|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5438 |
| Enzyme 1 Name |
D-amino-acid oxidase |
| Enzyme 1 Synonyms |
- DAAO
- DAMOX
- DAO
|
| Enzyme 1 Gene Name |
DAO |
| Enzyme 1 Protein Sequence |
>D-amino-acid oxidase
MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPN
NPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPR
ELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVN
CTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGG
IFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGP
SNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL
|
| Enzyme 1 Number of Residues |
347 |
| Enzyme 1 Molecular Weight |
39473.7 |
| Enzyme 1 Theoretical pI |
6.84 |
| Enzyme 1 GO Classification |
| Function |
- D-amino-acid oxidase activity
- binding
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-NH2 group of donors
- oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in D-amino-acid oxidase activity |
| Enzyme 1 Specific Function |
Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D- amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids |
| Enzyme 1 Pathways |
- Arginine and Proline Metabolism (map00330
)
- D-Arginine and D-ornithine Metabolism (map00472
)
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 1 Reactions |
- a D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2 [RN:R01340]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
30446  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P14920  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
OXDA_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1044 bp
ATGCGTGTGGTGGTGATTGGAGCAGGAGTCATCGGGCTGTCCACCGCCCTCTGCATCCAT
GAGCGCTACCACTCAGTCCTGCAGCCACTGCACATAAAGGTCTACGCGGACCGCTTCACC
CCACTCACCACCACCGACGTGGCTGCCGGCCTCTGGCAGCCCTACCTTTCTGACCCCAAC
AACCCACAGGAGGCGGACTGGAGCCAACAGACCTTTGACTATCTCCTGAGCCATGTCCAT
TCTCCCAACGCTGAAAACCTGGGCCTGTTCCTAATCTCGGGCTACAACCTCTTCCATGAA
GCCATTCCGGACCCTTCCTGGAAGGACACAGTTCTGGGATTTCGGAAGCTGACCCCCAGA
GAGCTGGATATGTTCCCAGATTACGGCTATGGCTGGTTCCACACAAGCCTAATTCTGGAG
GGAAAGAACTATCTACAGTGGCTGACTGAAAGGTTAACTGAGAGGGGAGTGAAGTTCTTC
CAGCGGAAAGTGGAGTCTTTTGAGGAGGTGGCAAGAGAAGGCGCAGACGTGATTGTCAAC
TGCACTGGGGTATGGGCTGGGGCGCTACAACGAGACCCCCTGCTGCAGCCAGGCCGGGGG
CAGATCATGAAGGTGGACGCCCCTTGGATGAAGCACTTCATTCTCACCCATGACCCAGAG
AGAGGCATCTACAATTCCCCGTACATCATCCCAGGGACCCAGACAGTTACTCTTGGAGGC
ATCTTCCAGTTGGGAAACTGGAGTGAACTAAACAATATCCAGGACCACAACACCATTTGG
GAAGGCTGCTGCAGACTGGAGCCCACACTGAAGAATGCAAGAATTATTGGTGAAGCAACT
GGCTTCCGGCCAGTACGCCCCCAGATTCGGCTAGAAAGAGAACAGCTTCGCACTGGACCT
TCAAACACAGAGGTCATCCACAACTATGGCCATGGAGGCTACGGGCTCACCATCCACTGG
GGATGTGCCCTGGAGGCAGCCAAGCTCTTTGGGAGAATCCTGGAAGAAAAGAAATTGTCC
AGAATGCCACCATCCCACCTCTGA
|
| Enzyme 1 GenBank Gene ID |
X13227  |
| Enzyme 1 GeneCard ID |
DAO  |
| Enzyme 1 GenAtlas ID |
DAO  |
| Enzyme 1 HGNC ID |
HGNC:2671  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
12q24 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Momoi K, Fukui K, Watanabe F, Miyake Y: Molecular cloning and sequence analysis of cDNA encoding human kidney D-amino acid oxidase. FEBS Lett. 1988 Sep 26;238(1):180-4. [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
]
- Fukui K, Miyake Y: Molecular cloning and chromosomal localization of a human gene encoding D-amino-acid oxidase. J Biol Chem. 1992 Sep 15;267(26):18631-8. [PubMed
]
- Kawazoe T, Tsuge H, Pilone MS, Fukui K: Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring. Protein Sci. 2006 Dec;15(12):2708-17. Epub 2006 Nov 6. [PubMed
]
