|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5393 |
| Enzyme 1 Name |
Amine oxidase [flavin-containing] B |
| Enzyme 1 Synonyms |
- Monoamine oxidase type B
- MAO-B
|
| Enzyme 1 Gene Name |
MAOB |
| Enzyme 1 Protein Sequence |
>Amine oxidase [flavin-containing] B
MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSY
VGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWR
TMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEV
SALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQ
TRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVY
YKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEER
LKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDR
IYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTT
FLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV
|
| Enzyme 1 Number of Residues |
520 |
| Enzyme 1 Molecular Weight |
58762.5 |
| Enzyme 1 Theoretical pI |
7.55 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in oxidoreductase activity |
| Enzyme 1 Specific Function |
Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2 [RN:R01853]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P27338  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
AOFB_HUMAN  |
| Enzyme 1 PDB ID |
2BK3  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1560 bp
ATGAGCAACAAATGCGACGTGGTCGTGGTGGGGGGCGGCATCTCAGGTATGGCAGCAGCC
AAACTTCTGCATGACTCTGGACTGAATGTGGTTGTTCTGGAAGCCCGGGACCGTGTGGGA
GGCAGGACTTACACTCTTAGGAACCAAAAGGTTAAATATGTGGACCTTGGAGGATCCTAT
GTTGGACCAACCCAGAATCGTATCTTGAGATTAGCCAAGGAGCTAGGATTGGAGACCTAC
AAAGTGAATGAGGTTGAGCGTCTGATCCACCATGTAAAGGGCAAATCATACCCCTTCAGG
GGGCCATTCCCACCTGTATGGAATCCAATTACCTACTTAGATCATAACAACTTTTGGAGG
ACAATGGATGACATGGGGCGAGAGATTCCGAGTGATGCCCCATGGAAGGCTCCCCTTGCA
GAAGAGTGGGACAACATGACAATGAAGGAGCTACTGGACAAGCTCTGCTGGACTGAATCT
GCAAAGCAGCTTGCCACTCTCTTTGTGAACCTGTGTGTCACTGCAGAGACCCATGAGGTC
TCTGCTCTCTGGTTCCTGTGGTATGTGAAGCAGTGTGGAGGCACAACAAGAATCATCTCG
ACAACAAATGGAGGACAGGAGAGGAAATTTGTGGGCGGATCTGGTCAAGTGAGTGAGCGG
ATAATGGACCTCCTTGGAGACCGAGTGAAGCTGGAGAGGCCTGTGATCTACATTGACCAG
ACAAGAGAAAATGTCCTTGTGGAGACCCTAAACCATGAGATGTATGAGGCTAAATATGTG
ATTAGTGCTATTCCTCCTACTCTGGGCATGAAGATTCACTTCAATCCCCCTCTGCCAATG
ATGAGAAACCAGATGATCACTCGTGTGCCTTTGGGTTCAGTCATCAAGTGTATAGTTTAT
TATAAAGAGCCTTTCTGGAGGAAAAAGGATTACTGTGGAACCATGATTATTGATGGAGAA
GAAGCTCCAGTTGCCTACACGTTGGATGATACCAAACCTGAAGGCAACTATGCTGCCATA
ATGGGATTTATCCTGGCCCACAAAGCCAGAAAACTGGCACGTCTTACCAAAGAGGAAAGG
TTGAAGAAACTTTGTGAACTCTATGCCAAGGTTCTGGGTTCCCTAGAAGCTCTGGAGCCA
GTGCATTATGAAGAAAAGAACTGGTGTGAGGAGCAGTACTCTGGGGGCTGCTACACAACT
TATTTCCCCCCTGGGATCCTGACTCAATATGGAAGGGTTCTACGCCAGCCAGTGGACAGG
ATTTACTTTGCAGGCACCGAGACTGCCACACACTGGAGCGGCTACATGGAGGGGGCTGTA
GAGGCCGGGGAGAGAGCAGCCCGAGAGATCCTGCATGCCATGGGGAAGATTCCAGAGGAT
GAAATCTGGCAGTCAGAACCAGAGTCTGTGGATGTCCCTGCACAGCCCATCACCACCACC
TTTTTGGAGAGACATTTGCCCTCCGTGCCAGGCCTGCTCAGGCTGATTGGATTGACCACC
ATCTTTTCAGCAACGGCTCTTGGCTTCCTGGCCCACAAAAGGGGGCTACTTGTGAGAGTC
|
| Enzyme 1 GenBank Gene ID |
S62734  |
| Enzyme 1 GeneCard ID |
MAOB  |
| Enzyme 1 GenAtlas ID |
MAOB  |
| Enzyme 1 HGNC ID |
HGNC:6834  |
| Enzyme 1 Chromosome Location |
Not Available |
| Enzyme 1 Locus |
Not Available |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Grimsby J, Chen K, Wang LJ, Lan NC, Shih JC: Human monoamine oxidase A and B genes exhibit identical exon-intron organization. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3637-41. [PubMed
]
- Bach AW, Lan NC, Johnson DL, Abell CW, Bembenek ME, Kwan SW, Seeburg PH, Shih JC: cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4934-8. [PubMed
]
- Chen K, Wu HF, Shih JC: The deduced amino acid sequences of human platelet and frontal cortex monoamine oxidase B are identical. J Neurochem. 1993 Jul;61(1):187-90. [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
]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed
]
- Zhu QS, Grimsby J, Chen K, Shih JC: Promoter organization and activity of human monoamine oxidase (MAO) A and B genes. J Neurosci. 1992 Nov;12(11):4437-46. [PubMed
]
- Newton-Vinson P, Hubalek F, Edmondson DE: High-level expression of human liver monoamine oxidase B in Pichia pastoris. Protein Expr Purif. 2000 Nov;20(2):334-45. [PubMed
]
- Cesura AM, Gottowik J, Lahm HW, Lang G, Imhof R, Malherbe P, Rothlisberger U, Da Prada M: Investigation on the structure of the active site of monoamine oxidase-B by affinity labeling with the selective inhibitor lazabemide and by site-directed mutagenesis. Eur J Biochem. 1996 Mar 15;236(3):996-1002. [PubMed
]
- Wu HF, Chen K, Shih JC: Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines. Mol Pharmacol. 1993 Jun;43(6):888-93. [PubMed
]
- Binda C, Newton-Vinson P, Hubalek F, Edmondson DE, Mattevi A: Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nat Struct Biol. 2002 Jan;9(1):22-6. [PubMed
]
- Binda C, Li M, Hubalek F, Restelli N, Edmondson DE, Mattevi A: Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures. Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):9750-5. Epub 2003 Aug 11. [PubMed
]
- Binda C, Hubalek F, Li M, Herzig Y, Sterling J, Edmondson DE, Mattevi A: Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class. J Med Chem. 2004 Mar 25;47(7):1767-74. [PubMed
]
- Hubalek F, Binda C, Khalil A, Li M, Mattevi A, Castagnoli N, Edmondson DE: Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors. J Biol Chem. 2005 Apr 22;280(16):15761-6. Epub 2005 Feb 14. [PubMed
]
- Binda C, Hubalek F, Li M, Herzig Y, Sterling J, Edmondson DE, Mattevi A: Binding of rasagiline-related inhibitors to human monoamine oxidases: a kinetic and crystallographic analysis. J Med Chem. 2005 Dec 29;48(26):8148-54. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5401 |
| Enzyme 2 Name |
Amine oxidase [flavin-containing] A |
| Enzyme 2 Synonyms |
- Monoamine oxidase type A
- MAO-A
|
| Enzyme 2 Gene Name |
MAOA |
| Enzyme 2 Protein Sequence |
>Amine oxidase [flavin-containing] A
MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHV
DYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIA
YLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNI
NVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKL
NHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPM
GAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADR
LAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYG
RVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKD
VPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS
|
| Enzyme 2 Number of Residues |
527 |
| Enzyme 2 Molecular Weight |
59681.3 |
| Enzyme 2 Theoretical pI |
7.96 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in oxidoreductase activity |
| Enzyme 2 Specific Function |
Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2 [RN:R01853]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
187355  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P21397  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
AOFA_HUMAN  |
| Enzyme 2 PDB ID |
1O5W  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1584 bp
ATGGAGAATCAAGAGAAGGCGAGTATCGCGGGCCACATGTTCGACGTAGTCGTGATCGGA
GGTGGCATTTCAGGACTATCTGCTGCCAAACTCTTGACTGAATATGGCGTTAGTGTTTTG
GTTTTAGAAGCTCGGGACAGGGTTGGAGGAAGAACATATACTATAAGGAATGAGCATGTT
GATTACGTAGATGTTGGTGGAGCTTATGTGGGACCAACCCAAAACAGAATCTTACGCTTG
TCTAAGGAGCTGGGCATAGAGACTTACAAAGTGAATGTCAGTGAGCGTCTCGTTCAATAT
GTCAAGGGGAAAACATATCCATTTCGGGGCGCCTTTCCACCAGTATGGAATCCCATTGCA
TATTTGGATTACAATAATCTGTGGAGGACAATAGATAACATGGGGAAGGAGATTCCAACT
GATGCACCCTGGGAGGCTCAACATGCTGACAAATGGGACAAAATGACCATGAAAGAGCTC
ATTGACAAAATCTGCTGGACAAAGACTGCTAGGCGGTTTGCTTATCTTTTTGTGAATATC
AATGTGACCTCTGAGCCTCACGAAGTGTCTGCCCTGTGGTTCTTGTGGTATGTGAAGCAG
TGCGGGGGCACCACTCGGATATTCTCTGTCACCAATGGTGGCCAGGAACGGAAGTTTGTA
GGTGGATCTGGTCAAGTGAGCGAACGGATAATGGACCTCCTCGGAGACCAAGTGAAGCTG
AACCATCCTGTCACTCACGTTGACCAGTCAAGTGACAACATCATCATAGAGACGCTGAAC
CATGAACATTATGAGTGCAAATACGTAATTAATGCGATCCCTCCGACCTTGACTGCCAAG
ATTCACTTCAGACCAGAGCTTCCAGCAGAGAGAAACCAGTTAATTCAGCGTCTTCCAATG
GGAGCTGTCATTAAGTGCATGATGTATTACAAGGAGGCCTTCTGGAAGAAGAAGGATTAC
TGTGGCTGCATGATCATTGAAGATGAAGATGCTCCAATTTCAATAACCTTGGATGACACC
AAGCCAGATGGGTCACTGCCTGCCATCATGGGCTTCATTCTTGCCCGGAAAGCTGATCGA
CTTGCTAAGCTACATAAGGAAATAAGGAAGAAGAAAATCTGTGAGCTCTATGCCAAAGTG
CTGGGATCCCAAGAAGCTTTACATCCAGTGCATTATGAAGAGAAGAACTGGTGTGAGGAG
CAGTACTCTGGGGGCTGCTACACGGCCTACTTCCCTCCTGGGATCATGACTCAATATGGA
AGGGTGATTCGTCAACCCGTGGGCAGGATTTTCTTTGCGGGCACAGAGACTGCCACAAAG
TGGAGCGGCTACATGGAAGGGGCAGTTGAGGCTGGAGAACGAGCAGCTAGGGAGGTCTTA
AATGGTCTCGGGAAGGTGACCGAGAAAGACATCTGGGTACAAGAACCTGAATCAAAGGAC
GTTCCAGCGGTAGAAATCACCCACACCTTCTGGGAAAGGAACCTGCCCTCTGTTTCTGGC
CTGCTGAAGATCATTGGATTTTCCACATCAGTAACTGCCCTGGGGTTTGTGCTGTACAAA
TACAAGCTCCTGCCACGGTCTTGA
|
| Enzyme 2 GenBank Gene ID |
M69226  |
| Enzyme 2 GeneCard ID |
MAOA  |
| Enzyme 2 GenAtlas ID |
MAOA  |
| Enzyme 2 HGNC ID |
HGNC:6833  |
| Enzyme 2 Chromosome Location |
Not Available |
| Enzyme 2 Locus |
Not Available |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Hsu YP, Weyler W, Chen S, Sims KB, Rinehart WB, Utterback MC, Powell JF, Breakefield XO: Structural features of human monoamine oxidase A elucidated from cDNA and peptide sequences. J Neurochem. 1988 Oct;51(4):1321-4. [PubMed
]
- Bach AW, Lan NC, Johnson DL, Abell CW, Bembenek ME, Kwan SW, Seeburg PH, Shih JC: cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4934-8. [PubMed
]
- Chen ZY, Hotamisligil GS, Huang JK, Wen L, Ezzeddine D, Aydin-Muderrisoglu N, Powell JF, Huang RH, Breakefield XO, Craig I, et al.: Structure of the human gene for monoamine oxidase type A. Nucleic Acids Res. 1991 Aug 25;19(16):4537-41. [PubMed
]
- Grimsby J, Chen K, Wang LJ, Lan NC, Shih JC: Human monoamine oxidase A and B genes exhibit identical exon-intron organization. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3637-41. [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
]
- Zhu QS, Grimsby J, Chen K, Shih JC: Promoter organization and activity of human monoamine oxidase (MAO) A and B genes. J Neurosci. 1992 Nov;12(11):4437-46. [PubMed
]
- Denney RM: The promoter of the human monoamine oxidase A gene. Prog Brain Res. 1995;106:57-66. [PubMed
]
- Denney RM, Sharma A, Dave SK, Waguespack A: A new look at the promoter of the human monoamine oxidase A gene: mapping transcription initiation sites and capacity to drive luciferase expression. J Neurochem. 1994 Sep;63(3):843-56. [PubMed
]
- Chen SA, Weyler W: Partial amino acid sequence analysis of human placenta monoamine oxidase A and bovine liver monoamine oxidase B. Biochem Biophys Res Commun. 1988 Oct 14;156(1):445-50. [PubMed
]
- Weyler W: Monoamine oxidase A from human placenta and monoamine oxidase B from bovine liver both have one FAD per subunit. Biochem J. 1989 Jun 15;260(3):725-9. [PubMed
]
- Li M, Hubalek F, Newton-Vinson P, Edmondson DE: High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae. Protein Expr Purif. 2002 Feb;24(1):152-62. [PubMed
]
- Wu HF, Chen K, Shih JC: Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines. Mol Pharmacol. 1993 Jun;43(6):888-93. [PubMed
]
- De Colibus L, Li M, Binda C, Lustig A, Edmondson DE, Mattevi A: Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12684-9. Epub 2005 Aug 29. [PubMed
]
- Brunner HG, Nelen M, Breakefield XO, Ropers HH, van Oost BA: Abnormal behavior associated with a point mutation in the structural gene for monoamine oxidase A. Science. 1993 Oct 22;262(5133):578-80. [PubMed
]
- Son SY, Ma J, Kondou Y, Yoshimura M, Yamashita E, Tsukihara T: Structure of human monoamine oxidase A at 2.2-A resolution: the control of opening the entry for substrates/inhibitors. Proc Natl Acad Sci U S A. 2008 Apr 15;105(15):5739-44. Epub 2008 Apr 7. [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
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5485 |
| Enzyme 3 Name |
Dopamine beta-hydroxylase |
| Enzyme 3 Synonyms |
- Dopamine beta-monooxygenase
- Soluble dopamine beta-hydroxylase
|
| Enzyme 3 Gene Name |
DBH |
| Enzyme 3 Protein Sequence |
>Dopamine beta-hydroxylase
MPALSRWASLPGPSMREAAFMYSTAVAIFLVILVAALQGSAPRESPLPYHIPLDPEGSLE
LSWNVSYTQEAIHFQLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSDQK
GQIHLDPQQDYQLLQVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSL
EAINGSGLQMGLQRVQLLKPNIPEPELPSDACTMEVQAPNIQIPSQETTYWCYIKELPKG
FSRHHIIKYEPIVTKGNEALVHHMEVFQCAPEMDSVPHFSGPCDSKMKPDRLNYCRHVLA
AWALGAKAFYYPEEAGLAFGGPGSSRYLRLEVHYHNPLVIEGRNDSSGIRLYYTAKLRRF
NAGIMELGLVYTPVMAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKV
VTVLVRDGREWEIVNQDNHYSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGG
FGILEEMCVNYVHYYPQTQLELCKSAVDAGFLQKYFHLINRFNNEDVCTCPQASVSQQFT
SVPWNSFNRDVLKALYSFAPISMHCNKSSAVRFQGEWNLQPLPKVISTLEEPTPQCPTSQ
GRSPAGPTVVSIGGGKG
|
| Enzyme 3 Number of Residues |
617 |
| Enzyme 3 Molecular Weight |
69064.4 |
| Enzyme 3 Theoretical pI |
6.39 |
| Enzyme 3 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- copper ion binding
- dopamine beta-monooxygenase activity
- ion binding
- metal ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
- transition metal ion binding
|
| Process |
- catecholamine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular amino acid metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- cellular process
- histidine catabolic process
- histidine family amino acid metabolic process
- histidine metabolic process
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in monooxygenase activity |
| Enzyme 3 Specific Function |
Conversion of dopamine to noradrenaline |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- 3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O [RN:R02535]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
123230459  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P09172  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
DOPO_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1854 bp
ATGCCCGCCCTCAGTCGCTGGGCCAGCCTGCCCGGCCCCAGCATGCGGGAGGCAGCCTTC
ATGTACAGCACAGCAGTGGCCATCTTCCTGGTCATCCTGGTGGCCGCACTGCAGGGCTCG
GCTCCCCGTGAGAGCCCCCTCCCCTATCACATCCCCCTGGACCCGGAGGGGTCCCTGGAG
CTCTCATGGAATGTCAGCTACACCCAGGAGGCCATCCATTTCCAGCTCCTGGTGCGGAGG
CTCAAGGCTGGCGTCCTGTTTGGGATGTCCGACCGTGGCGAGCTTGAGAACGCAGATCTC
GTGGTGCTCTGGACCGATGGGGACACTGCCTATTTTGCGGACGCCTGGAGTGACCAGAAG
GGGCAGATCCACCTGGATCCCCAGCAGGACTACCAGCTGCTGCAGGTGCAGAGGACCCCA
GAAGGCCTGACCCTGCTTTTCAAGAGGCCCTTTGGCACCTGCGACCCCAAGGATTACCTC
ATTGAAGACGGCACTGTCCACTTGGTCTACGGGATCCTGGAGGAGCCGTTCCGGTCACTG
GAGGCCATCAACGGCTCGGGCCTGCAGATGGGGCTGCAGAGGGTGCAGCTCCTGAAGCCC
AATATCCCCGAACCGGAGTTGCCCTCAGACGCGTGCACCATGGAGGTCCAAGCTCCCAAT
ATCCAGATCCCCAGCCAGGAGACCACGTACTGGTGCTACATTAAGGAGCTTCCAAAGGGC
TTCTCTCGGCACCACATTATCAAGTACGAGCCCATCGTCACCAAGGGCAATGAGGCCCTT
GTCCACCACATGGAAGTCTTCCAGTGCGCCCCCGAGATGGACAGCGTCCCCCACTTCAGC
GGGCCCTGCGACTCCAAGATGAAACCCGACCGCCTCAACTACTGCCGCCACGTGCTGGCC
GCCTGGGCCCTGGGTGCCAAGGCATTTTACTACCCAGAGGAAGCCGGCCTTGCCTTCGGG
GGTCCAGGGTCCTCCAGATATCTCCGCCTGGAAGTTCACTACCACAACCCACTGGTGATA
GAAGGACGAAACGACTCCTCAGGCATCCGCTTGTACTACACAGCCAAGCTGCGGCGCTTC
AACGCGGGGATCATGGAGCTGGGACTGGTGTACACGCCAGTGATGGCCATTCCACCACGG
GAGACCGCCTTCATCCTCACTGGCTACTGCACGGACAAGTGCACCCAGCTGGCACTGCCT
CCCTCCGGGATCCACATCTTCGCCTCTCAGCTCCACACACACCTGACTGGGAGAAAGGTG
GTCACAGTGCTGGTCCGGGACGGCCGGGAGTGGGAGATCGTGAACCAGGACAATCACTAC
AGCCCTCACTTCCAGGAGATCCGCATGTTGAAGAAGGTCGTGTCGGTCCATCCGGGAGAT
GTGCTCATCACCTCCTGCACGTACAACACAGAAGACCGGGAGCTGGCCACAGTGGGGGGC
TTCGGGATCCTGGAGGAGATGTGTGTCAACTACGTGCACTACTACCCCCAGACGCAGCTG
GAGCTCTGCAAGAGCGCTGTGGACGCCGGCTTCCTGCAGAAGTACTTCCACCTCATCAAC
AGGTTCAACAACGAGGATGTCTGCACCTGCCCTCAGGCGTCCGTGTCTCAGCAGTTCACC
TCTGTTCCCTGGAACTCCTTCAACCGCGACGTACTGAAGGCCCTGTACAGCTTCGCGCCC
ATCTCCATGCACTGCAACAAGTCCTCAGCCGTCCGCTTCCAGGGTGAATGGAACCTGCAG
CCCCTGCCCAAGGTCATCTCCACACTGGAAGAGCCCACCCCACAGTGCCCCACCAGCCAG
GGCCGAAGCCCTGCTGGCCCCACCGTTGTCAGCATTGGTGGGGGCAAAGGCTGA
|
| Enzyme 3 GenBank Gene ID |
AL365494  |
| Enzyme 3 GeneCard ID |
DBH  |
| Enzyme 3 GenAtlas ID |
DBH  |
| Enzyme 3 HGNC ID |
HGNC:2689  |
| Enzyme 3 Chromosome Location |
9 |
| Enzyme 3 Locus |
9q34 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Lamouroux A, Vigny A, Faucon Biguet N, Darmon MC, Franck R, Henry JP, Mallet J: The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme. EMBO J. 1987 Dec 20;6(13):3931-7. [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
]
- Kobayashi K, Kurosawa Y, Fujita K, Nagatsu T: Human dopamine beta-hydroxylase gene: two mRNA types having different 3'-terminal regions are produced through alternative polyadenylation. Nucleic Acids Res. 1989 Feb 11;17(3):1089-102. [PubMed
]
- Li B, Tsing S, Kosaka AH, Nguyen B, Osen EG, Bach C, Chan H, Barnett J: Expression of human dopamine beta-hydroxylase in Drosophila Schneider 2 cells. Biochem J. 1996 Jan 1;313 ( Pt 1):57-64. [PubMed
]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed
]
- Williams HJ, Bray N, Murphy KC, Cardno AG, Jones LA, Owen MJ: No evidence for allelic association between schizophrenia and a functional variant of the human dopamine beta-hydroxylase gene (DBH). Am J Med Genet. 1999 Oct 15;88(5):557-9. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
- Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed
]
- Kim CH, Zabetian CP, Cubells JF, Cho S, Biaggioni I, Cohen BM, Robertson D, Kim KS: Mutations in the dopamine beta-hydroxylase gene are associated with human norepinephrine deficiency. Am J Med Genet. 2002 Mar 1;108(2):140-7. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5504 |
| Enzyme 4 Name |
Catechol O-methyltransferase |
| Enzyme 4 Synonyms |
Not Available |
| Enzyme 4 Gene Name |
COMT |
| Enzyme 4 Protein Sequence |
>Catechol O-methyltransferase
MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRIL
NHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCG
YSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKY
DVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFE
CTHYQSFLEYREVVDGLEKAIYKGPGSEAGP
|
| Enzyme 4 Number of Residues |
271 |
| Enzyme 4 Molecular Weight |
30036.8 |
| Enzyme 4 Theoretical pI |
5.15 |
| Enzyme 4 GO Classification |
| Function |
- O-methyltransferase activity
- binding
- catalytic activity
- catechol O-methyltransferase activity
- cation binding
- ion binding
- magnesium ion binding
- metal ion binding
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- biological regulation
- catecholamine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- metabolic process
- neurotransmitter catabolic process
- neurotransmitter metabolic process
- regulation of biological quality
- regulation of neurotransmitter levels
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in magnesium ion binding |
| Enzyme 4 Specific Function |
Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol [RN:R07330]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
180920  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P21964  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
COMT_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>816 bp
ATGCCGGAGGCCCCGCCTCTGCTGTTGGCAGCTGTGTTGCTGGGCCTGGTGCTGCTGGTG
GTGCTGCTGCTGCTTCTGAGGCACTGGGGCTGGGGCCTGTGCCTTATCGGCTGGAACGAG
TTCATCCTGCAGCCCATCCACAACCTGCTCATGGGTGACACCAAGGAGCAGCGCATCCTG
AACCACGTGCTGCAGCATGCGGAGCCCGGGAACGCACAGAGCGTGCTGGAGGCCATTGAC
ACCTACTGCGAGCAGAAGGAGTGGGCCATGAACGTGGGCGACAAGAAAGGCAAGATCGTG
GACGCCGTGATTCAGGAGCACCAGCCCTCCGTGCTGCTGGAGCTGGGGGCCTACTGTGGC
TACTCAGCTGTGCGCATGGCCCGCCTGCTGTCACCAGGGGCGAGGCTCATCACCATCGAG
ATCAACCCCGACTGTGCCGCCATCACCCAGCGGATGGTGGATTTCGCTGGCGTGAAGGAC
AAGGTCACCCTTGTGGTTGGAGCGTCCCAGGACATCATCCCCCAGCTGAAGAAGAAGTAT
GATGTGGACACACTGGACATGGTCTTCCTCGACCACTGGAAGGACCGGTACCTGCCGGAC
ACGCTTCTCTTGGAGGAATGTGGCCTGCTGCGGAAGGGGACAGTGCTACTGGCTGACAAC
GTGATCTGCCCAGGTGCGCCAGACTTCCTAGCACACGTGCGCGGGAGCAGCTGCTTTGAG
TGCACACACTACCAATCGTTCCTGGAATACAGGGAGGTGGTGGACGGCCTGGAGAAGGCC
ATCTACAAGGGCCCAGGCAGCGAAGCAGGGCCCTGA
|
| Enzyme 4 GenBank Gene ID |
M65212  |
| Enzyme 4 GeneCard ID |
COMT  |
| Enzyme 4 GenAtlas ID |
COMT  |
| Enzyme 4 HGNC ID |
HGNC:2228  |
| Enzyme 4 Chromosome Location |
2 |
| Enzyme 4 Locus |
22q11.21-q11.23|22q11.21 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Lundstrom K, Salminen M, Jalanko A, Savolainen R, Ulmanen I: Cloning and characterization of human placental catechol-O-methyltransferase cDNA. DNA Cell Biol. 1991 Apr;10(3):181-9. [PubMed
]
- Bertocci B, Miggiano V, Da Prada M, Dembic Z, Lahm HW, Malherbe P: Human catechol-O-methyltransferase: cloning and expression of the membrane-associated form. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1416-20. [PubMed
]
- Tenhunen J, Salminen M, Lundstrom K, Kiviluoto T, Savolainen R, Ulmanen I: Genomic organization of the human catechol O-methyltransferase gene and its expression from two distinct promoters. Eur J Biochem. 1994 Aug 1;223(3):1049-59. [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
]
- Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [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
]
- Vilbois F, Caspers P, da Prada M, Lang G, Karrer C, Lahm HW, Cesura AM: Mass spectrometric analysis of human soluble catechol O-methyltransferase expressed in Escherichia coli. Identification of a product of ribosomal frameshifting and of reactive cysteines involved in S-adenosyl-L-methionine binding. Eur J Biochem. 1994 Jun 1;222(2):377-86. [PubMed
]
- Tilgmann C, Kalkkinen N: Purification and partial sequence analysis of the soluble catechol-O-methyltransferase from human placenta: comparison to the rat liver enzyme. Biochem Biophys Res Commun. 1991 Jan 31;174(2):995-1002. [PubMed
]
- Ulmanen I, Lundstrom K: Cell-free synthesis of rat and human catechol O-methyltransferase. Insertion of the membrane-bound form into microsomal membranes in vitro. Eur J Biochem. 1991 Dec 18;202(3):1013-20. [PubMed
]
- Rutherford K, Le Trong I, Stenkamp RE, Parson WW: Crystal structures of human 108V and 108M catechol O-methyltransferase. J Mol Biol. 2008 Jun 27;380(1):120-30. Epub 2008 Apr 23. [PubMed
]
- Lachman HM, Papolos DF, Saito T, Yu YM, Szumlanski CL, Weinshilboum RM: Human catechol-O-methyltransferase pharmacogenetics: description of a functional polymorphism and its potential application to neuropsychiatric disorders. Pharmacogenetics. 1996 Jun;6(3):243-50. [PubMed
]
- Tiihonen J, Hallikainen T, Lachman H, Saito T, Volavka J, Kauhanen J, Salonen JT, Ryynanen OP, Koulu M, Karvonen MK, Pohjalainen T, Syvalahti E, Hietala J: Association between the functional variant of the catechol-O-methyltransferase (COMT) gene and type 1 alcoholism. Mol Psychiatry. 1999 May;4(3):286-9. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
- Lee SG, Joo Y, Kim B, Chung S, Kim HL, Lee I, Choi B, Kim C, Song K: Association of Ala72Ser polymorphism with COMT enzyme activity and the risk of schizophrenia in Koreans. Hum Genet. 2005 Mar;116(4):319-28. Epub 2005 Jan 12. [PubMed
]
- Rutherford K, Alphandery E, McMillan A, Daggett V, Parson WW: The V108M mutation decreases the structural stability of catechol O-methyltransferase. Biochim Biophys Acta. 2008 Jul-Aug;1784(7-8):1098-105. Epub 2008 Apr 24. [PubMed
]
- Annerbrink K, Westberg L, Nilsson S, Rosmond R, Holm G, Eriksson E: Catechol O-methyltransferase val158-met polymorphism is associated with abdominal obesity and blood pressure in men. Metabolism. 2008 May;57(5):708-11. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5510 |
| Enzyme 5 Name |
Aromatic-L-amino-acid decarboxylase |
| Enzyme 5 Synonyms |
- AADC
- DOPA decarboxylase
- DDC
|
| Enzyme 5 Gene Name |
DDC |
| Enzyme 5 Protein Sequence |
>Aromatic-L-amino-acid decarboxylase
MNASEFRRRGKEMVDYVANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDV
EKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMD
WLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIM
EKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFN
PHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSL
KMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVN
EALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE
|
| Enzyme 5 Number of Residues |
480 |
| Enzyme 5 Molecular Weight |
53893.8 |
| Enzyme 5 Theoretical pI |
7.21 |
| Enzyme 5 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in carboxy-lyase activity |
| Enzyme 5 Specific Function |
Catalyzes the decarboxylation of L-3,4- dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- (1) 3,4-dihydroxy-L-phenylalanine = dopamine + CO2 [RN:R02080]
- (2) 5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2 [RN:R02701]
|
| 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 |
P20711  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
DDC_HUMAN  |
| Enzyme 5 PDB ID |
1JS3  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1443 bp
ATGAACGCAAGTGAATTCCGAAGGAGAGGGAAGGAGATGGTGGATTACGTGGCCAACTAC
ATGGAAGGCATTGAGGGACGCCAGGTCTACCCTGACGTGGAGCCCGGGTACCTGCGGCCG
CTGATCCCTGCCGCTGCCCCTCAGGAGCCAGACACGTTTGAGGACATCATCAACGACGTT
GAGAAGATAATCATGCCTGGGGTGACGCACTGGCACAGCCCCTACTTCTTCGCCTACTTC
CCCACTGCCAGCTCGTACCCGGCCATGCTTGCGGACATGCTGTGCGGGGCCATTGGCTGC
ATCGGCTTCTCCTGGGCGGCAAGCCCAGCATGCACAGAGCTGGAGACTGTGATGATGGAC
TGGCTCGGGAAGATGCTGGAACTACCAAAGGCATTTTTGAATGAGAAAGCTGGAGAAGGG
GGAGGAGTGATCCAGGGAAGTGCCAGTGAAGCCACCCTGGTGGCCCTGCTGGCCGCTCGG
ACCAAAGTGATCCATCGGCTGCAGGCAGCGTCCCCAGAGCTCACACAGGCCGCTATCATG
GAGAAGCTGGTGGCTTACTCATCCGATCAGGCACACTCCTCAGTGGAAAGAGCTGGGTTA
ATTGGTGGAGTGAAATTAAAAGCCATCCCCTCAGATGGCAACTTCGCCATGCGTGCGTCT
GCCCTGCAGGAAGCCCTGGAGAGAGACAAAGCGGCTGGCCTGATTCCTTTCTTTATGGTT
GCCACCCTGGGGACCACAACATGCTGCTCCTTTGACAATCTCTTAGAAGTCGGTCCTATC
TGCAACAAGGAAGACATATGGCTGCACGTTGATGCAGCCTACGCAGGCAGTGCATTCATC
TGCCCTGAGTTCCGGCACCTTCTGAATGGAGTGGAGTTTGCAGATTCATTCAACTTTAAT
CCCCACAAATGGCTATTGGTGAATTTTGACTGTTCTGCCATGTGGGTGAAAAAGAGAACA
GACTTAACGGGAGCCTTTAGACTGGACCCCACTTACCTGAAGCACAGCCATCAGGATTCA
GGGCTTATCACTGACTACCGGCATTGGCAGATACCACTGGGCAGAAGATTTCGCTCTTTG
AAAATGTGGTTTGTATTTAGGATGTATGGAGTCAAAGGACTGCAGGCTTATATCCGCAAG
CATGTCCAGCTGTCCCATGAGTTTGAGTCACTGGTGCGCCAGGATCCCCGCTTTGAAATC
TGTGTGGAAGTCATTCTGGGGCTTGTCTGCTTTCGGCTAAAGGGTTCCAACAAAGTGAAT
GAAGCTCTTCTGCAAAGAATAAACAGTGCCAAAAAAATCCACTTGGTTCCATGTCACCTC
AGGGACAAGTTTGTCCTGCGCTTTGCCATCTGTTCTCGCACGGTGGAATCTGCCCATGTG
CAGCGGGCCTGGGAACACATCAAAGAGCTGGCGGCCGACGTGCTGCGAGCAGAGAGGGAG
TAG
|
| Enzyme 5 GenBank Gene ID |
M76180  |
| Enzyme 5 GeneCard ID |
DDC  |
| Enzyme 5 GenAtlas ID |
DDC  |
| Enzyme 5 HGNC ID |
HGNC:2719  |
| Enzyme 5 Chromosome Location |
7 |
| Enzyme 5 Locus |
7p12.2 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Ichinose H, Kurosawa Y, Titani K, Fujita K, Nagatsu T: Isolation and characterization of a cDNA clone encoding human aromatic L-amino acid decarboxylase. Biochem Biophys Res Commun. 1989 Nov 15;164(3):1024-30. [PubMed
]
- Scherer LJ, McPherson JD, Wasmuth JJ, Marsh JL: Human dopa decarboxylase: localization to human chromosome 7p11 and characterization of hepatic cDNAs. Genomics. 1992 Jun;13(2):469-71. [PubMed
]
- Sumi-Ichinose C, Ichinose H, Takahashi E, Hori T, Nagatsu T: Molecular cloning of genomic DNA and chromosomal assignment of the gene for human aromatic L-amino acid decarboxylase, the enzyme for catecholamine and serotonin biosynthesis. Biochemistry. 1992 Mar 3;31(8):2229-38. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- 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
]
- Le Van Thai A, Coste E, Allen JM, Palmiter RD, Weber MJ: Identification of a neuron-specific promoter of human aromatic L-amino acid decarboxylase gene. Brain Res Mol Brain Res. 1993 Mar;17(3-4):227-38. [PubMed
]
- Craig SP, Thai AL, Weber M, Craig IW: Localisation of the gene for human aromatic L-amino acid decarboxylase (DDC) to chromosome 7p13-->p11 by in situ hybridisation. Cytogenet Cell Genet. 1992;61(2):114-6. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
- Chang YT, Sharma R, Marsh JL, McPherson JD, Bedell JA, Knust A, Brautigam C, Hoffmann GF, Hyland K: Levodopa-responsive aromatic L-amino acid decarboxylase deficiency. Ann Neurol. 2004 Mar;55(3):435-8. [PubMed
]
- Pons R, Ford B, Chiriboga CA, Clayton PT, Hinton V, Hyland K, Sharma R, De Vivo DC: Aromatic L-amino acid decarboxylase deficiency: clinical features, treatment, and prognosis. Neurology. 2004 Apr 13;62(7):1058-65. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5627 |
| Enzyme 6 Name |
Amiloride-sensitive amine oxidase [copper-containing] |
| Enzyme 6 Synonyms |
- DAO
- Diamine oxidase
- Amiloride-binding protein
- ABP
- Histaminase
- Kidney amine oxidase
- KAO
|
| Enzyme 6 Gene Name |
ABP1 |
| Enzyme 6 Protein Sequence |
>Amiloride-sensitive amine oxidase [copper-containing]
MPALGWAVAAILMLQTAMAEPSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSS
TTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAVIFFGDQEHPNVTEFAVGPLP
GPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDR
CLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNG
KFYGSPEELARKYADGEVDVVVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGP
RLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVHFGGERIAYEVSVQEAVALYG
GHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFE
MPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMH
ATGYVHATFYTPEGLRHGTRLHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENIT
NPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFTSPQENPWGHKRTYRLQIHSM
ADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWHPPVVFEQFLHNNENI
ENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRD
NGPNYVQRWIPEDRDCSMPPPFSYNGTYRPV
|
| Enzyme 6 Number of Residues |
751 |
| Enzyme 6 Molecular Weight |
85377.1 |
| Enzyme 6 Theoretical pI |
7.10 |
| Enzyme 6 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- cofactor binding
- copper ion binding
- ion binding
- metal ion binding
- 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
- primary amine oxidase activity
- quinone binding
- transition metal ion binding
|
| Process |
- amine metabolic process
- metabolic process
- nitrogen compound metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in copper ion binding |
| Enzyme 6 Specific Function |
Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2 [RN:R02150]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
73486661  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P19801  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
ABP1_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>2256 bp
ATGCCGGCCCTGGGCTGGGCCGTGGCTGCCATCCTGATGCTGCAGACGGCCATGGCGGAG
CCCTCCCCGGGGACTCTGCCCAGGAAGGCAGGGGTGTTTTCAGACCTAAGCAACCAAGAG
CTGAAGGCAGTGCACAGCTTCCTCTGGTCCAAGAAGGAGCTGAGGCTGCAGCCCTCCAGT
ACCACCACCATGGCCAAGAACACCGTGTTTCTCATCGAGATGCTGCTGCCCAAGAAGTAC
CATGTGCTGAGGTTTCTGGATAAAGGTGAAAGGCATCCTGTGCGGGAAGCCCGTGCCGTC
ATCTTCTTTGGTGACCAGGAGCATCCCAATGTCACCGAGTTTGCTGTGGGGCCCCTGCCA
GGGCCCTGCTACATGCGAGCACTGTCCCCCAGGCCTGGGTACCAGTCCTCCTGGGCATCG
AGGCCCATCTCCACAGCAGAGTATGCCCTCCTCTACCACACCCTGCAGGAAGCCACCAAG
CCCCTGCATCAGTTCTTCCTCAATACCACAGGCTTCTCATTCCAAGACTGCCATGACAGA
TGCCTGGCCTTCACCGATGTGGCCCCCCGGGGTGTGGCTTCTGGCCAGCGCCGCAGTTGG
CTTATCATACAGCGCTATGTAGAAGGCTACTTTCTGCACCCCACTGGGCTGGAGCTCCTC
GTGGATCATGGGAGCACAGATGCTGGGCACTGGGCCGTGGAGCAGGTGTGGTACAACGGG
AAGTTCTATGGGAGCCCAGAGGAACTGGCTCGGAAGTATGCAGATGGAGAGGTGGACGTG
GTGGTCCTGGAGGACCCGCTGCCTGGGGGCAAGGGGCATGACAGCACAGAGGAGCCGCCC
CTCTTCTCCTCCCACAAGCCCCGCGGGGACTTCCCCAGCCCCATCCATGTGAGCGGCCCC
CGCTTGGTCCAGCCCCACGGCCCTCGCTTCAGGCTGGAGGGCAACGCTGTGCTCTACGGC
GGCTGGAGCTTTGCCTTCCGGCTGCGCTCCTCCTCCGGGCTGCAGGTCCTGAACGTGCAC
TTCGGCGGAGAGCGCATTGCCTATGAGGTCAGCGTGCAAGAGGCAGTGGCGCTGTATGGA
GGACACACACCTGCAGGCATGCAGACCAAGTACCTCGATGTCGGCTGGGGCCTGGGCAGC
GTCACTCATGAGTTAGCCCCCGGCATCGACTGCCCGGAGACCGCCACCTTCCTGGACACT
TTCCACTACTATGATGCCGATGACCCGGTCCATTATCCCCGAGCCCTCTGCCTCTTTGAA
ATGCCCACAGGGGTGCCCCTTCGGCGGCACTTTAATTCCAACTTTAAAGGTGGCTTCAAC
TTCTATGCGGGGCTGAAGGGCCAGGTGCTGGTGCTGCGGACAACTTCAACTGTCTACAAT
TATGATTACATTTGGGACTTTATCTTCTACCCCAACGGGGTGATGGAGGCCAAGATGCAT
GCCACTGGCTACGTCCACGCCACCTTCTACACCCCCGAGGGGCTGCGCCACGGCACTCGC
CTGCACACCCACCTGATTGGCAACATACACACTCACTTGGTGCACTACCGCGTAGACCTG
GATGTGGCAGGCACCAAGAACAGCTTCCAGACACTGCAGATGAAGCTAGAAAACATCACC
AACCCCTGGAGCCCAAGACACCGCGTGGTCCAGCCAACTCTGGAGCAGACGCAGTACTCC
TGGGAGCGCCAGGCGGCCTTCCGCTTCAAAAGGAAGCTGCCTAAGTACCTGCTCTTTACC
AGCCCCCAGGAGAACCCCTGGGGCCACAAGCGCACGTACCGCCTGCAGATCCACTCCATG
GCCGACCAGGTGCTGCCCCCAGGCTGGCAGGAGGAGCAGGCCATCACCTGGGCAAGGTAC
CCCCTGGCAGTGACCAAGTACCGGGAGTCGGAGCTGTGCAGCAGCAGCATCTACCACCAG
AACGACCCCTGGCACCCGCCCGTGGTCTTTGAGCAGTTTCTTCACAACAACGAGAACATT
GAAAATGAGGACCTGGTGGCCTGGGTGACGGTGGGCTTCCTGCACATCCCCCACTCAGAG
GACATTCCCAACACAGCCACACCTGGGAACTCCGTGGGCTTCCTGCTCCGGCCATTCAAC
TTCTTCCCAGAGGACCCCTCCCTGGCATCCAGAGACACTGTGATCGTGTGGCCTCGGGAC
AACGGCCCCAACTACGTCCAGCGCTGGATCCCTGAGGACAGGGACTGCTCGATGCCTCCC
CCTTTTAGCTACAATGGGACCTATAGACCTGTGTGA
|
| Enzyme 6 GenBank Gene ID |
NM_001091.2  |
| Enzyme 6 GeneCard ID |
ABP1  |
| Enzyme 6 GenAtlas ID |
ABP1  |
| Enzyme 6 HGNC ID |
HGNC:80  |
| Enzyme 6 Chromosome Location |
7 |
| Enzyme 6 Locus |
7q34-q36 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Barbry P, Champe M, Chassande O, Munemitsu S, Champigny G, Lingueglia E, Maes P, Frelin C, Tartar A, Ullrich A, et al.: Human kidney amiloride-binding protein: cDNA structure and functional expression. Proc Natl Acad Sci U S A. 1990 Oct;87(19):7347-51. [PubMed
]
- Chassande O, Renard S, Barbry P, Lazdunski M: The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter. J Biol Chem. 1994 May 20;269(20):14484-9. [PubMed
]
- Zhang X, Kim J, McIntire WS: cDNA sequences of variant forms of human placenta diamine oxidase. Biochem Genet. 1995 Aug;33(7-8):261-8. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- 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
]
- Novotny WF, Chassande O, Baker M, Lazdunski M, Barbry P: Diamine oxidase is the amiloride-binding protein and is inhibited by amiloride analogues. J Biol Chem. 1994 Apr 1;269(13):9921-5. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5630 |
| Enzyme 7 Name |
Membrane primary amine oxidase |
| Enzyme 7 Synonyms |
- Copper amine oxidase
- HPAO
- Semicarbazide-sensitive amine oxidase
- SSAO
- Vascular adhesion protein 1
- VAP-1
|
| Enzyme 7 Gene Name |
AOC3 |
| Enzyme 7 Protein Sequence |
>Membrane primary amine oxidase
MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLF
ADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPP
AREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDID
QMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFL
HHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSW
SLKSPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGERLV
YEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLATYVDWHFLLESQ
APKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAETVLVVRSMSTLLNYDYVWDTVFH
PSGAIEIRFYATGYISSAFLFGATGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVW
AEDMVFVPMAVPWSPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHP
RGYRIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVDF
SDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSA
DSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGGFSHN
|
| Enzyme 7 Number of Residues |
763 |
| Enzyme 7 Molecular Weight |
84621.3 |
| Enzyme 7 Theoretical pI |
6.51 |
| Enzyme 7 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- cofactor binding
- copper ion binding
- ion binding
- metal ion binding
- 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
- primary amine oxidase activity
- quinone binding
- transition metal ion binding
|
| Process |
- amine metabolic process
- metabolic process
- nitrogen compound metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in copper ion binding |
| Enzyme 7 Specific Function |
Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin- independent fashion. Has a monoamine oxidase activity. May play a role in adipogenesis |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 [RN:R01853]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
Not Available |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q16853  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
AOC3_HUMAN  |
| Enzyme 7 PDB ID |
1PU4  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>2292 bp
ATGAACCAGAAGACAATCCTCGTGCTCCTCATTCTGGCCGTCATCACCATCTTTGCCTTG
GTTTGTGTCCTGCTGGTGGGCAGGGGTGGAGATGGGGGTGAACCCAGCCAGCTTCCCCAT
TGCCCCTCTGTATCTCCCAGTGCCCAGCCTTGGACACACCCTGGCCAGAGCCAGCTGTTT
GCAGACCTGAGCCGAGAGGAGCTGACGGCTGTGATGCGCTTTCTGACCCAGCGGCTGGGG
CCAGGGCTGGTGGATGCAGCCCAGGCCCGGCCCTCGGACAACTGTGTCTTCTCAGTGGAG
TTGCAGCTGCCTCCCAAGGCTGCAGCCCTGGCTCACTTGGACAGGGGGAGCCCCCCACCT
GCCCGGGAGGCACTGGCCATCGTCTTCTTTGGCAGGCAACCCCAGCCCAACGTGAGTGAG
CTGGTGGTGGGGCCACTGCCTCACCCCTCCTACATGCGGGACGTGACTGTGGAGCGTCAT
GGAGGCCCCCTGCCCTATCACCGACGCCCCGTGCTGTTCCAAGAGTACCTGGACATAGAC
CAGATGATCTTCAACAGAGAGCTGCCCCAGGCTTCTGGGCTTCTCCACCACTGTTGCTTC
TACAAGCACCGGGGACGGAACCTGGTGACAATGACCACGGCTCCCCGTGGTCTGCAATCA
GGGGACCGGGCCACCTGGTTTGGCCTCTACTACAACATCTCGGGCGCTGGGTTCTTCCTG
CACCACGTGGGCTTGGAGCTGCTAGTGAACCACAAGGCCCTTGACCCTGCCCGCTGGACT
ATCCAGAAGGTGTTCTATCAAGGCCGCTACTACGACAGCCTGGCCCAGCTGGAGGCCCAG
TTTGAGGCCGGCCTGGTGAATGTGGTGCTGATCCCAGACAATGGCACAGGTGGGTCCTGG
TCCCTGAAGTCCCCTGTGCCCCCGGGTCCAGCTCCCCCTCTACAGTTCTATCCCCAAGGC
CCCCGCTTCAGTGTCCAGGGAAGTCGAGTGGCCTCCTCACTGTGGACTTTCTCCTTTGGC
CTCGGAGCATTCAGTGGCCCAAGGATCTTTGACGTTCGCTTCCAAGGAGAAAGACTAGTT
TATGAGATAAGCCTCCAAGAGGCCTTGGCCATCTATGGTGGAAATTCCCCAGCAGCAATG
ACGACCCGCTATGTGGATGGAGGCTTTGGCATGGGCAAGTACACCACGCCCCTGACCCGT
GGGGTGGACTGCCCCTACTTGGCCACCTACGTGGACTGGCACTTCCTTTTGGAGTCCCAG
GCCCCCAAGACAATACGTGATGCCTTTTGTGTGTTTGAACAGAACCAGGGCCTCCCCCTG
CGGCGACACCACTCAGATCTCTACTCGCACTACTTTGGGGGTCTTGCGGAAACGGTGCTG
GTCGTCAGATCTATGTCCACCTTGCTCAACTATGACTATGTGTGGGATACGGTCTTCCAC
CCCAGTGGGGCCATAGAAATACGATTCTATGCCACGGGCTACATCAGCTCGGCATTCCTC
TTTGGTGCTACTGGGAAGTACGGGAACCAAGTGTCAGAGCACACCCTGGGCACGGTCCAC
ACCCACAGCGCCCACTTCAAGGTGGATCTGGATGTAGCAGGACTGGAGAACTGGGTCTGG
GCCGAGGATATGGTCTTTGTCCCCATGGCTGTGCCCTGGAGCCCTGAGCACCAGCTGCAG
AGGCTGCAGGTGACCCGGAAGCTGCTGGAGATGGAGGAGCAGGCCGCCTTCCTCGTGGGA
AGCGCCACCCCTCGCTACCTGTACCTGGCCAGCAACCACAGCAACAAGTGGGGTCACCCC
CGGGGCTACCGCATCCAGATGCTCAGCTTTGCTGGAGAGCCGCTGCCCCAAAACAGCTCC
ATGGCGAGAGGCTTCAGCTGGGAGAGGTACCAGCTGGCTGTGACCCAGCGGAAGGAGGAG
GAGCCCAGTAGCAGCAGCGTTTTCAATCAGAATGACCCTTGGGCCCCCACTGTGGATTTC
AGTGACTTCATCAACAATGAGACCATTGCTGGAAAGGATTTGGTGGCCTGGGTGACAGCT
GGTTTTCTGCATATCCCACATGCAGAGGACATTCCTAACACAGTGACTGTGGGGAACGGC
GTGGGCTTCTTCCTCCGACCCTATAACTTCTTTGACGAAGACCCCTCCTTCTACTCTGCC
GACTCCATCTACTTCCGAGGGGACCAGGATGCTGGGGCCTGCGAGGTCAACCCCCTAGCT
TGCCTGCCCCAGGCTGCTGCCTGTGCCCCCGACCTCCCTGCCTTCTCCCACGGGGGCTTC
TCTCACAACTAG
|
| Enzyme 7 GenBank Gene ID |
U39447  |
| Enzyme 7 GeneCard ID |
AOC3  |
| Enzyme 7 GenAtlas ID |
AOC3  |
| Enzyme 7 HGNC ID |
HGNC:550  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
17q21 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Zhang X, McIntire WS: Cloning and sequencing of a copper-containing, topa quinone-containing monoamine oxidase from human placenta. Gene. 1996 Nov 14;179(2):279-86. [PubMed
]
- Smith DJ, Salmi M, Bono P, Hellman J, Leu T, Jalkanen S: Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule. J Exp Med. 1998 Jul 6;188(1):17-27. [PubMed
]
- Zhang Q, Mashima Y, Noda S, Imamura Y, Kudoh J, Shimizu N, Nishiyama T, Umeda S, Oguchi Y, Tanaka Y, Iwata T: Characterization of AOC2 gene encoding a copper-binding amine oxidase expressed specifically in retina. Gene. 2003 Oct 30;318:45-53. [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
]
- Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed
]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed
]
- Bour S, Daviaud D, Gres S, Lefort C, Prevot D, Zorzano A, Wabitsch M, Saulnier-Blache JS, Valet P, Carpene C: Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes. Biochimie. 2007 Aug;89(8):916-25. Epub 2007 Feb 24. [PubMed
]
- Kaitaniemi S, Elovaara H, Gron K, Kidron H, Liukkonen J, Salminen T, Salmi M, Jalkanen S, Elima K: The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase. Cell Mol Life Sci. 2009 Aug;66(16):2743-57. Epub 2009 Jul 9. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
- Airenne TT, Nymalm Y, Kidron H, Smith DJ, Pihlavisto M, Salmi M, Jalkanen S, Johnson MS, Salminen TA: Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications. Protein Sci. 2005 Aug;14(8):1964-74. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5631 |
| Enzyme 8 Name |
Retina-specific copper amine oxidase |
| Enzyme 8 Synonyms |
- RAO
- Amine oxidase [copper-containing]
- Semicarbazide-sensitive amine oxidase
- SSAO
|
| Enzyme 8 Gene Name |
AOC2 |
| Enzyme 8 Protein Sequence |
>Retina-specific copper amine oxidase
MHLKIVLAFLALSLITIFALAYVLLTSPGGSSQPPHCPSVSHRAQPWPHPGQSQLFADLS
REELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREA
LAIVLFGGQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLRAEFTQMWRHLK
EVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRSGDRATWMALYHNISGVGLFLHPVGLE
LLLDHRALDPAHWTVQQVFYLGHYYADLGQLEREFKSGRLEVVRVPLPPPNGASSLRSRN
SPGPLPPLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQ
ECVSIYGADSPKTMLTRYLDSSFGLGRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLP
GAVCVFEEAQGLPLRRHHNYLQNHFYGGLASSALVVRSVSSVGNYDYIWDFVLYPNGALE
GRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDV
VFKPVAAPWNPEHWLQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLASNQTNAWGHQRGYR
IQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEESQSSSIYHQNDIWTPTVTFADFI
NNETLLGEDLVAWVTASFLHIPHAEDIPNTVTLGNRVGFLLRPYNFFDEDPSIFSPGSVY
FEKGQDAGLCSINPVACLPDLAACVPDLPPFSYHGF
|
| Enzyme 8 Number of Residues |
756 |
| Enzyme 8 Molecular Weight |
83672.7 |
| Enzyme 8 Theoretical pI |
7.03 |
| Enzyme 8 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- cofactor binding
- copper ion binding
- ion binding
- metal ion binding
- 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
- primary amine oxidase activity
- quinone binding
- transition metal ion binding
|
| Process |
- amine metabolic process
- metabolic process
- nitrogen compound metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in copper ion binding |
| Enzyme 8 Specific Function |
Has a monoamine oxidase activity with substrate specificity for 2-phenylethylamine and tryptamine. May play a role in adipogenesis. May be a critical modulator of signal transmission in retina |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 [RN:R01853]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
3510335  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
O75106  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
AOC2_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>2271 bp
ATGCATCTCAAGATAGTCCTGGCGTTCCTGGCACTGTCCCTCATTACCATCTTTGCCCTG
GCCTATGTTTTGCTGACCAGCCCAGGTGGTTCCAGCCAGCCTCCCCACTGCCCCTCTGTA
TCCCATAGGGCCCAGCCCTGGCCACACCCTGGCCAGAGCCAGCTGTTTGCAGACCTGAGC
CGAGAGGAGTTGACAGCTGTGATGCGCTTTCTGACCCAGCGGCTGGGGCCAGGGCTGGTG
GACGCAGCCCAGGCTCAGCCCTCGGACAACTGCATCTTCTCAGTGGAGCTGCAGCTGCCC
CCCAAGGCTGCAGCCCTGGCCCACCTGGACAGGGGGAGCCCCCCACCTGCCCGGGAGGCA
CTGGCCATCGTCCTCTTTGGTGGACAACCCCAACCCAATGTGAGTGAGCTGGTGGTGGGG
CCGCTGCCTCACCCCTCGTACATGCGGGATGTGACTGTGGAGCGTCACGGCGGGCCCCTG
CCCTATCACCGTCGCCCGGTGCTGAGAGCTGAGTTTACACAGATGTGGAGGCATCTGAAA
GATGTGGAGCTACCCAAGGCACCCATCTTCCTGTCGTCCACCTTCAACTACAATGGCTCT
ACCCTGGCAGCTGTGCATGCCACCCCTCGGGGCTTGCGCTCAAGGGAACGAACTACCTGG
ATGGCCCTCTACCATAACATCTCAGGGGTTGGTCTTTTCCTTCACCCCGTGGGGCTGGAG
CTACTACTGGACCACAGGGCCCTGGACCCTGCCCACTGGACTGTCCAGCAGGTCTTCTAC
CTTGGGCACTACTATGCAGACTTGGGCCAGTTGGAACGGGAGTTTAAGTCTGGCCGGTTG
GAAGTGGTTAGAGTCCCTCTACCTCCACCAAATGGAGCTTCATCCCTGAGGTCTCGGAAC
TCTCCAGGTCCTCTTCCCCCTCTTCAGTTCTCGCCCCAGGGTTCCCAGTACAGTGTGCAA
GGAAACCTGGTGGTATCCTCCCTCTGGTCATTTACCTTTGGCCATGGGGTGTTCAGCGGC
CTGAGGATTTTTGATGTTCGGTTCCAGGGTGAGCGAATAGCCTATGAAGTCAGTGTCCAG
GAGTGTGTATCTATCTATGGTGCCGATTCACCCAAGACGATGCTGACTCGCTATTTGGAT
AGCAGCTTTGGACTCGGCCGTAACAGCCGAGGCTTGGTGCGGGGAGTGGACTGCCCCTAT
CAAGCCACGATGGTGGACATCCATATATTAGTGGGCAAAGGGGCAGTCCAGCTGCTTCCA
GGGGCTGTGTGTGTATTTGAGGAAGCCCAGGGACTGCCCCTTCGAAGGCACCACAATTAC
CTTCAAAATCATTTCTATGGTGGTTTGGCCAGCTCAGCCCTTGTGGTCAGGTCTGTGTCA
TCTGTGGGCAACTATGACTACATTTGGGACTTTGTGTTGTACCCAAATGGGGCACTTGAA
GGGCGGGTCCATGCCACGGGTTATATCAACACAGCTTTCCTGAAAGGGGGAGAGGAGGGC
CTCCTCTTTGGGAACCGTGTGGGGGAAAGAGTGCTGGGAACGGTGCACACACATGCCTTC
CACTTCAAGCTGGACCTGGATGTGGCAGGGCTGAAAAACTGGGTGGTAGCTGAAGACGTG
GTGTTTAAACCTGTGGCTGCCCCCTGGAACCCGGAGCACTGGCTACAGCGCCCACAGCTG
ACTCGGCAGGTCCTGGGAAAGGAGGACCTGACAGCTTTTTCCTTGGGAAGCCCCCTACCC
CGCTACCTCTACCTGGCTAGCAACCAGACTAATGCGTGGGGTCACCAGCGCGGGTACCGA
ATCCAGATCCACAGCCCCCTTGGCATACAAATACCCCTGGAGAGTGACATGGAGAGGGCC
CTCAGCTGGGGGAGATACCAGCTTGTGGTGACCCAGAGAAAGGAGGAGGAGTCACAGAGC
AGTAGCATCTATCACCAGAATGACATCTGGACACCCACAGTTACCTTTGCTGACTTCATC
AACAATGAAACCCTCTTAGGAGAGGATCTGGTGGCTTGGGTCACAGCCAGCTTCCTGCAC
ATTCCCCATGCCGAGGACATCCCAAACACAGTGACTCTGGGGAACAGAGTTGGCTTCTTG
CTCCGACCCTATAACTTCTTTGATGAGGACCCCTCCATCTTCTCCCCTGGCAGTGTGTAC
TTTGAGAAGGGCCAGGATGCTGGGCTCTGCAGCATCAATCCTGTGGCCTGCCTCCCCGAC
CTGGCAGCCTGTGTCCCGGACTTACCCCCTTTCTCTTACCACGGCTTCTAG
|
| Enzyme 8 GenBank Gene ID |
AB012943  |
| Enzyme 8 GeneCard ID |
AOC2  |
| Enzyme 8 GenAtlas ID |
AOC2  |
| Enzyme 8 HGNC ID |
HGNC:549  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
17q21 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Imamura Y, Kubota R, Wang Y, Asakawa S, Kudoh J, Mashima Y, Oguchi Y, Shimizu N: Human retina-specific amine oxidase (RAO): cDNA cloning, tissue expression, and chromosomal mapping. Genomics. 1997 Mar 1;40(2):277-83. [PubMed
]
- Imamura Y, Noda S, Mashima Y, Kudoh J, Oguchi Y, Shimizu N: Human retina-specific amine oxidase: genomic structure of the gene (AOC2), alternatively spliced variant, and mRNA expression in retina. Genomics. 1998 Jul 15;51(2):293-8. [PubMed
]
- Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed
]
- 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
]
- Heniquez A, Meissonnier G, Visentin V, Prevot D, Carpene C: High expression of semicarbazide-sensitive amine oxidase genes AOC2 and AOC3, but not the diamine oxidase gene AOC1 in human adipocytes. Inflamm Res. 2003 Apr;52 Suppl 1:S74-5. [PubMed
]
- Bour S, Daviaud D, Gres S, Lefort C, Prevot D, Zorzano A, Wabitsch M, Saulnier-Blache JS, Valet P, Carpene C: Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes. Biochimie. 2007 Aug;89(8):916-25. Epub 2007 Feb 24. [PubMed
]
- Kaitaniemi S, Elovaara H, Gron K, Kidron H, Liukkonen J, Salminen T, Salmi M, Jalkanen S, Elima K: The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase. Cell Mol Life Sci. 2009 Aug;66(16):2743-57. Epub 2009 Jul 9. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
7086 |
| Enzyme 9 Name |
D(2) dopamine receptor |
| Enzyme 9 Synonyms |
- Dopamine D2 receptor
|
| Enzyme 9 Gene Name |
DRD2 |
| Enzyme 9 Protein Sequence |
>D(2) dopamine receptor
MDPLNLSWYDDDLERQNWSRPFNGSDGKADRPHYNYYATLLTLLIAVIVFGNVLVCMAVS
REKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWKFSRIHCDIFVTLDVMMCTA
SILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMISIVWVLSFTISCPLLFGLNNADQN
ECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIVLRRRRKRVNTKRSSRAFRAHLRAPL
KGNCTHPEDMKLCTVIMKSNGSFPVNRRRVEAARRAQELEMEMLSSTSPPERTRYSPIPP
SHHQLTLPDPSHHGLHSTPDSPAKPEKNGHAKDHPKIAKIFEIQTMPNGKTRTSLKTMSR
RKLSQQKEKKATQMLAIVLGVFIICWLPFFITHILNIHCDCNIPPVLYSAFTWLGYVNSA
VNPIIYTTFNIEFRKAFLKILHC
|
| Enzyme 9 Number of Residues |
443 |
| Enzyme 9 Molecular Weight |
50618.9 |
| Enzyme 9 Theoretical pI |
9.85 |
| Enzyme 9 GO Classification |
| Function |
- G-protein coupled amine receptor activity
- G-protein coupled receptor activity
- dopamine 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 9 General Function |
Involved in G-protein coupled receptor protein signaling pathway |
| Enzyme 9 Specific Function |
This is one of the five types (D1 to D5) of receptors for dopamine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
- 38-60
72-97
109-130
152-174
187-210
374-397
406-429
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
181432  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P14416  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
DRD2_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1332 bp
ATGGATCCACTGAATCTGTCCTGGTATGATGATGATCTGGAGAGGCAGAACTGGAGCCGG
CCCTTCAACGGGTCAGACGGGAAGGCGGACAGACCCCACTACAACTACTATGCCACACTG
CTCACCCTGCTCATCGCTGTCATCGTCTTCGGCAACGTGCTGGTGTGCATGGCTGTGTCC
CGCGAGAAGGCGCTGCAGACCACCACCAACTACCTGATCGTCAGCCTCGCAGTGGCCGAC
CTCCTCGTCGCCACACTGGTCATGCCATGGGTTGTCTACCTGGAGGTGGTAGGTGAGTGG
AAATTCAGCAGGATTCACTGTGACATCTTCGTCACTCTGGACGTCATGATGTGCACGGCG
AGCATCCTGAACTTGTGTGCCATCAGCATCGACAGGTACACAGCTGTGGCCATGCCCATG
CTGTACAATACGCGCTACAGCTCCAAGCGCCGGGTCACCGTCATGATCTCCATCGTCTGG
GTCCTGTCCTTCACCATCTCCTGCCCACTCCTCTTCGGACTCAATAACGCAGACCAGAAC
GAGTGCATCATTGCCAACCCGGCCTTCGTGGTCTACTCCTCCATCGTCTCCTTCTACGTG
CCCTTCATTGTCACCCTGCTGGTCTACATCAAGATCTACATTGTCCTCCGCAGACGCCGC
AAGCGAGTCAACACCAAACGCAGCAGCCGAGCTTTCAGGGCCCACCTGAGGGCTCCACTA
AAGGGCAACTGTACTCACCCCGAGGACATGAAACTCTGCACCGTTATCATGAAGTCTAAT
GGGAGTTTCCCAGTGAACAGGCGGAGAGTGGAGGCTGCCCGGCGAGCCCAGGAGCTGGAG
ATGGAGATGCTCTCCAGCACCAGCCCACCCGAGAGGACCCGGTACAGCCCCATCCCACCC
AGCCACCACCAGCTGACTCTCCCCGACCCGTCCCACCACGGTCTCCACAGCACTCCTGAC
AGCCCCGCCAAACCAGAGAAGAATGGGCATGCCAAAGACCACCCCAAGATTGCCAAGATC
TTTGAGATCCAGACCATGCCCAATGGCAAAACCCGGACCTCCCTCAAGACCATGAGCCGT
AGAAAGCTCTCCCAGCAGAAGGAGAAGAAAGCCACTCAGATGCTCGCCATTGTTCTCGGC
GTGTTCATCATCTGCTGGCTGCCCTTCTTCATCACACACATCCTGAACATACACTGTGAC
TGCAACATCCCGCCTGTCCTGTACAGCGCCTTCACGTGGCTGGGCTATGTCAACAGCGCC
GTGAACCCCATCATCTACACCACCTTCAACATTGAGTTCCGCAAGGCCTTCCTGAAGATC
CTTCACTGCTGA
|
| Enzyme 9 GenBank Gene ID |
M30625  |
| Enzyme 9 GeneCard ID |
DRD2  |
| Enzyme 9 GenAtlas ID |
DRD2  |
| Enzyme 9 HGNC ID |
HGNC:3023  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
11q23 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Selbie LA, Hayes G, Shine J: The major dopamine D2 receptor: molecular analysis of the human D2A subtype. DNA. 1989 Nov;8(9):683-9. [PubMed
]
- Dal Toso R, Sommer B, Ewert M, Herb A, Pritchett DB, Bach A, Shivers BD, Seeburg PH: The dopamine D2 receptor: two molecular forms generated by alternative splicing. EMBO J. 1989 Dec 20;8(13):4025-34. [PubMed
]
- Robakis NK, Mohamadi M, Fu DY, Sambamurti K, Refolo LM: Human retina D2 receptor cDNAs have multiple polyadenylation sites and differ from a pituitary clone at the 5' non-coding region. Nucleic Acids Res. 1990 Mar 11;18(5):1299. [PubMed
]
- Grandy DK, Marchionni MA, Makam H, Stofko RE, Alfano M, Frothingham L, Fischer JB, Burke-Howie KJ, Bunzow JR, Server AC, et al.: Cloning of the cDNA and gene for a human D2 dopamine receptor. Proc Natl Acad Sci U S A. 1989 Dec;86(24):9762-6. [PubMed
]
- Stormann TM, Gdula DC, Weiner DM, Brann MR: Molecular cloning and expression of a dopamine D2 receptor from human retina. Mol Pharmacol. 1990 Jan;37(1):1-6. [PubMed
]
- Selbie LA, Hayes G, Shine J: DNA homology screening: isolation and characterization of the human D2A dopamine receptor subtype. Adv Second Messenger Phosphoprotein Res. 1990;24:9-14. [PubMed
]
- Araki K, Kuwano R, Morii K, Hayashi S, Minoshima S, Shimizu N, Katagiri T, Usui H, Kumanishi T, Takahashi Y: Structure and expression of human and rat D2 dopamine receptor genes. Neurochem Int. 1992 Jul;21(1):91-8. [PubMed
]
- Dearry A, Falardeau P, Shores C, Caron MG: D2 dopamine receptors in the human retina: cloning of cDNA and localization of mRNA. Cell Mol Neurobiol. 1991 Oct;11(5):437-53. [PubMed
]
- Seeman P, Ohara K, Ulpian C, Seeman MV, Jellinger K, Van Tol HH, Niznik HB: Schizophrenia: normal sequence in the dopamine D2 receptor region that couples to G-proteins. DNA polymorphisms in D2. Neuropsychopharmacology. 1993 Feb;8(2):137-42. [PubMed
]
- Seeman P, Nam D, Ulpian C, Liu IS, Tallerico T: New dopamine receptor, D2(Longer), with unique TG splice site, in human brain. Brain Res Mol Brain Res. 2000 Mar 10;76(1):132-41. [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
]
- Binda AV, Kabbani N, Levenson R: Regulation of dense core vesicle release from PC12 cells by interaction between the D2 dopamine receptor and calcium-dependent activator protein for secretion (CAPS). Biochem Pharmacol. 2005 May 15;69(10):1451-61. [PubMed
]
- Itokawa M, Arinami T, Futamura N, Hamaguchi H, Toru M: A structural polymorphism of human dopamine D2 receptor, D2(Ser311-->Cys). Biochem Biophys Res Commun. 1993 Nov 15;196(3):1369-75. [PubMed
]
- Klein C, Brin MF, Kramer P, Sena-Esteves M, de Leon D, Doheny D, Bressman S, Fahn S, Breakefield XO, Ozelius LJ: Association of a missense change in the D2 dopamine receptor with myoclonus dystonia. Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):5173-6. [PubMed
]
- Johann M, Putzhammer A, Eichhammer P, Wodarz N: Association of the -141C Del variant of the dopamine D2 receptor (DRD2) with positive family history and suicidality in German alcoholics. Am J Med Genet B Neuropsychiatr Genet. 2005 Jan 5;132B(1):46-9. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
8029 |
| Enzyme 10 Name |
D(4) dopamine receptor |
| Enzyme 10 Synonyms |
- D(2C) dopamine receptor
- Dopamine D4 receptor
|
| Enzyme 10 Gene Name |
DRD4 |
| Enzyme 10 Protein Sequence |
>D(4) dopamine receptor
MGNRSTADADGLLAGRGPAAGASAGASAGLAGQGAAALVGGVLLIGAVLAGNSLVCVSVA
TERALQTPTNSFIVSLAAADLLLALLVLPLFVYSEVQGGAWLLSPRLCDALMAMDVMLCT
ASIFNLCAISVDRFVAVAVPLRYNRQGGSRRQLLLIGATWLLSAAVAAPVLCGLNDVRGR
DPAVCRLEDRDYVVYSSVCSFFLPCPLMLLLYWATFRGLQRWEVARRAKLHGRAPRRPSG
PGPPSPTPPAPRLPQDPCGPDCAPPAPGLPRGPCGPDCAPAAPGLPPDPCGPDCAPPAPG
LPQDPCGPDCAPPAPGLPRGPCGPDCAPPAPGLPQDPCGPDCAPPAPGLPPDPCGSNCAP
PDAVRAAALPPQTPPQTRRRRRAKITGRERKAMRVLPVVVGAFLLCWTPFFVVHITQALC
PACSVPPRLVSAVTWLGYVNSALNPVIYTVFNAEFRNVFRKALRACC
|
| Enzyme 10 Number of Residues |
467 |
| Enzyme 10 Molecular Weight |
48359.9 |
| Enzyme 10 Theoretical pI |
8.37 |
| Enzyme 10 GO Classification |
| Function |
- G-protein coupled amine receptor activity
- G-protein coupled receptor activity
- dopamine 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 10 General Function |
Involved in G-protein coupled receptor protein signaling pathway |
| Enzyme 10 Specific Function |
This is one of the five types (D1 to D5) of receptors for dopamine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
- 38-60
71-93
110-131
152-175
192-213
395-417
427-449
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
291946  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P21917  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
DRD4_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1404 bp
ATGGGGAACCGCAGCACCGCGGACGCGGACGGGCTGCTGGCTGGGCGCGGGCCGGCCGCG
GGGGCATCTGCGGGGGCATCTGCGGGGCTGGCTGGGCAGGGCGCGGCGGCGCTGGTGGGG
GGCGTGCTGCTCATCGGCGCGGTGCTCGCGGGGAACTCGCTCGTGTGCGTGAGCGTGGCC
ACCGAGCGCGCCCTGCAGACGCCCACCAACTCCTTCATCGTGAGCCTGGCGGCCGCCGAC
CTCCTCCTCGCTCTCCTGGTGCTGCCGCTCTTCGTCTACTCCGAGGTCCAGGGTGGCGCG
TGGCTGCTGAGCCCCCGCCTGTGCGACGCCCTCATGGCCATGGACGTCATGCTGTGCACC
GCCTCCATCTTCAACCTGTGCGCCATCAGCGTGGACAGGTTCGTGGCCGTGGCCGTGCCG
CTGCGCTACAACCGGCAGGGTGGGAGCCGCCGGCAGCTGCTGCTCATCGGCGCCACGTGG
CTGCTGTCCGCGGCGGTGGCGGCGCCCGTACTGTGCGGCCTCAACGACGTGCGCGGCCGC
GACCCCGCCGTGTGCCGCCTGGAGGACCGCGACTACGTGGTCTACTCGTCCGTGTGCTCC
TTCTTCCTACCCTGCCCGCTCATGCTGCTGCTCTACTGGGCCACGTTCCGCGGCCTGCAG
CGCTGGGAGGTGGCACGTCGCGCCAAGCTGCACGGCCGCGCGCCCCGCCGACCCAGCGGC
CCTGGCCCGCCTTCCCCCACGCCACCCGCGCCCCGCCTCCCCCAGGACCCCTGCGGCCCC
GACTGTGCGCCCCCCGCGCCCGGCCTTCCCCGGGGTCCCTGCGGCCCCGACTGTGCGCCC
GCCGCGCCCGGCCTCCCCCCGGACCCCTGCGGCCCCGACTGTGCGCCCCCCGCGCCCGGC
CTCCCCCAGGACCCCTGCGGCCCCGACTGTGCGCCCCCCGCGCCCGGCCTTCCCCGGGGT
CCCTGCGGCCCCGACTGTGCGCCCCCCGCGCCCGGCCTCCCCCAGGACCCCTGCGGCCCC
GACTGTGCGCCCCCCGCGCCCGGCCTCCCCCCGGACCCCTGCGGCTCCAACTGTGCTCCC
CCCGACGCCGTCAGAGCCGCCGCGCTCCCACCCCAGACTCCACCGCAGACCCGCAGGAGG
CGGCGTGCCAAGATCACCGGCCGGGAGCGCAAGGCCATGAGGGTCCTGCCGGTGGTGGTC
GGGGCCTTCCTGCTGTGCTGGACGCCCTTCTTCGTGGTGCACATCACGCAGGCGCTGTGT
CCTGCCTGCTCCGTGCCCCCGCGGCTGGTCAGCGCCGTCACCTGGCTGGGCTACGTCAAC
AGCGCCCTCAACCCCGTCATCTACACTGTCTTCAACGCCGAGTTCCGCAACGTCTTCCGC
AAGGCCCTGCGTGCCTGCTGCTGA
|
| Enzyme 10 GenBank Gene ID |
L12398  |
| Enzyme 10 GeneCard ID |
DRD4  |
| Enzyme 10 GenAtlas ID |
DRD4  |
| Enzyme 10 HGNC ID |
HGNC:3025  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
11p15.5 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Van Tol HH, Wu CM, Guan HC, Ohara K, Bunzow JR, Civelli O, Kennedy J, Seeman P, Niznik HB, Jovanovic V: Multiple dopamine D4 receptor variants in the human population. Nature. 1992 Jul 9;358(6382):149-52. [PubMed
]
- Van Tol HH, Bunzow JR, Guan HC, Sunahara RK, Seeman P, Niznik HB, Civelli O: Cloning of the gene for a human dopamine D4 receptor with high affinity for the antipsychotic clozapine. Nature. 1991 Apr 18;350(6319):610-4. [PubMed
]
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed
]
- Lichter JB, Barr CL, Kennedy JL, Van Tol HH, Kidd KK, Livak KJ: A hypervariable segment in the human dopamine receptor D4 (DRD4) gene. Hum Mol Genet. 1993 Jun;2(6):767-73. [PubMed
]
- Asghari V, Schoots O, van Kats S, Ohara K, Jovanovic V, Guan HC, Bunzow JR, Petronis A, Van Tol HH: Dopamine D4 receptor repeat: analysis of different native and mutant forms of the human and rat genes. Mol Pharmacol. 1994 Aug;46(2):364-73. [PubMed
]
- Whistler JL, Enquist J, Marley A, Fong J, Gladher F, Tsuruda P, Murray SR, Von Zastrow M: Modulation of postendocytic sorting of G protein-coupled receptors. Science. 2002 Jul 26;297(5581):615-20. [PubMed
]
- Livingstone CD, Strange PG, Naylor LH: Molecular modelling of D2-like dopamine receptors. Biochem J. 1992 Oct 1;287 ( Pt 1):277-82. [PubMed
]
- Seeman P, Ulpian C, Chouinard G, Van Tol HH, Dwosh H, Lieberman JA, Siminovitch K, Liu IS, Waye J, Voruganti P, et al.: Dopamine D4 receptor variant, D4GLYCINE194, in Africans, but not in Caucasians: no association with schizophrenia. Am J Med Genet. 1994 Dec 15;54(4):384-90. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
8046 |
| Enzyme 11 Name |
Sodium-dependent dopamine transporter |
| Enzyme 11 Synonyms |
- DA transporter
- DAT
- Solute carrier family 6 member 3
|
| Enzyme 11 Gene Name |
SLC6A3 |
| Enzyme 11 Protein Sequence |
>Sodium-dependent dopamine transporter
MSKSKCSVGLMSSVVAPAKEPNAVGPKEVELILVKEQNGVQLTSSTLTNPRQSPVEAQDR
ETWGKKIDFLLSVIGFAVDLANVWRFPYLCYKNGGGAFLVPYLLFMVIAGMPLFYMELAL
GQFNREGAAGVWKICPILKGVGFTVILISLYVGFFYNVIIAWALHYLFSSFTTELPWIHC
NNSWNSPNCSDAHPGDSSGDSSGLNDTFGTTPAAEYFERGVLHLHQSHGIDDLGPPRWQL
TACLVLVIVLLYFSLWKGVKTSGKVVWITATMPYVVLTALLLRGVTLPGAIDGIRAYLSV
DFYRLCEASVWIDAATQVCFSLGVGFGVLIAFSSYNKFTNNCYRDAIVTTSINSLTSFSS
GFVVFSFLGYMAQKHSVPIGDVAKDGPGLIFIIYPEAIATLPLSSAWAVVFFIMLLTLGI
DSAMGGMESVITGLIDEFQLLHRHRELFTLFIVLATFLLSLFCVTNGGIYVFTLLDHFAA
GTSILFGVLIEAIGVAWFYGVGQFSDDIQQMTGQRPSLYWRLCWKLVSPCFLLFVVVVSI
VTFRPPHYGAYIFPDWANALGWVIATSSMAMVPIYAAYKFCSLPGSFREKLAYAIAPEKD
RELVDRGEVRQFTLRHWLKV
|
| Enzyme 11 Number of Residues |
620 |
| Enzyme 11 Molecular Weight |
68494.3 |
| Enzyme 11 Theoretical pI |
6.92 |
| Enzyme 11 GO Classification |
| Function |
- dopamine:sodium symporter activity
- neurotransmitter transporter activity
- neurotransmitter:sodium symporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- establishment of localization
- neurotransmitter transport
- transport
|
| Component |
- cell part
- integral to membrane
- integral to plasma membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 11 General Function |
Involved in neurotransmitter:sodium symporter activity |
| Enzyme 11 Specific Function |
Amine transporter. Terminates the action of dopamine by its high affinity sodium-dependent reuptake into presynaptic terminals |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
- 69-89
96-116
140-160
238-256
265-282
318-335
347-368
401-420
447-465
481-501
522-541
560-578
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
181656  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q01959  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
SC6A3_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1863 bp
ATGAGTAAGAGCAAATGCTCCGTGGGACTCATGTCTTCCGTGGTGGCCCCGGCTAAGGAG
CCCAATGCCGTGGGCCCGAAGGAGGTGGAGCTCATCCTTGTCAAGGAGCAGAACGGAGTG
CAGCTCACCAGCTCCACCCTCACCAACCCGCGGCAGAGCCCCGTGGAGGCCCAGGATCGG
GAGACCTGGGGCAAGAAGATCGACTTTCTCCTGTCCGTCATTGGCTTTGCTGTGGACCTG
GCCAACGTCTGGCGGTTCCCCTACCTGTGCTACAAAAATGGTGGCGGTGCCTTCCTGGTC
CCCTACCTGCTCTTCATGGTCATTGCTGGGATGCCACTTTTCTACATGGAGCTGGCCCTC
GGCCAGTTCAACAGGGAAGGGGCCGCTGGTGTCTGGAAGATCTGCCCCATACTGAAAGGT
GTGGGCTTCACGGTCATCCTCATCTCACTGTATGTCGGCTTCTTCTACAACGTCATCATC
GCCTGGGCGCTGCACTATCTCTTCTCCTCCTTCACCACGGAGCTCCCCTGGATCCACTGC
AACAACTCCTGGAACAGCCCCAACTGCTCGGATGCCCATCCTGGTGACTCCAGTGGAGAC
AGCTCGGGCCTCAACGACACTTTTGGGACCACACCTGCTGCCGAGTACTTTGAACGTGGC
GTGCTGCACCTCCACCAGAGCCATGGCATCGACGACCTGGGGCCTCCGCGGTGGCAGCTC
ACAGCCTGCCTGGTGCTGGTCATCGTGCTGCTCTACTTCAGCCTCTGGAAGGGCGTGAAG
ACCTCAGGGAAGGTGGTATGGATCACAGCCACCATGCCATACGTGGTCCTCACTGCCCTG
CTCCTGCGTGGGGTCACCCTCCCTGGAGCCATAGACGGCATCAGAGCATACCTGAGCGTT
GACTTCTACCGGCTCTGCGAGGCGTCTGTTTGGATTGACGCGGCCACCCAGGTGTGCTTC
TCCCTGGGCGTGGGGTTCGGGGTGCTGATCGCCTTCTCCAGCTACAACAAGTTCACCAAC
AACTGCTACAGGGACGCGATTGTCACCACCTCCATCAACTCCCTGACGAGCTTCTCCTCC
GGCTTCGTCGTCTTCTCCTTCCTGGGGTACATGGCACAGAAGCACAGTGTGCCCATCGGG
GACGTGGCCAAGGACGGGCCAGGGCTGATCTTCATCATCTACCCGGAAGCCATCGCCACG
CTCCCTCTGTCCTCAGCCTGGGCCGTGGTCTTCTTCATCATGCTGCTCACCCTGGGTATC
GACAGCGCCATGGGTGGTATGGAGTCAGTGATCACCGGGCTCATCGATGAGTTCCAGCTG
CTGCACAGACACCGTGAGCTCTTCACGCTCTTCATCGTCCTGGCGACCTTCCTCCTGTCC
CTGTTCTGCGTCACCAACGGTGGCATCTACGTCTTCACGCTCCTGGACCATTTTGCAGCC
GGCACGTCCATCCTCTTTGGAGTGCTCATCGAAGCCATCGGAGTGGCCTGGTTCTATGGT
GTTGGGCAGTTCAGCGACGACATCCAGCAGATGACCGGGCAGCGGCCCAGCCTGTACTGG
CGGCTGTGCTGGAAGCTGGTCAGCCCCTGCTTTCTCCTGTTCGTGGTCGTGGTCAGCATT
GTGACCTTCAGACCCCCCCACTACGGAGCCTACATCTTCCCCGACTGGGCCAACGCGCTG
GGCTGGGTCATCGCCACATCCTCCATGGCCATGGTGCCCATCTATGCGGCCTACAAGTTC
TGCAGCCTGCCTGGGTCCTTTCGAGAGAAACTGGCCTACGCCATTGCACCCGAGAAGGAC
CGTGAGCTGGTGGACAGAGGGGAGGTGCGCCAGTTCACGCTCCGCCACTGGCTCAAGGTG
TAG
|
| Enzyme 11 GenBank Gene ID |
M95167  |
| Enzyme 11 GeneCard ID |
SLC6A3  |
| Enzyme 11 GenAtlas ID |
SLC6A3  |
| Enzyme 11 HGNC ID |
HGNC:11049  |
| Enzyme 11 Chromosome Location |
5 |
| Enzyme 11 Locus |
5p15.3 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Vandenbergh DJ, Persico AM, Uhl GR: A human dopamine transporter cDNA predicts reduced glycosylation, displays a novel repetitive element and provides racially-dimorphic TaqI RFLPs. Brain Res Mol Brain Res. 1992 Sep;15(1-2):161-6. [PubMed
]
- Giros B, el Mestikawy S, Godinot N, Zheng K, Han H, Yang-Feng T, Caron MG: Cloning, pharmacological characterization, and chromosome assignment of the human dopamine transporter. Mol Pharmacol. 1992 Sep;42(3):383-90. [PubMed
]
- Pristupa ZB, Wilson JM, Hoffman BJ, Kish SJ, Niznik HB: Pharmacological heterogeneity of the cloned and native human dopamine transporter: disassociation of [3H]WIN 35,428 and [3H]GBR 12,935 binding. Mol Pharmacol. 1994 Jan;45(1):125-35. [PubMed
]
- Kawarai T, Kawakami H, Yamamura Y, Nakamura S: Structure and organization of the gene encoding human dopamine transporter. Gene. 1997 Aug 11;195(1):11-8. [PubMed
]
- Vandenbergh DJ, Thompson MD, Cook EH, Bendahhou E, Nguyen T, Krasowski MD, Zarrabian D, Comings D, Sellers EM, Tyndale RF, George SR, O'Dowd BF, Uhl GR: Human dopamine transporter gene: coding region conservation among normal, Tourette's disorder, alcohol dependence and attention-deficit hyperactivity disorder populations. Mol Psychiatry. 2000 May;5(3):283-92. [PubMed
]
- Greenwood TA, Alexander M, Keck PE, McElroy S, Sadovnick AD, Remick RA, Kelsoe JR: Evidence for linkage disequilibrium between the dopamine transporter and bipolar disorder. Am J Med Genet. 2001 Mar 8;105(2):145-51. [PubMed
]
- Donovan DM, Vandenbergh DJ, Perry MP, Bird GS, Ingersoll R, Nanthakumar E, Uhl GR: Human and mouse dopamine transporter genes: conservation of 5'-flanking sequence elements and gene structures. Brain Res Mol Brain Res. 1995 Jun;30(2):327-35. [PubMed
]
- Bannon MJ, Poosch MS, Xia Y, Goebel DJ, Cassin B, Kapatos G: Dopamine transporter mRNA content in human substantia nigra decreases precipitously with age. Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):7095-9. [PubMed
]
- Torres GE, Yao WD, Mohn AR, Quan H, Kim KM, Levey AI, Staudinger J, Caron MG: Functional interaction between monoamine plasma membrane transporters and the synaptic PDZ domain-containing protein PICK1. Neuron. 2001 Apr;30(1):121-34. [PubMed
]
- Carneiro AM, Ingram SL, Beaulieu JM, Sweeney A, Amara SG, Thomas SM, Caron MG, Torres GE: The multiple LIM domain-containing adaptor protein Hic-5 synaptically colocalizes and interacts with the dopamine transporter. J Neurosci. 2002 Aug 15;22(16):7045-54. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
- 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
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
13244 |
| Enzyme 12 Name |
Neuron-specific vesicular protein calcyon |
| Enzyme 12 Synonyms |
Not Available |
| Enzyme 12 Gene Name |
CALY |
| Enzyme 12 Protein Sequence |
>Neuron-specific vesicular protein calcyon
MVKLGCSFSGKPGKDPGDQDGAAMDSVPLISPLDISQLQPPLPDQVVIKTQTEYQLSSPD
QQNFPDLEGQRLNCSHPEEGRRLPTARMIAFAMALLGCVLIMYKAIWYDQFTCPDGFLLR
HKICTPLTLEMYYTEMDPERHRSILAAIGAYPLSRKHGTETPAAWGDGYRAAKEERKGPT
QAGAAAAATEPPGKPSAKAEKEAARKAAGSAAPPPAQ
|
| Enzyme 12 Number of Residues |
217 |
| Enzyme 12 Molecular Weight |
23433.5 |
| Enzyme 12 Theoretical pI |
6.91 |
| Enzyme 12 GO Classification |
| Function |
- G-protein-coupled receptor binding
- binding
- dopamine receptor binding
- protein binding
- receptor binding
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- dopamine receptor signaling pathway
- signaling
- signaling pathway
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 12 General Function |
Involved in dopamine receptor binding |
| Enzyme 12 Specific Function |
Interacts with clathrin light chain A and stimulates clathrin self-assembly and clathrin-mediated endocytosis |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
Not Available |
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
Not Available |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q9NYX4  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
CALY_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>654 bp
ATGGTGAAGCTGGGCTGCAGCTTCTCTGGGAAGCCAGGTAAAGACCCTGGGGACCAGGAT
GGGGCTGCCATGGACAGTGTGCCTCTGATCAGCCCCTTGGACATCAGCCAGCTCCAGCCG
CCACTCCCTGACCAGGTGGTCATCAAGACACAGACAGAATACCAGCTGTCCTCCCCAGAC
CAGCAGAATTTCCCTGACCTGGAGGGCCAGAGGCTGAACTGCAGCCACCCAGAGGAAGGG
CGCAGGCTGCCCACCGCACGGATGATCGCCTTCGCCATGGCGCTACTGGGCTGCGTGCTG
ATCATGTACAAGGCCATCTGGTACGACCAGTTCACCTGCCCCGACGGCTTCCTGCTGCGG
CACAAGATCTGCACGCCGCTGACCCTGGAGATGTACTACACGGAGATGGACCCCGAGCGC
CACCGCAGCATCCTGGCGGCCATCGGGGCCTACCCGCTGAGCCGCAAGCACGGCACGGAG
ACGCCGGCGGCCTGGGGGGACGGCTACCGCGCAGCCAAGGAGGAGCGCAAGGGGCCCACC
CAGGCTGGGGCGGCGGCGGCGGCCACCGAACCCCCCGGGAAGCCGTCGGCCAAGGCGGAG
AAGGAGGCGGCGCGGAAGGCGGCCGGGAGCGCGGCGCCCCCGCCCGCGCAGTGA
|
| Enzyme 12 GenBank Gene ID |
AF225903  |
| Enzyme 12 GeneCard ID |
CALY  |
| Enzyme 12 GenAtlas ID |
CALY  |
| Enzyme 12 HGNC ID |
HGNC:17938  |
| Enzyme 12 Chromosome Location |
1 |
| Enzyme 12 Locus |
10q26.3 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Lezcano N, Mrzljak L, Eubanks S, Levenson R, Goldman-Rakic P, Bergson C: Dual signaling regulated by calcyon, a D1 dopamine receptor interacting protein. Science. 2000 Mar 3;287(5458):1660-4. [PubMed
]
- Lezcano N, Mrzljak L, Levenson R, Bergson C: Retraction. Science. 2006 Dec 15;314(5806):1681. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [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
]
- Koh PO, Bergson C, Undie AS, Goldman-Rakic PS, Lidow MS: Up-regulation of the D1 dopamine receptor-interacting protein, calcyon, in patients with schizophrenia. Arch Gen Psychiatry. 2003 Mar;60(3):311-9. [PubMed
]
- Ali MK, Bergson C: Elevated intracellular calcium triggers recruitment of the receptor cross-talk accessory protein calcyon to the plasma membrane. J Biol Chem. 2003 Dec 19;278(51):51654-63. Epub 2003 Oct 8. [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
]
- Xiao J, Dai R, Negyessy L, Bergson C: Calcyon, a novel partner of clathrin light chain, stimulates clathrin-mediated endocytosis. J Biol Chem. 2006 Jun 2;281(22):15182-93. Epub 2006 Apr 4. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
13261 |
| Enzyme 13 Name |
Calcium-dependent secretion activator 1 |
| Enzyme 13 Synonyms |
- Calcium-dependent activator protein for secretion 1
- CAPS-1
|
| Enzyme 13 Gene Name |
CADPS |
| Enzyme 13 Protein Sequence |
>Calcium-dependent secretion activator 1
MLDPSSSEEESDEIVEEESGKEVLGSAPSGARLSPSRTSEGSAGSAGLGGGGAGAGAGVG
AGGGGGSGASSGGGAGGLQPSSRAGGGRPSSPSPSVVSEKEKEELERLQKEEEERKKRLQ
LYVFVMRCIAYPFNAKQPTDMARRQQKISKQQLQTVKDRFQAFLNGETQIMADEAFMNAV
QSYYEVFLKSDRVARMVQSGGCSANDSREVFKKHIEKRVRSLPEIDGLSKETVLSSWMAK
FDAIYRGEEDPRKQQARMTASAASELILSKEQLYEMFQNILGIKKFEHQLLYNACQLDNP
DEQAAQIRRELDGRLQMADQIARERKFPKFVSKEMENMYIEELKSSVNLLMANLESMPVS
KGGEFKLQKLKRSHNASIIDMGEESENQLSKSDVVLSFSLEVVIMEVQGLKSLAPNRIVY
CTMEVEGGEKLQTDQAEASKPTWGTQGDFSTTHALPAVKVKLFTESTGVLALEDKELGRV
ILHPTPNSPKQSEWHKMTVSKNCPDQDLKIKLAVRMDKPQNMKHSGYLWAIGKNVWKRWK
KRFFVLVQVSQYTFAMCSYREKKAEPQELLQLDGYTVDYTDPQPGLEGGRAFFNAVKEGD
TVIFASDDEQDRILWVQAMYRATGQSHKPVPPTQVQKLNAKGGNVPQLDAPISQFYADRA
QKHGMDEFISSNPCNFDHASLFEMVQRLTLDHRLNDSYSCLGWFSPGQVFVLDEYCARNG
VRGCHRHLCYLRDLLERAENGAMIDPTLLHYSFAFCASHVHGNRPDGIGTVTVEEKERFE
EIKERLRVLLENQITHFRYCFPFGRPEGALKATLSLLERVLMKDIVTPVPQEEVKTVIRK
CLEQAALVNYSRLSEYAKIEENQKDAENVGRLITPAKKLEDTIRLAELVIEVLQQNEEHH
AEPHVDKGEAFAWWSDLMVEHAETFLSLFAVDMDAALEVQPPDTWDSFPLFQLLNDFLRT
DYNLCNGKFHKHLQDLFAPLVVRYVDLMESSIAQSIHRGFERESWEPVKSLTSNLPNVNL
PNVNLPKVPNLPVNIPLGIPQMPTFSAPSWMAAIYDADNGSGTSEDLFWKLDALQTFIRD
LHWPEEEFGKHLEQRLKLMASDMIESCVKRTRIAFEVKLQKTSRSTDFRVPQSICTMFNV
MVDAKAQSTKLCSMEMGQEHQYHSKIDELIEETVKEMITLLVAKFVTILEGVLAKLSRYD
EGTLFSSFLSFTVKAASKYVDVPKPGMDVADAYVTFVRHSQDVLRDKVNEEMYIERLFDQ
WYNSSMNVICTWLTDRMDLQLHIYQLKTLIRMVKKTYRDFRLQGVLDSTLNSKTYETIRN
RLTVEEATASVSEGGGLQGISMKDSDEEDEEDD
|
| Enzyme 13 Number of Residues |
1353 |
| Enzyme 13 Molecular Weight |
152785.4 |
| Enzyme 13 Theoretical pI |
5.44 |
| Enzyme 13 GO Classification |
Not Available |
| Enzyme 13 General Function |
Carbohydrate transport and metabolism |
| Enzyme 13 Specific Function |
Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates catecholamine loading of DCVs. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles by acting as a PtdIns(4,5)P2-binding protein that acts at prefusion step following ATP-dependent priming and participates in DCVs-membrane fusion. However, it may also participate in small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
Not Available |
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
34452715  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q9ULU8  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
CAPS1_HUMAN  |
| Enzyme 13 PDB ID |
1WI1  |
| Enzyme 13 PDB File |
Show |
| Enzyme 13 3D Structure |
|
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>4062 bp
ATGCTGGACCCTTCGTCCAGCGAAGAAGAATCGGATGAGATCGTGGAGGAGGAGAGCGGC
AAGGAGGTGCTCGGCTCGGCCCCGTCCGGCGCGCGCCTGTCTCCCAGCCGTACCAGCGAG
GGCTCGGCCGGCAGCGCCGGGCTGGGGGGCGGCGGCGCCGGCGCCGGAGCCGGGGTGGGT
GCAGGCGGCGGCGGGGGCAGCGGCGCGAGCAGCGGCGGCGGGGCCGGGGGGCTGCAACCC
AGCAGCCGCGCTGGCGGCGGCCGGCCCTCCAGCCCCAGCCCGTCGGTGGTGAGCGAGAAG
GAGAAGGAAGAGTTGGAGCGGCTGCAGAAAGAGGAGGAGGAGAGGAAGAAGAGGCTGCAG
CTGTATGTGTTCGTGATGCGCTGCATCGCCTACCCCTTTAATGCCAAGCAGCCCACCGAC
ATGGCTCGCCGGCAGCAGAAGATCAGCAAACAGCAGCTGCAGACAGTCAAGGACCGGTTT
CAGGCTTTCCTCAATGGGGAAACCCAGATCATGGCTGACGAAGCCTTCATGAACGCTGTG
CAGAGTTACTATGAGGTGTTCCTGAAGAGCGACCGTGTGGCCCGCATGGTTCAGAGTGGA
GGCTGTTCCGCCAACGACTCCCGGGAGGTCTTCAAGAAGCACATTGAGAAGAGAGTGCGC
AGCCTGCCTGAGATTGACGGCCTCAGCAAGGAGACTGTGCTGAGCTCCTGGATGGCCAAA
TTTGATGCCATCTACCGTGGAGAAGAGGACCCGCGGAAGCAGCAGGCCCGGATGACAGCC
AGCGCAGCCTCCGAGCTGATTCTGAGCAAGGAGCAACTCTATGAGATGTTCCAGAACATT
CTTGGGATCAAGAAGTTCGAACATCAGCTCCTTTACAATGCCTGCCAGCTGGACAATCCA
GATGAGCAAGCAGCCCAGATCAGACGAGAGCTGGATGGACGTCTACAAATGGCAGACCAA
ATAGCCAGGGAACGCAAATTTCCCAAGTTTGTATCCAAAGAAATGGAAAACATGTACATT
GAGGAGCTGAAGTCATCTGTCAACCTGCTCATGGCCAACTTGGAGAGCATGCCGGTATCC
AAAGGCGGGGAGTTCAAGCTCCAGAAACTCAAACGCAGCCACAATGCTTCCATCATCGAC
ATGGGCGAGGAGAGTGAGAACCAGCTCTCCAAGTCAGATGTCGTGCTGTCTTTCTCATTG
GAGGTGGTAATTATGGAAGTCCAAGGCCTCAAATCTTTGGCTCCAAATCGCATCGTATAT
TGCACAATGGAGGTGGAAGGAGGAGAGAAACTACAGACTGATCAGGCCGAGGCTTCTAAA
CCAACCTGGGGCACCCAGGGTGACTTCTCCACAACCCATGCACTGCCAGCTGTGAAGGTG
AAGCTGTTCACAGAGAGCACAGGCGTCCTGGCGTTGGAGGACAAGGAGCTTGGGCGGGTT
ATTCTCCATCCCACCCCGAACAGCCCCAAACAGTCAGAGTGGCACAAAATGACAGTCTCC
AAAAACTGCCCCGACCAAGATCTCAAAATCAAACTTGCTGTCCGAATGGATAAGCCTCAA
AACATGAAGCATTCTGGGTATTTATGGGCCATCGGTAAGAATGTCTGGAAGAGATGGAAG
AAAAGGTTTTTTGTATTGGTGCAGGTCAGTCAGTACACGTTTGCCATGTGCAGTTATCGG
GAGAAGAAAGCGGAGCCTCAGGAACTTCTACAATTGGATGGCTACACTGTGGATTACACC
GACCCCCAGCCAGGTTTGGAGGGTGGCCGAGCCTTCTTCAATGCTGTCAAGGAGGGAGAC
ACCGTGATATTTGCCAGTGACGATGAACAAGACCGCATCCTGTGGGTCCAGGCCATGTAT
CGGGCCACGGGGCAGTCACACAAGCCTGTGCCCCCGACCCAAGTCCAGAAACTCAACGCC
AAGGGAGGAAATGTACCTCAGCTGGATGCCCCTATCTCTCAATTTTACGCAGATAGAGCT
CAAAAACATGGCATGGATGAATTTATCTCTTCCAACCCCTGTAACTTTGACCACGCTTCC
CTCTTTGAGATGGTACAACGCCTTACTTTGGATCACAGACTTAATGATTCCTATTCTTGC
CTGGGCTGGTTCAGTCCTGGCCAGGTGTTTGTACTAGACGAGTATTGCGCCCGAAATGGA
GTCCGGGGGTGTCACCGACATCTCTGCTACCTCAGAGACTTGCTTGAACGGGCAGAAAAT
GGCGCCATGATCGACCCCACCCTTCTTCACTACAGCTTTGCCTTCTGTGCATCCCATGTC
CATGGGAACAGGCCTGATGGAATTGGAACTGTGACTGTTGAAGAAAAGGAACGTTTTGAA
GAAATCAAAGAGAGGCTCCGAGTTCTGCTAGAAAATCAGATTACACATTTTAGGTATTGC
TTTCCATTTGGTCGACCTGAAGGTGCTTTGAAAGCTACTCTCTCACTCTTGGAAAGGGTT
TTGATGAAAGATATTGTTACCCCAGTGCCACAAGAGGAGGTAAAAACAGTTATCCGTAAA
TGTCTGGAACAGGCTGCGTTAGTCAACTATTCTCGGCTCTCAGAGTATGCCAAAATCGAA
GAGAATCAAAAGGATGCAGAAAATGTAGGCCGGTTAATCACTCCTGCCAAAAAGCTTGAA
GATACAATACGTCTTGCTGAACTAGTCATTGAAGTTCTTCAGCAAAATGAGGAGCACCAC
GCAGAGCCACATGTTGATAAAGGAGAAGCCTTTGCGTGGTGGTCAGATTTAATGGTGGAG
CATGCGGAGACGTTCCTGTCACTCTTTGCAGTAGACATGGATGCAGCCTTAGAGGTGCAA
CCTCCAGACACATGGGACAGTTTTCCACTATTTCAGCTGCTGAATGATTTTCTCCGTACT
GACTATAATTTGTGCAATGGAAAATTTCACAAACACCTGCAAGACCTGTTTGCCCCACTT
GTTGTTAGATATGTGGATCTGATGGAGTCCTCAATTGCACAATCCATTCACAGGGGCTTT
GAGCGGGAGTCATGGGAACCAGTCAAGAGTTTAACCAGTAACCTACCCAATGTGAACCTA
CCCAATGTGAACCTTCCCAAAGTACCAAATCTACCAGTTAACATCCCTCTAGGCATCCCA
CAAATGCCTACTTTTTCGGCACCGTCATGGATGGCTGCTATATATGATGCGGATAATGGG
TCAGGCACCTCAGAAGATCTGTTTTGGAAACTTGACGCCCTTCAGACCTTCATTCGGGAC
CTGCACTGGCCTGAAGAAGAGTTTGGAAAGCACCTGGAACAACGGCTGAAGTTGATGGCA
AGTGACATGATCGAATCTTGTGTCAAAAGAACCAGGATTGCATTTGAAGTTAAGCTGCAA
AAAACCAGTCGATCAACAGATTTTCGAGTCCCACAGTCAATATGCACCATGTTTAATGTT
ATGGTTGATGCCAAAGCTCAATCAACAAAACTTTGCAGCATGGAAATGGGCCAAGAGCAT
CAATACCATTCAAAAATAGACGAACTAATTGAAGAAACTGTTAAAGAAATGATAACACTC
TTGGTTGCAAAGTTCGTTACTATCTTGGAAGGAGTGCTGGCAAAATTATCCAGATATGAC
GAAGGGACTTTGTTTTCTTCTTTTCTGTCATTTACCGTGAAGGCAGCTTCCAAATATGTG
GATGTACCTAAACCCGGGATGGACGTGGCCGACGCCTACGTGACTTTCGTCCGCCATTCT
CAGGATGTCCTGCGTGATAAGGTCAATGAGGAGATGTACATAGAAAGGTTATTTGATCAA
TGGTACAACAGCTCCATGAACGTGATCTGCACCTGGTTGACGGACCGGATGGACTTACAG
CTTCATATTTATCAGTTGAAAACACTAATTAGGATGGTAAAGAAAACCTACAGAGATTTC
CGATTGCAAGGGGTCCTGGACTCCACCTTAAACAGCAAGACCTATGAAACGATCCGGAAC
CGTCTCACTGTGGAGGAAGCCACAGCATCAGTGAGTGAAGGTGGGGGACTGCAGGGCATC
AGCATGAAGGACAGCGATGAGGAAGACGAAGAAGACGATTAG
|
| Enzyme 13 GenBank Gene ID |
NM_003716.3  |
| Enzyme 13 GeneCard ID |
CADPS  |
| Enzyme 13 GenAtlas ID |
CADPS  |
| Enzyme 13 HGNC ID |
HGNC:1426  |
| Enzyme 13 Chromosome Location |
3 |
| Enzyme 13 Locus |
3p14.2 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Cisternas FA, Vincent JB, Scherer SW, Ray PN: Cloning and characterization of human CADPS and CADPS2, new members of the Ca2+-dependent activator for secretion protein family. Genomics. 2003 Mar;81(3):279-91. [PubMed
]
- Hirosawa M, Nagase T, Ishikawa K, Kikuno R, Nomura N, Ohara O: Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain. DNA Res. 1999 Oct 29;6(5):329-36. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Ann K, Kowalchyk JA, Loyet KM, Martin TF: Novel Ca2+-binding protein (CAPS) related to UNC-31 required for Ca2+-activated exocytosis. J Biol Chem. 1997 Aug 8;272(32):19637-40. [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
]
- Binda AV, Kabbani N, Levenson R: Regulation of dense core vesicle release from PC12 cells by interaction between the D2 dopamine receptor and calcium-dependent activator protein for secretion (CAPS). Biochem Pharmacol. 2005 May 15;69(10):1451-61. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
13262 |
| Enzyme 14 Name |
Calcium-dependent secretion activator 2 |
| Enzyme 14 Synonyms |
- Calcium-dependent activator protein for secretion 2
- CAPS-2
|
| Enzyme 14 Gene Name |
CADPS2 |
| Enzyme 14 Protein Sequence |
>Calcium-dependent secretion activator 2
MLDPSSSEEESDEGLEEESRDVLVAAGSSQRAPPAPTREGRRDAPGRAGGGGAARSVSPS
PSVLSEGRDEPQRQLDDEQERRIRLQLYVFVVRCIAYPFNAKQPTDMARRQQKLNKQQLQ
LLKERFQAFLNGETQIVADEAFCNAVRSYYEVFLKSDRVARMVQSGGCSANDFREVFKKN
IEKRVRSLPEIDGLSKETVLSSWIAKYDAIYRGEEDLCKQPNRMALSAVSELILSKEQLY
EMFQQILGIKKLEHQLLYNACQLDNADEQAAQIRRELDGRLQLADKMAKERKFPKFIAKD
MENMYIEELRSSVNLLMANLESLPVSKGGPEFKLQKLKRSQNSAFLDIGDENEIQLSKSD
VVLSFTLEIVIMEVQGLKSVAPNRIVYCTMEVEGEKLQTDQAEASRPQWGTQGDFTTTHP
RPVVKVKLFTESTGVLALEDKELGRVILYPTSNSSKSAELHRMVVPKNSQDSDLKIKLAV
RMDKPAHMKHSGYLYALGQKVWKRWKKRYFVLVQVSQYTFAMCSYREKKSEPQELMQLEG
YTVDYTDPHPGLQGGCMFFNAVKEGDTVIFASDDEQDRILWVQAMYRATGQSYKPVPAIQ
TQKLNPKGGTLHADAQLSGKDADRFQKHGMDEFISANPCKLDHAFLFRILQRQTLDHRLN
DSYSCLGWFSPGQVFVLDEYCARYGVRGCHRHLCYLAELMEHSENGAVIDPTLLHYSFAF
CASHVHGNRPDGIGTVSVEEKERFEEIKERLSSLLENQISHFRYCFPFGRPEGALKATLS
LLERVLMKDIATPIPAEEVKKVVRKCLEKAALINYTRLTEYAKIEETMNQASPARKLEEI
LHLAELCIEVLQQNEEHHAEGREAFAWWPDLLAEHAEKFWALFTVDMDTALEAQPQDSWD
SFPLFQLLNNFLRNDTLLCNGKFHKHLQEIFVPLVVRYVDLMESSIAQSIHRGFEQETWQ
PVKNIANSLPNVALPKVPSLPLNLPQIPNISTASWMPSLYESTNGSATSEDLFWKLDALQ
MFVFDLHWPEQEFAHHLEQRLKLMASDMLEACVKRTRTAFELKLQKASKTTDLRIPASVC
TMFNVLVDAKKQSTKLCALDGGQEQQYHSKIDDLIDNSVKEIISLLVSKFVSVLEGVLSK
LSRYDEGTFFSSILSFTVKAAAKYVDVPKPGMDLADTYIMFVRQNQDILREKVNEEMYIE
KLFDQWYSSSMKVICVWLTDRLDLQLHIYQLKTLIKIVKKTYRDFRLQGVLEGTLNSKTY
DTVHRRLTVEEATASVSEGGGLQGITMKDSDEEEEG
|
| Enzyme 14 Number of Residues |
1296 |
| Enzyme 14 Molecular Weight |
147733.4 |
| Enzyme 14 Theoretical pI |
6.10 |
| Enzyme 14 GO Classification |
Not Available |
| Enzyme 14 General Function |
Involved in lipid binding |
| Enzyme 14 Specific Function |
Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates neurotrophin release from granule cells leading to regulate cell differentiation and survival during cerebellar development. May specifically mediate the Ca(2+)- dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
148839294  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q86UW7  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
CAPS2_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>3891 bp
ATGCTGGACCCGTCTTCCAGCGAAGAGGAGTCGGACGAGGGGCTGGAAGAGGAAAGCCGC
GATGTGCTGGTGGCAGCCGGCAGCTCGCAGCGAGCTCCTCCAGCCCCGACTCGGGAAGGG
CGGCGGGACGCGCCGGGGCGCGCGGGCGGCGGCGGCGCGGCCAGATCTGTGAGCCCGAGC
CCCTCTGTGCTCAGCGAGGGGCGAGACGAGCCCCAGCGGCAGCTGGACGATGAGCAGGAG
CGGAGGATCCGCCTGCAGCTCTACGTCTTCGTCGTGAGGTGCATCGCGTACCCCTTCAAC
GCCAAGCAGCCCACCGACATGGCCCGGAGGCAGCAGAAGCTTAACAAACAACAGTTGCAG
TTACTGAAAGAACGGTTCCAGGCCTTCCTCAATGGGGAAACCCAAATTGTAGCTGACGAA
GCATTTTGCAACGCAGTTCGGAGTTATTATGAGGTTTTTCTAAAGAGTGACCGAGTGGCC
AGAATGGTACAGAGTGGAGGGTGTTCTGCTAATGACTTCAGAGAAGTATTTAAGAAAAAC
ATAGAAAAACGTGTGCGGAGTTTGCCAGAAATAGATGGCTTGAGCAAAGAGACAGTGTTG
AGCTCATGGATAGCCAAATATGATGCCATTTACAGAGGTGAAGAGGACTTGTGCAAACAG
CCAAATAGAATGGCCCTAAGTGCAGTGTCTGAACTTATTCTGAGCAAGGAACAACTCTAT
GAAATGTTTCAGCAGATTCTGGGTATTAAAAAACTGGAACACCAGCTCCTTTATAATGCA
TGTCAGCTGGATAACGCAGATGAACAAGCAGCCCAGATCAGAAGGGAACTTGATGGCCGG
CTGCAATTGGCAGATAAAATGGCAAAGGAAAGAAAATTCCCCAAATTTATAGCAAAAGAT
ATGGAGAATATGTATATAGAAGAGTTGCGGTCTTCAGTGAATTTGCTAATGGCCAATTTG
GAAAGTCTTCCAGTTTCGAAAGGTGGTCCGGAATTTAAATTACAAAAATTAAAACGTTCA
CAGAACTCTGCATTTTTGGACATAGGAGATGAGAATGAGATTCAGCTGTCAAAGTCCGAC
GTGGTACTGTCATTCACCTTAGAGATTGTCATAATGGAAGTGCAAGGCCTGAAGTCAGTT
GCTCCCAATCGAATTGTTTACTGTACAATGGAAGTGGAAGGAGAAAAACTTCAGACAGAC
CAGGCCGAAGCCTCAAGGCCACAATGGGGGACTCAAGGAGATTTCACCACCACCCATCCT
CGGCCTGTGGTCAAAGTGAAACTCTTCACAGAAAGCACTGGAGTTCTGGCCCTGGAAGAT
AAAGAACTGGGAAGGGTGATATTATACCCAACTTCTAATAGCTCCAAATCAGCTGAATTA
CACCGAATGGTAGTTCCAAAAAATAGCCAGGATTCTGACTTAAAAATCAAACTGGCAGTG
CGAATGGATAAACCAGCACATATGAAGCATAGTGGATATCTGTATGCCCTTGGACAGAAG
GTTTGGAAAAGATGGAAAAAACGTTACTTTGTTCTAGTTCAGGTTAGCCAATATACCTTT
GCTATGTGCAGTTATAGAGAAAAGAAGTCTGAACCACAAGAATTAATGCAGCTTGAAGGC
TATACTGTGGATTATACCGATCCCCACCCAGGCCTTCAGGGTGGTTGTATGTTCTTTAAT
GCTGTTAAAGAAGGAGATACTGTAATCTTTGCCAGTGATGATGAACAGGACAGAATATTA
TGGGTTCAAGCCATGTATAGGGCCACAGGTCAATCATATAAACCAGTTCCTGCAATTCAA
ACCCAGAAACTGAATCCTAAAGGAGGAACTCTCCATGCAGATGCTCAGCTTTCTGGTAAA
GATGCAGATCGTTTTCAGAAACATGGTATGGATGAGTTTATTTCTGCAAACCCCTGCAAG
CTTGATCATGCCTTCCTTTTTAGAATACTCCAGAGGCAGACTTTGGATCACAGACTGAAT
GATTCCTATTCTTGCTTGGGATGGTTTAGCCCTGGCCAAGTCTTTGTGTTAGATGAGTAC
TGTGCCCGTTATGGTGTGAGAGGCTGTCACAGACATCTCTGCTACCTTGCAGAACTGATG
GAACATTCAGAAAATGGTGCTGTCATTGACCCTACCCTGCTCCATTACAGCTTTGCATTC
TGTGCCTCTCATGTGCACGGCAACAGGCCTGATGGAATTGGGACTGTTTCAGTGGAAGAA
AAAGAAAGATTTGAGGAGATAAAAGAGAGACTCTCTTCCCTTTTAGAAAATCAGATAAGC
CATTTCAGATACTGTTTTCCCTTTGGACGACCTGAAGGTGCTCTAAAAGCTACACTTTCA
TTACTTGAAAGGGTTTTAATGAAAGATATTGCCACTCCCATACCAGCAGAAGAGGTGAAG
AAAGTGGTCAGAAAATGTCTCGAGAAAGCTGCCTTGATCAATTACACTAGACTCACAGAA
TATGCCAAAATAGAAGAGACCATGAACCAGGCATCTCCTGCTAGAAAGCTGGAAGAGATT
CTTCATCTGGCAGAGCTCTGCATAGAAGTCTTACAGCAGAATGAAGAGCATCATGCAGAG
GGAAGAGAGGCATTTGCCTGGTGGCCTGATTTATTGGCTGAACATGCAGAGAAATTTTGG
GCTTTATTTACAGTGGATATGGACACTGCACTAGAGGCTCAACCGCAAGACTCCTGGGAT
AGTTTTCCTCTTTTCCAACTGCTTAATAATTTCCTCCGAAATGACACACTTTTGTGTAAT
GGAAAATTTCACAAACACTTGCAAGAAATCTTTGTACCCTTGGTTGTCCGCTATGTGGAT
CTCATGGAGTCTTCCATCGCCCAGTCAATTCACAGAGGTTTTGAGCAGGAGACATGGCAG
CCTGTCAAGAATATCGCCAACAGTCTTCCCAATGTAGCTCTTCCAAAAGTTCCAAGTCTG
CCTCTTAATCTTCCACAGATTCCTAACATTTCTACTGCTTCGTGGATGCCTTCTTTATAT
GAGTCCACCAATGGCTCAGCAACATCAGAAGACCTTTTTTGGAAGCTTGATGCACTGCAA
ATGTTTGTCTTTGATCTGCACTGGCCAGAACAGGAATTTGCCCACCACTTAGAGCAAAGA
CTTAAACTAATGGCCAGTGATATGCTAGAGGCCTGTGTCAAAAGAACAAGAACTGCATTT
GAACTCAAGCTACAAAAGGCAAGCAAAACAACTGACTTGCGCATTCCAGCTTCCGTTTGC
ACTATGTTTAATGTATTAGTCGATGCCAAAAAGCAAAGCACCAAACTCTGTGCCCTGGAT
GGAGGACAAGAGCAACAGTACCATTCAAAAATAGATGATCTGATCGACAACAGTGTAAAA
GAAATCATTTCACTGTTAGTTTCAAAGTTTGTTTCAGTGTTGGAAGGCGTGTTGTCTAAG
CTGTCAAGGTATGATGAAGGCACTTTCTTTTCATCCATTCTGTCATTCACTGTGAAAGCA
GCTGCAAAATATGTTGATGTTCCAAAACCAGGAATGGATCTGGCAGACACCTATATTATG
TTTGTTCGGCAAAACCAAGATATTCTTCGAGAAAAGGTCAATGAGGAAATGTATATAGAA
AAGTTATTTGATCAATGGTACAGCAGTTCCATGAAAGTCATTTGCGTGTGGTTGACTGAT
AGATTAGACCTCCAACTCCATATTTACCAGCTGAAGACGCTCATCAAGATTGTGAAGAAA
ACCTACAGGGACTTTCGATTGCAGGGTGTGTTGGAAGGAACACTGAACAGTAAGACTTAT
GATACTGTGCACAGACGTTTAACAGTAGAGGAGGCCACAGCCTCTGTTTCAGAAGGAGGA
GGACTTCAGGGCATTACTATGAAAGACAGTGACGAAGAAGAAGAAGGCTGA
|
| Enzyme 14 GenBank Gene ID |
NM_017954.10  |
| Enzyme 14 GeneCard ID |
CADPS2  |
| Enzyme 14 GenAtlas ID |
CADPS2  |
| Enzyme 14 HGNC ID |
HGNC:16018  |
| Enzyme 14 Chromosome Location |
7 |
| Enzyme 14 Locus |
7q31.3 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Speidel D, Varoqueaux F, Enk C, Nojiri M, Grishanin RN, Martin TF, Hofmann K, Brose N, Reim K: A family of Ca2+-dependent activator proteins for secretion: comparative analysis of structure, expression, localization, and function. J Biol Chem. 2003 Dec 26;278(52):52802-9. Epub 2003 Oct 6. [PubMed
]
- Cisternas FA, Vincent JB, Scherer SW, Ray PN: Cloning and characterization of human CADPS and CADPS2, new members of the Ca2+-dependent activator for secretion protein family. Genomics. 2003 Mar;81(3):279-91. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed
]
- 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
]
- 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
]
- Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Aug 31;7(4):273-81. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Binda AV, Kabbani N, Levenson R: Regulation of dense core vesicle release from PC12 cells by interaction between the D2 dopamine receptor and calcium-dependent activator protein for secretion (CAPS). Biochem Pharmacol. 2005 May 15;69(10):1451-61. [PubMed
]
- Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
16425 |
| Enzyme 15 Name |
cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a) |
| Enzyme 15 Synonyms |
Not Available |
| Enzyme 15 Gene Name |
MAOB |
| Enzyme 15 Protein Sequence |
>cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a)
MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSY
VGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWR
TMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEV
SALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQ
TRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVY
YKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEER
LKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDR
IYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTT
FLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV
|
| Enzyme 15 Number of Residues |
520 |
| Enzyme 15 Molecular Weight |
58764 |
| Enzyme 15 Theoretical pI |
7.55 |
| Enzyme 15 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Amino acid transport and metabolism |
| Enzyme 15 Specific Function |
Not Available |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
Not Available |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
B2R6R3  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
B2R6R3_HUMAN  |
| Enzyme 15 PDB ID |
2BK3  |
| Enzyme 15 PDB File |
Show |
| Enzyme 15 3D Structure |
|
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
Not Available |
| Enzyme 15 GenBank Gene ID |
AK312679  |
| Enzyme 15 GeneCard ID |
B2R6R3  |
| Enzyme 15 GenAtlas ID |
Not Available |
| Enzyme 15 HGNC ID |
Not Available |
| Enzyme 15 Chromosome Location |
Not Available |
| Enzyme 15 Locus |
Not Available |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
Not Available |
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
17081 |
| Enzyme 16 Name |
D(3) dopamine receptor |
| Enzyme 16 Synonyms |
- Dopamine D3 receptor
|
| Enzyme 16 Gene Name |
DRD3 |
| Enzyme 16 Protein Sequence |
>D(3) dopamine receptor
MASLSQLSSHLNYTCGAENSTGASQARPHAYYALSYCALILAIVFGNGLVCMAVLKERAL
QTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILN
LCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPTV
CSISNPDFVIYSSVVSFYLPFGVTVLVYARIYVVLKQRRRKRILTRQNSQCNSVRPGFPQ
QTLSPDPAHLELKRYYSICQDTALGGPGFQERGGELKREEKTRNSLSPTIAPKLSLEVRK
LSNGRLSTSLKLGPLQPRGVPLREKKATQMVAIVLGAFIVCWLPFFLTHVLNTHCQTCHV
SPELYSATTWLGYVNSALNPVIYTTFNIEFRKAFLKILSC
|
| Enzyme 16 Number of Residues |
400 |
| Enzyme 16 Molecular Weight |
44224.3 |
| Enzyme 16 Theoretical pI |
9.07 |
| Enzyme 16 GO Classification |
| Function |
- G-protein coupled amine receptor activity
- G-protein coupled receptor activity
- dopamine 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 16 General Function |
Involved in G-protein coupled receptor protein signaling pathway |
| Enzyme 16 Specific Function |
This is one of the five types (D1 to D5) of receptors for dopamine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Promotes cell proliferation |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
Not Available |
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
- 33-55
67-92
105-126
150-172
186-209
330-351
367-388
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
Not Available |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P35462  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
DRD3_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1203 bp
ATGGCATCTCTGAGTCAGCTGAGTAGCCACCTGAACTACACCTGTGGGGCAGAGAACTCC
ACAGGTGCCAGCCAGGCCCGCCCACATGCCTACTATGCCCTCTCCTACTGCGCGCTCATC
CTGGCCATCGTCTTCGGCAATGGCCTGGTGTGCATGGCTGTGCTGAAGGAGCGGGCCCTG
CAGACTACCACCAACTACTTAGTAGTGAGCCTGGCTGTGGCAGACTTGCTGGTGGCCACC
TTGGTGATGCCCTGGGTGGTATACCTGGAGGTGACAGGTGGAGTCTGGAATTTCAGCCGC
ATTTGCTGTGATGTTTTTGTCACCCTGGATGTCATGATGTGTACAGCCAGCATCCTTAAT
CTCTGTGCCATCAGCATAGACAGGTACACTGCAGTGGTCATGCCCGTTCACTACCAGCAT
GGCACGGGACAGAGCTCCTGTCGGCGCGTGGCCCTCATGATCACGGCCGTCTGGGTACTG
GCCTTTGCTGTGTCCTGCCCTCTTCTGTTTGGCTTTAATACCACAGGGGACCCCACTGTC
TGCTCCATCTCCAACCCTGATTTTGTCATCTACTCTTCAGTGGTGTCCTTCTACCTGCCC
TTTGGAGTGACTGTCCTTGTCTATGCCAGAATCTATGTGGTGCTGAAACAAAGGAGACGG
AAAAGGATCCTCACTCGACAGAACAGTCAGTGCAACAGTGTCAGGCCTGGCTTCCCCCAA
CAAACCCTCTCTCCTGACCCGGCACATCTGGAGCTGAAGCGTTACTACAGCATCTGCCAG
GACACTGCCTTGGGTGGACCAGGCTTCCAAGAAAGAGGAGGAGAGTTGAAAAGAGAGGAG
AAGACTCGGAATTCCCTGAGTCCCACCATAGCGCCCAAGCTCAGCTTAGAAGTTCGAAAA
CTCAGCAATGGCAGATTATCGACATCTTTGAAGCTGGGGCCCCTGCAACCTCGGGGAGTG
CCACTTCGGGAGAAGAAGGCAACCCAAATGGTGGCCATTGTGCTTGGGGCCTTCATTGTC
TGCTGGCTGCCCTTCTTCTTGACCCATGTTCTCAATACCCACTGCCAGACATGCCACGTG
TCCCCAGAGCTTTACAGTGCCACGACATGGCTGGGCTACGTGAATAGCGCCCTCAACCCT
GTGATCTATACCACCTTCAATATCGAGTTCCGGAAAGCCTTCCTCAAGATCCTGTCTTGC
TGA
|
| Enzyme 16 GenBank Gene ID |
U32499  |
| Enzyme 16 GeneCard ID |
DRD3  |
| Enzyme 16 GenAtlas ID |
DRD3  |
| Enzyme 16 HGNC ID |
HGNC:3024  |
| Enzyme 16 Chromosome Location |
3 |
| Enzyme 16 Locus |
3q13.3 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Giros B, Martres MP, Sokoloff P, Schwartz JC: [Gene cloning of human dopaminergic D3 receptor and identification of its chromosome] C R Acad Sci III. 1990;311(13):501-8. [PubMed
]
- Schmauss C, Haroutunian V, Davis KL, Davidson M: Selective loss of dopamine D3-type receptor mRNA expression in parietal and motor cortices of patients with chronic schizophrenia. Proc Natl Acad Sci U S A. 1993 Oct 1;90(19):8942-6. [PubMed
]
- Liu K, Bergson C, Levenson R, Schmauss C: On the origin of mRNA encoding the truncated dopamine D3-type receptor D3nf and detection of D3nf-like immunoreactivity in human brain. J Biol Chem. 1994 Nov 18;269(46):29220-6. [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
]
- Villar VA, Jones JE, Armando I, Palmes-Saloma C, Yu P, Pascua AM, Keever L, Arnaldo FB, Wang Z, Luo Y, Felder RA, Jose PA: G protein-coupled receptor kinase 4 (GRK4) regulates the phosphorylation and function of the dopamine D3 receptor. J Biol Chem. 2009 Aug 7;284(32):21425-34. Epub 2009 Jun 11. [PubMed
]
- Chen CH, Liu MY, Wei FC, Koong FJ, Hwu HG, Hsiao KJ: Further evidence of no association between Ser9Gly polymorphism of dopamine D3 receptor gene and schizophrenia. Am J Med Genet. 1997 Feb 21;74(1):40-3. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
- Lucotte G, Lagarde JP, Funalot B, Sokoloff P: Linkage with the Ser9Gly DRD3 polymorphism in essential tremor families. Clin Genet. 2006 May;69(5):437-40. [PubMed
]
- Jeanneteau F, Funalot B, Jankovic J, Deng H, Lagarde JP, Lucotte G, Sokoloff P: A functional variant of the dopamine D3 receptor is associated with risk and age-at-onset of essential tremor. Proc Natl Acad Sci U S A. 2006 Jul 11;103(28):10753-8. Epub 2006 Jun 29. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
17083 |
| Enzyme 17 Name |
D(1A) dopamine receptor |
| Enzyme 17 Synonyms |
- Dopamine D1 receptor
|
| Enzyme 17 Gene Name |
DRD1 |
| Enzyme 17 Protein Sequence |
>D(1A) dopamine receptor
MRTLNTSAMDGTGLVVERDFSVRILTACFLSLLILSTLLGNTLVCAAVIRFRHLRSKVTN
FFVISLAVSDLLVAVLVMPWKAVAEIAGFWPFGSFCNIWVAFDIMCSTASILNLCVISVD
RYWAISSPFRYERKMTPKAAFILISVAWTLSVLISFIPVQLSWHKAKPTSPSDGNATSLA
ETIDNCDSSLSRTYAISSSVISFYIPVAIMIVTYTRIYRIAQKQIRRIAALERAAVHAKN
CQTTTGNGKPVECSQPESSFKMSFKRETKVLKTLSVIMGVFVCCWLPFFILNCILPFCGS
GETQPFCIDSNTFDVFVWFGWANSSLNPIIYAFNADFRKAFSTLLGCYRLCPATNNAIET
VSINNNGAAMFSSHHEPRGSISKECNLVYLIPHAVGSSEDLKKEEAAGIARPLEKLSPAL
SVILDYDTDVSLEKIQPITQNGQHPT
|
| Enzyme 17 Number of Residues |
446 |
| Enzyme 17 Molecular Weight |
49292.8 |
| Enzyme 17 Theoretical pI |
8.34 |
| Enzyme 17 GO Classification |
| Function |
- G-protein coupled amine receptor activity
- G-protein coupled receptor activity
- dopamine 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 17 General Function |
Involved in G-protein coupled receptor protein signaling pathway |
| Enzyme 17 Specific Function |
This is one of the five types (D1 to D5) of receptors for dopamine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
Not Available |
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
- 24-49
61-87
97-119
139-163
193-218
273-299
313-337
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
30399  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
P21728  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
DRD1_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>1341 bp
ATGAGGACTCTGAACACCTCTGCCATGGACGGGACTGGGCTGGTGGTGGAGAGGGACTTC
TCTGTTCGTATCCTCACTGCCTGTTTCCTGTCGCTGCTCATCCTGTCCACGCTCCTGGGG
AACACGCTGGTCTGTGCTGCCGTTATCAGGTTCCGACACCTGCGGTCCAAGGTGACCAAC
TTCTTTGTCATCTCCTTGGCTGTGTCAGATCTCTTGGTGGCCGTCCTGGTCATGCCCTGG
AAGGCAGTGGCTGAGATTGCTGGCTTCTGGCCCTTTGGGTCCTTCTGTAACATCTGGGTG
GCCTTTGACATCATGTGCTCCACTGCATCCATCCTCAACCTCTGTGTGATCAGCGTGGAC
AGGTATTGGGCTATCTCCAGCCCTTTCCGGTATGAGAGAAAGATGACCCCCAAGGCAGCC
TTCATCCTGATCAGTGTGGCATGGACCTTGTCTGTACTCATCTCCTTCATCCCAGTGCAG
CTCAGCTGGCACAAGGCAAAACCCACAAGCCCCTCTGATGGAAATGCCACTTCCCTGGCT
GAGACCATAGACAACTGTGACTCCAGCCTCAGCAGGACATATGCCATCTCATCCTCTGTA
ATAAGCTTTTACATCCCTGTGGCCATCATGATTGTCACCTACACCAGGATCTACAGGATT
GCTCAGAAACAAATACGGCGCATTGCGGCCTTGGAGAGGGCAGCAGTCCACGCCAAGAAT
TGCCAGACCACCACAGGTAATGGAAAGCCTGTCGAATGTTCTCAACCGGAAAGTTCTTTT
AAGATGTCCTTCAAAAGAGAAACTAAAGTCCTGAAGACTCTGTCGGTGATCATGGGTGTG
TTTGTGTGCTGTTGGCTACCTTTCTTCATCTTGAACTGCATTTTGCCCTTCTGTGGGTCT
GGGGAGACGCAGCCCTTCTGCATTGATTCCAACACCTTTGACGTGTTTGTGTGGTTTGGG
TGGGCTAATTCATCCTTGAACCCCATCATTTATGCCTTTAATGCTGATTTTCGGAAGGCA
TTTTCAACCCTCTTAGGATGCTACAGACTTTGCCCTGCGACGAATAATGCCATAGAGACG
GTGAGTATCAATAACAATGGGGCCGCGATGTTTTCCAGCCATCATGAGCCACGAGGCTCC
ATCTCCAAGGAGTGCAATCTGGTTTACCTGATCCCACATGCTGTGGGCTCCTCTGAGGAC
CTGAAAAAGGAGGAGGCAGCTGGCATCGCCAGACCCTTGGAGAAGCTGTCCCCAGCCCTA
TCGGTCATATTGGACTATGACACTGACGTCTCTCTGGAGAAGATCCAACCCATGACACAA
AACGGTCAGCACCCAACCTGA
|
| Enzyme 17 GenBank Gene ID |
X58987  |
| Enzyme 17 GeneCard ID |
DRD1  |
| Enzyme 17 GenAtlas ID |
DRD1  |
| Enzyme 17 HGNC ID |
HGNC:3020  |
| Enzyme 17 Chromosome Location |
5 |
| Enzyme 17 Locus |
5q35.1 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Dearry A, Gingrich JA, Falardeau P, Fremeau RT Jr, Bates MD, Caron MG: Molecular cloning and expression of the gene for a human D1 dopamine receptor. Nature. 1990 Sep 6;347(6288):72-6. [PubMed
]
- Zhou QY, Grandy DK, Thambi L, Kushner JA, Van Tol HH, Cone R, Pribnow D, Salon J, Bunzow JR, Civelli O: Cloning and expression of human and rat D1 dopamine receptors. Nature. 1990 Sep 6;347(6288):76-80. [PubMed
]
- Sunahara RK, Niznik HB, Weiner DM, Stormann TM, Brann MR, Kennedy JL, Gelernter JE, Rozmahel R, Yang YL, Israel Y, et al.: Human dopamine D1 receptor encoded by an intronless gene on chromosome 5. Nature. 1990 Sep 6;347(6288):80-3. [PubMed
]
- Ohara K, Ulpian C, Seeman P, Sunahara RK, Van Tol HH, Niznik HB: Schizophrenia: dopamine D1 receptor sequence is normal, but has DNA polymorphisms. Neuropsychopharmacology. 1993 Feb;8(2):131-5. [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
]
- Jin H, Xie Z, George SR, O'Dowd BF: Palmitoylation occurs at cysteine 347 and cysteine 351 of the dopamine D(1) receptor. Eur J Pharmacol. 1999 Dec 15;386(2-3):305-12. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
17108 |
| Enzyme 18 Name |
D(1B) dopamine receptor |
| Enzyme 18 Synonyms |
- D(5) dopamine receptor
- D1beta dopamine receptor
- Dopamine D5 receptor
|
| Enzyme 18 Gene Name |
DRD5 |
| Enzyme 18 Protein Sequence |
>D(1B) dopamine receptor
MLPPGSNGTAYPGQFALYQQLAQGNAVGGSAGAPPLGPSQVVTACLLTLLIIWTLLGNVL
VCAAIVRSRHLRANMTNVFIVSLAVSDLFVALLVMPWKAVAEVAGYWPFGAFCDVWVAFD
IMCSTASILNLCVISVDRYWAISRPFRYKRKMTQRMALVMVGLAWTLSILISFIPVQLNW
HRDQAASWGGLDLPNNLANWTPWEEDFWEPDVNAENCDSSLNRTYAISSSLISFYIPVAI
MIVTYTRIYRIAQVQIRRISSLERAAEHAQSCRSSAACAPDTSLRASIKKETKVLKTLSV
IMGVFVCCWLPFFILNCMVPFCSGHPEGPPAGFPCVSETTFDVFVWFGWANSSLNPVIYA
FNADFQKVFAQLLGCSHFCSRTPVETVNISNELISYNQDIVFHKEIAAAYIHMMPNAVTP
GNREVDNDEEEGPFDRMFQIYQTSPDGDPVAESVWELDCEGEISLDKITPFTPNGFH
|
| Enzyme 18 Number of Residues |
477 |
| Enzyme 18 Molecular Weight |
52950.5 |
| Enzyme 18 Theoretical pI |
5.08 |
| Enzyme 18 GO Classification |
| Function |
- G-protein coupled amine receptor activity
- G-protein coupled receptor activity
- dopamine 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 18 General Function |
Involved in G-protein coupled receptor protein signaling pathway |
| Enzyme 18 Specific Function |
This is one of the five types (D1 to D5) of receptors for dopamine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase |
| Enzyme 18 Pathways |
Not Available |
| Enzyme 18 Reactions |
Not Available |
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
- 40-66
78-104
115-136
159-180
224-246
297-320
341-360
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
22658483  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
P21918  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
DRD5_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1434 bp
ATGCTGCCGCCAGGCAGCAACGGCACCGCGTACCCGGGGCAGTTCGCTCTATACCAGCAG
CTGGCGCAGGGGAACGCCGTGGGGGGCTCGGCGGGGGCACCGCCACTGGGGCCCTCACAG
GTGGTCACCGCCTGCCTGCTGACCCTACTCATCATCTGGACCCTGCTGGGCAACGTGCTG
GTGTGCGCAGCCATCGTGCGGAGCCGCCACCTGCGCGCCAACATGACCAACGTCTTCATC
GTGTCTCTGGCCGTGTCAGACCTTTTCGTGGCGCTGCTGGTCATGCCCTGGAAGGCAGTC
GCCGAGGTGGCCGGTTACTGGCCCTTTGGAGCGTTCTGCGACGTCTGGGTGGCCTTCGAC
ATCATGTGCTCCACTGCCTCCATCCTGAACCTGTGCGTCATCAGCGTGGACCGCTACTGG
GCCATCTCCAGGCCCTTCCGCTACAAGCGCAAGATGACTCAGCGCATGGCCTTGGTCATG
GTCGGCCTGGCATGGACCTTGTCCATCCTCATCTCCTTCATTCCGGTCCAGCTCAACTGG
CACAGGGACCAGGCGGCCTCTTGGGGCGGGCTGGACCTGCCAAACAACCTGGCCAACTGG
ACGCCCTGGGAGGAGGACTTTTGGGAGCCCGACGTGAATGCAGAGAACTGTGACTCCAGC
CTGAATCGAACCTACGCCATCTCTTCCTCGCTCATCAGCTTCTACATCCCCGTTGCCATC
ATGATCGTGACCTACACGCGCATCTACCGCATCGCCCAGGTGCAGATCCGCAGGATTTCC
TCCCTGGAGAGGGCCGCAGAGCACGCGCAGAGCTGCCGGAGCAGCGCAGCCTGCGCGCCC
GACWCCAGCCTGCGCGCTTCCATCAAGAAGGAGACCAAGGTTCTCAAGACCCTGTCGGTG
ATCATGGGGGTCTTCGTGTGTTGCTGGCTGCCCTTCTTCATCCTTAACTGCATGGTCCCT
TTCTGCAGTGGACACCCTGAAGGCCCTCCGGCCGGCTTCCCCTGCGTCAGTGAGACCACC
TTCGACGTCTTCGTCTGGTTCGGCTGGGCTAACTCCTCACTCAACCCCGTCATCTATGCC
TTCAACGCCGACTTTCAGAAGGTGTTTGCCCAGCTGCTGGGGTGCAGCCACTTCTGCTCC
CGCACGCCGGTGGAGACGGTGAACATCAGCAATGAGCTCATCTCCTACAACCAAGACATC
GTCTTCCACAAGGAAATCGCAGCTGCCTACATCCACATGATGCCCAACGCCGTTACCCCC
GGCAACCGGGAGGTGGACAACGACGAGGAGGAGGGTCCTTTCGATCGCATGTTCCAGATC
TATCAGACGTCCCCAGATGGTGACCCTGTTGCTGAGTCTGTCTGGGAGCTGGACTGCGAG
GGGGAGATTTCTTTAGACAAAATAACACCTTTCACCCCGAATGGATTCCATTAA
|
| Enzyme 18 GenBank Gene ID |
AY136750  |
| Enzyme 18 GeneCard ID |
DRD5  |
| Enzyme 18 GenAtlas ID |
DRD5  |
| Enzyme 18 HGNC ID |
HGNC:3026  |
| Enzyme 18 Chromosome Location |
4 |
| Enzyme 18 Locus |
4p16.1 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Sunahara RK, Guan HC, O'Dowd BF, Seeman P, Laurier LG, Ng G, George SR, Torchia J, Van Tol HH, Niznik HB: Cloning of the gene for a human dopamine D5 receptor with higher affinity for dopamine than D1. Nature. 1991 Apr 18;350(6319):614-9. [PubMed
]
- Grandy DK, Zhang YA, Bouvier C, Zhou QY, Johnson RA, Allen L, Buck K, Bunzow JR, Salon J, Civelli O: Multiple human D5 dopamine receptor genes: a functional receptor and two pseudogenes. Proc Natl Acad Sci U S A. 1991 Oct 15;88(20):9175-9. [PubMed
]
- Weinshank RL, Adham N, Macchi M, Olsen MA, Branchek TA, Hartig PR: Molecular cloning and characterization of a high affinity dopamine receptor (D1 beta) and its pseudogene. J Biol Chem. 1991 Nov 25;266(33):22427-35. [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
]
- Karpa KD, Lidow MS, Pickering MT, Levenson R, Bergson C: N-linked glycosylation is required for plasma membrane localization of D5, but not D1, dopamine receptors in transfected mammalian cells. Mol Pharmacol. 1999 Nov;56(5):1071-8. [PubMed
]
- Misbahuddin A, Placzek MR, Chaudhuri KR, Wood NW, Bhatia KP, Warner TT: A polymorphism in the dopamine receptor DRD5 is associated with blepharospasm. Neurology. 2002 Jan 8;58(1):124-6. [PubMed
]
- Sobell JL, Lind TJ, Sigurdson DC, Zald DH, Snitz BE, Grove WM, Heston LL, Sommer SS: The D5 dopamine receptor gene in schizophrenia: identification of a nonsense change and multiple missense changes but lack of association with disease. Hum Mol Genet. 1995 Apr;4(4):507-14. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
17111 |
| Enzyme 19 Name |
Dopamine D4 receptor |
| Enzyme 19 Synonyms |
Not Available |
| Enzyme 19 Gene Name |
dopamine D4 receptor |
| Enzyme 19 Protein Sequence |
>Dopamine D4 receptor
MGNRSTADADRLLAGRGPAAGASAGASAGLAGQGAAALVGGVLLIGAVLAGNSLVCVSVA
TERALQTPTNSFIVSLAAADLLLALLVLPLFVYSE
|
| Enzyme 19 Number of Residues |
95 |
| Enzyme 19 Molecular Weight |
9148.4 |
| Enzyme 19 Theoretical pI |
4.64 |
| Enzyme 19 GO Classification |
| Function |
| — |
| 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 19 General Function |
Involved in G-protein coupled receptor protein signaling pathway |
| Enzyme 19 Specific Function |
Not Available |
| Enzyme 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
Not Available |
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
1835971  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q99586  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
Q99586_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>285 bp
ATGGGGAACCGCAGCACCGCGGACGCGGACCGGCTGCTGGCTGGGCGCGGGCCGGCCGCG
GGGGCATCTGCGGGGGCATCTGCGGGGCTGGCTGGGCAGGGCGCGGCGGCGCTGGTGGGG
GGCGTGCTGCTCATCGGCGCGGTGCTCGCGGGGAACTCGCTCGTGTGCGTGAGCGTGGCC
ACCGAGCGCGCCCTGCAGACGCCCACCAACTCCTTCATCGTGAGCCTGGCGGCCGCCGAC
CTCCTCCTCGCTCTCCTGGTGCTGCCGCTCTTCGTCTACTCCGAG
|
| Enzyme 19 GenBank Gene ID |
S82917  |
| Enzyme 19 GeneCard ID |
dopamine D4 receptor  |
| Enzyme 19 GenAtlas ID |
dopamine+D4+receptor  |
| Enzyme 19 HGNC ID |
HGNC:3025  |
| Enzyme 19 Chromosome Location |
Not Available |
| Enzyme 19 Locus |
Not Available |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Cichon S, Nothen MM, Catalano M, Di Bella D, Maier W, Lichtermann D, Minges J, Albus M, Borrmann M, Franzek E, et al.: Identification of two novel polymorphisms and a rare deletion variant in the human dopamine D4 receptor gene. Psychiatr Genet. 1995 Fall;5(3):97-103. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
17112 |
| Enzyme 20 Name |
Dopamine D4 receptor |
| Enzyme 20 Synonyms |
Not Available |
| Enzyme 20 Gene Name |
dopamine D4 receptor |
| Enzyme 20 Protein Sequence |
>Dopamine D4 receptor
MGNRSTADADGLLAGRGPAAGASAGASAGLAGQGALLIGAVLAGNSLVCVSVATERALQT
PTNSFIVSLAAADLLLALLVLPLFVYSE
|
| Enzyme 20 Number of Residues |
88 |
| Enzyme 20 Molecular Weight |
8481.6 |
| Enzyme 20 Theoretical pI |
4.23 |
| Enzyme 20 GO Classification |
| Function |
| — |
| 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 20 General Function |
Involved in G-protein coupled receptor protein signaling pathway |
| Enzyme 20 Specific Function |
Not Available |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
1835973  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q99587  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
Q99587_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>264 bp
ATGGGGAACCGCAGCACCGCGGACGCGGACGGGCTGCTGGCTGGGCGCGGGCCGGCCGCG
GGGGCATCTGCGGGGGCATCTGCGGGGCTGGCTGGGCAGGGCGCGCTGCTCATCGGCGCG
GTGCTCGCGGGGAACTCGCTCGTGTGCGTGAGCGTGGCCACCGAGCGCGCCCTGCAGACG
CCCACCAACTCCTTCATCGTGAGCCTGGCGGCCGCCGACCTCCTCCTCGCTCTCCTGGTG
CTGCCGCTCTTCGTCTACTCCGAG
|
| Enzyme 20 GenBank Gene ID |
S82918  |
| Enzyme 20 GeneCard ID |
dopamine D4 receptor  |
| Enzyme 20 GenAtlas ID |
dopamine+D4+receptor  |
| Enzyme 20 HGNC ID |
HGNC:3025  |
| Enzyme 20 Chromosome Location |
Not Available |
| Enzyme 20 Locus |
Not Available |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Cichon S, Nothen MM, Catalano M, Di Bella D, Maier W, Lichtermann D, Minges J, Albus M, Borrmann M, Franzek E, et al.: Identification of two novel polymorphisms and a rare deletion variant in the human dopamine D4 receptor gene. Psychiatr Genet. 1995 Fall;5(3):97-103. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |