|
Drug Target 1
[top]
|
| Target 1 ID |
23 |
| Target 1 Name |
D(1A) dopamine receptor |
| Target 1 Synonyms |
Not Available |
| Target 1 Gene Name |
DRD1 |
| Target 1 Protein Sequence |
>D(1A) dopamine receptor
MRTLNTSAMDGTGLVVERDFSVRILTACFLSLLILSTLLGNTLVCAAVIRFRHLRSKVTN
FFVISLAVSDLLVAVLVMPWKAVAEIAGFWPFGSFCNIWVAFDIMCSTASILNLCVISVD
RYWAISSPFRYERKMTPKAAFILISVAWTLSVLISFIPVQLSWHKAKPTSPSDGNATSLA
ETIDNCDSSLSRTYAISSSVISFYIPVAIMIVTYTRIYRIAQKQIRRIAALERAAVHAKN
CQTTTGNGKPVECSQPESSFKMSFKRETKVLKTLSVIMGVFVCCWLPFFILNCILPFCGS
GETQPFCIDSNTFDVFVWFGWANSSLNPIIYAFNADFRKAFSTLLGCYRLCPATNNAIET
VSINNNGAAMFSSHHEPRGSISKECNLVYLIPHAVGSSEDLKKEEAAGIARPLEKLSPAL
SVILDYDTDVSLEKIQPITQNGQHPT
|
| Target 1 Number of Residues |
453 |
| Target 1 Molecular Weight |
49294 |
| Target 1 Theoretical pI |
8.34 |
| Target 1 GO Classification |
|
Function
|
signal transducer activity
receptor activity
transmembrane receptor activity
G-protein coupled receptor activity
rhodopsin-like receptor activity
amine receptor activity
dopamine receptor activity |
|
Process
|
cellular process
cell communication
signal transduction
cell surface receptor linked signal transduction
G-protein coupled receptor protein signaling pathway |
|
Component
|
cell
membrane
intrinsic to membrane
integral to membrane |
|
| Target 1 General Function |
Involved in dopamine receptor activity |
| Target 1 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 |
| Target 1 Pathways |
Not Available
|
| Target 1 Reactions |
Not Available |
| Target 1 Pfam Domain Function |
|
| Target 1 Signals |
|
| Target 1 Transmembrane Regions |
- 24-49
- 61-87
- 97-119
- 139-163
- 193-218
- 273-299
- 313-337
|
| Target 1 Essentiality |
Non-Essential |
| Target 1 GenBank ID Protein |
30397  |
| Target 1 UniProtKB/Swiss-Prot ID |
P21728  |
| Target 1 UniProtKB/Swiss-Prot Entry Name |
DRD1_HUMAN  |
| Target 1 PDB ID |
Not Available |
| Target 1 Cellular Location |
- Cell membrane
- endoplasmic reticulum membrane
- m
- multi-pass membrane protein. Endoplasmic reticulum
|
| Target 1 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
TCGGTCATATTGGACTATGACACTGACGTCTCTCTGGAGAAGATCCAACCCATCACACAA
AACGGTCAGCACCCAACCTGA
|
| Target 1 GenBank Gene ID |
|
| Target 1 GeneCard ID |
DRD1  |
| Target 1 GenAtlas ID |
DRD1  |
| Target 1 HGNC ID |
HGNC:3020  |
| Target 1 Chromosome Location |
5 |
| Target 1 Locus |
5q35.1 |
| Target 1 SNPs |
SNPJam Report  |
| Target 1 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| Target 1 Drug References |
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed
]
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed
]
|
|
Drug Target 2
[top]
|
| Target 2 ID |
828 |
| Target 2 Name |
Phenylalanine-4-hydroxylase |
| Target 2 Synonyms |
- EC 1.14.16.1
- PAH
- Phe-4- monooxygenase
|
| Target 2 Gene Name |
PAH |
| Target 2 Protein Sequence |
>Phenylalanine-4-hydroxylase
MSTAVLENPGLGRKLSDFGQETSYIEDNCNQNGAISLIFSLKEEVGALAKVLRLFEENDV
NLTHIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTVPW
FPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYM
EEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGF
RLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFA
QFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSE
KPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQR
IEVLDNTQQLKILADSINSEIGILCSALQKIK
|
| Target 2 Number of Residues |
459 |
| Target 2 Molecular Weight |
51863 |
| Target 2 Theoretical pI |
6.57 |
| Target 2 GO Classification |
|
Function
|
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
phenylalanine 4-monooxygenase activity
amine binding
amino acid binding
binding
ion binding
cation binding
transition metal ion binding
iron ion binding
catalytic activity
oxidoreductase activity
monooxygenase activity |
|
Process
|
L-phenylalanine metabolism
L-phenylalanine catabolism
physiological process
metabolism
cellular metabolism
amino acid and derivative metabolism
amino acid metabolism
aromatic amino acid family metabolism |
|
Component
|
| Not Available |
|
| Target 2 General Function |
Amino acid transport and metabolism |
| Target 2 Specific Function |
Not Available |
| Target 2 Pathways |
| Name |
SMPDB Link |
KEGG Link |
| Phenylalanine, tyrosine and tryptophan biosynthesis |
|
map00400  |
|
| Target 2 Reactions |
- L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
|
| Target 2 Pfam Domain Function |
|
| Target 2 Signals |
|
| Target 2 Transmembrane Regions |
|
| Target 2 Essentiality |
Non-Essential |
| Target 2 GenBank ID Protein |
189937  |
| Target 2 UniProtKB/Swiss-Prot ID |
P00439  |
| Target 2 UniProtKB/Swiss-Prot Entry Name |
PH4H_HUMAN  |
| Target 2 PDB ID |
2PHM  |
| Target 2 PDB File |
Show |
| Target 2 3D Structure |
|
| Target 2 Cellular Location |
Not Available |
| Target 2 Gene Sequence |
>1359 bp
ATGTCCACTGCGGTCCTGGAAAACCCAGGCTTGGGCAGGAAACTCTCTGACTTTGGACAG
GAAACAAGCTATATTGAAGACAACTGCAATCAAAATGGTGCCATATCACTGATCTTCTCA
CTCAAAGAAGAAGTTGGTGCATTGGCCAAAGTATTGCGCTTATTTGAGGAGAATGATGTA
AACCTGACCCACATTGAATCTAGACCTTCTCGTTTAAAGAAAGATGAGTATGAATTTTTC
ACCCATTTGGATAAACGTAGCCTGCCTGCTCTGACAAACATCATCAAGATCTTGAGGCAT
GACATTGGTGCCACTGTCCATGAGCTTTCACGAGATAAGAAGAAAGACACAGTGCCCTGG
TTCCCAAGAACCATTCAAGAGCTGGACAGATTTGCCAATCAGATTCTCAGCTATGGAGCG
GAACTGGATGCTGACCACCCTGGTTTTAAAGATCCTGTGTACCGTGCAAGACGGAAGCAG
TTTGCTGACATTGCCTACAACTACCGCCATGGGCAGCCCATCCCTCGAGTGGAATACATG
GAGGAAGAAAAGAAAACATGGGGCACAGTGTTCAAGACTCTGAAGTCCTTGTATAAAACC
CATGCTTGCTATGAGTACAATCACATTTTTCCACTTCTTGAAAAGTACTGTGGCTTCCAT
GAAGATAACATTCCCCAGCTGGAAGACGTTTCTCAATTCCTGCAGACTTGCACTGGTTTC
CGCCTCCGACCTGTGGCTGGCCTGCTTTCCTCTCGGGATTTCTTGGGTGGCCTGGCCTTC
CGAGTCTTCCACTGCACACAGTACATCAGACATGGATCCAAGCCCATGTATACCCCCGAA
CCTGACATCTGCCATGAGCTGTTGGGACATGTGCCCTTGTTTTCAGATCGCAGCTTTGCC
CAGTTTTCCCAGGAAATTGGCCTTGCCTCTCTGGGTGCACCTGATGAATACATTGAAAAG
CTCGCCACAATTTACTGGTTTACTGTGGAGTTTGGGCTCTGCAAACAAGGAGACTCCATA
AAGGCATATGGTGCTGGGCTCCTGTCATCCTTTGGTGAATTACAGTACTGCTTATCAGAG
AAGCCAAAGCTTCTCCCCCTGGAGCTGGAGAAGACAGCCATCCAAAATTACACTGTCACG
GAGTTCCAGCCCCTGTATTACGTGGCAGAGAGTTTTAATGATGCCAAGGAGAAAGTAAGG
AACTTTGCTGCCACAATACCTCGGCCCTTCTCAGTTCGCTACGACCCATACACCCAAAGG
ATTGAGGTCTTGGACAATACCCAGCAGCTTAAGATTTTGGCTGATTCCATTAACAGTGAA
ATTGGAATCCTTTGCAGTGCCCTCCAGAAAATAAAGTAA
|
| Target 2 GenBank Gene ID |
|
| Target 2 GeneCard ID |
PAH  |
| Target 2 GenAtlas ID |
PAH  |
| Target 2 HGNC ID |
HGNC:8582  |
| Target 2 Chromosome Location |
12 |
| Target 2 Locus |
12q22-q24.2 |
| Target 2 SNPs |
SNPJam Report  |
| Target 2 General References |
- Hennermann JB, Vetter B, Wolf C, Windt E, Buhrdel P, Seidel J, Monch E, Kulozik AE: Phenylketonuria and hyperphenylalaninemia in eastern Germany: a characteristic molecular profile and 15 novel mutations. Hum Mutat. 2000;15(3):254-60. [PubMed
]
- Erlandsen H, Bjorgo E, Flatmark T, Stevens RC: Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase. Biochemistry. 2000 Mar 7;39(9):2208-17. [PubMed
]
- Acosta A, Silva W Jr, Carvalho T, Gomes M, Zago M: Mutations of the phenylalanine hydroxylase (PAH) gene in Brazilian patients with phenylketonuria. Hum Mutat. 2001 Feb;17(2):122-30. [PubMed
]
- Gjetting T, Petersen M, Guldberg P, Guttler F: Missense mutations in the N-terminal domain of human phenylalanine hydroxylase interfere with binding of regulatory phenylalanine. Am J Hum Genet. 2001 Jun;68(6):1353-60. Epub 2001 Apr 20. [PubMed
]
- Yang Y, Drummond-Borg M, Garcia-Heras J: Molecular analysis of phenylketonuria (PKU) in newborns from Texas. Hum Mutat. 2001 Jun;17(6):523. [PubMed
]
- Gjetting T, Romstad A, Haavik J, Knappskog PM, Acosta AX, Silva WA Jr, Zago MA, Guldberg P, Guttler F: A phenylalanine hydroxylase amino acid polymorphism with implications for molecular diagnostics. Mol Genet Metab. 2001 Jul;73(3):280-4. [PubMed
]
- Andersen OA, Flatmark T, Hough E: High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin. J Mol Biol. 2001 Nov 23;314(2):279-91. [PubMed
]
- Eisensmith RC, Woo SL: Molecular basis of phenylketonuria and related hyperphenylalaninemias: mutations and polymorphisms in the human phenylalanine hydroxylase gene. Hum Mutat. 1992;1(1):13-23. [PubMed
]
- Lin CH, Hsiao KJ, Tsai TF, Chao HK, Su TS: Identification of a missense phenylketonuria mutation at codon 408 in Chinese. Hum Genet. 1992 Aug;89(6):593-6. [PubMed
]
- Economou-Petersen E, Henriksen KF, Guldberg P, Guttler F: Molecular basis for nonphenylketonuria hyperphenylalaninemia. Genomics. 1992 Sep;14(1):1-5. [PubMed
]
- 1363837 Jaruzelska J, Melle D, Matuszak R, Borski K, Munnich A: A new 15 bp deletion in exon 11 of the phenylalanine hydroxylase gene in phenylketonuria. Hum Mol Genet. 1992 Dec;1(9):763-4.
- 1363838 Desviat LR, Perez B, Ugarte M: A new PKU mutation associated with haplotype 12. Hum Mol Genet. 1992 Dec;1(9):765-6.
- 1671810 Dianzani I, Forrest SM, Camaschella C, Saglio G, Ponzone A, Cotton RG: Screening for mutations in the phenylalanine hydroxylase gene from Italian patients with phenylketonuria by using the chemical cleavage method: a new splice mutation. Am J Hum Genet. 1991 Mar;48(3):631-5.
- 1672290 Dworniczak B, Grudda K, Stumper J, Bartholome K, Aulehla-Scholz C, Horst J: Phenylalanine hydroxylase gene: novel missense mutation in exon 7 causing severe phenylketonuria. Genomics. 1991 Jan;9(1):193-9.
- 1672294 Okano Y, Wang T, Eisensmith RC, Longhi R, Riva E, Giovannini M, Cerone R, Romano C, Woo SL: Phenylketonuria missense mutations in the Mediterranean. Genomics. 1991 Jan;9(1):96-103.
- 1679029 Konecki DS, Lichter-Konecki U: The phenylketonuria locus: current knowledge about alleles and mutations of the phenylalanine hydroxylase gene in various populations. Hum Genet. 1991 Aug;87(4):377-88.
- 1679030 Konecki DS, Schlotter M, Trefz FK, Lichter-Konecki U: The identification of two mis-sense mutations at the PAH gene locus in a Turkish patient with phenylketonuria. Hum Genet. 1991 Aug;87(4):389-93.
- 1709636 Caillaud C, Lyonnet S, Rey F, Melle D, Frebourg T, Berthelon M, Vilarinho L, Vaz Osorio R, Rey J, Munnich A: A 3-base pair in-frame deletion of the phenylalanine hydroxylase gene results in a kinetic variant of phenylketonuria. J Biol Chem. 1991 May 25;266(15):9351-4.
- 1975559 Svensson E, Andersson B, Hagenfeldt L: Two mutations within the coding sequence of the phenylalanine hydroxylase gene. Hum Genet. 1990 Aug;85(3):300-4.
- 2014802 Hofman KJ, Steel G, Kazazian HH, Valle D: Phenylketonuria in U.S. blacks: molecular analysis of the phenylalanine hydroxylase gene. Am J Hum Genet. 1991 Apr;48(4):791-8.
- 2246858 Cotton RG: Heterogeneity of phenylketonuria at the clinical, protein and DNA levels. J Inherit Metab Dis. 1990;13(5):739-50.
- 2461704 Cotton RG, McAdam W, Jennings I, Morgan FJ: A monoclonal antibody to aromatic amino acid hydroxylases. Identification of the epitope. Biochem J. 1988 Oct 1;255(1):193-6.
- 2564729 Lyonnet S, Caillaud C, Rey F, Berthelon M, Frezal J, Rey J, Munnich A: Molecular genetics of phenylketonuria in Mediterranean countries: a mutation associated with partial phenylalanine hydroxylase deficiency. Am J Hum Genet. 1989 Apr;44(4):511-7.
- 2615649 Hofman KJ, Antonarakis SE, Missiou-Tsangaraki S, Boehm CD, Valle D: Phenylketonuria in the Greek population. Haplotype analysis of the phenylalanine hydroxylase gene and identification of a PKU mutation. Mol Biol Med. 1989 Jun;6(3):245-50.
- 2840952 Lichter-Konecki U, Konecki DS, DiLella AG, Brayton K, Marvit J, Hahn TM, Trefz FK, Woo SL: Phenylalanine hydroxylase deficiency caused by a single base substitution in an exon of the human phenylalanine hydroxylase gene. Biochemistry. 1988 Apr 19;27(8):2881-5.
- 2986678 Kwok SC, Ledley FD, DiLella AG, Robson KJ, Woo SL: Nucleotide sequence of a full-length complementary DNA clone and amino acid sequence of human phenylalanine hydroxylase. Biochemistry. 1985 Jan 29;24(3):556-61.
- 7833954 Benit P, Rey F, Melle D, Munnich A, Rey J: Five novel missense mutations of the phenylalanine hydroxylase gene in phenylketonuria. Hum Mutat. 1994;4(3):229-31.
- 8068076 Goebel-Schreiner B, Schreiner R: Identification of a new missense mutation in Japanese phenylketonuric patients. J Inherit Metab Dis. 1993;16(6):950-6.
- 8088845 Guldberg P, Henriksen KF, Thony B, Blau N, Guttler F: Molecular heterogeneity of nonphenylketonuria hyperphenylalaninemia in 25 Danish patients. Genomics. 1994 May 15;21(2):453-5.
- 8098245 Abadie V, Jaruzelska J, Lyonnet S, Millasseau P, Berthelon M, Rey F, Munnich A, Rey J: Illegitimate transcription of the phenylalanine hydroxylase gene in lymphocytes for identification of mutations in phenylketonuria. Hum Mol Genet. 1993 Jan;2(1):31-4.
- 8406445 Guldberg P, Henriksen KF, Guttler F: Molecular analysis of phenylketonuria in Denmark: 99% of the mutations detected by denaturing gradient gel electrophoresis. Genomics. 1993 Jul;17(1):141-6.
- 8594560 Hoang L, Byck S, Prevost L, Scriver CR: PAH Mutation Analysis Consortium Database: a database for disease-producing and other allelic variation at the human PAH locus. Nucleic Acids Res. 1996 Jan 1;24(1):127-31.
- 8889583 Knappskog PM, Eiken HG, Martinez A, Bruland O, Apold J, Flatmark T: PKU mutation (D143G) associated with an apparent high residual enzyme activity: expression of a kinetic variant form of phenylalanine hydroxylase in three different systems. Hum Mutat. 1996;8(3):236-46.
- 8889590 Guldberg P, Mallmann R, Henriksen KF, Guttler F: Phenylalanine hydroxylase deficiency in a population in Germany: mutational profile and nine novel mutations. Hum Mutat. 1996;8(3):276-9.
- 9048935 Argiolas A, Bosco P, Cali F, Ceratto N, Anello G, Riva E, Biasucci G, Carducci C, Romano V: Two novel PAH gene mutations detected in Italian phenylketonuric patients. Hum Genet. 1997 Feb;99(2):275-8.
- 9101291 Byck S, Tyfield L, Carter K, Scriver CR: Prediction of multiple hypermutable codons in the human PAH gene: codon 280 contains recurrent mutations in Quebec and other populations. Hum Mutat. 1997;9(4):316-21.
- 9406548 Erlandsen H, Fusetti F, Martinez A, Hough E, Flatmark T, Stevens RC: Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria. Nat Struct Biol. 1997 Dec;4(12):995-1000.
- 9450897 Waters PJ, Parniak MA, Nowacki P, Scriver CR: In vitro expression analysis of mutations in phenylalanine hydroxylase: linking genotype to phenotype and structure to function. Hum Mutat. 1998;11(1):4-17.
- 9452061 Park YS, Seoung CS, Lee SW, Oh KH, Lee DH, Yim J: Identification of three novel mutations in Korean phenylketonuria patients: R53H, N207D, and Y325X. Hum Mutat. 1998;Suppl 1:S121-2.
- 9452062 Michiels L, Francois B, Raus J, Vandevyver C: Identification of seven new mutations in the phenylalanine hydroxylase gene, associated with hyperphenylalaninemia in the Belgian population. Hum Mutat. 1998;Suppl 1:S123-4.
- 9521426 Bosco P, Cali F, Meli C, Mollica F, Zammarchi E, Cerone R, Vanni C, Palillo L, Greco D, Romano V: Eight new mutations of the phenylalanine hydroxylase gene in Italian patients with hyperphenylalaninemia. Hum Mutat. 1998;11(3):240-3.
- 9600453 De Lucca M, Perez B, Desviat LR, Ugarte M: Molecular basis of phenylketonuria in Venezuela: presence of two novel null mutations. Hum Mutat. 1998;11(5):354-9.
- 9642259 Fusetti F, Erlandsen H, Flatmark T, Stevens RC: Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria. J Biol Chem. 1998 Jul 3;273(27):16962-7.
- 9792407 Popescu T, Blazkova M, Kozak L, Jebeleanu G, Popescu A: Mutation spectrum and phenylalanine hydroxylase RFLP/VNTR background in 44 Romanian phenylketonuric alleles. Hum Mutat. 1998;12(5):314-9.
- 9792411 Waters PJ, Parniak MA, Hewson AS, Scriver CR: Alterations in protein aggregation and degradation due to mild and severe missense mutations (A104D, R157N) in the human phenylalanine hydroxylase gene (PAH). Hum Mutat. 1998;12(5):344-54.
- 9843368 Erlandsen H, Flatmark T, Stevens RC, Hough E: Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution. Biochemistry. 1998 Nov 10;37(45):15638-46.
- 9852673 Kibayashi M, Nagao M, Chiba S: Mutation analysis of the phenylalanine hydroxylase gene and its clinical implications in two Japanese patients with non-phenylketonuria hyperphenylalaninemia. J Hum Genet. 1998;43(4):231-6.
|
| Target 2 Drug References |
- Erlandsen H, Flatmark T, Stevens RC, Hough E: Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution. Biochemistry. 1998 Nov 10;37(45):15638-46. [PubMed
]
|
|
Drug Target 3
[top]
|
| Target 3 ID |
831 |
| Target 3 Name |
D(2) dopamine receptor |
| Target 3 Synonyms |
- Dopamine D2 receptor
|
| Target 3 Gene Name |
DRD2 |
| Target 3 Protein Sequence |
>D(2) dopamine receptor
MDPLNLSWYDDDLERQNWSRPFNGSDGKADRPHYNYYATLLTLLIAVIVFGNVLVCMAVS
REKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWKFSRIHCDIFVTLDVMMCTA
SILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMISIVWVLSFTISCPLLFGLNNADQN
ECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIVLRRRRKRVNTKRSSRAFRAHLRAPL
KGNCTHPEDMKLCTVIMKSNGSFPVNRRRVEAARRAQELEMEMLSSTSPPERTRYSPIPP
SHHQLTLPDPSHHGLHSTPDSPAKPEKNGHAKDHPKIAKIFEIQTMPNGKTRTSLKTMSR
RKLSQQKEKKATQMLAIVLGVFIICWLPFFITHILNIHCDCNIPPVLYSAFTWLGYVNSA
VNPIIYTTFNIEFRKAFLKILHC
|
| Target 3 Number of Residues |
450 |
| Target 3 Molecular Weight |
50620 |
| Target 3 Theoretical pI |
9.85 |
| Target 3 GO Classification |
|
Function
|
signal transducer activity
receptor activity
transmembrane receptor activity
G-protein coupled receptor activity
rhodopsin-like receptor activity
amine receptor activity
dopamine receptor activity |
|
Process
|
cellular process
cell communication
signal transduction
cell surface receptor linked signal transduction
G-protein coupled receptor protein signaling pathway |
|
Component
|
cell
membrane
intrinsic to membrane
integral to membrane |
|
| Target 3 General Function |
Involved in dopamine receptor activity |
| Target 3 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 |
| Target 3 Pathways |
Not Available
|
| Target 3 Reactions |
Not Available |
| Target 3 Pfam Domain Function |
|
| Target 3 Signals |
|
| Target 3 Transmembrane Regions |
- 38-60
- 72-97
- 109-130
- 152-174
- 187-210
- 374-397
- 406-429
|
| Target 3 Essentiality |
Non-Essential |
| Target 3 GenBank ID Protein |
181432  |
| Target 3 UniProtKB/Swiss-Prot ID |
P14416  |
| Target 3 UniProtKB/Swiss-Prot Entry Name |
DRD2_HUMAN  |
| Target 3 PDB ID |
Not Available |
| Target 3 Cellular Location |
- Membrane
- multi-pass membrane protein
|
| Target 3 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
|
| Target 3 GenBank Gene ID |
|
| Target 3 GeneCard ID |
DRD2  |
| Target 3 GenAtlas ID |
DRD2  |
| Target 3 HGNC ID |
HGNC:3023  |
| Target 3 Chromosome Location |
11 |
| Target 3 Locus |
11q23 |
| Target 3 SNPs |
SNPJam Report  |
| Target 3 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 7902708 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.
- 8471125 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.
|
| Target 3 Drug References |
- Mori A, Ohashi S, Nakai M, Moriizumi T, Mitsumoto Y: Neural mechanisms underlying motor dysfunction as detected by the tail suspension test in MPTP-treated C57BL/6 mice. Neurosci Res. 2005 Mar;51(3):265-74. Epub 2005 Jan 8. [PubMed
]
- Kovoor A, Seyffarth P, Ebert J, Barghshoon S, Chen CK, Schwarz S, Axelrod JD, Cheyette BN, Simon MI, Lester HA, Schwarz J: D2 dopamine receptors colocalize regulator of G-protein signaling 9-2 (RGS9-2) via the RGS9 DEP domain, and RGS9 knock-out mice develop dyskinesias associated with dopamine pathways. J Neurosci. 2005 Feb 23;25(8):2157-65. [PubMed
]
- Zappia M, Annesi G, Nicoletti G, Arabia G, Annesi F, Messina D, Pugliese P, Spadafora P, Tarantino P, Carrideo S, Civitelli D, De Marco EV, Ciro-Candiano IC, Gambardella A, Quattrone A: Sex differences in clinical and genetic determinants of levodopa peak-dose dyskinesias in Parkinson disease: an exploratory study. Arch Neurol. 2005 Apr;62(4):601-5. [PubMed
]
- Chang CC, Shiah IS, Chang HA, Mao WC: Does domperidone potentiate mirtazapine-associated restless legs syndrome? Prog Neuropsychopharmacol Biol Psychiatry. 2006 Mar;30(2):316-8. Epub 2005 Nov 23. [PubMed
]
- Dupre KB, Eskow KL, Negron G, Bishop C: The differential effects of 5-HT(1A) receptor stimulation on dopamine receptor-mediated abnormal involuntary movements and rotations in the primed hemiparkinsonian rat. Brain Res. 2007 Jul 16;1158:135-43. Epub 2007 May 8. [PubMed
]
|
|
Drug Target 4
[top]
|
| Target 4 ID |
3330 |
| Target 4 Name |
Phenylethylamine oxidase |
| Target 4 Synonyms |
- Amine oxidase
- EC 1.4.3.6
- Phenylethylamine oxidase precursor
|
| Target 4 Gene Name |
Not Available |
| Target 4 Protein Sequence |
>Phenylethylamine oxidase precursor
MTPSTIQTASPFRLASAGEISEVQGILRTAGLLGPEKRIAYLGVLDPARGAGSEAEDRRF
RVFIHDVSGARPQEVTVSVTNGTVISAVELDTAATGELPVLEEEFEVVEQLLATDERWLK
ALAARNLDVSKVRVAPLSAGVFEYAEERGRRILRGLAFVQDFPEDSAWAHPVDGLVAYVD
VVSKEVTRVIDTGVFPVPAEHGNYTDPELTGPLRTTQKPISITQPEGPSFTVTGGNHIEW
EKWSLDVGFDVREGVVLHNIAFRDGDRLRPIINRASIAEMVVPYGDPSPIRSWQNYFDTG
EYLVGQYANSLELGCDCLGDITYLSPVISDAFGNPREIRNGICMHEEDWGILAKHSDLWS
GINYTRRNRRMVISFFTTIGNYDYGFYWYLYLDGTIEFEAKATGVVFTSAFPEGGSDNIS
QLAPGLGAPFHQHIFSARLDMAIDGFTNRVEEEDVVRQTMGPGNERGNAFSRKRTVLTRE
SEAVREADARTGRTWIISNPESKNRLNEPVGYKLHAHNQPTLLADPGSSIARRAAFATKD
LWVTRYADDERYPTGDFVNQHSGGAGLPSYIAQDRDIDGQDIVVWHTFGLTHFPRVEDWP
IMPVDTVGFKLRPEGFFDRSPVLDVPANPSQSGSHCHG
|
| Target 4 Number of Residues |
648 |
| Target 4 Molecular Weight |
70647 |
| Target 4 Theoretical pI |
4.81 |
| Target 4 GO Classification |
|
Function
|
binding
ion binding
cation binding
transition metal ion binding
copper ion binding |
|
Process
|
| Not Available |
|
Component
|
| Not Available |
|
| Target 4 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Target 4 Specific Function |
RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2) |
| Target 4 Pathways |
| Name |
SMPDB Link |
KEGG Link |
| Glycine, serine and threonine metabolism |
SMP00004  |
map00260  |
|
| Target 4 Reactions |
- RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
|
| Target 4 Pfam Domain Function |
|
| Target 4 Signals |
|
| Target 4 Transmembrane Regions |
|
| Target 4 Essentiality |
Essential |
| Target 4 GenBank ID Protein |
Not Available |
| Target 4 UniProtKB/Swiss-Prot ID |
P46881  |
| Target 4 UniProtKB/Swiss-Prot Entry Name |
PAOX_ARTGO  |
| Target 4 PDB ID |
1IVU  |
| Target 4 PDB File |
Show |
| Target 4 3D Structure |
|
| Target 4 Cellular Location |
Not Available |
| Target 4 Gene Sequence |
>1917 bp
ATGACGCCCTCCACTATCCAAACAGCCAGCCCCTTCCGCCTTGCCTCAGCTGGGGAAATC
AGTGAGGTGCAGGGCATTCTTCGGACCGCGGGCCTCCTTGGCCCGGAGAAGCGCATTGCC
TACCTGGGCGTCCTTGACCCGGCCCGCGGCGCCGGCAGTGAAGCGGAAGACCGGCGCTTC
CGGGTTTTCATCCACGACGTCTCCGGCGCCCGGCCCCAGGAAGTCACTGTCTCGGTCACC
AACGGCACTGTGATCTCCGCCGTCGAACTCGATACCGCGGCCACCGGCGAACTGCCGGTC
CTGGAAGAGGAGTTCGAGGTTGTGGAGCAACTGCTGGCCACCGACGAACGGTGGCTGAAG
GCCCTGGCCGCCCGGAACCTTGACGTCAGCAAGGTGCGCGTTGCTCCGCTGTCCGCGGGT
GTCTTCGAGTATGCGGAGGAGAGGGGCCGCCGGATCCTCCGCGGGCTTGCCTTCGTACAG
GATTTTCCGGAGGACAGCGCTTGGGCTCATCCGGTTGACGGGCTGGTGGCCTACGTGGAC
GTGGTCAGCAAGGAAGTCACCCGGGTGATCGACACCGGCGTCTTCCCCGTCCCGGCAGAG
CACGGCAATTACACCGATCCCGAACTCACGGGTCCACTCCGCACCACCCAGAAACCCATC
AGCATCACCCAGCCCGAAGGCCCCAGCTTCACGGTGACCGGCGGCAACCACATCGAATGG
GAAAAATGGAGCCTGGACGTCGGCTTTGACGTCCGCGAGGGCGTGGTGCTGCACAACATT
GCCTTCCGGGACGGGGACCGGCTCCGGCCCATCATCAACCGCGCGTCGATCGCCGAGATG
GTGGTGCCGTACGGCGATCCGTCCCCGATCAGGTCCTGGCAGAACTACTTCGACACGGGG
GAGTACCTGGTGGGCCAGTACGCCAACTCCCTCGAACTGGGCTGCGACTGCCTCGGCGAC
ATCACCTACCTCAGCCCGGTCATCAGCGACGCCTTCGGCAACCCCCGCGAGATCCGCAAC
GGCATCTGCATGCACGAGGAGGACTGGGGCATCCTGGCCAAGCACAGCGACCTTTGGTCC
GGCATCAACTACACCCGCCGGAACCGCCGCATGGTGATCTCCTTCTTCACCACTATCGGC
AACTACGACTACGGCTTCTACTGGTACCTCTACCTCGACGGCACCATCGAATTCGAAGCG
AAAGCCACCGGCGTCGTCTTCACGTCCGCATTCCCGGAAGGCGGCTCGGACAACATTTCC
CAGCTGGCACCGGGCCTGGGAGCGCCGTTCCACCAGCACATCTTCAGCGCCCGCCTGGAC
ATGGCCATCGACGGCTTCACCAACAGGGTGGAGGAAGAGGACGTGGTCCGGCAAACCATG
GGCCCGGGCAACGAGCGCGGCAACGCGTTCTCCCGAAAGCGCACCGTGCTGACCCGTGAG
TCGGAGGCTGTCCGCGAGGCCGATGCCCGCACCGGCCGGACCTGGATCATCTCCAACCCC
GAATCCAAGAACCGTCTCAACGAGCCGGTGGGCTACAAGCTGCACGCCCACAACCAGCCC
ACCCTGCTGGCCGATCCCGGGTCCTCCATTGCGCGGCGGGCCGCCTTTGCCACCAAGGAC
CTGTGGGTCACCCGCTACGCCGACGACGAGCGCTACCCCACCGGCGACTTCGTCAACCAG
CACTCCGGCGGCGCGGGCCTGCCCTCCTACATCGCCCAGGACCGCGACATCGACGGCCAG
GACATCGTCGTGTGGCACACCTTCGGACTGACCCACTTCCCGCGCGTGGAGGACTGGCCC
ATCATGCCGGTGGACACCGTCGGCTTCAAGCTCCGTCCCGAGGGCTTCTTCGACCGCAGC
CCGGTCCTCGATGTCCCGGCCAACCCCAGCCAGTCCGGCTCCCACTGCCACGGCTAG
|
| Target 4 GenBank Gene ID |
|
| Target 4 GeneCard ID |
Not Available |
| Target 4 GenAtlas ID |
Not Available |
| Target 4 HGNC ID |
Not Available |
| Target 4 Chromosome Location |
Not Available |
| Target 4 Locus |
Not Available |
| Target 4 SNPs |
Not Available |
| Target 4 General References |
- Tanizawa K, Matsuzaki R, Shimizu E, Yorifuji T, Fukui T: Cloning and sequencing of phenylethylamine oxidase from Arthrobacter globiformis and implication of Tyr-382 as the precursor to its covalently bound quinone cofactor. Biochem Biophys Res Commun. 1994 Mar 30;199(3):1096-102. [PubMed
]
- Wilce MC, Dooley DM, Freeman HC, Guss JM, Matsunami H, McIntire WS, Ruggiero CE, Tanizawa K, Yamaguchi H: Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone. Biochemistry. 1997 Dec 23;36(51):16116-33. [PubMed
]
|
| Target 4 Drug References |
Not Available |
|
Drug Target 5
[top]
|
| Target 5 ID |
3810 |
| Target 5 Name |
Catechol O-methyltransferase |
| Target 5 Synonyms |
- EC 2.1.1.6
|
| Target 5 Gene Name |
COMT |
| Target 5 Protein Sequence |
>Catechol O-methyltransferase
MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRIL
NHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCG
YSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKY
DVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFE
CTHYQSFLEYREVVDGLEKAIYKGPGSEAGP
|
| Target 5 Number of Residues |
275 |
| Target 5 Molecular Weight |
30037 |
| Target 5 Theoretical pI |
5.15 |
| Target 5 GO Classification |
|
Function
|
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
O-methyltransferase activity |
|
Process
|
| Not Available |
|
Component
|
| Not Available |
|
| Target 5 General Function |
Involved in O-methyltransferase activity |
| Target 5 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 |
| Target 5 Pathways |
|
| Target 5 Reactions |
- S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol
|
| Target 5 Pfam Domain Function |
|
| Target 5 Signals |
|
| Target 5 Transmembrane Regions |
|
| Target 5 Essentiality |
Non-Essential |
| Target 5 GenBank ID Protein |
180920  |
| Target 5 UniProtKB/Swiss-Prot ID |
P21964  |
| Target 5 UniProtKB/Swiss-Prot Entry Name |
COMT_HUMAN  |
| Target 5 PDB ID |
Not Available |
| Target 5 Cellular Location |
- Isoform S-COMT:Cytoplasm. Isoform MB-COMT:Cell membrane
- extra
- single-pass type II membrane protein
|
| Target 5 Gene Sequence |
>816 bp
ATGCCGGAGGCCCCGCCTCTGCTGTTGGCAGCTGTGTTGCTGGGCCTGGTGCTGCTGGTG
GTGCTGCTGCTGCTTCTGAGGCACTGGGGCTGGGGCCTGTGCCTTATCGGCTGGAACGAG
TTCATCCTGCAGCCCATCCACAACCTGCTCATGGGTGACACCAAGGAGCAGCGCATCCTG
AACCACGTGCTGCAGCATGCGGAGCCCGGGAACGCACAGAGCGTGCTGGAGGCCATTGAC
ACCTACTGCGAGCAGAAGGAGTGGGCCATGAACGTGGGCGACAAGAAAGGCAAGATCGTG
GACGCCGTGATTCAGGAGCACCAGCCCTCCGTGCTGCTGGAGCTGGGGGCCTACTGTGGC
TACTCAGCTGTGCGCATGGCCCGCCTGCTGTCACCAGGGGCGAGGCTCATCACCATCGAG
ATCAACCCCGACTGTGCCGCCATCACCCAGCGGATGGTGGATTTCGCTGGCGTGAAGGAC
AAGGTCACCCTTGTGGTTGGAGCGTCCCAGGACATCATCCCCCAGCTGAAGAAGAAGTAT
GATGTGGACACACTGGACATGGTCTTCCTCGACCACTGGAAGGACCGGTACCTGCCGGAC
ACGCTTCTCTTGGAGGAATGTGGCCTGCTGCGGAAGGGGACAGTGCTACTGGCTGACAAC
GTGATCTGCCCAGGTGCGCCAGACTTCCTAGCACACGTGCGCGGGAGCAGCTGCTTTGAG
TGCACACACTACCAATCGTTCCTGGAATACAGGGAGGTGGTGGACGGCCTGGAGAAGGCC
ATCTACAAGGGCCCAGGCAGCGAAGCAGGGCCCTGA
|
| Target 5 GenBank Gene ID |
|
| Target 5 GeneCard ID |
COMT  |
| Target 5 GenAtlas ID |
COMT  |
| Target 5 HGNC ID |
HGNC:2228  |
| Target 5 Chromosome Location |
22 |
| Target 5 Locus |
22q11.21-q11.23|22q11.21 |
| Target 5 SNPs |
SNPJam Report  |
| Target 5 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Target 5 Drug References |
Not Available |