- Kawazoe T, Tsuge H, Imagawa T, Aki K, Kuramitsu S, Fukui K: Structural basis of D-DOPA oxidation by D-amino acid oxidase: alternative pathway for dopamine biosynthesis. Biochem Biophys Res Commun. 2007 Apr 6;355(2):385-91. Epub 2007 Feb 8. [PubMed
]
- Sparey T, Abeywickrema P, Almond S, Brandon N, Byrne N, Campbell A, Hutson PH, Jacobson M, Jones B, Munshi S, Pascarella D, Pike A, Prasad GS, Sachs N, Sakatis M, Sardana V, Venkatraman S, Young MB: The discovery of fused pyrrole carboxylic acids as novel, potent D-amino acid oxidase (DAO) inhibitors. Bioorg Med Chem Lett. 2008 Jun 1;18(11):3386-91. Epub 2008 Apr 13. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5540 |
| Enzyme 2 Name |
Pyrroline-5-carboxylate reductase 2 |
| Enzyme 2 Synonyms |
- P5C reductase 2
- P5CR 2
|
| Enzyme 2 Gene Name |
PYCR2 |
| Enzyme 2 Protein Sequence |
>Pyrroline-5-carboxylate reductase 2
MSVGFIGAGQLAYALARGFTAAGILSAHKIIASSPEMNLPTVSALRKMGVNLTRSNKETV
KHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPAPKVIRC
MTNTPVVVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAY
AFMALDALADGGVKMGLPRRLAIQLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIH
ALHFLESGGFRSLLINAVEASCIRTRELQSMADQEKISPAALKKTLLDRVKLESPTVSTL
TPSSPGKLLTRSLALGGKKD
|
| Enzyme 2 Number of Residues |
320 |
| Enzyme 2 Molecular Weight |
33636.8 |
| Enzyme 2 Theoretical pI |
7.87 |
| Enzyme 2 GO Classification |
| Function |
- binding
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-NH group of donors
- oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
- pyrroline-5-carboxylate reductase activity
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glutamine family amino acid metabolic process
- metabolic process
- oxidation reduction
- proline biosynthetic process
- proline metabolic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in oxidoreductase activity |
| Enzyme 2 Specific Function |
L-proline + NAD(P)(+) = 1-pyrroline-5- carboxylate + NAD(P)H |
| Enzyme 2 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 2 Reactions |
- L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+ [RN:R01248 R01251]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
33150582  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q96C36  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
P5CR2_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>963 bp
ATGAGCGTGGGCTTCATCGGGGCCGGCCAGCTGGCTAATGCTCTGGCGCGGGGCTTCACG
GCCGCAGCATTCCTGTCGGCTCACAAGATAATAGCCAGCTCCCCAGAAATGAACCTGCCC
ACGGTGTCCGCGCTCAGGAAGATGGGTGTGAACCTGACACGCAGCAACAAGGAGACGGTG
AAGCACAGCGACGTCCTGTTTCTGGCTGTGAAGCACATTATCATCCCCTTCATCCTGGAT
GAGATTGGGGCCGACGTGCAAGCCAGACACATCGTGGTCTCCTGTGCGGCTGGTGTCACC
ATCAGCTCTGTGGAGAAGAAGCTGATGGCATTCCAGCCAGCCCCCAAAGTGATTCGCTGC
ATGACCAACACACCTGTGGTAGTGCAGGAAGGCGCTACAGTGTACGCCACGGGCACCCAT
GCCCTGGTGGAGGATGGGCAGCTCCTGGAGCAGCTCATGAGCAGCGTGGGCTTCTGCACT
GAGGTGGAAGAGGACCTCATCGATGCCGTCACGGGGCTCAGTGGCAGCGGGCCTGCCTAT
GCATTCATGGCTCTGGACGCATTGGCTGATGGTGGGGTGAAGATGGGTTTGCCACGGCGC
CTGGCAATCCAACTCGGGGCCCAGGCTTTGCTGGGAGCTGCCAAGATGCTGCTGGACTCG
GAGCAGCATCCATGCCAGCTTAAGGACAATGTCTGCTCCCCTGGGGGAGCCACCATCCAC
GCCCTGCACTTTCTAGAGAGTGGGGGCTTCCGCTCTCTGCTCATCAATGCAGTTGAGGCC
TCCTGTATCCGAACACGAGAGCTACAGTCCATGGCCGACCAAGAAAAGATCTCCCCAGCT
GCCCTTAAGAAGACCCTCTTAGACAGAGTGAAGCTGGAATCCCCCACAGTCTCCACACTG
ACCCCCTCCAGCCCAGGGAAGCTCCTCACAAGAAGCCTGGCCCTGGGAGGCAAGAAGGAC
TAA
|
| Enzyme 2 GenBank Gene ID |
AF087859  |
| Enzyme 2 GeneCard ID |
PYCR2  |
| Enzyme 2 GenAtlas ID |
PYCR2  |
| Enzyme 2 HGNC ID |
HGNC:30262  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1q42.12 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
