTGGTTATGCCATTCGGGATCTGTGTCAAGCTCGTGACTGTCAGAACCCCAACGCC
TTTCAACCATGGGAGTTACTTGGTGTGCTAAAAAATGTGACATTCACTGATGGATGGAAT
TCATTTCATTTTGATGCTCACGGGGATTTAAATACTGGATATGATGTTGTGCTCTGGAAG
GAGATCAATGGACACATGACTGTCACTAAGATGGCAGAATATGACCTACAGAATGATGTC
TTCATCATCCCAGATCAGGAAACAAAAAATGAGTTCAGGAATCTTAAGCAAATTCAATCT
AAATGCTCCAAGGAATGCAGTCCTGGGCAAATGAAGAAAACTACAAGAAGTCAACACATC
TGTTGCTATGAATGTCAGAACTGTCCTGAAAATCATTACACTAATCAGACAGATATGCCT
CACTGCCTTTTATGCAACAACAAAACTCACTGGGCCCCTGTTAGGAGCACTATGTGCTTT
GAAAAGGAAGTGGAATATCTCAACTGGAATGACTCCTTGGCCATCCTACTCCTGATTCTC
TCCCTACTGGGAATCATATTTGTTCTGGTTGTTGGCATAATATTTACAAGAAACCTGAAC
ACACCTGTTGTGAAATCATCCGGGGGATTAAGAGTCTGCTATGTGATCCTTCTCTGTCAT
TTCCTCAATTTTGCCAGCACGAGCTTTTTCATTGGAGAACCACAAGACTTCACATGTAAA
ACCAGGCAGACAATGTTTGGAGTGAGCTTTACTCTTTGCATCTCCTGCATTTTGACGAAG
TCTCTGAAAATTTTGCTAGCCTTCAGCTTTGATCCCAAATTACAGAAATTTCTGAAGTGC
CTCTATAGACCGATCCTTATTATCTTCACTTGCACGGGCATCCAGGTTGTCATTTGCACA
CTCTGGCTAATCTTTGCAGCACCTACTGTAGAGGTGAATGTCTCCTTGCCCAGAGTCATC
ATCCTGGAGTGTGAGGAGGGATCCATACTTGCATTTGGCACCATGCTGGGCTACATTGCC
ATCCTGGCCTTCATTTGCTTCATATTTGCTTTCAAAGGCAAATATGAGAATTACAATGAA
GCCAAATTCATTACATTTGGCATGCTCATTTACTTCATAGCTTGGATCACATTCATCCCT
ATCTATGCTACCACATTTGGCAAATATGTACCAGCTGTGGAGATTATTGTCATATTAATA
TCTAACTATGGAATCCTGTATTGCACATTCATCCCCAAATGCTATGTTATTATTTGTAAG
CAAGAGATTAACACAAAGTCTGCCTTTCTCAAGATGATCTACAGTTATTCTTCCCATAGT
GTGAGCAGCATTGCCCTGAGTCCTGCTTCACTGGACTCCATGAGCGGCAATGTCACAATG
ACCAATCCCAGCTCTAGTGGCAAGTCTGCAACCTGGCAGAAAAGCAAAGATCTTCAGGCA
CAAGCATTTGCACACATATGCAGGGAAAATGCCACAAGTGTATCTAAAACTTTGCCTCGA
AAAAGAATGTCAAGTATATGA
|
| Enzyme 6 GenBank Gene ID |
NM_148963.2  |
| Enzyme 6 GeneCard ID |
GPRC6A  |
| Enzyme 6 GenAtlas ID |
GPRC6A  |
| Enzyme 6 HGNC ID |
HGNC:18510  |
| Enzyme 6 Chromosome Location |
6 |
| Enzyme 6 Locus |
6q22.1 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Wellendorph P, Brauner-Osborne H: Molecular cloning, expression, and sequence analysis of GPRC6A, a novel family C G-protein-coupled receptor. Gene. 2004 Jun 23;335:37-46. [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
]
- 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
]
- Wellendorph P, Hansen KB, Balsgaard A, Greenwood JR, Egebjerg J, Brauner-Osborne H: Deorphanization of GPRC6A: a promiscuous L-alpha-amino acid receptor with preference for basic amino acids. Mol Pharmacol. 2005 Mar;67(3):589-97. Epub 2004 Dec 2. [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 |
45761.8 |
| Enzyme 7 Theoretical pI |
6.07 |
| Enzyme 7 GO Classification |
| Function |
- allantoicase 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 |
| — |
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in allantoicase activity |
| 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 |
- allantoate + H2O = (S)-ureidoglycolate + urea [RN:R02422]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
144953901  |
| 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 |
>1176 bp
ATGGACATGGCATCTGAATCCGTAGGAGGAAAAATTTTATTTGCAACAGATGACTTTTTT
GCTCCTGCAGAAAACCTCATAAAGAGTGACAGCCCGTGCTTCAAAGAGCATGAATATACG
GAGTTTGGGAAATGGATGGATGGCTGGGAGACCAGGAGGAAAAGGATTCCAGGTCACGAC
TGGTGTGTCCTCAGGCTGGGGATCCAAGGAGTCATCCGGGGCTTCGACGTGGACGTTTCT
TACTTCACGGGAGATTACGCTCCTCGAGTGTCCATTCAAGCAGCAAACTTGGAAGAAGAT
AAACTACCAGAAATCCCAGAAAGAGGAACCAGGACAGGAGCTGCAGCCACTCCTGAGGAG
TTTGAAGCCATTGCTGAGCTAAAATCCGACGACTGGAGTTACTTGGTTCCCATGACTGAG
CTTAAGCCAGGAAACCCTGCTTCCGGCCACAACTATTTTCTTGTCAATTCCCAGCAGAGA
TGGACTCATATCAGACTCAACATTTTCCCAGATGGTGGAATTGCACGACTTAGAGTATTC
GGTACTGGACAAAAAGACTGGACTGCAACTGACCCCAAAGAACCTGCAGACCTAGTGGCC
ATCGCTTTTGGGGGTGTCTGTGTAGGATTTAGTAATGCTAAGTTTGGGCACCCAAACAAT
ATAATAGGAGTTGGCGGGGCAAAGTCTATGGCGGATGGTTGGGAAACTGCAAGAAGGCTG
GACCGGCCACCAATATTAGAAAATGATGAGAATGGCATTCTCTTGGTTCCGGGTTGTGAA
TGGGCAGTTTTCCGATTGGCACATCCTGGAGTAATAACTCGAATTGAAATTGACACAAAA
TATTTTGAAGGCAATGCTCCTGACAGCTGTAAAGTGGATGGGTGCATCCTGACAACTCAG
GAAGAAGAAGCCGTGATCAGGCAAAAGTGGATTCTCCCGGCCCACAAGTGGAAACCACTG
CTTCCAGTGACCAAGTTGTCTCCCAACCAAAGTCATCTGTTCGATAGCCTGACCCTAGAG
CTCCAAGATGTCATCACTCACGCCAGGCTCACCATCGTCCCCGACGGGGGAGTGAGCCGC
CTTCGGCTCCGGGGCTTCCCCAGCTCCATCTGCCTCCTGAGGCCCCGGGAGAAGCCCATG
TTGAAGTTCTCGGTGAGCTTCAAAGCAAACCCTTAA
|
| Enzyme 7 GenBank Gene ID |
Not Available |
| Enzyme 7 GeneCard ID |
ALLC  |
| Enzyme 7 GenAtlas ID |
ALLC  |
| Enzyme 7 HGNC ID |
HGNC:17377  |
| Enzyme 7 Chromosome Location |
2 |
| Enzyme 7 Locus |
2q35 |
| 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
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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 |
Allantoicase, isoform CRA_a |
| Enzyme 9 Synonyms |
- SubName: cDNA FLJ60951, highly similar to Probable allantoicase (EC 3.5.3.4)
|
| Enzyme 9 Gene Name |
ALLC |
| Enzyme 9 Protein Sequence |
>Allantoicase, isoform CRA_a
MDMASESVGGKILFATDDFFAPAENLIKSDSPCFKEHEYTEFGKWMDGWETRRKRIPGHD
WCVLRLGIQGVIRGFDVDVSYFTGDYAPRVSIQAANLEEDKLPEIPERGTRTGAAATPEE
FEAIAELKSDDWSYLVPMTELKPGNPASGHNYFLVNSQQRWTHIRLNIFPDGGIARLRVF
GTGQKDWTATDPKEPADLVAIAFGGVCVGFSNAKFGHPNNIIGVGGAKSMADGWETARRL
DRPPILENDENGILLVPGCEWAVFRLAHPGVITRIEIDTKYFEGNAPDSCKVDGCILTTQ
EEEAVIRQKWILPAHKWKPLLPVTKLSPNQSHLFDSLTLELQDVITHARLTIVPDGGVSR
LRLRGFPSSICLLRPREKPMLKFSVSFKANP
|
| Enzyme 9 Number of Residues |
391 |
| Enzyme 9 Molecular Weight |
43558.2 |
| Enzyme 9 Theoretical pI |
6.07 |
| Enzyme 9 GO Classification |
| Function |
- allantoicase 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 |
| — |
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in allantoicase activity |
| 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 |
194379346  |
| 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 |
>1176 bp
ATGGACATGGCATCTGAATCCGTAGGAGGAAAAATTTTATTTGCAACAGATGACTTTTTT
GCTCCTGCAGAAAACCTCATAAAGAGTGACAGCCCGTGCTTCAAAGAGCATGAATATACG
GAGTTTGGGAAATGGATGGATGGCTGGGAGACCAGGAGGAAAAGGATTCCAGGTCACGAC
TGGTGTGTCCTCAGGCTGGGGATCCAAGGAGTCATCCGGGGCTTCGACGTGGACGTTTCT
TACTTCACGGGAGATTACGCTCCTCGAGTGTCCATTCAAGCAGCAAACTTGGAAGAAGAT
AAACTACCAGAAATCCCAGAAAGAGGAACCAGGACAGGAGCTGCAGCCACTCCTGAGGAG
TTTGAAGCCATTGCTGAGCTAAAATCCGACGACTGGAGTTACTTGGTTCCCATGACTGAG
CTTAAGCCAGGAAACCCTGCTTCCGGCCACAACTATTTTCTTGTCAATTCCCAGCAGAGA
TGGACTCATATCAGACTCAACATTTTCCCAGATGGTGGAATTGCACGACTTAGAGTATTC
GGTACTGGACAAAAAGACTGGACTGCAACTGACCCCAAAGAACCTGCAGACCTAGTGGCC
ATCGCTTTTGGGGGTGTCTGTGTAGGATTTAGTAATGCTAAGTTTGGGCACCCAAACAAT
ATAATAGGAGTTGGCGGGGCAAAGTCTATGGCGGATGGTTGGGAAACTGCAAGAAGGCTG
GACCGGCCACCAATATTAGAAAATGATGAGAATGGCATTCTCTTGGTTCCGGGTTGTGAA
TGGGCAGTTTTCCGATTGGCACATCCTGGAGTAATAACTCGAATTGAAATTGACACAAAA
TATTTTGAAGGCAATGCTCCTGACAGCTGTAAAGTGGATGGGTGCATCCTGACAACTCAG
GAAGAAGAAGCCGTGATCAGGCAAAAGTGGATTCTCCCGGCCCACAAGTGGAAACCACTG
CTTCCAGTGACCAAGTTGTCTCCCAACCAAAGTCATCTGTTCGATAGCCTGACCCTAGAG
CTCCAAGATGTCATCACTCACGCCAGGCTCACCATCGTCCCCGACGGGGGAGTGAGCCGC
