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Human Metabolome Database Version 2.5

 

Showing metabocard for Dopamine (HMDB00073)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:40
Accession Number HMDB00073
Secondary Accession Numbers Not Available
Common Name Dopamine
Description Dopamine is a member of the catecholamine (Neurotransmitters) family in the brain, and is a precursor to epinephrine (adrenaline) and norepinephrine (noradrenaline). Dopamine is synthesized in the body (mainly by nervous tissue and adrenal glands) first by the hydration of the amino acid tyrosine to DOPA by tyrosine hydroxylase and then by the decarboxylation of DOPA by aromatic-L-amino-acid decarboxylase. Dopamine is a major transmitter in the extrapyramidal system of the brain, and important in regulating movement. A family of receptors (Dopamine receptors) mediates its action. --PubChem
Synonyms
  1. 2-(3,4-Dihydroxyphenyl)ethylamine
  2. 3,4-Dihydroxyphenethylamine
  3. 3,4-Dihydroxyphenylethylamine
  4. 3-Hydroxytyramine
  5. 4-(2-Aminoethyl)-1,2-benzenediol
  6. 4-(2-aminoethyl)-Pyrocatechol
  7. 4-(2-Aminoethyl)catechol
  8. 4-(2-Aminoethyl)pyrocatechol
  9. a-(3,4-Dihydroxyphenyl)-b-aminoethane
  10. alpha-(3,4-Dihydroxyphenyl)-beta-aminoethane
  11. deoxyepinephrine
  12. Dopamin
  13. Dopamine
  14. Dopaminum
  15. Dopastat
  16. Dophamine
  17. Dynatra
  18. Hydroxytyramin
  19. hydroxytyramine
  20. Intropin
  21. Oxytyramine
  22. Revivan
Chemical IUPAC Name 4-(2-aminoethyl)benzene-1,2-diol
Chemical Formula C8H11NO2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Catecholamines and Derivatives
Sub Class
  • Dopamines
Family
  • Mammalian Metabolite
Species
  • phenol or hydroxyhetarene
  • 1,2-diphenol
  • primary amine
  • primary aliphatic amine (alkylamine)
  • aromatic compound
Biofunction
  • Component of Tyrosine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 153.178
Monoisotopic Molecular Weight 153.078979
Isomeric SMILES NCCC1=CC=C(O)C(O)=C1
Canonical SMILES NCCC1=CC=C(O)C(O)=C1
KEGG Compound ID C03758 Link Image
BioCyc ID DOPAMINE Link Image
BiGG ID 42467 Link Image
Wikipedia Link Dopamine Link Image
NuGOwiki Link HMDB00073 Link Image
Metagene Link HMDB00073 Link Image
METLIN ID 64 Link Image
PubChem Compound 681 Link Image
PubChem Substance 6517 Link Image
ChEBI ID 18243 Link Image
CAS Registry Number 62-31-7
InChI Identifier InChI=1/C8H11NO2/c9-4-3-6-1-2-7(10)8(11)5-6/h1-2,5,10-11H,3-4,9H2
Synthesis Reference Budnik, Josef. 2-(3,4-Dihydroxyphenyl)ethylamine hydrochloride. Czech. (1986), 2 pp.
Melting Point (Experimental) 128 oC
Experimental Water Solubility 535 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 1000.0 mg/mL [MEYLAN,WM et al. (1996)]; 7.43 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 1
State Solid
Experimental LogP/Hydrophobicity -0.98 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -0.40 [Predicted by ALOGPS]; 0.548 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • Extracellular
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Adipose Tissue
Adrenal Cortex
Adrenal Gland
Adrenal Medulla
Bladder
Brain
Epidermis
Fibroblasts
Kidney
Muscle
Myelin
Nerve Cells
Neuron
Pancreas
Placenta
Platelet
Skeletal Muscle
Spleen
Striatum
Testes
Concentrations (Normal)
Biofluid Blood
Value 22.50 +/- 4.50 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid CSF
Value 0.002+/-0.002 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. [PubMed Link Image]
Biofluid CSF
Value 0.0059 +/- 0.002 uM
Age Elderly:>65 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Raskind MA, Peskind ER, Holmes C, Goldstein DS: Patterns of cerebrospinal fluid catechols support increased central noradrenergic responsiveness in aging and Alzheimer's disease. Biol Psychiatry. 1999 Sep 15;46(6):756-65. [PubMed Link Image]
Biofluid CSF
Value 0.0045 +/- 0.0026 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Raskind MA, Peskind ER, Holmes C, Goldstein DS: Patterns of cerebrospinal fluid catechols support increased central noradrenergic responsiveness in aging and Alzheimer's disease. Biol Psychiatry. 1999 Sep 15;46(6):756-65. [PubMed Link Image]
Biofluid Urine
Value 0.22 +/- 0.07 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Cucchi ML, Frattini P, Santagostino G, Preda S, Orecchia G: Catecholamines increase in the urine of non-segmental vitiligo especially during its active phase. Pigment Cell Res. 2003 Apr;16(2):111-6. [PubMed Link Image]
Biofluid Urine
Value 0.44 +/- 0.13 umol/mmol creatinine
Age Adolescent:13-18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Cucchi ML, Frattini P, Santagostino G, Preda S, Orecchia G: Catecholamines increase in the urine of non-segmental vitiligo especially during its active phase. Pigment Cell Res. 2003 Apr;16(2):111-6. [PubMed Link Image]
Biofluid Urine
Value 0.107 (0.043-0.172) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Nikolelis DP, Drivelos DA, Simantiraki MG, Koinis S: An optical spot test for the detection of dopamine in human urine using stabilized in air lipid films. Anal Chem. 2004 Apr 15;76(8):2174-80. [PubMed Link Image]
Biofluid Urine
Value 0.10 (0.066-0.16) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 860 (179-1541) nmol/mmol creatinine
Age Infant:0-1 yr old
Sex N/A
Patient information Normal
Comments Free dopamine levels
References
  • Abdenur JE, Abeling N, Specola N, Jorge L, Schenone AB, van Cruchten AC, Chamoles NA: Aromatic l-aminoacid decarboxylase deficiency: unusual neonatal presentation and additional findings in organic acid analysis. Mol Genet Metab. 2006 Jan;87(1):48-53. Epub 2005 Nov 9. [PubMed Link Image]
Biofluid Urine
Value 2626 (30-5221) nmol/mmol creatinine
Age Infant:0-1 yr old
Sex N/A
Patient information Normal
Comments Total dopamine levels
References
  • Abdenur JE, Abeling N, Specola N, Jorge L, Schenone AB, van Cruchten AC, Chamoles NA: Aromatic l-aminoacid decarboxylase deficiency: unusual neonatal presentation and additional findings in organic acid analysis. Mol Genet Metab. 2006 Jan;87(1):48-53. Epub 2005 Nov 9. [PubMed Link Image]
Biofluid Urine
Value 9.2 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 18.0284 +/- 2.4552 uM
Age Elderly:>65 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid CSF
Value 0.000021 (0.000015-0.000027) uM
Age Adult:>18 yrs old
Sex Both
Condition Hypothyroidism
Comments Not Available
References
  • Sjoberg S, Eriksson M, Nordin C: L-thyroxine treatment and neurotransmitter levels in the cerebrospinal fluid of hypothyroid patients: a pilot study. Eur J Endocrinol. 1998 Nov;139(5):493-7. [PubMed Link Image]
Biofluid CSF
Value 0.000078 (0.0000065-0.00015) uM
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Raskind MA, Peskind ER, Holmes C, Goldstein DS: Patterns of cerebrospinal fluid catechols support increased central noradrenergic responsiveness in aging and Alzheimer's disease. Biol Psychiatry. 1999 Sep 15;46(6):756-65. [PubMed Link Image]
Biofluid CSF
Value 0.00002 +/- 0.000006 uM
Age Adult:>18 yrs old
Sex Both
Condition Hypothyroidism
Comments Not Available
References
  • Sjoberg S, Eriksson M, Nordin C: L-thyroxine treatment and neurotransmitter levels in the cerebrospinal fluid of hypothyroid patients: a pilot study. Eur J Endocrinol. 1998 Nov;139(5):493-7. [PubMed Link Image]
Biofluid CSF
Value 0.34 +/- 0.10 uM
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid Urine
Value 0.49 +/- 0.06 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Condition Vitiligo
Comments Not Available
References
  • Cucchi ML, Frattini P, Santagostino G, Preda S, Orecchia G: Catecholamines increase in the urine of non-segmental vitiligo especially during its active phase. Pigment Cell Res. 2003 Apr;16(2):111-6. [PubMed Link Image]
Biofluid Urine
Value 0.37 +/- 0.03 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Condition Vitiligo
Comments Age group: 1-5 years old
References
  • Cucchi ML, Frattini P, Santagostino G, Preda S, Orecchia G: Catecholamines increase in the urine of non-segmental vitiligo especially during its active phase. Pigment Cell Res. 2003 Apr;16(2):111-6. [PubMed Link Image]
Biofluid Urine
Value 0.4 +/- 0.05 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Condition Vitiligo
Comments Age group: 6-10 years old
References
  • Cucchi ML, Frattini P, Santagostino G, Preda S, Orecchia G: Catecholamines increase in the urine of non-segmental vitiligo especially during its active phase. Pigment Cell Res. 2003 Apr;16(2):111-6. [PubMed Link Image]
Biofluid Urine
Value 2426 +/- 0 nmol/mmol creatinine
Age Infant:0-1 yr old
Sex Male
Condition Aromatic L-amino acid decarboxylase deficiency
Comments Free dopamine levels
References
  • Abdenur JE, Abeling N, Specola N, Jorge L, Schenone AB, van Cruchten AC, Chamoles NA: Aromatic l-aminoacid decarboxylase deficiency: unusual neonatal presentation and additional findings in organic acid analysis. Mol Genet Metab. 2006 Jan;87(1):48-53. Epub 2005 Nov 9. [PubMed Link Image]
Biofluid Urine
Value 3119 +/- 0 nmol/mmol creatinine
Age Infant:0-1 yr old
Sex Male
Condition Aromatic L-amino acid decarboxylase deficiency
Comments Total dopamine levels
References
  • Abdenur JE, Abeling N, Specola N, Jorge L, Schenone AB, van Cruchten AC, Chamoles NA: Aromatic l-aminoacid decarboxylase deficiency: unusual neonatal presentation and additional findings in organic acid analysis. Mol Genet Metab. 2006 Jan;87(1):48-53. Epub 2005 Nov 9. [PubMed Link Image]
Associated Disorders
Condition References
Alzheimer's disease
Aromatic L-amino acid decarboxylase deficiency
  • Abdenur JE, Abeling N, Specola N, Jorge L, Schenone AB, van Cruchten AC, Chamoles NA: Aromatic l-aminoacid decarboxylase deficiency: unusual neonatal presentation and additional findings in organic acid analysis. Mol Genet Metab. 2006 Jan;87(1):48-53. Epub 2005 Nov 9. [PubMed Link Image]
Hypothyroidism
  • Sjoberg S, Eriksson M, Nordin C: L-thyroxine treatment and neurotransmitter levels in the cerebrospinal fluid of hypothyroid patients: a pilot study. Eur J Endocrinol. 1998 Nov;139(5):493-7. [PubMed Link Image]
Vitiligo
  • Cucchi ML, Frattini P, Santagostino G, Preda S, Orecchia G: Catecholamines increase in the urine of non-segmental vitiligo especially during its active phase. Pigment Cell Res. 2003 Apr;16(2):111-6. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Catecholamine Biosynthesis SMP00012 Link Image map00350 Link Image
Tyrosine Metabolism SMP00006 Link Image map00350 Link Image
General References
  1. Raskind MA, Peskind ER, Holmes C, Goldstein DS: Patterns of cerebrospinal fluid catechols support increased central noradrenergic responsiveness in aging and Alzheimer's disease. Biol Psychiatry. 1999 Sep 15;46(6):756-65. [PubMed Link Image]
  2. Mannelli M, Ianni L, Lazzeri C, Castellani W, Pupilli C, La Villa G, Barletta G, Serio M, Franchi F: In vivo evidence that endogenous dopamine modulates sympathetic activity in man. Hypertension. 1999 Sep;34(3):398-402. [PubMed Link Image]
  3. Jiang H, Betancourt L, Smith RG: Ghrelin amplifies dopamine signaling by cross talk involving formation of growth hormone secretagogue receptor/dopamine receptor subtype 1 heterodimers. Mol Endocrinol. 2006 Aug;20(8):1772-85. Epub 2006 Apr 6. [PubMed Link Image]
  4. Brody AL, Mandelkern MA, Olmstead RE, Scheibal D, Hahn E, Shiraga S, Zamora-Paja E, Farahi J, Saxena S, London ED, McCracken JT: Gene variants of brain dopamine pathways and smoking-induced dopamine release in the ventral caudate/nucleus accumbens. Arch Gen Psychiatry. 2006 Jul;63(7):808-16. [PubMed Link Image]
  5. Bauman A: Unilateral adrenal catecholamine excess. Pheochromocytoma or possible sporadic medullary hyperplasia. Arch Intern Med. 1982 Feb;142(2):377-8. [PubMed Link Image]
  6. Goldstein DS, Eisenhofer G, Kopin IJ: Sources and significance of plasma levels of catechols and their metabolites in humans. J Pharmacol Exp Ther. 2003 Jun;305(3):800-11. Epub 2003 Mar 20. [PubMed Link Image]
  7. King BM: The rise, fall, and resurrection of the ventromedial hypothalamus in the regulation of feeding behavior and body weight. Physiol Behav. 2006 Feb 28;87(2):221-44. Epub 2006 Jan 18. [PubMed Link Image]
  8. Cucchi ML, Frattini P, Santagostino G, Preda S, Orecchia G: Catecholamines increase in the urine of non-segmental vitiligo especially during its active phase. Pigment Cell Res. 2003 Apr;16(2):111-6. [PubMed Link Image]
  9. Sjoberg S, Eriksson M, Nordin C: L-thyroxine treatment and neurotransmitter levels in the cerebrospinal fluid of hypothyroid patients: a pilot study. Eur J Endocrinol. 1998 Nov;139(5):493-7. [PubMed Link Image]
  10. Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. [PubMed Link Image]
  11. Kobayashi K, Yasuhara T, Agari T, Muraoka K, Kameda M, Ji Yuan W, Hayase H, Matsui T, Miyoshi Y, Shingo T, Date I: Control of dopamine-secretion by Tet-Off system in an in vivo model of parkinsonian rat. Brain Res. 2006 Aug 2;1102(1):1-11. Epub 2006 Jun 27. [PubMed Link Image]
  12. Schenarts PJ, Sagraves SG, Bard MR, Toschlog EA, Goettler CE, Newell MA, Rotondo MF: Low-dose dopamine: a physiologically based review. Curr Surg. 2006 May-Jun;63(3):219-25. [PubMed Link Image]
  13. Piazza O, Zito G, Valente A, Tufano R: Effects of dopamine infusion on forearm blood flow in critical patients. Med Sci Monit. 2006 Feb;12(2):CR90-3. Epub 2006 Jan 26. [PubMed Link Image]
  14. Wang HY, Xiao Y, Han J, Chang XS: Simultaneous determination of dopamine and carvedilol in human serum and urine by first-order derivative fluorometry. Anal Sci. 2005 Nov;21(11):1281-5. [PubMed Link Image]
  15. Elchisak MA, Carlson JH: Assay of free and conjugated catecholamines by high-performance liquid chromatography with electrochemical detection. J Chromatogr. 1982 Dec 10;233:79-88. [PubMed Link Image]
  16. Eklundh T, Eriksson M, Sjoberg S, Nordin C: Monoamine precursors, transmitters and metabolites in cerebrospinal fluid: a prospective study in healthy male subjects. J Psychiatr Res. 1996 May-Jun;30(3):201-8. [PubMed Link Image]
  17. Kopieniak M, Wieczorkiewicz-Plaza A, Maciejewski R: Dopamine activity changes in cerebral cortex in the course of experimental acute pancreatitis. Ann Univ Mariae Curie Sklodowska [Med]. 2004;59(1):382-6. [PubMed Link Image]
  18. Raw I, Schmidt BJ, Merzel J: Catecholamines and congenital pain insensitivity. Braz J Med Biol Res. 1984;17(3-4):271-9. [PubMed Link Image]
  19. Nikolelis DP, Drivelos DA, Simantiraki MG, Koinis S: An optical spot test for the detection of dopamine in human urine using stabilized in air lipid films. Anal Chem. 2004 Apr 15;76(8):2174-80. [PubMed Link Image]
  20. Eisenhofer G, Aneman A, Friberg P, Hooper D, Fandriks L, Lonroth H, Hunyady B, Mezey E: Substantial production of dopamine in the human gastrointestinal tract. J Clin Endocrinol Metab. 1997 Nov;82(11):3864-71. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Amine oxidase [flavin-containing] A
  2. Dopamine beta-hydroxylase precursor
  3. Catechol O-methyltransferase
  4. Aromatic-L-amino-acid decarboxylase
  5. Amiloride-sensitive amine oxidase [copper-containing] precursor
  6. Membrane copper amine oxidase
  7. Retina-specific copper amine oxidase precursor
  8. D(2) dopamine receptor
  9. D(4) dopamine receptor
  10. Sodium-dependent dopamine transporter
  11. D1 dopamine receptor-interacting protein calcyon
  12. Calcium-dependent secretion activator 1
  13. Calcium-dependent secretion activator 2
  14. cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a)
  15. D(3) dopamine receptor
  16. D(1A) dopamine receptor
  17. D(1B) dopamine receptor
  18. Dopamine D4 receptor
  19. Dopamine D4 receptor
Enzyme 1 [top]
Enzyme 1 ID 5401
Enzyme 1 Name Amine oxidase [flavin-containing] A
Enzyme 1 Synonyms
  1. Monoamine oxidase type A
  2. 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
  • None
Enzyme 1 Transmembrane Regions
  • 498-518
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 187353 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P21397 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AOFA_HUMAN Link Image
Enzyme 1 PDB ID 1O5W Link Image
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 Link Image
Enzyme 1 GeneCard ID MAOA Link Image
Enzyme 1 GenAtlas ID MAOA Link Image
Enzyme 1 HGNC ID HGNC:6833 Link Image
Enzyme 1 Chromosome Location X
Enzyme 1 Locus Xp11.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. Denney RM: The promoter of the human monoamine oxidase A gene. Prog Brain Res. 1995;106:57-66. [PubMed Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5485
Enzyme 2 Name Dopamine beta-hydroxylase precursor
Enzyme 2 Synonyms
  1. 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
  • 1-25
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 30474 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P09172 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name DOPO_HUMAN Link Image
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 Link Image
Enzyme 2 GeneCard ID DBH Link Image
Enzyme 2 GenAtlas ID DBH Link Image
Enzyme 2 HGNC ID HGNC:2689 Link Image
Enzyme 2 Chromosome Location 9
Enzyme 2 Locus 9q34
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
Enzyme 2 Metabolite References Not Available
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
  • 1-32
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 180920 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P21964 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name COMT_HUMAN Link Image
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 Link Image
Enzyme 3 GeneCard ID COMT Link Image
Enzyme 3 GenAtlas ID COMT Link Image
Enzyme 3 HGNC ID HGNC:2228 Link Image
Enzyme 3 Chromosome Location 22
Enzyme 3 Locus 22q11.21-q11.23|22q11.21
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5510
Enzyme 4 Name Aromatic-L-amino-acid decarboxylase
Enzyme 4 Synonyms
  1. AADC
  2. DOPA decarboxylase
  3. 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
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 181521 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P20711 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name DDC_HUMAN Link Image
Enzyme 4 PDB ID 1JS3 Link Image
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 Link Image
Enzyme 4 GeneCard ID DDC Link Image
Enzyme 4 GenAtlas ID DDC Link Image
Enzyme 4 HGNC ID HGNC:2719 Link Image
Enzyme 4 Chromosome Location 7
Enzyme 4 Locus 7p11
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
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
  1. Diamine oxidase
  2. DAO
  3. Amiloride-binding protein
  4. ABP
  5. Histaminase
  6. Kidney amine oxidase
  7. 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
  • 1-19
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 177960 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P19801 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name ABP1_HUMAN Link Image
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 Link Image
Enzyme 5 GeneCard ID ABP1 Link Image
Enzyme 5 GenAtlas ID ABP1 Link Image
Enzyme 5 HGNC ID HGNC:80 Link Image
Enzyme 5 Chromosome Location 7
Enzyme 5 Locus 7q34-q36
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5630
Enzyme 6 Name Membrane copper amine oxidase
Enzyme 6 Synonyms
  1. Semicarbazide-sensitive amine oxidase
  2. SSAO
  3. Vascular adhesion protein 1
  4. VAP-1
  5. 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
  • 1-19
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 1399032 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q16853 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name AOC3_HUMAN Link Image
Enzyme 6 PDB ID 1PU4 Link Image
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 Link Image
Enzyme 6 GeneCard ID AOC3 Link Image
Enzyme 6 GenAtlas ID AOC3 Link Image
Enzyme 6 HGNC ID HGNC:550 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. 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 Link Image]
  2. 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 Link Image]
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
  1. RAO
  2. 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
  • 1-32
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 1906806 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O75106 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name AOC2_HUMAN Link Image
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 Link Image
Enzyme 7 GeneCard ID AOC2 Link Image
Enzyme 7 GenAtlas ID AOC2 Link Image
Enzyme 7 HGNC ID HGNC:549 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 7086
Enzyme 8 Name D(2) dopamine receptor
Enzyme 8 Synonyms
  1. 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
  • None
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 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P14416 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name DRD2_HUMAN Link Image
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 Link Image
Enzyme 8 GeneCard ID DRD2 Link Image
Enzyme 8 GenAtlas ID DRD2 Link Image
Enzyme 8 HGNC ID HGNC:3023 Link Image
Enzyme 8 Chromosome Location 11
Enzyme 8 Locus 11q23
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
  10. 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 Link Image]
  11. 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 Link Image]
  12. 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 Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 8029
Enzyme 9 Name D(4) dopamine receptor
Enzyme 9 Synonyms
  1. Dopamine D4 receptor
  2. 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
  • None
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 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P21917 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name DRD4_HUMAN Link Image
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 Link Image
Enzyme 9 GeneCard ID DRD4 Link Image
Enzyme 9 GenAtlas ID DRD4 Link Image
Enzyme 9 HGNC ID HGNC:3025 Link Image
Enzyme 9 Chromosome Location 11
Enzyme 9 Locus 11p15.5
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. Livingstone CD, Strange PG, Naylor LH: Molecular modelling of D2-like dopamine receptors. Biochem J. 1992 Oct 1;287 ( Pt 1):277-82. [PubMed Link Image]
  4. 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 Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 8046
Enzyme 10 Name Sodium-dependent dopamine transporter
Enzyme 10 Synonyms
  1. DA transporter
  2. 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
  • None
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 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q01959 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name SC6A3_HUMAN Link Image
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 Link Image
Enzyme 10 GeneCard ID SLC6A3 Link Image
Enzyme 10 GenAtlas ID SLC6A3 Link Image
Enzyme 10 HGNC ID HGNC:11049 Link Image
Enzyme 10 Chromosome Location 5
Enzyme 10 Locus 5p15.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
  10. 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 Link Image]
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
  • None
Enzyme 11 Transmembrane Regions
  • 88-108
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 6980076 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q9NYX4 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name D1IP_HUMAN Link Image
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 Link Image
Enzyme 11 GeneCard ID Q9NYX4 Link Image
Enzyme 11 GenAtlas ID CALY Link Image
Enzyme 11 HGNC ID HGNC:17938 Link Image
Enzyme 11 Chromosome Location 10
Enzyme 11 Locus 10q26.3
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. 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 Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 13261
Enzyme 12 Name Calcium-dependent secretion activator 1
Enzyme 12 Synonyms
  1. Calcium-dependent activator protein for secretion 1
  2. 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
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 21541504 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9ULU8 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name CAPS1_HUMAN Link Image
Enzyme 12 PDB ID 1WI1 Link Image
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 Link Image
Enzyme 12 GeneCard ID Q9ULU8 Link Image
Enzyme 12 GenAtlas ID CADPS Link Image
Enzyme 12 HGNC ID HGNC:1426 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 13262
Enzyme 13 Name Calcium-dependent secretion activator 2
Enzyme 13 Synonyms
  1. Calcium-dependent activator protein for secretion 2
  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
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 30349347 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q86UW7 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name CAPS2_HUMAN Link Image
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 Link Image
Enzyme 13 GeneCard ID Q86UW7 Link Image
Enzyme 13 GenAtlas ID CADPS2 Link Image
Enzyme 13 HGNC ID HGNC:16018 Link Image
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. 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 Link Image]
  2. 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 Link Image]
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
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID B2R6R3 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name B2R6R3_HUMAN Link Image
Enzyme 14 PDB ID 2BK3 Link Image
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 Link Image
Enzyme 14 GeneCard ID B2R6R3 Link Image
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 Link Image
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
  • None
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 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name DRD3_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID U32499 Link Image
Enzyme 15 GeneCard ID P35462 Link Image
Enzyme 15 GenAtlas ID DRD3 Link Image
Enzyme 15 HGNC ID HGNC:3024 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
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
  • None
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 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name DRD1_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence Not Available
Enzyme 16 GenBank Gene ID X55760 Link Image
Enzyme 16 GeneCard ID P21728 Link Image
Enzyme 16 GenAtlas ID DRD1 Link Image
Enzyme 16 HGNC ID HGNC:3020 Link Image
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 17108
Enzyme 17 Name D(1B) dopamine receptor
Enzyme 17 Synonyms
  1. D1beta dopamine receptor
  2. 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
  • None
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 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name DRD5_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence Not Available
Enzyme 17 GenBank Gene ID X58454 Link Image
Enzyme 17 GeneCard ID P21918 Link Image
Enzyme 17 GenAtlas ID DRD5 Link Image
Enzyme 17 HGNC ID HGNC:3026 Link Image
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus Not Available
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
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
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein Not Available
Enzyme 18 UniProtKB/Swiss-Prot ID Q99586 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name Q99586_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence Not Available
Enzyme 18 GenBank Gene ID S82917 Link Image
Enzyme 18 GeneCard ID Q99586 Link Image
Enzyme 18 GenAtlas ID dopamine D4 receptor Link Image
Enzyme 18 HGNC ID HGNC:3025 Link Image
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. 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 Link Image]
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
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein Not Available
Enzyme 19 UniProtKB/Swiss-Prot ID Q99587 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name Q99587_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID S82918 Link Image
Enzyme 19 GeneCard ID Q99587 Link Image
Enzyme 19 GenAtlas ID dopamine D4 receptor Link Image
Enzyme 19 HGNC ID HGNC:3025 Link Image
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. 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 Link Image]
Enzyme 19 Metabolite References Not Available