7521 |
| Enzyme 3 Name |
Proline dehydrogenase, mitochondrial |
| Enzyme 3 Synonyms |
- Proline oxidase
- Proline oxidase 2
- p53-induced gene 6 protein
|
| Enzyme 3 Gene Name |
PRODH |
| Enzyme 3 Protein Sequence |
>Proline dehydrogenase, mitochondrial
MLEFVMREWKKSRKLLGQRLFNKLMKMTFYGHFVAGEDQESIQPLLRHYRAFGVSAILDY
GVEEDLSPEEAEHKEMESCTSAAERDGSGTNKRDKQYQAHRAFGDRRNGVISARTYFYAN
EAKCDSHMETFLRCIEASGRVSDDGFIAIKLTALGRPQFLLQFSEVLAKWRCFFHQMAVE
QGQAGLAAMDTKLEVAVLQESVAKLGIASRAEIEDWFTAETLGVSGTMDLLDWSSLIDSR
TKLSKHLVVPNAQTGQLEPLLSRFTEEEELQMTRMLQRMDVLAKKATEMGVRLMVDAEQT
YFQPAISRLTLEMQRKFNVEKPLIFNTYQCYLKDAYDNVTLDVELARREGWCFGAKLVRG
AYLAQERARAAEIGYEDPINPTYEATNAMYHRCLDYVLEELKHNAKAKVMVASHNEDTVR
FALRRMEELGLHPADHQVYFGQLLGMCDQISFPLGQAGYPVYKYVPYGPVMEVLPYLSRR
ALENSSLMKGTHRERQLLWLELLRRLRTGNLFHRPA
|
| Enzyme 3 Number of Residues |
516 |
| Enzyme 3 Molecular Weight |
59230.4 |
| Enzyme 3 Theoretical pI |
6.88 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-NH group of donors
- proline dehydrogenase activity
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glutamate biosynthetic process
- glutamate metabolic process
- glutamine family amino acid metabolic process
- metabolic process
- oxidation reduction
- proline catabolic process
- proline metabolic process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in proline dehydrogenase activity |
| Enzyme 3 Specific Function |
Converts proline to delta-1-pyrroline-5-carboxylate |
| Enzyme 3 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 3 Reactions |
- L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor [RN:R01253]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
2677802  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
O43272  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
PROD_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1551 bp
ATGCTGGAATTTGTGATGAGAGAGTGGAAAAAATCCAGGAAACTTCTAGGACAGAGGCTA
TTCAACAAGCTCATGAAGATGACCTTCTATGGGCATTTTGTAGCCGGGGAGGACCAGGAG
TCCATCCAGCCCCTGCTTCGGCACTACAGGGCCTTCGGTGTCAGCGCCATCCTGGACTAT
GGAGTGGAGGAGGACCTGAGCCCCGAGGAGGCAGAGCACAAGGAGATGGAGTCCTGCTCC
TCGGCTGCGGAGAGGGATGGCAGTGGCACGAATAAGCGGGACAAGCAATACCAGGCCCAC
CGGGCTTTCGGGGACCGCAGGAATGGTGTCATCAGTGCCCGCACCTACTTCTACGCCAAT
GAGGCCAAGTGCGACAGCCACATGGAGACATTCTTGCGCTGCATCGAAGCCTCAGGTAGA
GTCAGCGATGACGGCTTCATAGCCATTAAGCTCACAGCACTGGGGAGACCCCAGTTTCTG
CTGCAGTTCTCAGAGGTGCTGGCCAAGTGGAGGTGCTTCTTTCACCAAATGGCTGTGGAG
CAAGGGCAGGCGGGCCTGGCTGCCATGGACACCAAGCTGGAGGTGGCGGTGCTGCAGGAA
AGTGTCGCAAAGTTGGGCATCGCATCCAGGGCTGAGATTGAGGACTGGTTCACGGCAGAG
ACCCTGGGAGTGTCTGGCACCATGGACCTGCTGGACTGGAGCAGCCTCATCGACAGCAGG
ACCAAGCTGTCCAAGCACCTGGTAGTCCCCAACGCACAGACAGGACAGCTGGAGCCCCTG
CTGTCCCGGTTCACTGAGGAGGAGGAGCTACAGATGACCAGGATGCTACAGCGGATGGAT
GTCCTGGCCAAGAAAGCCACAGAGATGGGCGTGCGGCTGATGGTGGATGCCGAGCAGACC
TACTTCCAGCCGGCCATCAGCCGCCTGACGCTGGAGATGCAGCGGAAGTTCAATGTGGAG
AAGCCGCTCATCTTCAACACATACCAGTGCTACCTCAAGGATGCCTATGACAATGTGACC
CTGGACGTGGAGCTGGCTCGCCGTGAGGGCTGGTGTTTTGGGGCCAAGCTGGTGCGGGGC
GCATACCTGGCCCAGGAGCGAGCCCGTGCGGCAGAGATCGGCTATGAGGACCCCATCAAC
CCCACGTACGAGGCCACCAACGCCATGTACCACAGGTGCCTGGACTACGTGTTGGAGGAG
CTGAAGCACAACGCCAAGGCCAAGGTGATGGTGGCCTCCCACAATGAGGACACAGTGCGC
TTCGCACTGCGCAGGATGGAGGAGCTGGGCCTGCATCCTGCTGACCACCAGGTGTACTTT
GGACAGCTGCTAGGCATGTGTGACCAGATCAGCTTCCCGCTGGGCCAGGCCGGCTACCCC
GTGTACAAGTACGTGCCCTATGGCCCCGTGATGGAGGTGCTGCCCTACTTGTCCCGCCGT
GCCCTGGAGAACAGCAGCCTCATGAAGGGCACCCATCGGGAGCGGCAGTTGCTGTGGCTG
GAGCTCTTGAGGCGGCTCCGAACTGGCAACCTCTTCCATCGCCCTGCCTAG
|
| Enzyme 3 GenBank Gene ID |
U82381  |
| Enzyme 3 GeneCard ID |
PRODH  |
| Enzyme 3 GenAtlas ID |