CTTCGGCTCCGGGGCTTCCCCAGCTCCATCTGCCTCCTGAGGCCCCGGGAGAAGCCCATG
TTGAAGTTCTCGGTGAGCTTCAAAGCAAACCCTTAA
|
| Enzyme 9 GenBank Gene ID |
AK302299  |
| Enzyme 9 GeneCard ID |
ALLC  |
| Enzyme 9 GenAtlas ID |
ALLC  |
| Enzyme 9 HGNC ID |
HGNC:17377  |
| Enzyme 9 Chromosome Location |
2 |
| Enzyme 9 Locus |
2q35 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed
]
|
| 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 |
17107.6 |
| 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
- peptidase activity, acting on L-amino acid peptides
|
| Process |
- macromolecule metabolic process
- metabolic process
- protein metabolic process
- proteolysis
|
| Component |
|
|
| Enzyme 10 General Function |
Involved in nucleic acid binding |
| 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 |
- Processing at the authentic HIV-1 PR recognition site and release of the mature p17 matrix and the p24 capsid protein, as a result of the cleavage of the -SQNY!PIVQ- cleavage site.
|
| 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 |
Not Available |
| Enzyme 10 GeneCard ID |
Not Available |
| 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
]
- Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [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 |
3988.6 |
| Enzyme 11 Theoretical pI |
7.54 |
| Enzyme 11 GO Classification |
| Function |
- amide transmembrane transporter activity
- substrate-specific transmembrane transporter activity
- transmembrane transporter activity
- transporter activity
- urea transmembrane transporter activity
|
| Process |
- amide transport
- establishment of localization
- transport
- urea transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 11 General Function |
Involved in urea transmembrane transporter activity |
| 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 |
17225555  |
| 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 |
>112 bp
CCCAATTTTCTCAAGTGCATTGAATTCCATGCTCAGCAAATGGGACCTCCCCGTCTTCAC
CCTCCCTTTCAACATGGCGTTGTCAATGTACCTTTCAGCCACAGGACATTAG
|
| Enzyme 11 GenBank Gene ID |
AF328890  |
| Enzyme 11 GeneCard ID |
JK  |
| Enzyme 11 GenAtlas ID |
JK  |
| Enzyme 11 HGNC ID |
HGNC:10918  |
| Enzyme 11 Chromosome Location |
Not Available |
| Enzyme 11 Locus |
Not Available |
| 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 |
5627.5 |
| Enzyme 12 Theoretical pI |
3.88 |
| Enzyme 12 GO Classification |
| Function |
- amide transmembrane transporter activity
- substrate-specific transmembrane transporter activity
- transmembrane transporter activity
- transporter activity
- urea transmembrane transporter activity
|
| Process |
- amide transport
- establishment of localization
- transport
- urea transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 12 General Function |
Involved in urea transmembrane transporter activity |
| 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 |
3820490  |
| 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 |
>164 bp
AGATCTATGGCTGTGATAATCCATGGACAGGGGGCATTTTCCTGGGAGCCATCCTACTCT
CCTCCCCACTCATGTGCCTGCATGCTGCCATAGGATCATTGCTGGGCATAGCAGCGGGAC
TCAGTCTTTCAGCCCCATTTGAGGACATCTACTTTGGACTCTGG
|
| Enzyme 12 GenBank Gene ID |
AF046026  |
| Enzyme 12 GeneCard ID |
HUT11  |
| 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
]
|
| Enzyme 12 Metabolite References |
Not Available |