|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5401 |
| Enzyme 1 Name |
Amine oxidase [flavin-containing] A |
| Enzyme 1 Synonyms |
- Monoamine oxidase type A
- MAO-A
|
| Enzyme 1 Gene Name |
MAOA |
| Enzyme 1 Protein Sequence |
>Amine oxidase [flavin-containing] A
MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHV
DYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIA
YLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNI
NVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKL
NHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPM
GAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADR
LAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYG
RVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKD
VPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS
|
| Enzyme 1 Number of Residues |
527 |
| Enzyme 1 Molecular Weight |
59682 |
| Enzyme 1 Theoretical pI |
7.96 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Amino acid transport and metabolism |
| 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. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
187353  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P21397  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
AOFA_HUMAN  |
| Enzyme 1 PDB ID |
1O5W  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1584 bp
ATGGAGAATCAAGAGAAGGCGAGTATCGCGGGCCACATGTTCGACGTAGTCGTGATCGGA
GGTGGCATTTCAGGACTATCTGCTGCCAAACTCTTGACTGAATATGGCGTTAGTGTTTTG
GTTTTAGAAGCTCGGGACAGGGTTGGAGGAAGAACATATACTATAAGGAATGAGCATGTT
GATTACGTAGATGTTGGTGGAGCTTATGTGGGACCAACCCAAAACAGAATCTTACGCTTG
TCTAAGGAGCTGGGCATAGAGACTTACAAAGTGAATGTCAGTGAGCGTCTCGTTCAATAT
GTCAAGGGGAAAACATATCCATTTCGGGGCGCCTTTCCACCAGTATGGAATCCCATTGCA
TATTTGGATTACAATAATCTGTGGAGGACAATAGATAACATGGGGAAGGAGATTCCAACT
GATGCACCCTGGGAGGCTCAACATGCTGACAAATGGGACAAAATGACCATGAAAGAGCTC
ATTGACAAAATCTGCTGGACAAAGACTGCTAGGCGGTTTGCTTATCTTTTTGTGAATATC
AATGTGACCTCTGAGCCTCACGAAGTGTCTGCCCTGTGGTTCTTGTGGTATGTGAAGCAG
TGCGGGGGCACCACTCGGATATTCTCTGTCACCAATGGTGGCCAGGAACGGAAGTTTGTA
GGTGGATCTGGTCAAGTGAGCGAACGGATAATGGACCTCCTCGGAGACCAAGTGAAGCTG
AACCATCCTGTCACTCACGTTGACCAGTCAAGTGACAACATCATCATAGAGACGCTGAAC
CATGAACATTATGAGTGCAAATACGTAATTAATGCGATCCCTCCGACCTTGACTGCCAAG
ATTCACTTCAGACCAGAGCTTCCAGCAGAGAGAAACCAGTTAATTCAGCGGCTTCCAATG
GGAGCTGTCATTAAGTGCATGATGTATTACAAGGAGGCCTTCTGGAAGAAGAAGGATTAC
TGTGGCTGCATGATCATTGAAGATGAAGATGCTCCAATTTCAATAACCTTGGATGACACC
AAGCCTGATGGGTCACTGCCTGCCATCATGGGCTTCATTCTTGCCCGGAAAGCTGATCGA
CTTGCTAAGCTACATAAGGAAATAAGGAAGAAGAAAATCTGTGAGCTCTATGCCAAAGTG
CTGGGATCCCAAGAAGCTTTACATCCAGTGCATTATGAAGAGAAGAACTGGTGTGAGGAG
CAGTACTCTGGGGGCTGCTACACGGCCTACTTCCCTCCTGGGATCATGACTCAATATGGA
AGGGTGATTCGTCAACCCGTGGGCAGGATTTTCTTTGCGGGCACAGAGACTGCCACAAAG
TGGAGCGGCTACATGGAAGGGGCAGTTGAGGCTGGAGAACGAGCAGCTAGGGAGGTCTTA
AATGGTCTCGGGAAGGTGACCGAGAAAGATATCTGGGTACAAGAACCTGAATCAAAGGAC
GTTCCAGCGGTAGAAATCACCCACACCTTCTGGGAAAGGAACCTGCCCTCTGTTTCTGGC
CTGCTGAAGATCATTGGATTTTCCACATCAGTAACTGCCCTGGGGTTTGTGCTGTACAAA
TACAAGCTCCTGCCACGGTCTTGA
|
| Enzyme 1 GenBank Gene ID |
M68840  |
| Enzyme 1 GeneCard ID |
MAOA  |
| Enzyme 1 GenAtlas ID |
MAOA  |
| Enzyme 1 HGNC ID |
HGNC:6833  |
| Enzyme 1 Chromosome Location |
X |
| Enzyme 1 Locus |
Xp11.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 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
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5485 |
| Enzyme 2 Name |
Dopamine beta-hydroxylase precursor |
| Enzyme 2 Synonyms |
- Dopamine beta- monooxygenase
|
| Enzyme 2 Gene Name |
DBH |
| Enzyme 2 Protein Sequence |
>Dopamine beta-hydroxylase precursor
MREAAFMYSTAVAIFLVILVAALQGSAPRESPLPYHIPLDPEGSLELSWNVSYTQEAIHF
QLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSDQKGQIHLDPQQDYQLL
QVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSLEAINGSGLQMGLQR
VQLLKPNIPEPELPSDACTMEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEPIVT
KGNEALVHHMEVFQCAPEMDSVPHFSGPCDSKMKPDRLNYCRHVLAAWALGAKAFYYPEE
AGLAFGGPGSSRYLRLEVHYHNPLVIEGRNDSSGIRLYYTAKLRRFNAGIMELGLVYTPV
MAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKVVTVLVRDGREWEIV
NQDNHYSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHY
YPQTQLELCKSAVDAGFLQKYFHLINRFNNEDVCTCPQASVSQQFTSVPWNSFNRDVLKA
LYSFAPISMHCNKSSAVRFQGEWNLQPLPKVISTLEEPTPQCPTSQGRSPAGPTVVSIGG
GKG
|
| Enzyme 2 Number of Residues |
603 |
| Enzyme 2 Molecular Weight |
67614 |
| Enzyme 2 Theoretical pI |
6.31 |
| Enzyme 2 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- copper ion binding
- dopamine beta-monooxygenase activity
- 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 |
- amino acid and derivative metabolism
- amino acid derivative metabolism
- amino acid metabolism
- biogenic amine metabolism
- catecholamine metabolism
- cellular metabolism
- histidine catabolism
- histidine family amino acid metabolism
- histidine metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
Conversion of dopamine to noradrenaline |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- 3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
Not Available |
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
30474  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P09172  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
DOPO_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1812 bp
ATGCGGGAGGCAGCCTTCATGTACAGCACAGCAGTGGCCATCTTCCTGGTCATCCTGGTG
GCCGCACTGCAGGGCTCGGCTCCCCGTGAGAGCCCCCTCCCCTATCACATCCCCCTGGAC
CCGGAGGGGTCCCTGGAGCTCTCATGGAATGTCAGCTACACCCAGGAGGCCATCCATTTC
CAGCTCCTGGTGCGGAGGCTCAAGGCTGGCGTCCTGTTTGGGATGTCCGACCGTGGCGAG
CTTGAGAACGCAGATCTCGTGGTGCTCTGGACCGATGGGGACACTGCCTATTTTGCGGAC
GCCTGGAGTGACCAGAAGGGGCAGATCCACCTGGATCCCCAGCAGGACTACCAGCTGCTG
CAGGTGCAGAGGACCCCAGAAGGCCTGACCCTGCTTTTCAAGAGGCCCTTTGGCACCTGC
GACCCCAAGGATTACCTCATTGAAGACGGCACTGTCCACTTGGTCTACGGGATCCTGGAG
GAGCCGTTCCGGTCACTGGAGGCCATCAACGGCTCGGGCCTGCAGATGGGGCTGCAGAGG
GTGCAGCTCCTGAAGCCCAATATCCCCGAACCGGAGTTGCCCTCAGACGCGTGCACCATG
GAGGTCCAAGCTCCCAATATCCAGATCCCCAGCCAGGAGACCACGTACTGGTGCTACATT
AAGGAGCTTCCAAAGGGCTTCTCTCGGCACCACATTATCAAGTACGAGCCCATCGTCACC
AAGGGCAATGAGGCCCTTGTCCACCACATGGAAGTCTTCCAGTGCGCCCCCGAGATGGAC
AGCGTCCCCCACTTCAGCGGGCCCTGCGACTCCAAGATGAAACCCGACCGCCTCAACTAC
TGCCGCCACGTGCTGGCCGCCTGGGCCCTGGGTGCCAAGGCATTTTACTACCCAGAGGAA
GCCGGCCTTGCCTTCGGGGGTCCAGGGTCCTCCAGATATCTCCGCCTGGAAGTTCACTAC
CACAACCCACTGGTGATAGAAGGACGAAACGACTCCTCAGGCATCCGCTTGTACTACACA
GCCAAGCTGCGGCGCTTCAACGCGGGGATCATGGAGCTGGGACTGGTGTACACGCCAGTG
ATGGCCATTCCACCACGGGAGACCGCCTTCATCCTCACTGGCTACTGCACGGACAAGTGC
ACCCAGCTGGCACTGCCTCCCTCCGGGATCCACATCTTCGCCTCTCAGCTCCACACACAC
CTGACTGGGAGAAAGGTGGTCACAGTGCTGGTCCGGGACGGCCGGGAGTGGGAGATCGTG
AACCAGGACAATCACTACAGCCCTCACTTCCAGGAGATCCGCATGTTGAAGAAGGTCGTG
TCGGTCCATCCGGGAGATGTGCTCATCACCTCCTGCACGTACAACACGGAAGACCGGGAG
CTGGCCACAGTGGGGGGCTTCGGGATCCTGGAGGAGATGTGTGTCAACTACGTGCACTAC
TACCCCCAGACGCAGCTGGAGCTCTGCAAGACGGCTGTGGACGCCGGCTTCCTGCAGAAG
TACTTCCACCTCATCAACAGGTTCAACAACGAGGATGTCTGCACCTGCCCTCAGGCGTCC
GTGTCTCAGCAGTTCACCTCTGTTCCCTGGAACTCCTTCAACCGCGACGTACTGAAGGCC
CTGTACAGCTTCGCGCCCATCTCCATGCACTGCAACAAGTCCTCAGCCGTCCGCTTCCAG
GGTGAATGGAACCTGCAGCCCCTGCCCAAGGTCATCTCCACACTGGAAGAGCCCACCCCA
CAGTGCCCCACCAGCCAGGGCCGAAGCCCTGCTGGCCCCACCGTTGTCAGCATTGGTGGG
GGCAAAGGCTGA
|
| Enzyme 2 GenBank Gene ID |
X13255  |
| Enzyme 2 GeneCard ID |
DBH  |
| Enzyme 2 GenAtlas ID |
DBH  |
| Enzyme 2 HGNC ID |
HGNC:2689  |
| Enzyme 2 Chromosome Location |
9 |
| Enzyme 2 Locus |
9q34 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
- 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
]
- 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
]
- 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 2 Metabolite References |
Not Available |
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Enzyme 3
[top]
|
| Enzyme 3 ID |
5504 |
| Enzyme 3 Name |
Catechol O-methyltransferase |
| Enzyme 3 Synonyms |
Not Available |
| Enzyme 3 Gene Name |
COMT |
| Enzyme 3 Protein Sequence |
>Catechol O-methyltransferase
MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRIL
NHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCG
YSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKY
DVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFE
CTHYQSFLEYREVVDGLEKAIYKGPGSEAGP
|
| Enzyme 3 Number of Residues |
271 |
| Enzyme 3 Molecular Weight |
30037 |
| Enzyme 3 Theoretical pI |
5.15 |
| Enzyme 3 GO Classification |
| Function |
- O-methyltransferase activity
- catalytic activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 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 3 Pathways |
|
| Enzyme 3 Reactions |
- S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
Not Available |
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
180920  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P21964  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
COMT_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>816 bp
ATGCCGGAGGCCCCGCCTCTGCTGTTGGCAGCTGTGTTGCTGGGCCTGGTGCTGCTGGTG
GTGCTGCTGCTGCTTCTGAGGCACTGGGGCTGGGGCCTGTGCCTTATCGGCTGGAACGAG
TTCATCCTGCAGCCCATCCACAACCTGCTCATGGGTGACACCAAGGAGCAGCGCATCCTG
AACCACGTGCTGCAGCATGCGGAGCCCGGGAACGCACAGAGCGTGCTGGAGGCCATTGAC
ACCTACTGCGAGCAGAAGGAGTGGGCCATGAACGTGGGCGACAAGAAAGGCAAGATCGTG
GACGCCGTGATTCAGGAGCACCAGCCCTCCGTGCTGCTGGAGCTGGGGGCCTACTGTGGC
TACTCAGCTGTGCGCATGGCCCGCCTGCTGTCACCAGGGGCGAGGCTCATCACCATCGAG
ATCAACCCCGACTGTGCCGCCATCACCCAGCGGATGGTGGATTTCGCTGGCGTGAAGGAC
AAGGTCACCCTTGTGGTTGGAGCGTCCCAGGACATCATCCCCCAGCTGAAGAAGAAGTAT
GATGTGGACACACTGGACATGGTCTTCCTCGACCACTGGAAGGACCGGTACCTGCCGGAC
ACGCTTCTCTTGGAGGAATGTGGCCTGCTGCGGAAGGGGACAGTGCTACTGGCTGACAAC
GTGATCTGCCCAGGTGCGCCAGACTTCCTAGCACACGTGCGCGGGAGCAGCTGCTTTGAG
TGCACACACTACCAATCGTTCCTGGAATACAGGGAGGTGGTGGACGGCCTGGAGAAGGCC
ATCTACAAGGGCCCAGGCAGCGAAGCAGGGCCCTGA
|
| Enzyme 3 GenBank Gene ID |
M65212  |
| Enzyme 3 GeneCard ID |
COMT  |
| Enzyme 3 GenAtlas ID |
COMT  |
| Enzyme 3 HGNC ID |
HGNC:2228  |
| Enzyme 3 Chromosome Location |
22 |
| Enzyme 3 Locus |
22q11.21-q11.23|22q11.21 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 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
]
- 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
]
- 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
]
- 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 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5510 |
| Enzyme 4 Name |
Aromatic-L-amino-acid decarboxylase |
| Enzyme 4 Synonyms |
- AADC
- DOPA decarboxylase
- DDC
|
| Enzyme 4 Gene Name |
DDC |
| Enzyme 4 Protein Sequence |
>Aromatic-L-amino-acid decarboxylase
MNASEFRRRGKEMVDYVANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDV
EKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMD
WLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIM
EKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFN
PHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSL
KMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVN
EALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE
|
| Enzyme 4 Number of Residues |
480 |
| Enzyme 4 Molecular Weight |
53895 |
| Enzyme 4 Theoretical pI |
7.21 |
| Enzyme 4 GO Classification |
| Function |
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- lyase activity
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Amino acid transport and metabolism |
| Enzyme 4 Specific Function |
Catalyzes the decarboxylation of L-3,4- dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- L-tryptophan = tryptamine + CO2
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
181521  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P20711  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
DDC_HUMAN  |
| Enzyme 4 PDB ID |
1JS3  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 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 4 GenBank Gene ID |
M76180  |
| Enzyme 4 GeneCard ID |
DDC  |
| Enzyme 4 GenAtlas ID |
DDC  |
| Enzyme 4 HGNC ID |
HGNC:2719  |
| Enzyme 4 Chromosome Location |
7 |
| Enzyme 4 Locus |
7p11 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 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
]
- 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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5627 |
| Enzyme 5 Name |
Amiloride-sensitive amine oxidase [copper-containing] precursor |
| Enzyme 5 Synonyms |
- Diamine oxidase
- DAO
- Amiloride-binding protein
- ABP
- Histaminase
- Kidney amine oxidase
- KAO
|
| Enzyme 5 Gene Name |
ABP1 |
| Enzyme 5 Protein Sequence |
>Amiloride-sensitive amine oxidase [copper-containing] precursor
MPALGWAVAAILMLQTAMAEPSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSS
TTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAVIFFGDQEHPNVTEFAVGPLP
GPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDR
CLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNG
KFYGSPEELARKYADGEVDVVVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGP
RLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVHFGGERIAYEVSVQEAVALYG
GHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFE
MPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMH
ATGYVHATFYTPEGLRHGTRLHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENIT
NPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFTSPQENPWGHKRSYRLQIHSM
ADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWDPPVVFEQFLHNNENI
ENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRD
NGPNYVQRWIPEDRDCSMPPPFSYNGTYRPV
|
| Enzyme 5 Number of Residues |
751 |
| Enzyme 5 Molecular Weight |
85342 |
| Enzyme 5 Theoretical pI |
7.01 |
| Enzyme 5 GO Classification |
| Function |
- binding
- cation binding
- copper ion binding
- ion binding
- transition metal ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 5 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 5 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 5 Pathways |
|
| Enzyme 5 Reactions |
- RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
Not Available |
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
177960  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P19801  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
ABP1_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>2142 bp
ATGCCGGCCCTGGGCTGGGCCGTGGCTGCCATCCTGATGCTGCAGACGGCCATGGCGGAG
CCCTCCCCGGGGACTCTGCCCAGGAAGGCAGGGGTGTTTTCAGACCTAAGCAACCAAGAG
CTGAAGGCAGTGCACAGCTTCCTCTGGTCCAAGAAGGAGCTGAGGCTGCAGCCCTCCAGT
ACCACCACCATGGCCAAGAACACCGTGTTTCTCATCGAGATGCTGCTGCCCAAGAAGTAC
CATGTGCTGAGGTTTCTGGATAAAGGTGAAAGGCATCCTGTGCGGGAAGCCCGTGCCGTC
ATCTTCTTTGGTGACCAGGAGCATCCCAATGTCACCGAGTTTGCTGTGGGGCCCCTGCCA
GGGCCCTGCTACATGCGAGCACTGTCCCCCAGGCCTGGGTACCAGTCCTCCTGGGCATCG
AGGCCCATCTCCACAGCAGAGTATGCCCTCCTCTACCACACCCTGCAGGAAGCCACCAAG
CCCCTGCATCAGTTCTTCCTCAATACCACAGGCTTCTCATTCCAAGACTGCCATGACAGA
TGCCTGGCCTTCACCGATGTGGCCCCCCGGGGTGTGGCTTCTGGCCAGCGCCGCAGTTGG
CTTATCATACAGCGCTATGTAGAAGGCTACTTTCTGCACCCCACTGGGCTGGAGCTCCTC
GTGGATCATGGGAGCACAGATGCTGGGCACTGGGCCGTGGAGCAGGTGTGGTACAACGGG
AAGTTCTATGGGAGCCCAGAGGAACTGGCACGGAAGTATGCAGATGGAGAGGTGGACGTG
GTGGTCCTGGAGGACCGCTGCCTGGGGGCAAGGGGCATGACAGCACAGAGGAGCCGGCCC
TCTTCTCCTCCACAAGCCCCGCGGGACTTTCCCCAGCCCCATCCATGTGAGCGGCCCCCG
CTTGGTCCAGCCCCACGGCCCTCGCTTCAGGCTGGAGGGCAACGCTGTGCTCTACGGCGG
CTGGAGCTTTGCCTTCCGGTGCGCTCCTCCTCCGGGCTGCAGGTCCTGAACGTGCACTTC
GGCGGAGAGCGCATTGCCTATGAGGTCAGCGTGCAAGAGGCAGTGGCGCTGTATGGAGGA
CACACACCTGCAGGCATGCAGACCAAGTACCTCGATGTCGGCTGGGGCCTGGGCAGCGTC
ACTCATGAGTTAGCCCCCGGCATCGACTGCCCGGAGACCGCCACCTTCCTGGACACTTTC
CACTACTATGATGCCGATGACCCGGTCCATTATCCCCGAGCCCTCTGCCTCTTTGAAATG
CCCACAGGGGTGCCCCTTCGGCGGCACTTTAATTCCAACTTTAAAGGTGGCTTCAACTTC
TATGCAGGGCTGAAGGGCCAGGTGCTGGTGCTGCGGACAACTTCAACTGTCTACAATTAT
GATTACATTTGGGACTTTATCTTCTACCCCAACGGGGTGATGGAGGCCAAGATGCATGCC
ACTGGCTACGTCCACGCCACCTTCTACACCCCCGAGGGCTGCGCACGGCACTCGCCTGCA
CACCCACCTGATTGGCAACATACACACTCACTTGTGCACTACCGCGTAGACCTGGATGTG
GCAGGCACCAAGAACAGCTTCCAGACACTGCAGATGAAGCTAGAAAACATCACCAACCCC
TGGAGCCCGAGACACCGCGTGGTCCAGCCAACTCTGGAGCAGACGCAGTACTCCTGGGAG
CGCCAGGCGGCCTTCCGCTTCAAAAGGAGGCTGCCCAAGTACCTGCTCTTTACCAGCCCC
CAGGAGAACCCCTGGGGCCACAAGCGCAGCTACCGCCTGCAGATCCACTCCATGGCCGAC
CAGGTGCTGCCCCCAGGCTGGCAGGAGGAGCAGGCCATCACCTGGGCAAGGTACCCCCTG
GCAGTGACCAAGTACCGGGAGTCAGAGCTGTGCAGCAGCAGCATCTACCACCAGAACGAC
CCCTGGGACCCGCCCGTGGTCTTTGAGCAGTTTCTTCACAACAACGAGAACATTGAAAAT
GAGGACCTGGTGGCCTGGGTGACGGTGGGCTTCCTGCACATCCCCCACTCAGAGGACATT
CCCAACACAGCCACACCTGGGAACTCCGTGGGCTTCCTGCTCCGGCCATTCAACTTCTTC
CCAGAGGACCCCTCCCCTCCCTGGCATCCAGAGACACTGTGA
|
| Enzyme 5 GenBank Gene ID |
M55602  |
| Enzyme 5 GeneCard ID |
ABP1  |
| Enzyme 5 GenAtlas ID |
ABP1  |
| Enzyme 5 HGNC ID |
HGNC:80  |
| Enzyme 5 Chromosome Location |
7 |
| Enzyme 5 Locus |
7q34-q36 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 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
]
- 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 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5630 |
| Enzyme 6 Name |
Membrane copper amine oxidase |
| Enzyme 6 Synonyms |
- Semicarbazide-sensitive amine oxidase
- SSAO
- Vascular adhesion protein 1
- VAP-1
- HPAO
|
| Enzyme 6 Gene Name |
AOC3 |
| Enzyme 6 Protein Sequence |
>Membrane copper amine oxidase
MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLF
ADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPP
AREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDID
QMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFL
HHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSW
SLKSPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGERLV
YEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLATYVDWHFLLESQ
APKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAETVLVVRSMSTLLNYDYVWDTVFH
PSGAIEIRFYATGYISSAFLFGATGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVW
AEDMVFVPMAVPWSPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHP
RGYRIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVDF
SDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSA
DSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGGFSHN
|
| Enzyme 6 Number of Residues |
763 |
| Enzyme 6 Molecular Weight |
84623 |
| Enzyme 6 Theoretical pI |
6.51 |
| Enzyme 6 GO Classification |
| Function |
- binding
- cation binding
- copper ion binding
- ion binding
- transition metal ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 6 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 6 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 |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
1399032  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q16853  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
AOC3_HUMAN  |
| Enzyme 6 PDB ID |
1PU4  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 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 6 GenBank Gene ID |
U39447  |
| Enzyme 6 GeneCard ID |
AOC3  |
| Enzyme 6 GenAtlas ID |
AOC3  |
| Enzyme 6 HGNC ID |
HGNC:550  |
| Enzyme 6 Chromosome Location |
Not Available |
| Enzyme 6 Locus |
Not Available |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 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
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5631 |
| Enzyme 7 Name |
Retina-specific copper amine oxidase precursor |
| Enzyme 7 Synonyms |
- RAO
- Amine oxidase [copper-containing]
|
| Enzyme 7 Gene Name |
AOC2 |
| Enzyme 7 Protein Sequence |
>Retina-specific copper amine oxidase precursor
MHLKIVLAFLALSLITIFALAYVLLTSPGGSSQPPHCPSVSHRAQPWPHPGQSQLFADLS
REELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREA
LAIVLFGGQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLRAEFTQMWRHLK
EVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRSGDRATWMALYHNISGVGLFLHPVGLE
LLLDHRALDPAHWTVQQVFYLGHYYADLGQLEREFKSGRLEVVRVPLPPPNGASSLRSRN
SPGPLPPLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQ
ECVSIYGADSPKTMLTRYLDSSFGLGRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLP
GAVCVFEEAQGLPLRRHHNYLQNHFYGGLASSALVVRSVSSVGNYDYIWDFVLYPNGALE
GRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDV
VFKPVAAPWNPEHWLQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLASNQTNAWGHQRGYR
IQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEESQSSSIYHQNDIWTPTVTFADFI
NNETLLGEDLVAWVTASFLHIPHAEDIPNTVTLGNRVGFLLRPYNFFDEDPSIFSPGSVY
FEKGQDAGLCSINPVACLPDLAACVPDLPPFSYHGF
|
| Enzyme 7 Number of Residues |
756 |
| Enzyme 7 Molecular Weight |
83674 |
| Enzyme 7 Theoretical pI |
7.03 |
| Enzyme 7 GO Classification |
| Function |
- binding
- cation binding
- copper ion binding
- ion binding
- transition metal ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 7 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 7 Specific Function |
May be a critical modulator of signal transmission in retina, possibly by degrading the biogenic amines dopamine, histamine, and putrescine |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
Not Available |
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
1906806  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
O75106  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
AOC2_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>2190 bp
ATGCATCTCAAGATAGTCCTGGCGTTCCTGGCACTGTCCCTCATTACCATCTTTGCCCTG
GCCTATGTTTTGCTGACCAGCCCAGGTGGTTCCAGCCAGCCTCCCCACTGCCCCTCTGTA
TCCCATAGGGCCCAGCCCTGGCCACACCCTGGCCAGAGCCAGCTGTTTGCAGACCTGAGC
CGAGAGGAGTTGACAGCTGTGATGCGCTTTCTGACCCAGCGGCTGGGGCCAGGGCTGGTG
GACGCAGCCCAGGCTCAGCCCTCGGACAACTGCATCTTCTCAGTGGAGCTGCAGCTGCCC
CCCAAGGCTGCAGCCCTGGCCCACCTGGACAGGGGGAGCCCCCCACCTGCCCGGGAGGCA
CTGGCCATCGTCCTCTTTGGTGGACAACCCCAACCCAATGTGAGTGAGCTGGTGGTGGGG
CCGCTGCCTCACCCCTCGTACATGCGGGATGTGACTGTGGAGCGTCACGGCGGGCCCCTG
CCCTATCACCGTCGCCCGGTGCTGAGAGCTGAGTTTACACAGATGTGGAGGCATCTGAAA
GATGTGGAGCTACCCAAGGCACCCATCTTCCTGTCGTCCACCTTCAACTACAATGGCTCT
ACCCTGGCAGCTGTGCATGCCACCCCTCGGGGCTTGCGCTCAAGGGAACGAACTACCTGG
ATTGGCCTCTACCATAACATCTCAGGGGTTGGTCTTTTCCTTCACCCCGTGGGGCTGGAG
CTACTACTGGACCACAGGGCCCTGGACCCTGCCCACTGGACTGTCCAGCAGGTCTTCTAC
CTTGGGCACTACTATGCAGACTTGGGCCAGTTGGAACGGGAGTTTAAGTCTGGCCGGTTG
GAAGTGGTTAGAGTCCCTCTACCTCCACCAAATGGAGCTTCATCCCTGAGGTCTCGGAAC
TCTCCAGGTCCTCTTCCCCCTCTTCAGTTCTCGCCCCAGGGTTCCCAGTACAGTGTGCAA
GGAAACCTGGTGGTATCCTCCCTCTGGTCATTTACCTTTGGCCATGGGGTGTTCAGCGGC
CTGAGGATTTTTGATGTTCGGTTCCAGGGTGAGCGAATAGCCTATGAAGTCAGTGTCCAG
GAGTGTGTATCTATCTATGGTGCCGATTCACCCAAGACGATGCTGACTCGCTATTTGGAT
AGCAGCTTTGGACTCGGCCGTAACAGCCGAGGCTTGGTGCGGGGAGTGGACTGCCCCTAT
CAAGCCACGATGGTGGACATCCATATATTAGTGGGCAAAGGGGCAGTCCAGCTGCTTCCA
GGGGCTGTGTGTGTATTTGAGGAAGCCCAGGGACTGCCCCTTCGAAGGCACCACAATTAC
CTTCAAAATCATTTCTATGGTGGTTTGGCCAGCTCAGCCCTTGTGGTCAGGTCTGTGTCA
TCTGTGGGCAACTATGACTACATTTGGGACTTTGTGTTGTACCCAAATGGGGCACTTGAA
GGGCGGGTCCATGCCACGGGTTATATCAACACAGCTTTCCTGAAAGGGGGAGAGGAGGGC
CTCCTCTTTGGGAACCGTGTGGGGGAAAGAGTGCTGGGAACGGTGCACACACATGCCTTC
CACTTCAAGCTGGACCTGGATGTGGCAGGGCTGAAAAACTGGGTGGTAGCTGAAGACGTG
GTGTTTAAACCTGTGGCTGCCCCCTGGAACCCGGAGCACTGGCTACAGCGCCCACAGCTG
ACTCGGCAGGTCCTGGGAAAGGAGGACCTGACAGCTTTTTCCTTGGGAAGCCCCCTACCC
CGCTACCTCTACCTGGCTAGCAACCAGACTAATGCGTGGGGTCACCAGCGCGGATACCAG
CTTGTGGTGACCCAGAGAAAGGAGGAGGAGTCACAGAGCAGTAGCATCTATCACCAGAAT
GACATCTGGACACCCACAGTTACCTTTGCTGACTTCATCAACAATGAAACCCTCTTAGGA
GAGGATCTGGTGGCTTGGGTCACAGCCAGCTTCCTGCACATTCCCCATGCCGAGGACATC
CCAAACACAGTGACTCTGGGGAACAGAGTTGGCTTCTTGCTCCGACCCTATAACTTCTTT
GATGAGGACCCCTCCATCTTCTCCCCTGGCAGTGTGTACTTTGAGAAGGGCCAGGATGCT
GGGCTCTGCAGCATCAATCCTGTGGCCTGCCTCCCCGACCTGGCAGCCTGTGTCCCGGAC
TTACCCCCTTTCTCTTACCACGGCTTCTAG
|
| Enzyme 7 GenBank Gene ID |
D88213  |
| Enzyme 7 GeneCard ID |
AOC2  |
| Enzyme 7 GenAtlas ID |
AOC2  |
| Enzyme 7 HGNC ID |
HGNC:549  |
| Enzyme 7 Chromosome Location |
Not Available |
| Enzyme 7 Locus |
Not Available |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 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
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
7086 |
| Enzyme 8 Name |
D(2) dopamine receptor |
| Enzyme 8 Synonyms |
- Dopamine D2 receptor
|
| Enzyme 8 Gene Name |
DRD2 |
| Enzyme 8 Protein Sequence |
>D(2) dopamine receptor
MDPLNLSWYDDDLERQNWSRPFNGSDGKADRPHYNYYATLLTLLIAVIVFGNVLVCMAVS
REKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWKFSRIHCDIFVTLDVMMCTA
SILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMISIVWVLSFTISCPLLFGLNNADQN
ECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIVLRRRRKRVNTKRSSRAFRAHLRAPL
KGNCTHPEDMKLCTVIMKSNGSFPVNRRRVEAARRAQELEMEMLSSTSPPERTRYSPIPP
SHHQLTLPDPSHHGLHSTPDSPAKPEKNGHAKDHPKIAKIFEIQTMPNGKTRTSLKTMSR
RKLSQQKEKKATQMLAIVLGVFIICWLPFFITHILNIHCDCNIPPVLYSAFTWLGYVNSA
VNPIIYTTFNIEFRKAFLKILHC
|
| Enzyme 8 Number of Residues |
443 |
| Enzyme 8 Molecular Weight |
50620 |
| Enzyme 8 Theoretical pI |
9.85 |
| Enzyme 8 GO Classification |
| Function |
- G-protein coupled receptor activity
- amine receptor activity
- dopamine receptor activity
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 8 General Function |
Not Available |
| Enzyme 8 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 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
- 38-60
72-97
109-130
152-174
187-210
374-397
406-429
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
563756  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P14416  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
DRD2_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>66 bp
ATGCGGCGGGAGCTGGAAGCCTCAAGCAGCCGGCGCCGTCTCTGCCCCCGGGGCCCTATG
GCTTGA
|
| Enzyme 8 GenBank Gene ID |
M30625  |
| Enzyme 8 GeneCard ID |
DRD2  |
| Enzyme 8 GenAtlas ID |
DRD2  |
| Enzyme 8 HGNC ID |
HGNC:3023  |
| Enzyme 8 Chromosome Location |
11 |
| Enzyme 8 Locus |
11q23 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 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
]
- 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
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
8029 |
| Enzyme 9 Name |
D(4) dopamine receptor |
| Enzyme 9 Synonyms |
- Dopamine D4 receptor
- D(2Cdopamine receptor
|
| Enzyme 9 Gene Name |
DRD4 |
| Enzyme 9 Protein Sequence |
>D(4) dopamine receptor
MGNRSTADADGLLAGRGPAAGASAGASAGLAGQGAAALVGGVLLIGAVLAGNSLVCVSVA
TERALQTPTNSFIVSLAAADLLLALLVLPLFVYSEVQGGAWLLSPRLCDALMAMDVMLCT
ASIFNLCAISVDRFVAVAVPLRYNRQGGSRRQLLLIGATWLLSAAVAAPVLCGLNDVRGR
DPAVCRLEDRDYVVYSSVCSFFLPCPLMLLLYWATFRGLQRWEVARRAKLHGRAPRRPSG
PGPPSPTPPAPRLPQDPCGPDCAPPAPGLPRGPCGPDCAPAAPGLPPDPCGPDCAPPAPG
LPQDPCGPDCAPPAPGLPRGPCGPDCAPPAPGLPQDPCGPDCAPPAPGLPPDPCGSNCAP
PDAVRAAALPPQTPPQTRRRRRAKITGRERKAMRVLPVVVGAFLLCWTPFFVVHITQALC
PACSVPPRLVSAVTWLGYVNSALNPVIYTVFNAEFRNVFRKALRACC
|
| Enzyme 9 Number of Residues |
467 |
| Enzyme 9 Molecular Weight |
48361 |
| Enzyme 9 Theoretical pI |
8.37 |
| Enzyme 9 GO Classification |
| Function |
- G-protein coupled receptor activity
- amine receptor activity
- dopamine receptor activity
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 9 General Function |
Cell cycle control, cell division, chromosome partitioning |
| 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
71-93
110-131
152-175
192-213
395-417
427-449
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
291946  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P21917  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
DRD4_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 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 9 GenBank Gene ID |
L12398  |
| Enzyme 9 GeneCard ID |
DRD4  |
| Enzyme 9 GenAtlas ID |
DRD4  |
| Enzyme 9 HGNC ID |
HGNC:3025  |
| Enzyme 9 Chromosome Location |
11 |
| Enzyme 9 Locus |
11p15.5 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 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
]
- 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 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
8046 |
| Enzyme 10 Name |
Sodium-dependent dopamine transporter |
| Enzyme 10 Synonyms |
- DA transporter
- DAT
|
| Enzyme 10 Gene Name |
SLC6A3 |
| Enzyme 10 Protein Sequence |
>Sodium-dependent dopamine transporter
MSKSKCSVGLMSSVVAPAKEPNAVGPKEVELILVKEQNGVQLTSSTLTNPRQSPVEAQDR
ETWGKKIDFLLSVIGFAVDLANVWRFPYLCYKNGGGAFLVPYLLFMVIAGMPLFYMELAL
GQFNREGAAGVWKICPILKGVGFTVILISLYVGFFYNVIIAWALHYLFSSFTTELPWIHC
NNSWNSPNCSDAHPGDSSGDSSGLNDTFGTTPAAEYFERGVLHLHQSHGIDDLGPPRWQL
TACLVLVIVLLYFSLWKGVKTSGKVVWITATMPYVVLTALLLRGVTLPGAIDGIRAYLSV
DFYRLCEASVWIDAATQVCFSLGVGFGVLIAFSSYNKFTNNCYRDAIVTTSINSLTSFSS
GFVVFSFLGYMAQKHSVPIGDVAKDGPGLIFIIYPEAIATLPLSSAWAVVFFIMLLTLGI
DSAMGGMESVITGLIDEFQLLHRHRELFTLFIVLATFLLSLFCVTNGGIYVFTLLDHFAA
GTSILFGVLIEAIGVAWFYGVGQFSDDIQQMTGQRPSLYWRLCWKLVSPCFLLFVVVVSI
VTFRPPHYGAYIFPDWANALGWVIATSSMAMVPIYAAYKFCSLPGSFREKLAYAIAPEKD
RELVDRGEVRQFTLRHWLKV
|
| Enzyme 10 Number of Residues |
620 |
| Enzyme 10 Molecular Weight |
68496 |
| Enzyme 10 Theoretical pI |
6.92 |
| Enzyme 10 GO Classification |
| Function |
- dopamine:sodium symporter activity
- neurotransmitter transporter activity
- neurotransmitter:sodium symporter activity
- transporter activity
|
| Process |
- cellular physiological process
- neurotransmitter transport
- physiological process
- transport
|
| Component |
- cell
- integral to membrane
- integral to plasma membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 10 General Function |
Not Available |
| Enzyme 10 Specific Function |
Amine transporter. Terminates the action of dopamine by its high affinity sodium-dependent reuptake into presynaptic terminals |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 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 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
553260  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q01959  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
SC6A3_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>278 bp
GCTGCACTATCTCTTCTCCTCCTTCACCACGGAGCTCCCCTGGATCCACTGCAACAACTC
CTGGAACAGCCCCAACTGCTCGGATGCCCATCCTGGTGACTCCAGTGGAGACAGCTCGGG
CCTCAACGACACTTTTGGGACCACACCTGCTGCCGAGTACTTTGAACGTGGCGTGCTGCA
CCTCCACCAGAGCCATGGCATCGACGACCTGGGGCCTCCGCGGTGGCAGCTCACAGCCTG
CCTGGTGCTGGTCATCGTGCTGCTCTACTTCAGCCTCT
|
| Enzyme 10 GenBank Gene ID |
M96670  |
| Enzyme 10 GeneCard ID |
SLC6A3  |
| Enzyme 10 GenAtlas ID |
SLC6A3  |
| Enzyme 10 HGNC ID |
HGNC:11049  |
| Enzyme 10 Chromosome Location |
5 |
| Enzyme 10 Locus |
5p15.3 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 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
]
- 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 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
13244 |
| Enzyme 11 Name |
D1 dopamine receptor-interacting protein calcyon |
| Enzyme 11 Synonyms |
Not Available |
| Enzyme 11 Gene Name |
DRD1IP |
| Enzyme 11 Protein Sequence |
>D1 dopamine receptor-interacting protein calcyon
MVKLGCSFSGKPGKDPGDQDGAAMDSVPLISPLDISQLQPPLPDQVVIKTQTEYQLSSPD
QQNFPDLEGQRLNCSHPEEGRRLPTARMIAFAMALLGCVLIMYKAIWYDQFTCPDGFLLR
HKICTPLTLEMYYTEMDPERHRSILAAIGAYPLSRKHGTETPAAWGDGYRAAKEERKGPT
QAGAAAAATEPPGKPSAKAEKEAARKAAGSAAPPPAQ
|
| Enzyme 11 Number of Residues |
217 |
| Enzyme 11 Molecular Weight |
23434 |
| Enzyme 11 Theoretical pI |
6.91 |
| Enzyme 11 GO Classification |
| Function |
- G-protein-coupled receptor binding
- dopamine receptor binding
- receptor binding
- signal transducer activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- dopamine receptor signaling pathway
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 11 General Function |
Not Available |
| Enzyme 11 Specific Function |
May have a role in potentiating calcium ion-dependent signaling |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
6980076  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q9NYX4  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
D1IP_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>654 bp
ATGGTGAAGCTGGGCTGCAGCTTCTCTGGGAAGCCAGGTAAAGACCCTGGGGACCAGGAT
GGGGCTGCCATGGACAGTGTGCCTCTGATCAGCCCCTTGGACATCAGCCAGCTCCAGCCG
CCACTCCCTGACCAGGTGGTCATCAAGACACAGACAGAATACCAGCTGTCCTCCCCAGAC
CAGCAGAATTTCCCTGACCTGGAGGGCCAGAGGCTGAACTGCAGCCACCCAGAGGAAGGG
CGCAGGCTGCCCACCGCACGGATGATCGCCTTCGCCATGGCGCTACTGGGCTGCGTGCTG
ATCATGTACAAGGCCATCTGGTACGACCAGTTCACCTGCCCCGACGGCTTCCTGCTGCGG
CACAAGATCTGCACGCCGCTGACCCTGGAGATGTACTACACGGAGATGGACCCCGAGCGC
CACCGCAGCATCCTGGCGGCCATCGGGGCCTACCCGCTGAGCCGCAAGCACGGCACGGAG
ACGCCGGCGGCCTGGGGGGACGGCTACCGCGCAGCCAAGGAGGAGCGCAAGGGGCCCACC
CAGGCTGGGGCGGCGGCGGCGGCCACCGAACCCCCCGGGAAGCCGTCGGCCAAGGCGGAG
AAGGAGGCGGCGCGGAAGGCGGCCGGGAGCGCGGCGCCCCCGCCCGCGCAGTGA
|
| Enzyme 11 GenBank Gene ID |
AF225903  |
| Enzyme 11 GeneCard ID |
Q9NYX4  |
| Enzyme 11 GenAtlas ID |
CALY  |
| Enzyme 11 HGNC ID |
HGNC:17938  |
| Enzyme 11 Chromosome Location |
10 |
| Enzyme 11 Locus |
10q26.3 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 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
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
13261 |
| Enzyme 12 Name |
Calcium-dependent secretion activator 1 |
| Enzyme 12 Synonyms |
- Calcium-dependent activator protein for secretion 1
- CAPS-1
|
| Enzyme 12 Gene Name |
CADPS |
| Enzyme 12 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 12 Number of Residues |
1353 |
| Enzyme 12 Molecular Weight |
152788 |
| Enzyme 12 Theoretical pI |
5.44 |
| Enzyme 12 GO Classification |
Not Available |
| Enzyme 12 General Function |
Carbohydrate transport and metabolism |
| Enzyme 12 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 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 |
21541504  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q9ULU8  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
CAPS1_HUMAN  |
| Enzyme 12 PDB ID |
1WI1  |
| Enzyme 12 PDB File |
Show |
| Enzyme 12 3D Structure |
|
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>3825 bp
ATGCTGGACCCTTCGTCCAGCGAAGAAGAATCGGATGAGATCGTGGAGGAGGAGAGCGGC
AAGGAGGTGCTCGGCTCGGCCCCGTCCGGCGCGCGCCTGTCTCCCAGCCGTACCAGCGAG
GGCTCGGCCGGCAGCGCCGGGCTGGGGGGCGGCGGCGCCGGCGCCGGAGCCGGGGTGGGT
GCAAGCGGCGGCGGGGGCAGCGGCGCGAGCAGCGGCGGCGGGGCCGGGGGGCTGCAACCC
AGCAGCCGCGCTGGCGGCGGCCGGCCCTCCAGCCCCAGCCCGTCGGTGGTGAGCGAGAAG
GAGAAGGAAGAGTTGGAGCGGCTGCAGAAAGAGGAGGAGGAGAGGAAGAAGAGGCTGCAG
CTGTATGTGTTCGTGATGCGCTGCATCGCCTACCCCTTTAATGCCAAGCAGCCCACCGAC
ATGGCTCGCCGGCAGCAGAAGATCAGCAAACAGCAGCTGCAGACAGTCAAGGACCGGTTT
CAGGCTTTCCTCAATGGGGAAACCCAGATCATGGCTGACGAAGCCTTCATGAACGCTGTG
CAGAGTTACTATGAGGTGTTCCTGAAGAGCGACCGTGTGGCCCGCATGGTTCAGAGTGGA
GGCTGTTCCGCCAACGACTCCCGGGAGGTCTTCAAGAAGCACATTGAGAAGAGAGTGCGC
AGCCTGCCTGAGATTGACGGCCTCAGCAAGGAGACTGTGCTGAGCTCCTGGATGGCCAAA
TTTGATGCCATCTACCGTGGAGAAGAGGACCCGCGGAAGCAGCAGGCCCGGATGACAGCC
AGCGCAGCCTCCGAGCTGATTCTGAGCAAGGAGCAACTCTATGAGATGTTCCAGAACATT
CTTGGGATCAAGAAGTTCGAACATCAGCTCCTTTACAATGCCTGCCAGCTGGACAATCCA
GATGAGCAGGCAGCCCAGATCAGACGAGAGCTGGATGGACGTCTACAAATGGCAGACCAA
ATAGCCAGGGAACGCAAATTTCCCAAGTTTGTATCCAAAGAAATGGAAAACATGTACATT
GAGGAGCTGAAGTCATCTGTCAACCTGCTCATGGCCAACTTGGAGAGCATGCCGGTATCC
AAAGGCGGGGAGTTCAAGCTCCAGAAACTCAAACGCAGCCACAATGCTTCCATCATCGAC
ATGGGCGAGGAGAGTGAGAACCAGCTCTCCAAGTCAGATGTCGTGCTGTCTTTCTCATTG
GAGGTGGTAATTATGGAAGTCCAAGGCCTCAAATCTTTGGCTCCAAATCGCATCGTATAT
TGCACAATGGAGGTGGAAGGAGGAGAGAAACTACAGACTGATCAGGCCGAGGCTTCTAAA
CCAACCTGGGGCACCCAGGGTGACTTCTCCACAACCCATGCACTGCCAGCTGTGAAGGTG
AAGCTGTTCACAGAGAGCACAGGCGTCCTGGCGTTGGAGGACAAGGAGCTTGGGCGGGTT
ATTCTCCATCCCACCCCGAACAGCCCAAAACAGTCAGAGTGGCACAAAATGACAGTCTCC
AAAAACTGCCCCGACCAAGATCTCAAAATCAAACTTGCTGTCCGAATGGATAAGCCTCAA
AACATGAAGCATTCTGGGTATTTATGGGCCATCGGTAAGAATGTCTGGAAGAGATGGAAG
AAAAGGTTTTTTGTATTGGTGCAGGTCAGTCAGTACACGTTTGCCATGTGCAGTTATCGG
GAGAAGAAAGCGGAGCCTCAGGAACTTTTACAATTGGATGGCTACACTGTGGATTACACC
GACCCCCAGCCAGGTTTGGAGGGTGGCCGAGCCTTCTTCAATGCTGTCAAGGAGGGAGAC
ACCGTGATATTTGCCAGTGACGATGAACAAGACCGCATCCTGTGGGTCCAGGCCATGTAT
CGGGCCACGGGGCAGTCACACAAGCCTGTGCCCCCGACCCAAGTCCAGAAACTCAACGCC
AAGGGAGGAAATGTACCTCAGCTGGATGCCCCTATCTCTCAATTTTACGCAGATAGAGCT
CAAAAACATGGCATGGATGAATTTATCTCTTCCAACCCCTGTAACTTTGACCACGCTTCC
CTCTTTGAGATGGGCTGGTTCAGTCCTGGCCAGGTGTTTGTACTAGACGAGTATTGCGCC
CGAAATGGAGTCCGGGGGTGTCACCGACATCTCTGCTACCTCAGAGACTTGCTTGAACGG
GCAGAAAATGGCGCCATGATCGACCCCACCCTTCTTCACTACAGCTTTGCCTTCTGTGCA
TCCCATGTCCATGGGAACAGGCCTGATGGAATTGGAACTGTGACTGTTGAAGAAAAGGAA
CGTTTTGAAGAAATCAAAGAGAGGCTCCGAGTTCTGCTAGAAAATCAGATTACACATTTT
AGGTATTGCTTTCCATTTGGTCGACCTGAAGGTGCTTTGAAAGCTACTCTCTCACTCTTG
GAAAGGGTTTTGATGAAAGATATTGTTACCCCAGTGCCACAAGAGGAGGTAAAAACAGTT
ATCCGTAAATGTCTGGAACAGGCTGCGTTAGTCAACTATTCTCGGCTCTCAGAGTATGCC
AAAATCGAAGAAAATGTAGGCCGGTTAATCACTCCTGCCAAAAAGCTTGAAGATACAATA
CGTCTTGCTGAACTAGTCATTGAAGTTCTTCAGCAAAATGAGGAGCACCACGCCGAGGCC
TTTGCGTGGTGGTCAGATTTAATGGTGGAGCATGCGGAGACGTTCCTGTCACTCTTTGCA
GTAGACATGGATGCAGCCTTAGAGGTGCAACCTCCAGACACATGGGACAGTTTTCCACTA
TTTCAGCTGCTGAATGATTTTCTCCGTACTGACTATAATTTGTGCAATGGAAAATTTCAC
AAACACCTGCAAGACCTGTTTGCCCCACTTGTTGTTAGATATGTGGATCTGATGGAGTCC
TCAATTGCACAATCCATTCACAGGGGCTTTGAGCGGGAGTCATGGGAACCAGTCAATAAT
GGGTCAGGCACCTCAGAAGATCTGTTTTGGAAACTTGACGCCCTTCAGACCTTCATTCGG
GACCTGCACTGGCCTGAAGAAGAGTTTGGAAAGCACCTGGAACAACGGCTGAAGTTGATG
GCAAGTGACATGATCGAATCTTGTGTCAAAAGAACCAGGATTGCATTTGAAGTTAAGCTG
CAAAAAACCAGTCGATCAACAGATTTTCGAGTCCCACAGTCAATATGCACCATGTTTAAT
GTTATGGTTGATGCCAAAGCTCAATCAACAAAACTTTGCAGCATGGAAATGGGCCAAGAG
CATCAATACCATTCAAAAATAGACGAACTAATTGAAGAAACTGTTAAAGAAATGATAACA
CTCTTGGTTGCAAAGTTCGTTACTATCTTGGAAGGAGTGCTGGCAAAATTATCCAGATAT
GACGAAGGGACTTTGTTTTCTTCTTTTCTGTCATTTACCGTGAAGGCAGCTTCCAAATAT
GTGGATGTACCTAAACCCGGGATGGACGTGGCCGACGCCTACGTGACTTTCGTCCGCCAT
TCTCAGGATGTCCTGCGTGATAAGGTCAATGGGGAGATGTACATAGAAAGGTTATTTGAT
CAATGGTACAACAGCTCCATGAACGTGATCTGCACCTGGTTGACGGACCGGATGGACTTA
CAGCTTCATATTTATCAGTTGAAAACACTAATTAGGATGGTAAAGAAAACCTACAGAGAT
TTCCGATTGCAAGGGGTCCTGGACTCCACCTTTAACAGCAAGACCTATGAAACGATCCGG
AACCGTCTCACTGTGGAGGAAGCCACAGCATCAGTGAGTGAAGGTGGGGGACTGCAGGGC
ATCAGCATGAAGGACAGCGATGAGGAAGACGAAGAAGACGATTAG
|
| Enzyme 12 GenBank Gene ID |
AF458662  |
| Enzyme 12 GeneCard ID |
Q9ULU8  |
| Enzyme 12 GenAtlas ID |
CADPS  |
| Enzyme 12 HGNC ID |
HGNC:1426  |
| Enzyme 12 Chromosome Location |
Not Available |
| Enzyme 12 Locus |
Not Available |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 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
]
- 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
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
13262 |
| Enzyme 13 Name |
Calcium-dependent secretion activator 2 |
| Enzyme 13 Synonyms |
- Calcium-dependent activator protein for secretion 2
- CAPS-2
|
| Enzyme 13 Gene Name |
CADPS2 |
| Enzyme 13 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 13 Number of Residues |
1296 |
| Enzyme 13 Molecular Weight |
147736 |
| Enzyme 13 Theoretical pI |
6.10 |
| Enzyme 13 GO Classification |
Not Available |
| Enzyme 13 General Function |
Not Available |
| 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 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 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 |
30349347  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q86UW7  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
CAPS2_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>3891 bp
ATGCTGGACCCGTCTTCCAGCGAAGAGGAGTCGGACGAGGGGCTGGAAGAGGAAAGCCGC
GATGTGCTGGTGGCAGCCGGCAGCTCGCAGCGAGCTCCTCCAGCCCCGACTCGGGAAGGG
CGGCGGGACGCGCCGGGGCGCGCGGGCGGCGGCGGCGCGGCCAGATCTGTGAGCCCGAGC
CCCTCTGTGCTCAGCGAGGGGCGAGACGAGCCCCAGCGGCAGCTGGACGATGAGCAGGAG
CGGAGGATCCGCCTGCAGCTCTACGTCCTCGTCGTGAGGTGCATCGCGTACCCCTTCAAC
GCCAAGCAGCCCACCGACATGGCCCGGAGGCAGCAGAAGCTTAACAAACAACAGTTGCAG
TTACTGAAAGAACGGTTCCAGGCCTTCCTCAATGGGGAAACCCAAATTGTAGCTGACGAA
GCATTTTGCAACGCAGTTCGGAGTTATTATGAGGTTTTTCTAAAGAGTGACCGAGTGGCC
AGAATGGTACAGAGTGGAGGGTGTTCTGCTAATGACTTCAGAGAAGTATTTAAGAAAAAC
ATAGAAAAACGTGTGCGGAGTTTGCCAGAAATAGATGGCTTGAGCAAAGAGACAGTGTTG
AGCTCATGGATAGCCAAATATGATGCCATTTACAGAGGTGAAGAGGACTTGTGCAAACAG
CCAAATAGAATGGCCCTAAGTGCAGTGTCTGAACTTATTCTGAGCAAGGAACAACTCTAT
GAAATGTTTCAGCAGATTCTGGGTATTAAAAAACTAGAACACCAGCTCCTTTATAATGCA
TGTCAGCTGGATAACGCAGATGAACAAGCAGCCCAGATCAGAAGGGAACTTGATGGCCGG
CTGCAATTGGCAGATAAAATGGCAAAGGAAAGAAAATTCCCCAAATTTATAGCAAAAGAT
ATGGAGAATATGTATATAGAAGAGTTGCGGTCTTCAGTGAATTTGCTAATGGCCAATTTG
GAAAGTCTTCCAGTTTCGAAAGGTGGTCCGGAATTTAAATTACAAAAATTAAAACGTTCA
CAGAACTCTGCATTTTTGGACATAGGAGATGAGAATGAGATTCAGCTGTCAAAGTCCGGC
GTGGTACTGTCATTCACCTTAGAGATTGTCATAATGGAAGTGCAAGGCCTGAAGTCAGTT
GCTCCCAATCGAATTGTTTACTGTACAATGGAAGTGGAAGGAGAAAAACTTCAGACAGAC
CAGGCCGAAGCCTCAAGGCCACAATGGGGGACTCAAGGAGATTTCACCACCACCCATCCT
CGGCCTGTGGTCAAAGTGAAACTCTTCACAGAAAGCACTGGAGTTCTGGCCCTGGAAGAT
AAAGAACTGGGAAGGGTGATATTATACCCAACTTCTAATAGCTCCAAATCAGCTGAATTA
CACCGAATGGTAGTTCCAAAAAATAGCCAGGATTCTGACTTAAAAATCAAACTGGCAGTG
CGAATGGATAAACCAGCACATATGAAGCATAGTGGATATCTGTATGCCCTTGGACAGAAG
GTTTGGAAAAGATGGAAAAAACGTTACTTTGTTCTAGTTCAGGTTAGCCAATATACCTTT
GCTATGTGCAGTTATAGAGAAAAGAAGTCTGAACCACAAGAATTAATGCAGCTTGAAGGC
TATACTGTGGATTATACCGATCCCCACCCAGGCCTTCAGGGTGGTTGTATGTTCTTTAAT
GCTGTTAAAGAAGGAGATACTGTAATCTTTGCCAGTGATGATGAACAGGACAGAATATTA
TGGGTTCAAGCCATGTATAGGGCCACAGGTCAATCATATAAACCAGTTCCTGCAATTCAA
ACCCAGAAACTGAATCCTAAAGGAGGAACTCTCCATGCAGATGCTCAGCTTTCTGGTAAA
GATGCAGATCGTTTTCAGAAACATGGTATGGATGAGTTTATTTCTGCAAACCCCTGCAAG
CTTGATCATGCCTTCCTTTTTAGAATACTCCAGAGGCAGACTTTGGATCACAGACTGAAT
GATTCCTATTCTTGCTTGGGATGGTTTAGCCCTGGCCAAGTCTTTGTGTTAGATGAGTAC
TGTGCCCGTTATGGTGTGAGAGGCTGTCACAGACATCTCTGCTACCTTGCAGAACTGATG
GAACATTCAGAAAATGGTGCTGTCATTGACCCTACCCTGCTCCATTACAGCTTTGCATTC
TGTGCCTCTCATGTGCACGGCAACAGGCCTGATGGAATTGGGACTGTTTCAGTGGAAGAA
AAAGAAAGATTTGAGGAGATAAAAGAGAGACTCTCTTCCCTTTTAGAAAATCAGATAAGC
CATTTCAGATACTGTTTTCCCTTTGGACGACCTGAAGGTGCTCTAAAAGCTACACTTTCA
TTACTTGAAAGGGTTTTAATGAAAGATATTGCCACTCCCATACCAGCAGAAGAGGTGAAG
AAAGTGGTCAGAAAATGTCTCGAGAAAGCTGCCTTGATCAATTACACTAGACTCACCGAA
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 13 GenBank Gene ID |
AY264289  |
| Enzyme 13 GeneCard ID |
Q86UW7  |
| Enzyme 13 GenAtlas ID |
CADPS2  |
| Enzyme 13 HGNC ID |
HGNC:16018  |
| Enzyme 13 Chromosome Location |
Not Available |
| Enzyme 13 Locus |
Not Available |
| 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
]
- 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
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
16425 |
| Enzyme 14 Name |
cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a) |
| Enzyme 14 Synonyms |
Not Available |
| Enzyme 14 Gene Name |
MAOB |
| Enzyme 14 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 14 Number of Residues |
520 |
| Enzyme 14 Molecular Weight |
58764 |
| Enzyme 14 Theoretical pI |
7.55 |
| Enzyme 14 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Amino acid transport and metabolism |
| Enzyme 14 Specific Function |
Not Available |
| 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 |
Not Available |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
B2R6R3  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
B2R6R3_HUMAN  |
| Enzyme 14 PDB ID |
2BK3  |
| Enzyme 14 PDB File |
Show |
| Enzyme 14 3D Structure |
|
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
Not Available |
| Enzyme 14 GenBank Gene ID |
AK312679  |
| Enzyme 14 GeneCard ID |
B2R6R3  |
| Enzyme 14 GenAtlas ID |
Not Available |
| Enzyme 14 HGNC ID |
Not Available |
| Enzyme 14 Chromosome Location |
Not Available |
| Enzyme 14 Locus |
Not Available |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
Not Available |
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
17081 |
| Enzyme 15 Name |
D(3) dopamine receptor |
| Enzyme 15 Synonyms |
Not Available |
| Enzyme 15 Gene Name |
DRD3 |
| Enzyme 15 Protein Sequence |
>D(3) dopamine receptor
MASLSQLSSHLNYTCGAENSTGASQARPHAYYALSYCALILAIVFGNGLVCMAVLKERAL
QTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILN
LCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPTV
CSISNPDFVIYSSVVSFYLPFGVTVLVYARIYVVLKQRRRKRILTRQNSQCNSVRPGFPQ
QTLSPDPAHLELKRYYSICQDTALGGPGFQERGGELKREEKTRNSLSPTIAPKLSLEVRK
LSNGRLSTSLKLGPLQPRGVPLREKKATQMVAIVLGAFIVCWLPFFLTHVLNTHCQTCHV
SPELYSATTWLGYVNSALNPVIYTTFNIEFRKAFLKILSC
|
| Enzyme 15 Number of Residues |
400 |
| Enzyme 15 Molecular Weight |
44225 |
| Enzyme 15 Theoretical pI |
9.07 |
| Enzyme 15 GO Classification |
| Function |
- G-protein coupled receptor activity
- amine receptor activity
- dopamine receptor activity
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 15 General Function |
Not Available |
| Enzyme 15 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 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
- 33-55
67-92
105-126
150-172
186-209
330-351
367-388
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
Not Available |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P35462  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
DRD3_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
Not Available |
| Enzyme 15 GenBank Gene ID |
U32499  |
| Enzyme 15 GeneCard ID |
P35462  |
| Enzyme 15 GenAtlas ID |
DRD3  |
| Enzyme 15 HGNC ID |
HGNC:3024  |
| Enzyme 15 Chromosome Location |
Not Available |
| Enzyme 15 Locus |
Not Available |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 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
]
- 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
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
17083 |
| Enzyme 16 Name |
D(1A) dopamine receptor |
| Enzyme 16 Synonyms |
Not Available |
| Enzyme 16 Gene Name |
DRD1 |
| Enzyme 16 Protein Sequence |
>D(1A) dopamine receptor
MRTLNTSAMDGTGLVVERDFSVRILTACFLSLLILSTLLGNTLVCAAVIRFRHLRSKVTN
FFVISLAVSDLLVAVLVMPWKAVAEIAGFWPFGSFCNIWVAFDIMCSTASILNLCVISVD
RYWAISSPFRYERKMTPKAAFILISVAWTLSVLISFIPVQLSWHKAKPTSPSDGNATSLA
ETIDNCDSSLSRTYAISSSVISFYIPVAIMIVTYTRIYRIAQKQIRRIAALERAAVHAKN
CQTTTGNGKPVECSQPESSFKMSFKRETKVLKTLSVIMGVFVCCWLPFFILNCILPFCGS
GETQPFCIDSNTFDVFVWFGWANSSLNPIIYAFNADFRKAFSTLLGCYRLCPATNNAIET
VSINNNGAAMFSSHHEPRGSISKECNLVYLIPHAVGSSEDLKKEEAAGIARPLEKLSPAL
SVILDYDTDVSLEKIQPITQNGQHPT
|
| Enzyme 16 Number of Residues |
446 |
| Enzyme 16 Molecular Weight |
49294 |
| Enzyme 16 Theoretical pI |
8.34 |
| Enzyme 16 GO Classification |
| Function |
- G-protein coupled receptor activity
- amine receptor activity
- dopamine receptor activity
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 16 General Function |
Not Available |
| 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 activate adenylyl cyclase |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
Not Available |
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
- 24-49
61-87
97-119
139-163
193-218
273-299
313-337
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
Not Available |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P21728  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
DRD1_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
Not Available |
| Enzyme 16 GenBank Gene ID |
X55760  |
| Enzyme 16 GeneCard ID |
P21728  |
| Enzyme 16 GenAtlas ID |
DRD1  |
| Enzyme 16 HGNC ID |
HGNC:3020  |
| Enzyme 16 Chromosome Location |
Not Available |
| Enzyme 16 Locus |
Not Available |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 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
]
- 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 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
17108 |
| Enzyme 17 Name |
D(1B) dopamine receptor |
| Enzyme 17 Synonyms |
- D1beta dopamine receptor
- D(5) dopamine receptor
|
| Enzyme 17 Gene Name |
DRD5 |
| Enzyme 17 Protein Sequence |
>D(1B) dopamine receptor
MLPPGSNGTAYPGQFALYQQLAQGNAVGGSAGAPPLGPSQVVTACLLTLLIIWTLLGNVL
VCAAIVRSRHLRANMTNVFIVSLAVSDLFVALLVMPWKAVAEVAGYWPFGAFCDVWVAFD
IMCSTASILNLCVISVDRYWAISRPFRYKRKMTQRMALVMVGLAWTLSILISFIPVQLNW
HRDQAASWGGLDLPNNLANWTPWEEDFWEPDVNAENCDSSLNRTYAISSSLISFYIPVAI
MIVTYTRIYRIAQVQIRRISSLERAAEHAQSCRSSAACAPDTSLRASIKKETKVLKTLSV
IMGVFVCCWLPFFILNCMVPFCSGHPEGPPAGFPCVSETTFDVFVWFGWANSSLNPVIYA
FNADFQKVFAQLLGCSHFCSRTPVETVNISNELISYNQDIVFHKEIAAAYIHMMPNAVTP
GNREVDNDEEEGPFDRMFQIYQTSPDGDPVAESVWELDCEGEISLDKITPFTPNGFH
|
| Enzyme 17 Number of Residues |
477 |
| Enzyme 17 Molecular Weight |
52951 |
| Enzyme 17 Theoretical pI |
5.08 |
| Enzyme 17 GO Classification |
| Function |
- G-protein coupled receptor activity
- amine receptor activity
- dopamine receptor activity
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 17 General Function |
Not Available |
| 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 |
- 40-66
78-104
115-136
159-180
224-246
297-320
341-360
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
Not Available |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
P21918  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
DRD5_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
Not Available |
| Enzyme 17 GenBank Gene ID |
X58454  |
| Enzyme 17 GeneCard ID |
P21918  |
| Enzyme 17 GenAtlas ID |
DRD5  |
| Enzyme 17 HGNC ID |
HGNC:3026  |
| Enzyme 17 Chromosome Location |
Not Available |
| Enzyme 17 Locus |
Not Available |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 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
]
- 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 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
17111 |
| Enzyme 18 Name |
Dopamine D4 receptor |
| Enzyme 18 Synonyms |
Not Available |
| Enzyme 18 Gene Name |
dopamine D4 receptor |
| Enzyme 18 Protein Sequence |
>Dopamine D4 receptor
MGNRSTADADRLLAGRGPAAGASAGASAGLAGQGAAALVGGVLLIGAVLAGNSLVCVSVA
TERALQTPTNSFIVSLAAADLLLALLVLPLFVYSE
|
| Enzyme 18 Number of Residues |
95 |
| Enzyme 18 Molecular Weight |
9149 |
| Enzyme 18 Theoretical pI |
4.64 |
| Enzyme 18 GO Classification |
| Function |
- G-protein coupled receptor activity
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 18 General Function |
Not Available |
| Enzyme 18 Specific Function |
Not Available |
| Enzyme 18 Pathways |
Not Available |
| Enzyme 18 Reactions |
Not Available |
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
Not Available |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q99586  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
Q99586_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
Not Available |
| Enzyme 18 GenBank Gene ID |
S82917  |
| Enzyme 18 GeneCard ID |
Q99586  |
| Enzyme 18 GenAtlas ID |
dopamine D4 receptor  |
| Enzyme 18 HGNC ID |
HGNC:3025  |
| Enzyme 18 Chromosome Location |
Not Available |
| Enzyme 18 Locus |
Not Available |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 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 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
17112 |
| 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
MGNRSTADADGLLAGRGPAAGASAGASAGLAGQGALLIGAVLAGNSLVCVSVATERALQT
PTNSFIVSLAAADLLLALLVLPLFVYSE
|
| Enzyme 19 Number of Residues |
88 |
| Enzyme 19 Molecular Weight |
8482 |
| Enzyme 19 Theoretical pI |
4.23 |
| Enzyme 19 GO Classification |
| Function |
- G-protein coupled receptor activity
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 19 General Function |
Not Available |
| 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 |
Not Available |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q99587  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
Q99587_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
Not Available |
| Enzyme 19 GenBank Gene ID |
S82918  |
| Enzyme 19 GeneCard ID |
Q99587  |
| 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 |