PRODH  |
| Enzyme 3 HGNC ID |
HGNC:9453  |
| Enzyme 3 Chromosome Location |
2 |
| Enzyme 3 Locus |
22q11.21 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Campbell HD, Webb GC, Young IG: A human homologue of the Drosophila melanogaster sluggish-A (proline oxidase) gene maps to 22q11.2, and is a candidate gene for type-I hyperprolinaemia. Hum Genet. 1997 Nov;101(1):69-74. [PubMed
]
- Gogos JA, Santha M, Takacs Z, Beck KD, Luine V, Lucas LR, Nadler JV, Karayiorgou M: The gene encoding proline dehydrogenase modulates sensorimotor gating in mice. Nat Genet. 1999 Apr;21(4):434-9. [PubMed
]
- Bender HU, Almashanu S, Steel G, Hu CA, Lin WW, Willis A, Pulver A, Valle D: Functional consequences of PRODH missense mutations. Am J Hum Genet. 2005 Mar;76(3):409-20. Epub 2005 Jan 20. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- 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
]
- Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B: A model for p53-induced apoptosis. Nature. 1997 Sep 18;389(6648):300-5. [PubMed
]
- Jacquet H, Raux G, Thibaut F, Hecketsweiler B, Houy E, Demilly C, Haouzir S, Allio G, Fouldrin G, Drouin V, Bou J, Petit M, Campion D, Frebourg T: PRODH mutations and hyperprolinemia in a subset of schizophrenic patients. Hum Mol Genet. 2002 Sep 15;11(19):2243-9. [PubMed
]
- Liu H, Heath SC, Sobin C, Roos JL, Galke BL, Blundell ML, Lenane M, Robertson B, Wijsman EM, Rapoport JL, Gogos JA, Karayiorgou M: Genetic variation at the 22q11 PRODH2/DGCR6 locus presents an unusual pattern and increases susceptibility to schizophrenia. Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3717-22. Epub 2002 Mar 12. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
- Raux G, Bumsel E, Hecketsweiler B, van Amelsvoort T, Zinkstok J, Manouvrier-Hanu S, Fantini C, Breviere GM, Di Rosa G, Pustorino G, Vogels A, Swillen A, Legallic S, Bou J, Opolczynski G, Drouin-Garraud V, Lemarchand M, Philip N, Gerard-Desplanches A, Carlier M, Philippe A, Nolen MC, Heron D, Sarda P, Lacombe D, Coizet C, Alembik Y, Layet V, Afenjar A, Hannequin D, Demily C, Petit M, Thibaut F, Frebourg T, Campion D: Involvement of hyperprolinemia in cognitive and psychiatric features of the 22q11 deletion syndrome. Hum Mol Genet. 2007 Jan 1;16(1):83-91. Epub 2006 Nov 29. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
12995 |
| Enzyme 4 Name |
cDNA FLJ75752, highly similar to Homo sapiens pyrroline-5-carboxylate reductase family, member 2 |
| Enzyme 4 Synonyms |
- PYCR2, mRNA
- Pyrroline-5-carboxylate reductase family, member 2, isoform CRA_b
|
| Enzyme 4 Gene Name |
PYCR2 |
| Enzyme 4 Protein Sequence |
>cDNA FLJ75752, highly similar to Homo sapiens pyrroline-5-carboxylate reductase family, member 2
MSVGFIGAGQLAYALARGFTAAGILSAHKIIASSPEMNLPTVSALRKMGVNLTRSNKETV
KHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPAPKVIRC
MTNTPVVVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAY
AFMALDALADGGVKMGLPRRLAIQLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIH
ALHFLESGGFRSLLINAVEASCIRTRELQSMADQEKISPAALKKTLLDRVKLESPTVSTL
TPSSPGKLLTRSLALGGKKD
|
| Enzyme 4 Number of Residues |
320 |
| Enzyme 4 Molecular Weight |
33638 |
| Enzyme 4 Theoretical pI |
7.87 |
| Enzyme 4 GO Classification |
Not Available |
| Enzyme 4 General Function |
Amino acid transport and metabolism |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
Not Available |
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
158257258  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
A8K798  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
A8K798_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
Not Available |
| Enzyme 4 GenBank Gene ID |
AK291913  |
| Enzyme 4 GeneCard ID |
A8K798  |
| Enzyme 4 GenAtlas ID |
Not Available |
| Enzyme 4 HGNC ID |
Not Available |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
12996 |
| Enzyme 5 Name |
Uncharacterized protein PRODH |
| Enzyme 5 Synonyms |
Not Available |
| Enzyme 5 Gene Name |
PRODH |
| Enzyme 5 Protein Sequence |
>Uncharacterized protein PRODH
RHGSEARPARAAPLHSPLRPAVHGAGLPRAARSGPSGRARRWVGHGSAAAGARRGLRQRA
GGVPQPANLGAGAEPAGAALVRLARAAGAPRAAAVCFQETSRTEAIQQAHEDDLLWAFCS
RGGESIQPLLRHYRAFGVSAILDYGVEEDLSPEEAEHKEMESCTSAAERDGSGTNKRDKQ
YQAHWAFGDRRNGVISARTYFYANEAKCDSHMETFLRCIEASGRVSDDGFIAIKLTALGR
PQFLLQFSEVLAKWRCFFHQMAVEQGQAGLAAMDTKLEVAVLQESVAKLGIASRAEIEDW
FTAETLGVSGTMDLLDWSSLIDSRTKLSKHLVVPNAQTGQLEPLLSRFTEEEELQMTRML
QRMDVLAKKATEMGVRLMVDAEQTYFQPAISRLTLEMQRKFNVEKPLIFNTYQPHPADAY
DNVTLDVELARREGWCFGAKLVRGAYLAQERARAAEIGYEDPINPTYEATNAMYHRCLDY
VLEELKHNAKAKVMVASHNEDTVRFALRRMEELGLHPADHRVYFGQLLGMCDQISFPLGQ
AGYPVYKYVPYGPVMEVLPYLSRRALENSSLMKGTHRERQLLWLELLRRLRTGNLFHRPA
|
| Enzyme 5 Number of Residues |
600 |
| Enzyme 5 Molecular Weight |
66921 |
| Enzyme 5 Theoretical pI |
8.01 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-NH group of donors
- proline dehydrogenase activity
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- glutamate biosynthesis
- glutamate metabolism
- glutamine family amino acid metabolism
- metabolism
- physiological process
- proline catabolism
- proline metabolism
|
| Component |
| — |
|
| Enzyme 5 General Function |
Amino acid transport and metabolism |
| Enzyme 5 Specific Function |
Not Available |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
Not Available |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
A6NF53  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
A6NF53_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
Not Available |
| Enzyme 5 GenBank Gene ID |
AC007326  |
| Enzyme 5 GeneCard ID |
A6NF53  |
| Enzyme 5 GenAtlas ID |
PRODH  |
| Enzyme 5 HGNC ID |
HGNC:9453  |
| Enzyme 5 Chromosome Location |
Not Available |
| Enzyme 5 Locus |
Not Available |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
12997 |
| Enzyme 6 Name |
Melastatin 1 splicing variant |
| Enzyme 6 Synonyms |
Not Available |
| Enzyme 6 Gene Name |
MLSN1 |
| Enzyme 6 Protein Sequence |
>Melastatin 1 splicing variant
MYIRVSYDTKPDSLLHLMVKDWQLELPKLLISVHGGLQNFEMQPKLKQVFGKGLIKAAMT
TGAWIFTGGVSTGVISHVGDALKDHSSKSRGRVCAIGIAPWGIVENKEDLVGKDVTRVYQ
TMSNPLSKLSVLNNSHTHFILADNGTLGKYGAEVKLRRLLEKHISLQKINTRLGQGVPLV
GLVVEGGPNVVSIVLEYLQEEPPIPVVICDGSGRASDILSFAHKYCEEGG
|
| Enzyme 6 Number of Residues |
230 |
| Enzyme 6 Molecular Weight |
25053 |
| Enzyme 6 Theoretical pI |
8.79 |
| Enzyme 6 GO Classification |
Not Available |
| Enzyme 6 General Function |
Not Available |
| Enzyme 6 Specific Function |
Not Available |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
Not Available |
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
33235690  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q7Z4N3  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
Q7Z4N3_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
Not Available |
| Enzyme 6 GenBank Gene ID |
AB115500  |
| Enzyme 6 GeneCard ID |
Q7Z4N3  |
| Enzyme 6 GenAtlas ID |
TRPM1  |
| Enzyme 6 HGNC ID |
HGNC:7146  |
| Enzyme 6 Chromosome Location |
Not Available |
| Enzyme 6 Locus |
Not Available |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
Not Available |
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
13791 |
| Enzyme 7 Name |
Transient receptor potential cation channel subfamily M member 1 |
| Enzyme 7 Synonyms |
- Long transient receptor potential channel 1
- LTrpC1
- Melastatin-1
|
| Enzyme 7 Gene Name |
TRPM1 |
| Enzyme 7 Protein Sequence |
>Transient receptor potential cation channel subfamily M member 1
MKDSNRCCCGQFTNQHIPPLPSATPSKNEEESKQVETQPEKWSVAKHTQSYPTDSYGVLE
FQGGGYSNKAMYIRVSYDTKPDSLLHLMVKDWQLELPKLLISVHGGLQNFEMQPKLKQVF
GKGLIKAAMTTGAWIFTGGVSTGVISHVGDALKDHSSKSRGRVCAIGIAPWGIVENKEDL
VGKDVTRVYQTMSNPLSKLSVLNNSHTHFILADNGTLGKYGAEVKLRRLLEKHISLQKIN
TRLGQGVPLVGLVVEGGPNVVSIVLEYLQEEPPIPVVICDGSGRASDILSFAHKYCEEGG
IINESLREQLLVTIQKTFNYNKAQSHQLFAIIMECMKKKELVTVFRMGSEGQQDIEMAIL
TALLKGTNVSAPDQLSLALAWNRVDIARSQIFVFGPHWPPLGSLAPPTDSKATEKEKKPP
MATTKGGRGKGKGKKKGKVKEEVEEETDPRKIELLNWVNALEQAMLDALVLDRVDFVKLL
IENGVNMQHFLTIPRLEELYNTRLGPPNTLHLLVRDVKKSNLPPDYHISLIDIGLVLEYL
MGGAYRCNYTRKNFRTLYNNLFGPKRPKALKLLGMEDDEPPAKGKKKKKKKKEEEIDIDV
DDPAVSRFQYPFHELMVWAVLMKRQKMAVFLWQRGEESMAKALVACKLYKAMAHESSESD
LVDDISQDLDNNSKDFGQLALELLDQSYKHDEQIAMKLLTYELKNWSNSTCLKLAVAAKH
RDFIAHTCSQMLLTDMWMGRLRMRKNPGLKVIMGILLPPTILFLEFRTYDDFSYQTSKEN
EDGKEKEEENTDANADAGSRKGDEENEHKKQRSIPIGTKICEFYNAPIVKFWFYTISYLG
YLLLFNYVILVRMDGWPSLQEWIVISYIVSLALEKIREILMSEPGKLSQKIKVWLQEYWN
ITDLVAISTFMIGAILRLQNQPYMGYGRVIYCVDIIFWYIRVLDIFGVNKYLGPYVMMIG
KMMIDMLYFVVIMLVVLMSFGVARQAILHPEEKPSWKLARNIFYMPYWMIYGEVFADQID
LYAMEINPPCGENLYDEEGKRLPPCIPGAWLTPALMACYLLVANILLVNLLIAVFNNTFF
EVKSISNQVWKFQRYQLIMTFHDRPVLPPPMIILSHIYIIIMRLSGRCRKKREGDQEERD
RGLKLFLSDEELKRLHEFEEQCVQEHFREKEDEQQSSSDERIRVTSERVENMSMRLEEIN
ERETFMKTSLQTVDLRLAQLEELSNRMVNALENLAGIDRSDLIQARSRASSECEATYLLR
QSSINSADGYSLYRYHFNGEELLFEDTSLSTSPGTGVRKKTCSFRIKEEKDVKTHLVPEC
QNSLHLSLGTSTSATPDGSHLAVDDLKNAEESKLGPDIGISKEDDERQTDSKKEETISPS
LNKTDVIHGQDKSDVQNTQLTVETTNIEGTISYPLEETKITRYFPDETINACKTMKSRSF
VYSRGRKLVGGVNQDVEYSSITDQQLTTEWQCQVQKITRSHSTDIPYIVSEAAVQAEHKE
QFADMQDEHHVAEAIPRIPRLSLTITDRNGMENLLSVKPDQTLGFPSLRSKSLHGHPRNV
KSIQGKLDRSGHASSVSSLVIVSGMTAEEKKVKKEKASTETEC
|
| Enzyme 7 Number of Residues |
1603 |
| Enzyme 7 Molecular Weight |
182177.0 |
| Enzyme 7 Theoretical pI |
6.82 |
| Enzyme 7 GO Classification |
| Function |
- ion channel activity
- ion transmembrane transporter activity
- substrate-specific transmembrane transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- establishment of localization
- ion transport
- transmembrane transport
- transport
|
| Component |
|
|
| Enzyme 7 General Function |
Involved in ion channel activity |
| Enzyme 7 Specific Function |
Cation channel essential for the depolarizing photoresponse of retinal ON bipolar cells. It is part of the GRM6 signaling cascade. May play a role in metastasis suppression. May act as a spontaneously active, calcium-permeable plasma membrane channel |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
Not Available |
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
- 525-545
746-766
831-851
853-873
898-918
929-949
962-982
1055-1075
1106-1126
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
94538366  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q7Z4N2  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
TRPM1_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>4812 bp
ATGAAAGACTCTAACAGGTGTTGCTGTGGCCAGTTCACCAACCAGCATATCCCCCCTCTG
CCAAGTGCAACACCCAGCAAAAATGAAGAGGAAAGCAAACAGGTGGAGACTCAGCCTGAG
AAATGGTCTGTTGCCAAGCACACCCAGAGCTACCCAACAGATTCCTATGGAGTTCTTGAA
TTCCAGGGTGGCGGATATTCCAATAAAGCCATGTATATCCGTGTATCCTATGACACCAAG
CCAGACTCACTGCTCCATCTCATGGTGAAAGATTGGCAGCTGGAACTCCCCAAGCTCTTA
ATATCTGTGCATGGAGGCCTCCAGAACTTTGAGATGCAGCCCAAGCTGAAACAAGTCTTT
GGGAAAGGCCTGATCAAGGCTGCTATGACCACCGGGGCCTGGATCTTCACCGGGGGTGTC
AGCACAGGTGTTATCAGCCACGTAGGGGATGCCTTGAAAGACCACTCCTCCAAGTCCAGA
GGCCGGGTTTGTGCTATAGGAATTGCTCCATGGGGCATCGTGGAGAATAAGGAAGACCTG
GTTGGAAAGGATGTAACAAGAGTGTACCAGACCATGTCCAACCCTCTAAGTAAGCTCTCT
GTGCTCAACAACTCCCACACCCACTTCATCCTGGCTGACAATGGCACCCTGGGCAAGTAT
GGCGCCGAGGTGAAGCTGCGAAGGCTGCTGGAAAAGCACATCTCCCTGCAGAAGATCAAC
ACAAGACTGGGGCAGGGCGTGCCCCTCGTGGGTCTCGTGGTGGAGGGGGGCCCTAACGTG
GTGTCCATCGTCTTGGAATACCTGCAAGAAGAGCCTCCCATCCCTGTGGTGATTTGTGAT
GGCAGCGGACGTGCCTCGGACATCCTGTCCTTTGCGCACAAGTACTGTGAAGAAGGCGGA
ATAATAAATGAGTCCCTCAGGGAGCAGCTTCTAGTTACCATTCAGAAAACATTTAATTAT
AATAAGGCACAATCACATCAGCTGTTTGCAATTATAATGGAGTGCATGAAGAAGAAAGAA
CTCGTCACTGTGTTCAGAATGGGTTCTGAGGGCCAGCAGGACATCGAGATGGCAATTTTA
ACTGCCCTGCTGAAAGGAACAAACGTATCTGCTCCAGATCAGCTGAGCTTGGCACTGGCT
TGGAACCGCGTGGACATAGCACGAAGCCAGATCTTTGTCTTTGGGCCCCACTGGCCGCCC
CTGGGAAGCCTGGCACCCCCGACGGACAGCAAAGCCACGGAGAAGGAGAAGAAGCCACCC
ATGGCCACCACCAAGGGAGGAAGAGGAAAAGGGAAAGGCAAGAAGAAAGGGAAAGTGAAA
GAGGAAGTGGAGGAAGAAACTGACCCCCGGAAGATAGAGCTGCTGAACTGGGTGAATGCT
TTGGAGCAAGCGATGCTAGATGCTTTAGTCTTAGATCGTGTCGACTTTGTGAAGCTCCTG
ATTGAAAACGGAGTGAACATGCAACACTTTCTGACCATTCCGAGGCTGGAGGAGCTTTAT
AACACAAGACTGGGTCCACCAAACACACTTCATCTGCTGGTGAGGGATGTGAAAAAGAGC
AACCTTCCGCCTGATTACCACATCAGCCTCATAGACATCGGGCTCGTGCTGGAGTACCTC
ATGGGAGGAGCCTACCGCTGCAACTACACTCGGAAAAACTTTCGGACCCTTTACAACAAC
TTGTTTGGACCAAAGAGGCCTAAAGCTCTTAAACTTCTGGGAATGGAAGATGATGAGCCT
CCAGCTAAAGGGAAGAAAAAGAAAAAGAAGAAAAAGGAGGAAGAGATCGACATTGATGTG
GACGACCCTGCCGTGAGTCGGTTCCAGTATCCCTTCCACGAGCTGATGGTGTGGGCAGTG
CTGATGAAACGCCAGAAAATGGCAGTGTTCCTCTGGCAGCGAGGGGAAGAGAGCATGGCC
AAGGCCCTGGTGGCCTGCAAGCTCTACAAGGCCATGGCCCACGAGTCCTCCGAGAGTGAT
CTGGTGGATGACATCTCCCAGGACTTGGATAACAATTCCAAAGACTTCGGCCAGCTTGCT
TTGGAGTTATTAGACCAGTCCTATAAGCATGACGAGCAGATCGCTATGAAACTCCTGACC
TACGAGCTGAAAAACTGGAGCAACTCGACCTGCCTCAAACTGGCCGTGGCAGCCAAACAC
CGGGACTTCATTGCTCACACCTGCAGCCAGATGCTGCTGACCGATATGTGGATGGGAAGA
CTGCGGATGCGGAAGAACCCCGGCCTGAAGGTTATCATGGGGATTCTTCTACCCCCCACC
ATCTTGTTTTTGGAATTTCGCACATATGATGATTTCTCGTATCAAACATCCAAGGAAAAT
GAGGATGGCAAAGAAAAAGAAGAGGAAAATACGGATGCAAATGCAGATGCTGGCTCAAGA
AAGGGGGATGAGGAGAACGAGCACAAAAAACAGAGAAGTATTCCCATCGGAACAAAGATC
TGTGAATTCTATAACGCGCCCATTGTCAAGTTCTGGTTTTACACAATATCATACTTGGGC
TACCTGCTGCTGTTTAACTACGTCATCCTGGTGCGGATGGATGGCTGGCCGTCCCTCCAG
GAGTGGATCGTCATCTCCTACATCGTGAGCCTGGCGTTAGAGAAGATACGAGAGATCCTC
ATGTCAGAACCAGGCAAACTCAGCCAGAAAATCAAAGTTTGGCTTCAGGAGTACTGGAAC
ATCACAGATCTCGTGGCCATTTCCACATTCATGATTGGAGCAATTCTTCGCCTACAGAAC
CAGCCCTACATGGGCTATGGCCGGGTGATCTACTGTGTGGATATCATCTTCTGGTACATC
CGTGTCCTGGACATCTTTGGTGTCAACAAGTATCTGGGGCCATACGTGATGATGATTGGA
AAGATGATGATCGACATGCTGTACTTTGTGGTCATCATGCTGGTCGTGCTCATGAGTTTC
GGAGTAGCCCGTCAAGCCATTCTGCATCCAGAGGAGAAGCCCTCTTGGAAACTGGCCCGA
AACATCTTCTACATGCCCTACTGGATGATCTATGGAGAGGTGTTTGCAGACCAGATAGAC
CTCTACGCCATGGAAATTAATCCTCCTTGTGGTGAGAACCTATATGATGAGGAGGGCAAG
CGGCTTCCTCCCTGTATCCCCGGCGCCTGGCTCACTCCAGCACTCATGGCGTGCTATCTA
CTGGTCGCCAACATCCTGCTGGTGAACCTGCTGATTGCTGTGTTCAACAATACCTTCTTT
GAAGTAAAATCAATATCCAACCAGGTGTGGAAGTTCCAGCGATATCAGCTGATTATGACA
TTTCATGACAGGCCAGTCCTGCCCCCACCGATGATCATTTTAAGCCACATCTACATCATC
ATTATGCGTCTCAGCGGCCGCTGCAGGAAAAAGAGAGAAGGGGACCAAGAGGAACGGGAT
CGTGGATTGAAGCTCTTCCTTAGCGACGAGGAGCTAAAGAGGCTGCATGAGTTCGAGGAG
CAGTGCGTGCAGGAGCACTTCCGGGAGAAGGAGGATGAGCAGCAGTCGTCCAGCGACGAG
CGCATCCGGGTCACTTCTGAAAGAGTTGAAAATATGTCAATGAGGTTGGAAGAAATCAAT
GAAAGAGAAACTTTTATGAAAACTTCCCTGCAGACTGTTGACCTTCGACTTGCTCAGCTA
GAAGAATTATCTAACAGAATGGTGAATGCTCTTGAAAATCTTGCGGGAATCGACAGGTCT
GACCTGATCCAGGCACGGTCCCGGGCTTCTTCTGAATGTGAGGCAACGTATCTTCTCCGG
CAAAGCAGCATCAATAGCGCTGATGGCTACAGCTTGTATCGATATCATTTTAACGGAGAA
GAGTTATTATTTGAGGATACATCTCTCTCCACGTCACCAGGGACAGGAGTCAGGAAAAAA
ACCTGTTCCTTCCGTATAAAGGAAGAGAAGGACGTGAAAACGCACCTAGTCCCAGAATGT
CAGAACAGTCTTCACCTTTCACTGGGCACAAGCACATCAGCAACCCCAGATGGCAGTCAC
CTTGCAGTAGATGACTTAAAGAACGCTGAAGAGTCAAAATTAGGTCCAGATATTGGGATT
TCAAAGGAAGATGATGAAAGACAGACAGACTCTAAAAAAGAAGAAACTATTTCCCCAAGT
TTAAATAAAACAGATGTGATACATGGACAGGACAAATCAGATGTTCAAAACACTCAGCTA
ACAGTGGAAACGACAAATATAGAAGGCACTATTTCCTATCCCCTGGAAGAAACCAAAATT
ACACGCTATTTCCCCGATGAAACGATCAATGCTTGTAAAACAATGAAGTCCAGAAGCTTC
GTCTATTCCCGGGGAAGAAAGCTGGTCGGTGGGGTTAACCAGGATGTAGAGTACAGTTCA
ATCACGGACCAGCAATTGACGACGGAATGGCAATGCCAAGTTCAAAAGATCACGCGCTCT
CATAGCACAGATATTCCTTACATTGTGTCGGAAGCTGCAGTGCAAGCTGAGCATAAAGAG
CAGTTTGCAGATATGCAAGATGAACACCATGTCGCTGAAGCAATTCCTCGAATCCCTCGC
TTGTCCCTAACCATTACTGACAGAAATGGGATGGAAAACTTACTGTCTGTGAAGCCAGAT
CAAACTTTGGGATTCCCATCTCTCAGGTCAAAAAGTTTACATGGACATCCTAGGAATGTG
AAATCCATTCAGGGAAAGTTAGACAGATCTGGACATGCCAGTAGTGTAAGCAGCTTAGTA
ATTGTGTCTGGAATGACAGCAGAAGAAAAAAAGGTTAAGAAAGAGAAAGCTTCCACAGAA
ACTGAATGCTAG
|
| Enzyme 7 GenBank Gene ID |
NM_002420.4  |
| Enzyme 7 GeneCard ID |
TRPM1  |
| Enzyme 7 GenAtlas ID |
TRPM1  |
| Enzyme 7 HGNC ID |
HGNC:7146  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
15q13.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Hunter JJ, Shao J, Smutko JS, Dussault BJ, Nagle DL, Woolf EA, Holmgren LM, Moore KJ, Shyjan AW: Chromosomal localization and genomic characterization of the mouse melastatin gene (Mlsn1). Genomics. 1998 Nov 15;54(1):116-23. [PubMed
]
- Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed
]
- Duncan LM, Deeds J, Hunter J, Shao J, Holmgren LM, Woolf EA, Tepper RI, Shyjan AW: Down-regulation of the novel gene melastatin correlates with potential for melanoma metastasis. Cancer Res. 1998 Apr 1;58(7):1515-20. [PubMed
]
- Fang D, Setaluri V: Expression and Up-regulation of alternatively spliced transcripts of melastatin, a melanoma metastasis-related gene, in human melanoma cells. Biochem Biophys Res Commun. 2000 Dec 9;279(1):53-61. [PubMed
]
- Xu XZ, Moebius F, Gill DL, Montell C: Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform. Proc Natl Acad Sci U S A. 2001 Sep 11;98(19):10692-7. Epub 2001 Sep 4. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Li Z, Sergouniotis PI, Michaelides M, Mackay DS, Wright GA, Devery S, Moore AT, Holder GE, Robson AG, Webster AR: Recessive mutations of the gene TRPM1 abrogate ON bipolar cell function and cause complete congenital stationary night blindness in humans. Am J Hum Genet. 2009 Nov;85(5):711-9. Epub 2009 Oct 29. [PubMed
]
- van Genderen MM, Bijveld MM, Claassen YB, Florijn RJ, Pearring JN, Meire FM, McCall MA, Riemslag FC, Gregg RG, Bergen AA, Kamermans M: Mutations in TRPM1 are a common cause of complete congenital stationary night blindness. Am J Hum Genet. 2009 Nov;85(5):730-6. Epub 2009 Nov 5. [PubMed
]
- Audo I, Kohl S, Leroy BP, Munier FL, Guillonneau X, Mohand-Said S, Bujakowska K, Nandrot EF, Lorenz B, Preising M, Kellner U, Renner AB, Bernd A, Antonio A, Moskova-Doumanova V, Lancelot ME, Poloschek CM, Drumare I, Defoort-Dhellemmes S, Wissinger B, Leveillard T, Hamel CP, Schorderet DF, De Baere E, Berger W, Jacobson SG, Zrenner E, Sahel JA, Bhattacharya SS, Zeitz C: TRPM1 is mutated in patients with autosomal-recessive complete congenital stationary night blindness. Am J Hum Genet. 2009 Nov;85(5):720-9. Epub 2009 Nov 5. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |