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Human Metabolome Database Version 2.5

 

Showing metabocard for Cyclic AMP (HMDB00058)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-07 11:41:00
Accession Number HMDB00058
Secondary Accession Numbers Not Available
Common Name Cyclic AMP
Description Cyclic AMP is an adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH. cAMP is synthesized from ATP by adenylate cyclase. Adenylate cyclase is located at the cell membranes. Adenylate cyclase is activated by the hormones glucagon and adrenaline and by G protein. Liver adenylate cyclase responds more strongly to glucagon, and muscle adenylate cyclase responds more strongly to adrenaline. cAMP decomposition into AMP is catalyzed by the enzyme phosphodiesterase.
Synonyms
  1. Cyclic AMP
  2. 3'5'-cyclic AMP
  3. 6-(6-Amino-9H-purin-9-yl)tetrahydro-4H-furo[3,2-d][1,3,2]dioxaphosphinine-2,7-diol 2-oxide
  4. Acrasin
  5. Adenosine 3',5'-cyclic monophosphate
  6. Adenosine 3',5'-cyclic phosphate
  7. Adenosine 3',5'-cyclophosphate
  8. Adenosine 3',5'-monophosphate
  9. Adenosine 3,5'-cyclic monophosphorate
  10. Adenosine 3,5'-cyclic monophosphoric acid
  11. Adenosine cyclic monophosphate
  12. Cyclic 3',5'-AMP
  13. Cyclic 3',5'-adenylate
  14. Cyclic 3',5'-adenylic acid
  15. Cyclic adenosine 3',5'-phosphate
  16. adenosine cyclic-monophosphate
  17. adenosine-cyclic-phosphate
  18. adenosine-cyclic-phosphoric-acid
  19. cAMP
Chemical IUPAC Name cyclic 3',5'-(hydrogen phosphate)Adenosine
Chemical Formula C10H12N5O6P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide monophosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Second messenger
  • Component of Purine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 329.206
Monoisotopic Molecular Weight 329.052521
Isomeric SMILES NC1=NC=NC2=C1N=CN2[C@@H]1O[C@@H]2COP(O)(=O)O[C@H]2[C@H]1O
Canonical SMILES NC1=NC=NC2=C1N=CN2C1OC2COP(O)(=O)OC2C1O
KEGG Compound ID C00575 Link Image
BioCyc ID CAMP Link Image
BiGG ID 1484809 Link Image
Wikipedia Link Cyclic AMP Link Image
NuGOwiki Link HMDB00058 Link Image
Metagene Link HMDB00058 Link Image
METLIN ID 5120 Link Image
PubChem Compound 6076 Link Image
PubChem Substance 820438 Link Image
ChEBI ID 17489 Link Image
CAS Registry Number 60-92-4
InChI Identifier InChI=1/C10H12N5O6P/c11-8-5-9(13-2-12-8)15(3-14-5)10-6(16)7-4(20-10)1-19-22(17,18)21-7/h2-4,6-7,10,16H,1H2,(H,17,18)(H2,11,12,13)/t4-,6-,7-,10-/m1/s1
Synthesis Reference Genieser, H. G.; Butt, E.; Bottin, U.; Dostmann, W.; Jastorff, B. Synthesis of the 3',5'-cyclic phosphates from unprotected nucleosides. Synthesis (1989), (1), 53-4.
Melting Point (Experimental) 219-220 oC
Experimental Water Solubility 4 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 136.0 mg/mL [MEYLAN,WM et al. (1996)]; 3.58 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity -2.96 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -2.29 [Predicted by ALOGPS]; -2.5 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
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 Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Extracellular
  • golgi apparatus
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
All Tissues
Concentrations (Normal)
Biofluid Blood
Value 0.0085 +/- 0.0005 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Kruuse C, Frandsen E, Schifter S, Thomsen LL, Birk S, Olesen J: Plasma levels of cAMP, cGMP and CGRP in sildenafil-induced headache. Cephalalgia. 2004 Jul;24(7):547-53. [PubMed Link Image]
Biofluid CSF
Value 0.020 +/- 0.004 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid CSF
Value 0.024 (0.022-0.026) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Liu H, Chang L, Chen Y, Xia S, Zhang X: Clinical implication of the changes of cAMP, TXA2 and PGI2 in CSF of asphyxiated newborns. J Huazhong Univ Sci Technolog Med Sci. 2003;23(2):195-7, 200. [PubMed Link Image]
Biofluid CSF
Value 0.021 +/- 0.008 uM
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 C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 0.020 (0.016-0.024) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid CSF
Value 0.020+/- 0.004 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid CSF
Value 0.0202 +/- 0.004 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Initial slight suspicion of meningitis with normal CSF
Comments Not Available
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid Urine
Value 0.22 +/- 0.055 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Raij K, Harkonen M: Determination of cyclic adenosine 3',5'-monophosphate in urine. Scand J Clin Lab Invest. 1976 Mar;36(2):161-8. [PubMed Link Image]
Biofluid Urine
Value 0.38 +/- 0.14 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Daniels CK, Zhang L, Musser B, Vestal RE: A solid-phase radioimmunoassay for cyclic AMP. J Pharmacol Toxicol Methods. 1994 Feb;31(1):41-6. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.0077 +/- 0.0003 uM
Age Adult:>18 yrs old
Sex Male
Condition Headache
Comments Not Available
References
  • Kruuse C, Frandsen E, Schifter S, Thomsen LL, Birk S, Olesen J: Plasma levels of cAMP, cGMP and CGRP in sildenafil-induced headache. Cephalalgia. 2004 Jul;24(7):547-53. [PubMed Link Image]
Biofluid CSF
Value 0.0110 +/- 0.0028 uM
Age Adult:>18 yrs old
Sex Both
Condition Idiopathic polyneuritis
Comments Not Available
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid CSF
Value 0.00860 (0.00620-0.0110) uM
Age Adult:>18 yrs old
Sex Both
Condition Hypoxic-ischemic encephalopathy
Comments Moderate to severe Hypoxic-ischemic encephalopathy
References
  • Liu H, Chang L, Chen Y, Xia S, Zhang X: Clinical implication of the changes of cAMP, TXA2 and PGI2 in CSF of asphyxiated newborns. J Huazhong Univ Sci Technolog Med Sci. 2003;23(2):195-7, 200. [PubMed Link Image]
Biofluid CSF
Value 0.014 (0.012-0.017) uM
Age Adult:>18 yrs old
Sex Both
Condition Hypoxic-ischemic encephalopathy
Comments Mild Hypoxic-ischemic encephalopathy
References
  • Liu H, Chang L, Chen Y, Xia S, Zhang X: Clinical implication of the changes of cAMP, TXA2 and PGI2 in CSF of asphyxiated newborns. J Huazhong Univ Sci Technolog Med Sci. 2003;23(2):195-7, 200. [PubMed Link Image]
Biofluid CSF
Value 0.034 (0.021-0.046) uM
Age Adult:>18 yrs old
Sex Both
Condition Meningitis
Comments serious meningitis
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid CSF
Value 0.011 (0.0082-0.014) uM
Age Adult:>18 yrs old
Sex Both
Condition Idiopathic polyneuritis
Comments Not Available
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid CSF
Value 0.033 +/- 0.012 uM
Age Adult:>18 yrs old
Sex N/A
Condition Meningitis
Comments Serious case.
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid Urine
Value 0.24 +/- 0.028 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Chronic renal failure
Comments Not Available
References
  • Dimitrakov D, Kumchev E, Lyutakova E, Ledzhev I, Nikolov D, Tsekov V: Cyclic adenosine monophosphate (cAMP) levels in predialysis patients with chronic renal failure. Folia Med (Plovdiv). 1997;39(1):29-33. [PubMed Link Image]
Associated Disorders
Condition References
Chronic renal failure
  • Dimitrakov D, Kumchev E, Lyutakova E, Ledzhev I, Nikolov D, Tsekov V: Cyclic adenosine monophosphate (cAMP) levels in predialysis patients with chronic renal failure. Folia Med (Plovdiv). 1997;39(1):29-33. [PubMed Link Image]
Headache
  • Kruuse C, Frandsen E, Schifter S, Thomsen LL, Birk S, Olesen J: Plasma levels of cAMP, cGMP and CGRP in sildenafil-induced headache. Cephalalgia. 2004 Jul;24(7):547-53. [PubMed Link Image]
Hypoxic-ischemic encephalopathy
  • Liu H, Chang L, Chen Y, Xia S, Zhang X: Clinical implication of the changes of cAMP, TXA2 and PGI2 in CSF of asphyxiated newborns. J Huazhong Univ Sci Technolog Med Sci. 2003;23(2):195-7, 200. [PubMed Link Image]
Idiopathic polyneuritis
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Meningitis
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References
  1. Imashuku S, Todo S, Nakajima F: [Intra-aortic prostaglandin E1 infusion in the treatment of advanced neuroblastoma] Gan To Kagaku Ryoho. 1983 Sep;10(9):1936-43. [PubMed Link Image]
  2. Wine JJ, Joo NS: Submucosal glands and airway defense. Proc Am Thorac Soc. 2004;1(1):47-53. [PubMed Link Image]
  3. Onali P, Strada SJ, Chang L, Epstein PM, Hersh EM, Thompson WJ: Purification and characterization of high-affinity cyclic adenosine 5'-monophosphate phosphodiesterases from human acute myelogenous leukemic cells. Cancer Res. 1985 Mar;45(3):1384-91. [PubMed Link Image]
  4. Rademaker MT, Charles CJ, Lewis LK, Yandle TG, Cooper GJ, Coy DH, Richards AM, Nicholls MG: Beneficial hemodynamic and renal effects of adrenomedullin in an ovine model of heart failure. Circulation. 1997 Sep 16;96(6):1983-90. [PubMed Link Image]
  5. Mashayekhi F, Aghahoseini F, Rezaie A, Zamani MJ, Khorasani R, Abdollahi M: Alteration of cyclic nucleotides levels and oxidative stress in saliva of human subjects with periodontitis. J Contemp Dent Pract. 2005 Nov 15;6(4):46-53. [PubMed Link Image]
  6. Sugo T, Tachimoto H, Chikatsu T, Murakami Y, Kikukawa Y, Sato S, Kikuchi K, Nagi T, Harada M, Ogi K, Ebisawa M, Mori M: Identification of a lysophosphatidylserine receptor on mast cells. Biochem Biophys Res Commun. 2006 Mar 24;341(4):1078-87. Epub 2006 Jan 25. [PubMed Link Image]
  7. Watanabe K, Beinborn M, Nagamatsu S, Ishida H, Takahashi S: Menetrier's disease in a patient with Helicobacter pylori infection is linked to elevated glucagon-like peptide-2 activity. Scand J Gastroenterol. 2005 Apr;40(4):477-81. [PubMed Link Image]
  8. Naef A, Keller HU: A short transient increase in cyclic adenosine 3', 5'-monophosphate levels of neutrophil granulocytes following exposure to chemotactic factors. Adv Exp Med Biol. 1982;141:39-48. [PubMed Link Image]
  9. Kukreja SC, Shevrin DH, Wimbiscus SA, Ebeling PR, Danks JA, Rodda CP, Wood WI, Martin TJ: Antibodies to parathyroid hormone-related protein lower serum calcium in athymic mouse models of malignancy-associated hypercalcemia due to human tumors. J Clin Invest. 1988 Nov;82(5):1798-802. [PubMed Link Image]
  10. Wickenheisser JK, Nelson-DeGrave VL, McAllister JM: Human ovarian theca cells in culture. Trends Endocrinol Metab. 2006 Mar;17(2):65-71. Epub 2006 Feb 7. [PubMed Link Image]
  11. Fouassier L, Chinet T, Robert B, Carayon A, Balladur P, Mergey M, Paul A, Poupon R, Capeau J, Barbu V, Housset C: Endothelin-1 is synthesized and inhibits cyclic adenosine monophosphate- dependent anion secretion by an autocrine/paracrine mechanism in gallbladder epithelial cells. J Clin Invest. 1998 Jun 15;101(12):2881-8. [PubMed Link Image]
  12. Carceles MD, Ribo AR, Davalos R, Martinez T, Hernandez J: Effect of diazepam on adenosine 3',5'-cyclic monophosphate (cAMP) plasma levels in anesthetized patients. Clin Ther. 2004 May;26(5):737-43. [PubMed Link Image]
  13. Chu MS, Chang CF, Yang CC, Bau YC, Ho LL, Hung SC: Signalling pathway in the induction of neurite outgrowth in human mesenchymal stem cells. Cell Signal. 2006 Apr;18(4):519-30. Epub 2005 Aug 11. [PubMed Link Image]
  14. Rudman D, O'Brien MS, McKinney AS, Hoffman JC Jr, Patterson JH: Observations on the cyclic nucleotide concentrations in human cerebrospinal fluid. J Clin Endocrinol Metab. 1976 Jun;42(6):1088-97. [PubMed Link Image]
  15. Machen TE: Innate immune response in CF airway epithelia: hyperinflammatory? Am J Physiol Cell Physiol. 2006 Aug;291(2):C218-30. [PubMed Link Image]
  16. Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
  17. Ruppert D, Weithmann KU: HL 725, an extremely potent inhibitor of platelet phosphodiesterase and induced platelet aggregation in vitro. Life Sci. 1982 Nov 8;31(19):2037-43. [PubMed Link Image]
  18. Tanaka Y, Horinouchi T, Koike K: New insights into beta-adrenoceptors in smooth muscle: distribution of receptor subtypes and molecular mechanisms triggering muscle relaxation. Clin Exp Pharmacol Physiol. 2005 Jul;32(7):503-14. [PubMed Link Image]
  19. Fischer JA, Bourne HR, Dambacher MA, Tschopp F, De Meyer R, Devogelaer JP, Werder EA, Nagant De Deuxchaisnes C: Pseudohypoparathyroidism: inheritance and expression of deficient receptor-cyclase coupling protein activity. Clin Endocrinol (Oxf). 1983 Dec;19(6):747-54. [PubMed Link Image]
  20. Liu H, Chang L, Chen Y, Xia S, Zhang X: Clinical implication of the changes of cAMP, TXA2 and PGI2 in CSF of asphyxiated newborns. J Huazhong Univ Sci Technolog Med Sci. 2003;23(2):195-7, 200. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Histone acetyltransferase p300
  2. CREB-binding protein
  3. Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
  4. Hormone-sensitive lipase
  5. Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
  6. Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
  7. High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
  8. Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
  9. cGMP-inhibited 3',5'-cyclic phosphodiesterase B
  10. High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A
  11. cGMP-inhibited 3',5'-cyclic phosphodiesterase A
  12. cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
  13. Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
  14. cAMP-specific 3',5'-cyclic phosphodiesterase 4B
  15. cAMP-specific 3',5'-cyclic phosphodiesterase 7B
  16. High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
  17. cGMP-dependent 3',5'-cyclic phosphodiesterase
  18. High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B
  19. cAMP-specific 3',5'-cyclic phosphodiesterase 4C
  20. cAMP-specific 3',5'-cyclic phosphodiesterase 4D
  21. Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
  22. Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
  23. cAMP-specific 3',5'-cyclic phosphodiesterase 4A
  24. cGMP-specific 3',5'-cyclic phosphodiesterase
  25. Adenylate cyclase type 7
  26. Adenylate cyclase type 4
  27. Adenylate cyclase type 6
  28. Adenylate cyclase type 5
  29. Adenylate cyclase type 8
  30. Adenylate cyclase type 9
  31. Adenylate cyclase type 3
  32. Adenylate cyclase type 1
  33. Adenylate cyclase type 2
  34. Steroid 17-alpha-hydroxylase/17,20 lyase
  35. Cyclic nucleotide-gated cation channel alpha-3
  36. Cyclic nucleotide-gated cation channel beta-3
  37. Rap guanine nucleotide exchange factor 2
  38. Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
  39. cAMP-dependent protein kinase catalytic subunit gamma
  40. cAMP-dependent protein kinase catalytic subunit alpha
  41. Serine/threonine-protein kinase PRKY
  42. cAMP-dependent protein kinase catalytic subunit beta
  43. Ribosomal protein S6 kinase alpha-5
  44. Serine/threonine-protein kinase PRKX
  45. Serine/threonine-protein kinase 11
  46. ATP-binding cassette sub-family A member 1
  47. Na(+)/H(+) exchange regulatory cofactor NHE-RF1
  48. Aryl hydrocarbon receptor
  49. Cyclic AMP-responsive element-binding protein 5
  50. Class E basic helix-loop-helix protein 40
  51. Splicing factor, proline- and glutamine-rich
  52. Ras-related protein Rap-1A
  53. Calcitonin gene-related peptide 1
  54. Cyclic AMP-responsive element-binding protein 1
  55. Thyrotropin receptor
  56. Glial cell line-derived neurotrophic factor
  57. Potassium voltage-gated channel subfamily H member 2
  58. Potassium voltage-gated channel subfamily H member 6
  59. Methyl-CpG-binding domain protein 2
  60. Relaxin receptor 1
  61. cAMP-responsive element modulator
  62. Adiponectin
  63. cAMP-dependent protein kinase type I-alpha regulatory subunit
  64. Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
  65. Cortistatin
  66. Perilipin-1
  67. Prostaglandin D2 receptor
  68. Rap guanine nucleotide exchange factor 3
  69. Platelet basic protein
  70. Vasodilator-stimulated phosphoprotein
  71. Inositol 1,4,5-trisphosphate receptor type 1
  72. Rap guanine nucleotide exchange factor 4
  73. Steroidogenic factor 1
  74. Sodium bicarbonate cotransporter 3
  75. Adenylate cyclase type 10
  76. Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A
  77. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
  78. Lysophosphatidic acid receptor 6
  79. Adenylate cyclase 1
  80. A-kinase anchor protein 7 isoforms alpha and beta
  81. A-kinase anchor protein 13
  82. Cyclic nucleotide-gated cation channel alpha-4
  83. CREB-regulated transcription coactivator 1
  84. CREB-regulated transcription coactivator 2
  85. Guanine nucleotide-binding protein G(t) subunit alpha-3
  86. Protein phosphatase 1 regulatory subunit 1A
  87. Transient receptor potential cation channel subfamily V member 2
  88. ATP-binding cassette sub-family C member 11
  89. ADM2
  90. A-kinase anchor protein 7 isoform gamma
  91. A-kinase anchor protein 2
  92. A-kinase anchor protein 5
  93. A-kinase anchor protein 8
  94. Agouti-signaling protein
  95. Cyclic AMP-dependent transcription factor ATF-1
  96. Cyclic AMP-dependent transcription factor ATF-2
  97. Cyclic AMP-dependent transcription factor ATF-3
  98. Cyclic AMP-dependent transcription factor ATF-4
  99. Cyclic AMP-dependent transcription factor ATF-5
  100. Cyclic AMP-dependent transcription factor ATF-7
  101. Basic leucine zipper transcriptional factor ATF-like
  102. Cyclic nucleotide-gated olfactory channel
  103. Cyclic AMP-responsive element-binding protein 3-like protein 1
  104. Cyclic AMP-responsive element-binding protein 3-like protein 2
  105. Cyclic AMP-responsive element-binding protein 3-like protein 3
  106. Cyclic AMP-responsive element-binding protein 3
  107. Luc7-like protein 3
  108. CREB-regulated transcription coactivator 3
  109. Dematin
  110. Erythrocyte membrane protein band 4.2
  111. FERM, RhoGEF and pleckstrin domain-containing protein 1
  112. G-protein coupled bile acid receptor 1
  113. Glycoprotein hormone alpha-2
  114. Glycoprotein hormone beta-5
  115. Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
  116. Histamine H4 receptor
  117. cAMP-dependent protein kinase inhibitor alpha
  118. cAMP-dependent protein kinase inhibitor beta
  119. cAMP-dependent protein kinase inhibitor gamma
  120. Jun dimerization protein 2
  121. cAMP-dependent protein kinase type I-beta regulatory subunit
  122. cAMP-dependent protein kinase type II-alpha regulatory subunit
  123. cAMP-dependent protein kinase type II-beta regulatory subunit
  124. Potassium voltage-gated channel subfamily A member 10
  125. Potassium voltage-gated channel subfamily E member 3
  126. Potassium voltage-gated channel subfamily H member 1
  127. Potassium voltage-gated channel subfamily H member 3
  128. Potassium voltage-gated channel subfamily H member 4
  129. Potassium voltage-gated channel subfamily H member 5
  130. Potassium voltage-gated channel subfamily H member 7
  131. Potassium voltage-gated channel subfamily H member 8
  132. Leucine zipper putative tumor suppressor 1
  133. Homeobox protein Meis1
  134. Mas-related G-protein coupled receptor member D
  135. Mas-related G-protein coupled receptor member X2
  136. Myomegalin
  137. Na(+)/H(+) exchange regulatory cofactor NHE-RF2
  138. Non-POU domain-containing octamer-binding protein
  139. Pre-B-cell leukemia transcription factor 1
  140. Prostaglandin E2 receptor EP2 subtype
  141. Phosducin
  142. Paired mesoderm homeobox protein 2B
  143. Phospholemman
  144. Protein prune homolog
  145. Tyrosine-protein phosphatase non-receptor type 7
  146. Ras-related protein Rap-1b
  147. Ras-related protein Rap-2a
  148. FMRFamide-related peptides
  149. Rhophilin-2
  150. Synembryn-B
  151. Relaxin-3 receptor 1
  152. Relaxin-3 receptor 2
  153. Ras-related protein Rap-1b-like protein
  154. Rap guanine nucleotide exchange factor 6
  155. 40S ribosomal protein S27
  156. Relaxin receptor 2
  157. Solute carrier organic anion transporter family member 4C1
  158. A-kinase anchor protein SPHKAP
  159. Ras GTPase-activating protein SynGAP
  160. Transmembrane protein 132A
  161. Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3
  162. 3',5'-cyclic nucleotide phosphodiesterase 10A2
  163. Adenylate cyclase 9 (Adenylate cyclase 9, isoform CRA_a)
  164. Phosphodiesterase 7B (Phosphodiesterase 7B, isoform CRA_b)
  165. cDNA FLJ38065 fis, clone CTONG2015316, highly similar to cAMP-specific 3',5'-cyclic phosphodiesterase 4C (EC 3.1.4.17)
  166. cDNA FLJ16206 fis, clone CTONG2019590, highly similar to Adenylate cyclase type 4 (EC 4.6.1.1)
  167. Cyclic nucleotide-gated cation channel beta-1
Enzyme 1 [top]
Enzyme 1 ID 5240
Enzyme 1 Name Histone acetyltransferase p300
Enzyme 1 Synonyms
  1. p300 HAT
  2. E1A-associated protein p300
Enzyme 1 Gene Name EP300
Enzyme 1 Protein Sequence >Histone acetyltransferase p300
MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGD
INQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINS
MVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGMNAGMNPGMLAA
GNGQGIMPNQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQ
PLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMP
NMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGE
VRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNA
GDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQM
PTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQ
NPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAAL
KDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPN
AAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPNQMMPRITPQSGLNQFGQMSM
AQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNI
PLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTP
TPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPS
LPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQVSNPPSTSST
EVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELK
TEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVD
PQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYK
YCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHF
CEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVL
HHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGE
VTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQE
YGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPP
SEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKE
LPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNK
SSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIP
CDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETR
WHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQ
SLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENK
CPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTG
QQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPG
PPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHL
EPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISP
LKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPI
PGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGG
MSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYP
PQQQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSP
QQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHV
SPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNS
DLNSNLSQSTLDIH
Enzyme 1 Number of Residues 2414
Enzyme 1 Molecular Weight 264159.7
Enzyme 1 Theoretical pI 8.59
Enzyme 1 GO Classification
Function
  • N-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • binding
  • catalytic activity
  • cation binding
  • histone acetyltransferase activity
  • ion binding
  • lysine N-acetyltransferase activity
  • metal ion binding
  • protein binding
  • transcription coactivator activity
  • transcription cofactor activity
  • transcription factor binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • cellular component organization at cellular level
  • cellular process
  • chromatin modification
  • chromatin organization
  • chromosome organization
  • covalent chromatin modification
  • histone acetylation
  • histone modification
  • organelle organization
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • histone acetyltransferase complex
  • intracellular membrane-bounded organelle
  • macromolecular complex
  • membrane-bounded organelle
  • nucleus
  • organelle
  • protein complex
Enzyme 1 General Function Involved in transcription cofactor activity
Enzyme 1 Specific Function Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • acetyl-CoA + histone = CoA + acetylhistone
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 56202870 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q09472 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name EP300_HUMAN Link Image
Enzyme 1 PDB ID 1JSP Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >7245 bp
ATGGCCGAGAATGTGGTGGAACCGGGGCCGCCTTCAGCCAAGCGGCCTAAACTCTCATCT
CCGGCCCTCTCGGCGTCCGCCAGCGATGGCACAGATTTTGGCTCTCTATTTGACTTGGAG
CACGACTTACCAGATGAATTAATCAACTCTACAGAATTGGGACTAACCAATGGTGGTGAT
ATTAATCAGCTTCAGACAAGTCTTGGCATGGTACAAGATGCAGCTTCTAAACATAAACAG
CTGTCAGAATTGCTGCGATCTGGTAGTTCCCCTAACCTCAATATGGGAGTTGGTGGCCCA
GGTCAAGTCATGGCCAGCCAGGCCCAACAGAGCAGTCCTGGATTAGGTTTGATAAATAGC
ATGGTCAAAAGCCCAATGACACAGGCAGGCTTGACTTCTCCCAACATGGGGATGGGCACT
AGTGGACCAAATCAGGGTCCTACGCAGTCAACAGGTATGATGAACAGTCCAGTAAATCAG
CCTGCCATGGGAATGAACACAGGGATGAATGCGGGCATGAATCCTGGAATGTTGGCTGCA
GGCAATGGACAAGGGATAATGCCTAATCAAGTCATGAACGGTTCAATTGGAGCAGGCCGA
GGGCGACAGAATATGCAGTACCCAAACCCAGGCATGGGAAGTGCTGGCAACTTACTGACT
GAGCCTCTTCAGCAGGGCTCTCCCCAGATGGGAGGACAAACAGGATTGAGAGGCCCCCAG
CCTCTTAAGATGGGAATGATGAACAACCCCAATCCTTATGGTTCACCATATACTCAGAAT
CCTGGACAGCAGATTGGAGCCAGTGGCCTTGGTCTCCAGATTCAGACAAAAACTGTACTA
TCAAATAACTTATCTCCATTTGCTATGGACAAAAAGGCAGTTCCTGGTGGAGGAATGCCC
AACATGGGTCAACAGCCAGCCCCGCAGGTCCAGCAGCCAGGCCTGGTGACTCCAGTTGCC
CAAGGGATGGGTTCTGGAGCACATACAGCTGATCCAGAGAAGCGCAAGCTCATCCAGCAG
CAGCTTGTTCTCCTTTTGCATGCTCACAAGTGCCAGCGCCGGGAACAGGCCAATGGGGAA
GTGAGGCAGTGCAACCTTCCCCACTGTCGCACAATGAAGAATGTCCTAAACCACATGACA
CACTGCCAGTCAGGCAAGTCTTGCCAAGTGGCACACTGTGCATCTTCTCGACAAATCATT
TCACACTGGAAGAATTGTACAAGACATGATTGTCCTGTGTGTCTCCCCCTCAAAAATGCT
GGTGATAAGAGAAATCAACAGCCAATTTTGACTGGAGCACCCGTTGGACTTGGAAATCCT
AGCTCTCTAGGGGTGGGTCAACAGTCTGCCCCCAACCTAAGCACTGTTAGTCAGATTGAT
CCCAGCTCCATAGAAAGAGCCTATGCAGCTCTTGGACTACCCTATCAAGTAAATCAGATG
CCGACACAACCCCAGGTGCAAGCAAAGAACCAGCAGAATCAGCAGCCTGGGCAGTCTCCC
CAAGGCATGCGGCCCATGAGCAACATGAGTGCTAGTCCTATGGGAGTAAATGGAGGTGTA
GGAGTTCAAACGCCGAGTCTTCTTTCTGACTCAATGTTGCATTCAGCCATAAATTCTCAA
AACCCAATGATGAGTGAAAATGCCAGTGTGCCCTCCCTGGGTCCTATGCCAACAGCAGCT
CAACCATCCACTACTGGAATTCGGAAACAGTGGCACGAAGATATTACTCAGGATCTTCGA
AATCATCTTGTTCACAAACTCGTCCAAGCCATATTTCCTACGCCGGATCCTGCTGCTTTA
AAAGACAGACGGATGGAAAACCTAGTTGCATATGCTCGGAAAGTTGAAGGGGACATGTAT
GAATCTGCAAACAATCGAGCGGAATACTACCACCTTCTAGCTGAGAAAATCTATAAGATC
CAGAAAGAACTAGAAGAAAAACGAAGGACCAGACTACAGAAGCAGAACATGCTACCAAAT
GCTGCAGGCATGGTTCCAGTTTCCATGAATCCAGGGCCTAACATGGGACAGCCGCAACCA
GGAATGACTTCTAATGGCCCTCTACCTGACCCAAGTATGATCCGTGGCAGTGTGCCAAAC
CAGATGATGCCTCGAATAACTCCACAATCTGGTTTGAATCAATTTGGCCAGATGAGCATG
GCCCAGCCCCCTATTGTACCCCGGCAAACCCCTCCTCTTCAGCACCATGGACAGTTGGCT
CAACCTGGAGCTCTCAACCCGCCTATGGGCTATGGGCCTCGTATGCAACAGCCTTCCAAC
CAGGGCCAGTTCCTTCCTCAGACTCAGTTCCCATCACAGGGAATGAATGTAACAAATATC
CCTTTGGCTCCGTCCAGCGGTCAAGCTCCAGTGTCTCAAGCACAAATGTCTAGTTCTTCC
TGCCCGGTGAACTCTCCTATAATGCCTCCAGGGTCTCAGGGGAGCCACATTCACTGTCCC
CAGCTTCCTCAACCAGCTCTTCATCAGAATTCACCCTCGCCTGTACCTAGTCGTACCCCC
ACCCCTCACCATACTCCCCCAAGCATAGGGGCTCAGCAGCCACCAGCAACAACAATTCCA
GCCCCTGTTCCTACACCTCCTGCCATGCCACCTGGGCCACAGTCCCAGGCTCTACATCCC
CCTCCAAGGCAGACACCTACACCACCAACAACACAACTTCCCCAACAAGTGCAGCCTTCA
CTTCCTGCTGCACCTTCTGCTGACCAGCCCCAGCAGCAGCCTCGCTCACAGCAGAGCACA
GCAGCGTCTGTTCCTACCCCAACAGCACCGCTGCTTCCTCCGCAGCCTGCAACTCCACTT
TCCCAGCCAGCTGTAAGCATTGAAGGACAGGTATCAAATCCTCCATCTACTAGTAGCACA
GAAGTGAATTCTCAGGCCATTGCTGAGAAGCAGCCTTCCCAGGAAGTGAAGATGGAGGCC
AAAATGGAAGTGGATCAACCAGAACCAGCAGATACTCAGCCGGAGGATATTTCAGAGTCT
AAAGTGGAAGACTGTAAAATGGAATCTACCGAAACAGAAGAGAGAAGCACTGAGTTAAAA
ACTGAAATAAAAGAGGAGGAAGACCAGCCAAGTACTTCAGCTACCCAGTCATCTCCGGCT
CCAGGACAGTCAAAGAAAAAGATTTTCAAACCAGAAGAACTACGACAGGCACTGATGCCA
ACTTTGGAGGCACTTTACCGTCAGGATCCAGAATCCCTTCCCTTTCGTCAACCTGTGGAC
CCTCAGCTTTTAGGAATCCCTGATTACTTTGATATTGTGAAGAGCCCCATGGATCTTTCT
ACCATTAAGAGGAAGTTAGACACTGGACAGTATCAGGAGCCCTGGCAGTATGTCGATGAT
ATTTGGCTTATGTTCAATAATGCCTGGTTATATAACCGGAAAACATCACGGGTATACAAA
TACTGCTCCAAGCTCTCTGAGGTCTTTGAACAAGAAATTGACCCAGTGATGCAAAGCCTT
GGATACTGTTGTGGCAGAAAGTTGGAGTTCTCTCCACAGACACTGTGTTGCTACGGCAAA
CAGTTGTGCACAATACCTCGTGATGCCACTTATTACAGTTACCAGAACAGGTATCATTTC
TGTGAGAAGTGTTTCAATGAGATCCAAGGGGAGAGCGTTTCTTTGGGGGATGACCCTTCC
CAGCCTCAAACTACAATAAATAAAGAACAATTTTCCAAGAGAAAAAATGACACACTGGAT
CCTGAACTGTTTGTTGAATGTACAGAGTGCGGAAGAAAGATGCATCAGATCTGTGTCCTT
CACCATGAGATCATCTGGCCTGCTGGATTCGTCTGTGATGGCTGTTTAAAGAAAAGTGCA
CGAACTAGGAAAGAAAATAAGTTTTCTGCTAAAAGGTTGCCATCTACCAGACTTGGCACC
TTTCTAGAGAATCGTGTGAATGACTTTCTGAGGCGACAGAATCACCCTGAGTCAGGAGAG
GTCACTGTTAGAGTAGTTCATGCTTCTGACAAAACCGTGGAAGTAAAACCAGGCATGAAA
GCAAGGTTTGTGGACAGTGGAGAGATGGCAGAATCCTTTCCATACCGAACCAAAGCCCTC
TTTGCCTTTGAAGAAATTGATGGTGTTGACCTGTGCTTCTTTGGCATGCATGTTCAAGAG
TATGGCTCTGACTGCCCTCCACCCAACCAGAGGAGAGTATACATATCTTACCTCGATAGT
GTTCATTTCTTCCGTCCTAAATGCTTGAGGACTGCAGTCTATCATGAAATCCTAATTGGA
TATTTAGAATATGTCAAGAAATTAGGTTACACAACAGGGCATATTTGGGCATGTCCACCA
AGTGAGGGAGATGATTATATCTTCCATTGCCATCCTCCTGACCAGAAGATACCCAAGCCC
AAGCGACTGCAGGAATGGTACAAAAAAATGCTTGACAAGGCTGTATCAGAGCGTATTGTC
CATGACTACAAGGATATTTTTAAACAAGCTACTGAAGATAGATTAACAAGTGCAAAGGAA
TTGCCTTATTTCGAGGGTGATTTCTGGCCCAATGTTCTGGAAGAAAGCATTAAGGAACTG
GAACAGGAGGAAGAAGAGAGAAAACGAGAGGAAAACACCAGCAATGAAAGCACAGATGTG
ACCAAGGGAGACAGCAAAAATGCTAAAAAGAAGAATAATAAGAAAACCAGCAAAAATAAG
AGCAGCCTGAGTAGGGGCAACAAGAAGAAACCCGGGATGCCCAATGTATCTAACGACCTC
TCACAGAAACTATATGCCACCATGGAGAAGCATAAAGAGGTCTTCTTTGTGATCCGCCTC
ATTGCTGGCCCTGCTGCCAACTCCCTGCCTCCCATTGTTGATCCTGATCCTCTCATCCCC
TGCGATCTGATGGATGGTCGGGATGCGTTTCTCACGCTGGCAAGGGACAAGCACCTGGAG
TTCTCTTCACTCCGAAGAGCCCAGTGGTCCACCATGTGCATGCTGGTGGAGCTGCACACG
CAGAGCCAGGACCGCTTTGTCTACACCTGCAATGAATGCAAGCACCATGTGGAGACACGC
TGGCACTGTACTGTCTGTGAGGATTATGACTTGTGTATCACCTGCTATAACACTAAAAAC
CATGACCACAAAATGGAGAAACTAGGCCTTGGCTTAGATGATGAGAGCAACAACCAGCAG
GCTGCAGCCACCCAGAGCCCAGGCGATTCTCGCCGCCTGAGTATCCAGCGCTGCATCCAG
TCTCTGGTCCATGCTTGCCAGTGTCGGAATGCCAATTGCTCACTGCCATCCTGCCAGAAG
ATGAAGCGGGTTGTGCAGCATACCAAGGGTTGCAAACGGAAAACCAATGGCGGGTGCCCC
ATCTGCAAGCAGCTCATTGCCCTCTGCTGCTACCATGCCAAGCACTGCCAGGAGAACAAA
TGCCCGGTGCCGTTCTGCCTAAACATCAAGCAGAAGCTCCGGCAGCAACAGCTGCAGCAC
CGACTACAGCAGGCCCAAATGCTTCGCAGGAGGATGGCCAGCATGCAGCGGACTGGTGTG
GTTGGGCAGCAACAGGGCCTCCCTTCCCCCACTCCTGCCACTCCAACGACACCAACTGGC
CAACAGCCAACCACCCCGCAGACGCCCCAGCCCACTTCTCAGCCTCAGCCTACCCCTCCC
AATAGCATGCCACCCTACTTGCCCAGGACTCAAGCTGCTGGCCCTGTGTCCCAGGGTAAG
GCAGCAGGCCAGGTGACCCCTCCAACCCCTCCTCAGACTGCTCAGCCACCCCTTCCAGGG
CCCCCACCTGCAGCAGTGGAAATGGCAATGCAGATTCAGAGAGCAGCGGAGACGCAGCGC
CAGATGGCCCACGTGCAAATTTTTCAAAGGCCAATCCAACACCAGATGCCCCCGATGACT
CCCATGGCCCCCATGGGTATGAACCCACCTCCCATGACCAGAGGTCCCAGTGGGCATTTG
GAGCCAGGGATGGGACCGACAGGGATGCAGCAACAGCCACCCTGGAGCCAAGGAGGATTG
CCTCAGCCCCAGCAACTACAGTCTGGGATGCCAAGGCCAGCCATGATGTCAGTGGCCCAG
CATGGTCAACCTTTGAACATGGCTCCACAACCAGGATTGGGCCAGGTAGGTATCAGCCCA
CTCAAACCAGGCACTGTGTCTCAACAAGCCTTACAAAACCTTTTGCGGACTCTCAGGTCT
CCCAGCTCTCCCCTGCAGCAGCAACAGGTGCTTAGTATCCTTCACGCCAACCCCCAGCTG
TTGGCTGCATTCATCAAGCAGCGGGCTGCCAAGTATGCCAACTCTAATCCACAACCCATC
CCTGGGCAGCCTGGCATGCCCCAGGGGCAGCCAGGGCTACAGCCACCTACCATGCCAGGT
CAGCAGGGGGTCCACTCCAATCCAGCCATGCAGAACATGAATCCAATGCAGGCGGGCGTT
CAGAGGGCTGGCCTGCCCCAGCAGCAACCACAGCAGCAACTCCAGCCACCCATGGGAGGG
ATGAGCCCCCAGGCTCAGCAGATGAACATGAACCACAACACCATGCCTTCACAATTCCGA
GACATCTTGAGACGACAGCAAATGATGCAACAGCAGCAGCAACAGGGAGCAGGGCCAGGA
ATAGGCCCTGGAATGGCCAACCATAACCAGTTCCAGCAACCCCAAGGAGTTGGCTACCCA
CCACAGCAGCAGCAGCGGATGCAGCATCACATGCAACAGATGCAACAAGGAAATATGGGA
CAGATAGGCCAGCTTCCCCAGGCCTTGGGAGCAGAGGCAGGTGCCAGTCTACAGGCCTAT
CAGCAGCGACTCCTTCAGCAACAGATGGGGTCCCCTGTTCAGCCCAACCCCATGAGCCCC
CAGCAGCATATGCTCCCAAATCAGGCCCAGTCCCCACACCTACAAGGCCAGCAGATCCCT
AATTCTCTCTCCAATCAAGTGCGCTCTCCCCAGCCTGTCCCTTCTCCACGGCCACAGTCC
CAGCCCCCCCACTCCAGTCCTTCCCCAAGGATGCAGCCTCAGCCTTCTCCACACCACGTT
TCCCCACAGACAAGTTCCCCACATCCTGGACTGGTAGCTGCCCAGGCCAACCCCATGGAA
CAAGGGCATTTTGCCAGCCCGGACCAGAATTCAATGCTTTCTCAGCTTGCTAGCAATCCA
GGCATGGCAAACCTCCATGGTGCAAGCGCCACGGACCTGGGACTCAGCACCGATAACTCA
GACTTGAATTCAAACCTCTCACAGAGTACACTAGACATACACTAG
Enzyme 1 GenBank Gene ID AL035658 Link Image
Enzyme 1 GeneCard ID EP300 Link Image
Enzyme 1 GenAtlas ID EP300 Link Image
Enzyme 1 HGNC ID HGNC:3373 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 22q13.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Eckner R, Ewen ME, Newsome D, Gerdes M, DeCaprio JA, Lawrence JB, Livingston DM: Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev. 1994 Apr 15;8(8):869-84. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  3. Chaffanet M, Gressin L, Preudhomme C, Soenen-Cornu V, Birnbaum D, Pebusque MJ: MOZ is fused to p300 in an acute monocytic leukemia with t(8;22). Genes Chromosomes Cancer. 2000 Jun;28(2):138-44. [PubMed Link Image]
  4. Lundblad JR, Kwok RP, Laurance ME, Harter ML, Goodman RH: Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP. Nature. 1995 Mar 2;374(6517):85-8. [PubMed Link Image]
  5. Xu W, Chen H, Du K, Asahara H, Tini M, Emerson BM, Montminy M, Evans RM: A transcriptional switch mediated by cofactor methylation. Science. 2001 Dec 21;294(5551):2507-11. Epub 2001 Nov 8. [PubMed Link Image]
  6. Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y: The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 1996 Nov 29;87(5):953-9. [PubMed Link Image]
  7. Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 1996 Jul 25;382(6589):319-24. [PubMed Link Image]
  8. Arany Z, Huang LE, Eckner R, Bhattacharya S, Jiang C, Goldberg MA, Bunn HF, Livingston DM: An essential role for p300/CBP in the cellular response to hypoxia. Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12969-73. [PubMed Link Image]
  9. Bex F, Yin MJ, Burny A, Gaynor RB: Differential transcriptional activation by human T-cell leukemia virus type 1 Tax mutants is mediated by distinct interactions with CREB binding protein and p300. Mol Cell Biol. 1998 Apr;18(4):2392-405. [PubMed Link Image]
  10. Fryer CJ, Archer TK: Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex. Nature. 1998 May 7;393(6680):88-91. [PubMed Link Image]
  11. Kiernan RE, Vanhulle C, Schiltz L, Adam E, Xiao H, Maudoux F, Calomme C, Burny A, Nakatani Y, Jeang KT, Benkirane M, Van Lint C: HIV-1 tat transcriptional activity is regulated by acetylation. EMBO J. 1999 Nov 1;18(21):6106-18. [PubMed Link Image]
  12. Miyake S, Sellers WR, Safran M, Li X, Zhao W, Grossman SR, Gan J, DeCaprio JA, Adams PD, Kaelin WG Jr: Cells degrade a novel inhibitor of differentiation with E1A-like properties upon exiting the cell cycle. Mol Cell Biol. 2000 Dec;20(23):8889-902. [PubMed Link Image]
  13. MacLellan WR, Xiao G, Abdellatif M, Schneider MD: A novel Rb- and p300-binding protein inhibits transactivation by MyoD. Mol Cell Biol. 2000 Dec;20(23):8903-15. [PubMed Link Image]
  14. Ko L, Cardona GR, Chin WW: Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator. Proc Natl Acad Sci U S A. 2000 May 23;97(11):6212-7. [PubMed Link Image]
  15. Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F: Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. Virology. 2000 Nov 25;277(2):278-95. [PubMed Link Image]
  16. Xu X, Chackalaparampil I, Monroy MA, Cannella MT, Pesek E, Chrivia J, Yaciuk P: Adenovirus DNA binding protein interacts with the SNF2-related CBP activator protein (SrCap) and inhibits SrCap-mediated transcription. J Virol. 2001 Nov;75(21):10033-40. [PubMed Link Image]
  17. Scoggin KE, Ulloa A, Nyborg JK: The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to mediate transcriptional activation. Mol Cell Biol. 2001 Aug;21(16):5520-30. [PubMed Link Image]
  18. Zhang W, Nisbet JW, Albrecht B, Ding W, Kashanchi F, Bartoe JT, Lairmore MD: Human T-lymphotropic virus type 1 p30(II) regulates gene transcription by binding CREB binding protein/p300. J Virol. 2001 Oct;75(20):9885-95. [PubMed Link Image]
  19. Gizard F, Lavallee B, DeWitte F, Hum DW: A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression. J Biol Chem. 2001 Sep 7;276(36):33881-92. Epub 2001 May 10. [PubMed Link Image]
  20. Vadlamudi RK, Wang RA, Mazumdar A, Kim Y, Shin J, Sahin A, Kumar R: Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha. J Biol Chem. 2001 Oct 12;276(41):38272-9. Epub 2001 Jul 31. [PubMed Link Image]
  21. Yamamoto N, Yamamoto S, Inagaki F, Kawaichi M, Fukamizu A, Kishi N, Matsuno K, Nakamura K, Weinmaster G, Okano H, Nakafuku M: Role of Deltex-1 as a transcriptional regulator downstream of the Notch receptor. J Biol Chem. 2001 Nov 30;276(48):45031-40. Epub 2001 Sep 19. [PubMed Link Image]
  22. Hasan S, Stucki M, Hassa PO, Imhof R, Gehrig P, Hunziker P, Hubscher U, Hottiger MO: Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300. Mol Cell. 2001 Jun;7(6):1221-31. [PubMed Link Image]
  23. Yamamoto H, Kihara-Negishi F, Yamada T, Suzuki M, Nakano T, Oikawa T: Interaction between the hematopoietic Ets transcription factor Spi-B and the coactivator CREB-binding protein associated with negative cross-talk with c-Myb. Cell Growth Differ. 2002 Feb;13(2):69-75. [PubMed Link Image]
  24. Braganca J, Swingler T, Marques FI, Jones T, Eloranta JJ, Hurst HC, Shioda T, Bhattacharya S: Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2. J Biol Chem. 2002 Mar 8;277(10):8559-65. Epub 2001 Dec 14. [PubMed Link Image]
  25. Lee YH, Koh SS, Zhang X, Cheng X, Stallcup MR: Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities. Mol Cell Biol. 2002 Jun;22(11):3621-32. [PubMed Link Image]
  26. Shiseki M, Nagashima M, Pedeux RM, Kitahama-Shiseki M, Miura K, Okamura S, Onogi H, Higashimoto Y, Appella E, Yokota J, Harris CC: p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity. Cancer Res. 2003 May 15;63(10):2373-8. [PubMed Link Image]
  27. Hecht A, Stemmler MP: Identification of a promoter-specific transcriptional activation domain at the C terminus of the Wnt effector protein T-cell factor 4. J Biol Chem. 2003 Feb 7;278(6):3776-85. Epub 2002 Nov 22. [PubMed Link Image]
  28. Ammanamanchi S, Freeman JW, Brattain MG: Acetylated sp3 is a transcriptional activator. J Biol Chem. 2003 Sep 12;278(37):35775-80. Epub 2003 Jun 30. [PubMed Link Image]
  29. Fujii Y, Kumatori A, Nakamura M: SATB1 makes a complex with p300 and represses gp91(phox) promoter activity. Microbiol Immunol. 2003;47(10):803-11. [PubMed Link Image]
  30. An W, Kim J, Roeder RG: Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. Cell. 2004 Jun 11;117(6):735-48. [PubMed Link Image]
  31. Thevenet L, Mejean C, Moniot B, Bonneaud N, Galeotti N, Aldrian-Herrada G, Poulat F, Berta P, Benkirane M, Boizet-Bonhoure B: Regulation of human SRY subcellular distribution by its acetylation/deacetylation. EMBO J. 2004 Aug 18;23(16):3336-45. Epub 2004 Aug 5. [PubMed Link Image]
  32. Wang H, Fang R, Cho JY, Libermann TA, Oettgen P: Positive and negative modulation of the transcriptional activity of the ETS factor ESE-1 through interaction with p300, CREB-binding protein, and Ku 70/86. J Biol Chem. 2004 Jun 11;279(24):25241-50. Epub 2004 Apr 8. [PubMed Link Image]
  33. Thompson PR, Wang D, Wang L, Fulco M, Pediconi N, Zhang D, An W, Ge Q, Roeder RG, Wong J, Levrero M, Sartorelli V, Cotter RJ, Cole PA: Regulation of the p300 HAT domain via a novel activation loop. Nat Struct Mol Biol. 2004 Apr;11(4):308-15. Epub 2004 Mar 7. [PubMed Link Image]
  34. Aizawa H, Hu SC, Bobb K, Balakrishnan K, Ince G, Gurevich I, Cowan M, Ghosh A: Dendrite development regulated by CREST, a calcium-regulated transcriptional activator. Science. 2004 Jan 9;303(5655):197-202. [PubMed Link Image]
  35. Roelfsema JH, White SJ, Ariyurek Y, Bartholdi D, Niedrist D, Papadia F, Bacino CA, den Dunnen JT, van Ommen GJ, Breuning MH, Hennekam RC, Peters DJ: Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the CBP and EP300 genes cause disease. Am J Hum Genet. 2005 Apr;76(4):572-80. Epub 2005 Feb 10. [PubMed Link Image]
  36. Lee YH, Coonrod SA, Kraus WL, Jelinek MA, Stallcup MR: Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination. Proc Natl Acad Sci U S A. 2005 Mar 8;102(10):3611-6. Epub 2005 Feb 24. [PubMed Link Image]
  37. Karanam B, Jiang L, Wang L, Kelleher NL, Cole PA: Kinetic and mass spectrometric analysis of p300 histone acetyltransferase domain autoacetylation. J Biol Chem. 2006 Dec 29;281(52):40292-301. Epub 2006 Oct 25. [PubMed Link Image]
  38. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  39. Hung JJ, Wang YT, Chang WC: Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription. Mol Cell Biol. 2006 Mar;26(5):1770-85. [PubMed Link Image]
  40. Shima Y, Shima T, Chiba T, Irimura T, Pandolfi PP, Kitabayashi I: PML activates transcription by protecting HIPK2 and p300 from SCFFbx3-mediated degradation. Mol Cell Biol. 2008 Dec;28(23):7126-38. Epub 2008 Sep 22. [PubMed Link Image]
  41. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  42. Huang C, Han Y, Wang Y, Sun X, Yan S, Yeh ET, Chen Y, Cang H, Li H, Shi G, Cheng J, Tang X, Yi J: SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation. EMBO J. 2009 Sep 16;28(18):2748-62. Epub 2009 Aug 13. [PubMed Link Image]
  43. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  44. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  45. Freedman SJ, Sun ZY, Poy F, Kung AL, Livingston DM, Wagner G, Eck MJ: Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha. Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5367-72. [PubMed Link Image]
  46. Liu X, Wang L, Zhao K, Thompson PR, Hwang Y, Marmorstein R, Cole PA: The structural basis of protein acetylation by the p300/CBP transcriptional coactivator. Nature. 2008 Feb 14;451(7180):846-50. [PubMed Link Image]
  47. Feng H, Jenkins LM, Durell SR, Hayashi R, Mazur SJ, Cherry S, Tropea JE, Miller M, Wlodawer A, Appella E, Bai Y: Structural basis for p300 Taz2-p53 TAD1 binding and modulation by phosphorylation. Structure. 2009 Feb 13;17(2):202-10. [PubMed Link Image]
  48. Gayther SA, Batley SJ, Linger L, Bannister A, Thorpe K, Chin SF, Daigo Y, Russell P, Wilson A, Sowter HM, Delhanty JD, Ponder BA, Kouzarides T, Caldas C: Mutations truncating the EP300 acetylase in human cancers. Nat Genet. 2000 Mar;24(3):300-3. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5243
Enzyme 2 Name CREB-binding protein
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name CREBBP
Enzyme 2 Protein Sequence >CREB-binding protein
MAENLLDGPPNPKRAKLSSPGFSANDSTDFGSLFDLENDLPDELIPNGGELGLLNSGNLV
PDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSANMASLSAMGK
SPLSQGDSSAPSLPKQAASTSGPTPAASQALNPQAQKQVGLATSSPATSQTGPGICMNAN
FNQTHPGLLNSNSGHSLINQASQGQAQVMNGSLGAAGRGRGAGMPYPTPAMQGASSSVLA
ETLTQVSPQMTGHAGLNTAQAGGMAKMGITGNTSPFGQPFSQAGGQPMGATGVNPQLASK
QSMVNSLPTFPTDIKNTSVTNVPNMSQMQTSVGIVPTQAIATGPTADPEKRKLIQQQLVL
LLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWK
NCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGTGQQNATSLSNPNPIDPSS
MQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPQTHQQMRTLNPLGNNPMNIPAGGITTDQ
QPPNLISESALPTSLGATNPLMNDGSNSGNIGTLSTIPTAAPPSSTGVRKGWHEHVTQDL
RSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYK
IQKELEEKRRSRLHKQGILGNQPALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQG
MNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPNMMGAHT
NNMMAQAPAQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPLNMLGPQA
SQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPVSSSGQTPT
PTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTP
LSQAAASIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRSE
MMEEDLQGASQVKEETDIAEQKSEPMEVDEKKPEVKVEVKEEEESSSNGTASQSTSPSQP
RKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKR
KLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCC
GRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQT
TISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRK
ENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFV
DSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDCPPPNTRRVYISYLDSIHFF
RPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQ
EWYKKMLDKAFAERIIHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEE
EERKKEESTAASETTEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQK
LYATMEKHKEVFFVIHLHAGPVINTLPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSS
LRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAH
KMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKR
VVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQ
QAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVSMSPAG
FPSVARTQPPTTVSTGKPTSQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRVNINNS
MPPGRTGMGTPGSQMAPVSLNVPRPNQVSGPVMPSMPPGQWQQAPLPQQQPMPGLPRPVI
SMQAQAAVAGPRMPSVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAF
IKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPQQQA
MGGLNPQGQALNIMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAG
MAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQHLPLQGSSMGQMAAQMGQLGQMGQPGLG
ADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLS
NQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSIDQGHL
GNPEQSAMLPQLNTPSRSALSSELSLVGDTTGDTLEKFVEGL
Enzyme 2 Number of Residues 2442
Enzyme 2 Molecular Weight 265349.8
Enzyme 2 Theoretical pI 8.63
Enzyme 2 GO Classification
Function
  • N-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • binding
  • catalytic activity
  • cation binding
  • histone acetyltransferase activity
  • ion binding
  • lysine N-acetyltransferase activity
  • metal ion binding
  • protein binding
  • transcription coactivator activity
  • transcription cofactor activity
  • transcription factor binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • cellular component organization at cellular level
  • cellular process
  • chromatin modification
  • chromatin organization
  • chromosome organization
  • covalent chromatin modification
  • histone acetylation
  • histone modification
  • organelle organization
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • histone acetyltransferase complex
  • intracellular membrane-bounded organelle
  • macromolecular complex
  • membrane-bounded organelle
  • nucleus
  • organelle
  • protein complex
Enzyme 2 General Function Involved in transcription cofactor activity
Enzyme 2 Specific Function Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 coactivator. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • acetyl-CoA + histone = CoA + acetylhistone
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID Q92793 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CBP_HUMAN Link Image
Enzyme 2 PDB ID 1JSP Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >7329 bp
ATGGCTGAGAACTTGCTGGACGGACCGCCCAACCCCAAAAGAGCCAAACTCAGCTCGCCC
GGTTTCTCGGCGAATGACAGCACAGATTTTGGATCATTGTTTGACTTGGAAAATGATCTT
CCTGATGAGCTGATACCCAATGGAGGAGAATTAGGCCTTTTAAACAGTGGGAACCTTGTT
CCAGATGCTGCTTCCAAACATAAACAACTGTCGGAGCTTCTACGAGGAGGCAGCGGCTCT
AGTATCAACCCAGGAATAGGAAATGTGAGCGCCAGCAGCCCCGTGCAGCAGGGCCTGGGT
GGCCAGGCTCAAGGGCAGCCGAACAGTGCTAACATGGCCAGCCTCAGTGCCATGGGCAAG
AGCCCTCTGAGCCAGGGAGATTCTTCAGCCCCCAGCCTGCCTAAACAGGCAGCCAGCACC
TCTGGGCCCACCCCCGCTGCCTCCCAAGCACTGAATCCGCAAGCACAAAAGCAAGTGGGG
CTGGCGACTAGCAGCCCTGCCACGTCACAGACTGGACCTGGTATCTGCATGAATGCTAAC
TTTAACCAGACCCACCCAGGCCTCCTCAATAGTAACTCTGGCCATAGCTTAATTAATCAG
GCTTCACAAGGGCAGGCGCAAGTCATGAATGGATCTCTTGGGGCTGCTGGCAGAGGAAGG
GGAGCTGGAATGCCGTACCCTACTCCAGCCATGCAGGGCGCCTCGAGCAGCGTGCTGGCT
GAGACCCTAACGCAGGTTTCCCCGCAAATGACTGGTCACGCGGGACTGAACACCGCACAG
GCAGGAGGCATGGCCAAGATGGGAATAACTGGGAACACAAGTCCATTTGGACAGCCCTTT
AGTCAAGCTGGAGGGCAGCCAATGGGAGCCACTGGAGTGAACCCCCAGTTAGCCAGCAAA
CAGAGCATGGTCAACAGTTTGCCCACCTTCCCTACAGATATCAAGAATACTTCAGTCACC
AACGTGCCAAATATGTCTCAGATGCAAACATCAGTGGGAATTGTACCCACACAAGCAATT
GCAACAGGCCCCACTGCAGATCCTGAAAAACGCAAACTGATACAGCAGCAGCTGGTTCTA
CTGCTTCATGCTCATAAGTGTCAGAGACGAGAGCAAGCAAACGGAGAGGTTCGGGCCTGC
TCGCTCCCGCATTGTCGAACCATGAAAAACGTTTTGAATCACATGACGCATTGTCAGGCT
GGGAAAGCCTGCCAAGTTGCCCATTGTGCATCTTCACGACAAATCATCTCTCATTGGAAG
AACTGCACACGACATGACTGTCCTGTTTGCCTCCCTTTGAAAAATGCCAGTGACAAGCGA
AACCAACAAACCATCCTGGGGTCTCCAGCTAGTGGAATTCAAAACACAATTGGTTCTGTT
GGCACAGGGCAACAGAATGCCACTTCTTTAAGTAACCCAAATCCCATAGACCCCAGCTCC
ATGCAGCGAGCCTATGCTGCTCTCGGACTCCCCTACATGAACCAGCCCCAGACGCAGCTG
CAGCCTCAGGTTCCTGGCCAGCAACCAGCACAGCCTCAAACCCACCAGCAGATGAGGACT
CTCAACCCCCTGGGAAATAATCCAATGAACATTCCAGCAGGAGGAATAACAACAGATCAG
CAGCCCCCAAACTTGATTTCAGAATCAGCTCTTCCGACTTCCCTGGGGGCCACAAACCCA
CTGATGAACGATGGCTCCAACTCTGGTAACATTGGAACCCTCAGCACTATACCAACAGCA
GCTCCTCCTTCTAGCACCGGTGTAAGGAAAGGCTGGCACGAACATGTCACTCAGGACCTG
CGGAGCCATCTAGTGCATAAACTCGTCCAAGCCATCTTCCCAACACCTGATCCCGCAGCT
CTAAAGGATCGCCGCATGGAAAACCTGGTAGCCTATGCTAAGAAAGTGGAAGGGGACATG
TACGAGTCTGCCAACAGCAGGGATGAATATTATCACTTATTAGCAGAGAAAATCTACAAG
ATACAAAAAGAACTAGAAGAAAAACGGAGGTCGCGTTTACATAAACAAGGCATCTTGGGG
AACCAGCCAGCCTTACCAGCCCCGGGGGCTCAGCCCCCTGTGATTCCACAGGCACAACCT
GTGAGACCTCCAAATGGACCCCTGTCCCTGCCAGTGAATCGCATGCAAGTTTCTCAAGGG
ATGAATTCATTTAACCCCATGTCCTTGGGGAACGTCCAGTTGCCACAAGCACCCATGGGA
CCTCGTGCAGCCTCCCCAATGAACCACTCTGTCCAGATGAACAGCATGGGCTCAGTGCCA
GGGATGGCCATTTCTCCTTCCCGAATGCCTCAGCCTCCGAACATGATGGGTGCACACACC
AACAACATGATGGCCCAGGCGCCCGCTCAGAGCCAGTTTCTGCCACAGAACCAGTTCCCG
TCATCCAGCGGGGCGATGAGTGTGGGCATGGGGCAGCCGCCAGCCCAAACAGGCGTGTCA
CAGGGACAGGTGCCTGGTGCTGCTCTTCCTAACCCTCTCAACATGCTGGGGCCTCAGGCC
AGCCAGCTACCTTGCCCTCCAGTGACACAGTCACCACTGCACCCAACACCGCCTCCTGCT
TCCACGGCTGCTGGCATGCCATCTCTCCAGCACACGACACCACCTGGGATGACTCCTCCC
CAGCCAGCAGCTCCCACTCAGCCATCAACTCCTGTGTCGTCTTCCGGGCAGACTCCCACC
CCGACTCCTGGCTCAGTGCCCAGTGCTACCCAAACCCAGAGCACCCCTACAGTCCAGGCA
GCAGCCCAGGCCCAGGTGACCCCGCAGCCTCAAACCCCAGTTCAGCCCCCGTCTGTGGCT
ACCCCTCAGTCATCGCAGCAACAGCCGACGCCTGTGCACGCCCAGCCTCCTGGCACACCG
CTTTCCCAGGCAGCAGCCAGCATTGATAACAGAGTCCCTACCCCCTCCTCGGTGGCCAGC
GCAGAAACCAATTCCCAGCAGCCAGGACCTGACGTACCTGTGCTGGAAATGAAGACGGAG
ACCCAAGCAGAGGACACTGAGCCCGATCCTGGTGAATCCAAAGGGGAGCCCAGGTCTGAG
ATGATGGAGGAGGATTTGCAAGGAGCTTCCCAAGTTAAAGAAGAAACAGACATAGCAGAG
CAGAAATCAGAACCAATGGAAGTGGATGAAAAGAAACCTGAAGTGAAAGTAGAAGTTAAA
GAGGAAGAAGAGAGTAGCAGTAACGGCACAGCCTCTCAGTCAACATCTCCTTCGCAGCCG
CGCAAAAAAATCTTTAAACCAGAGGAGTTACGCCAGGCCCTCATGCCAACCCTAGAAGCA
CTGTATCGACAGGACCCAGAGTCATTACCTTTCCGGCAGCCTGTAGATCCCCAGCTCCTC
GGAATTCCAGACTATTTTGACATCGTAAAGAATCCCATGGACCTCTCCACCATCAAGCGG
AAGCTGGACACAGGGCAATACCAAGAGCCCTGGCAGTACGTGGACGACGTCTGGCTCATG
TTCAACAATGCCTGGCTCTATAATCGCAAGACATCCCGAGTCTATAAGTTTTGCAGTAAG
CTTGCAGAGGTCTTTGAGCAGGAAATTGACCCTGTCATGCAGTCCCTTGGATATTGCTGT
GGACGCAAGTATGAGTTTTCCCCACAGACTTTGTGCTGCTATGGGAAGCAGCTGTGTACC
ATTCCTCGCGATGCTGCCTACTACAGCTATCAGAATAGGTATCATTTCTGTGAGAAGTGT
TTCACAGAGATCCAGGGCGAGAATGTGACCCTGGGTGACGACCCTTCACAGCCCCAGACG
ACAATTTCAAAGGATCAGTTTGAAAAGAAGAAAAATGATACCTTAGACCCCGAACCTTTC
GTTGATTGCAAGGAGTGTGGCCGGAAGATGCATCAGATTTGCGTTCTGCACTATGACATC
ATTTGGCCTTCAGGTTTTGTGTGCGACAACTGCTTGAAGAAAACTGGCAGACCTCGAAAA
GAAAACAAATTCAGTGCTAAGAGGCTGCAGACCACAAGACTGGGAAACCACTTGGAAGAC
CGAGTGAACAAATTTTTGCGGCGCCAGAATCACCCTGAAGCCGGGGAGGTTTTTGTCCGA
GTGGTGGCCAGCTCAGACAAGACGGTGGAGGTCAAGCCCGGGATGAAGTCACGGTTTGTG
GATTCTGGGGAAATGTCTGAATCTTTCCCATATCGAACCAAAGCTCTGTTTGCTTTTGAG
GAAATTGACGGCGTGGATGTCTGCTTTTTTGGAATGCACGTCCAAGAATACGGCTCTGAT
TGCCCCCCTCCAAACACGAGGCGTGTGTACATTTCTTATCTGGATAGTATTCATTTCTTC
CGGCCACGTTGCCTCCGCACAGCCGTTTACCATGAGATCCTTATTGGATATTTAGAGTAT
GTGAAGAAATTAGGGTATGTGACAGGGCACATCTGGGCCTGTCCTCCAAGTGAAGGAGAT
GATTACATCTTCCATTGCCACCCACCTGATCAAAAAATACCCAAGCCAAAACGACTGCAG
GAGTGGTACAAAAAGATGCTGGACAAGGCGTTTGCAGAGCGGATCATCCATGACTACAAG
GATATTTTCAAACAAGCAACTGAAGACAGGCTCACCAGTGCCAAGGAACTGCCCTATTTT
GAAGGTGATTTCTGGCCCAATGTGTTAGAAGAGAGCATTAAGGAACTAGAACAAGAAGAA
GAGGAGAGGAAAAAGGAAGAGAGCACTGCAGCCAGTGAAACCACTGAGGGCAGTCAGGGC
GACAGCAAGAATGCCAAGAAGAAGAACAACAAGAAAACCAACAAGAACAAAAGCAGCATC
AGCCGCGCCAACAAGAAGAAGCCCAGCATGCCCAACGTGTCCAATGACCTGTCCCAGAAG
CTGTATGCCACCATGGAGAAGCACAAGGAGGTCTTCTTCGTGATCCACCTGCACGCTGGG
CCTGTCATCAACACCCTGCCCCCCATCGTCGACCCCGACCCCCTGCTCAGCTGTGACCTC
ATGGATGGGCGCGACGCCTTCCTCACCCTCGCCAGAGACAAGCACTGGGAGTTCTCCTCC
TTGCGCCGCTCCAAGTGGTCCACGCTCTGCATGCTGGTGGAGCTGCACACCCAGGGCCAG
GACCGCTTTGTCTACACCTGCAACGAGTGCAAGCACCACGTGGAGACGCGCTGGCACTGC
ACTGTGTGCGAGGACTACGACCTCTGCATCAACTGCTATAACACGAAGAGCCATGCCCAT
AAGATGGTGAAGTGGGGGCTGGGCCTGGATGACGAGGGCAGCAGCCAGGGCGAGCCACAG
TCAAAGAGCCCCCAGGAGTCACGCCGGCTGAGCATCCAGCGCTGCATCCAGTCGCTGGTG
CACGCGTGCCAGTGCCGCAACGCCAACTGCTCGCTGCCATCCTGCCAGAAGATGAAGCGG
GTGGTGCAGCACACCAAGGGCTGCAAACGCAAGACCAACGGGGGCTGCCCGGTGTGCAAG
CAGCTCATCGCCCTCTGCTGCTACCACGCCAAGCACTGCCAAGAAAACAAATGCCCCGTG
CCCTTCTGCCTCAACATCAAACACAAGCTCCGCCAGCAGCAGATCCAGCACCGCCTGCAG
CAGGCCCAGCTCATGCGCCGGCGGATGGCCACCATGAACACCCGCAACGTGCCTCAGCAG
AGTCTGCCTTCTCCTACCTCAGCACCGCCCGGGACCCCCACACAGCAGCCCAGCACACCC
CAGACGCCGCAGCCCCCTGCCCAGCCCCAACCCTCACCCGTGAGCATGTCACCAGCTGGC
TTCCCCAGCGTGGCCCGGACTCAGCCCCCCACCACGGTGTCCACAGGGAAGCCTACCAGC
CAGGTGCCGGCCCCCCCACCCCCGGCCCAGCCCCCTCCTGCAGCGGTGGAAGCGGCTCGG
CAGATCGAGCGTGAGGCCCAGCAGCAGCAGCACCTGTACCGGGTGAACATCAACAACAGC
ATGCCCCCAGGACGCACGGGCATGGGGACCCCGGGGAGCCAGATGGCCCCCGTGAGCCTG
AATGTGCCCCGACCCAACCAGGTGAGCGGGCCCGTCATGCCCAGCATGCCTCCCGGGCAG
TGGCAGCAGGCGCCCCTTCCCCAGCAGCAGCCCATGCCAGGCTTGCCCAGGCCTGTGATA
TCCATGCAGGCCCAGGCGGCCGTGGCTGGGCCCCGGATGCCCAGCGTGCAGCCACCCAGG
AGCATCTCACCCAGCGCTCTGCAAGACCTGCTGCGGACCCTGAAGTCGCCCAGCTCCCCT
CAGCAGCAACAGCAGGTGCTGAACATTCTCAAATCAAACCCGCAGCTAATGGCAGCTTTC
ATCAAACAGCGCACAGCCAAGTACGTGGCCAATCAGCCCGGCATGCAGCCCCAGCCTGGC
CTCCAGTCCCAGCCCGGCATGCAACCCCAGCCTGGCATGCACCAGCAGCCCAGCCTGCAG
AACCTGAATGCCATGCAGGCTGGCGTGCCGCGGCCCGGTGTGCCTCCACAGCAGCAGGCG
ATGGGAGGCCTGAACCCCCAGGGCCAGGCCTTGAACATCATGAACCCAGGACACAACCCC
AACATGGCGAGTATGAATCCACAGTACCGAGAAATGTTACGGAGGCAGCTGCTGCAGCAG
CAGCAGCAACAGCAGCAGCAACAACAGCAGCAACAGCAGCAGCAGCAAGGGAGTGCCGGC
ATGGCTGGGGGCATGGCGGGGCACGGCCAGTTCCAGCAGCCTCAAGGACCCGGAGGCTAC
CCACCGGCCATGCAGCAGCAGCAGCGCATGCAGCAGCATCTCCCCCTCCAGGGCAGCTCC
ATGGGCCAGATGGCGGCTCAGATGGGACAGCTTGGCCAGATGGGGCAGCCGGGGCTGGGG
GCAGACAGCACCCCCAACATCCAGCAAGCCCTGCAGCAGCGGATTCTGCAGCAACAGCAG
ATGAAGCAGCAGATTGGGTCCCCAGGCCAGCCGAACCCCATGAGCCCCCAGCAACACATG
CTCTCAGGACAGCCACAGGCCTCGCATCTCCCTGGCCAGCAGATCGCCACGTCCCTTAGT
AACCAGGTGCGGTCTCCAGCCCCTGTCCAGTCTCCACGGCCCCAGTCCCAGCCTCCACAT
TCCAGCCCGTCACCACGGATACAGCCCCAGCCTTCGCCACACCACGTCTCACCCCAGACT
GGTTCCCCCCACCCCGGACTCGCAGTCACCATGGCCAGCTCCATAGATCAGGGACACTTG
GGGAACCCCGAACAGAGTGCAATGCTCCCCCAGCTGAACACCCCCAGCAGGAGTGCGCTG
TCCAGCGAACTGTCCCTGGTCGGGGACACCACGGGGGACACGCTAGAGAAGTTTGTGGAG
GGCTTGTAG
Enzyme 2 GenBank Gene ID U85962 Link Image
Enzyme 2 GeneCard ID CREBBP Link Image
Enzyme 2 GenAtlas ID CREBBP Link Image
Enzyme 2 HGNC ID HGNC:2348 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 16p13.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Sobulo OM, Borrow J, Tomek R, Reshmi S, Harden A, Schlegelberger B, Housman D, Doggett NA, Rowley JD, Zeleznik-Le NJ: MLL is fused to CBP, a histone acetyltransferase, in therapy-related acute myeloid leukemia with a t(11;16)(q23;p13.3). Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8732-7. [PubMed Link Image]
  2. Giles RH, Petrij F, Dauwerse HG, den Hollander AI, Lushnikova T, van Ommen GJ, Goodman RH, Deaven LL, Doggett NA, Peters DJ, Breuning MH: Construction of a 1.2-Mb contig surrounding, and molecular analysis of, the human CREB-binding protein (CBP/CREBBP) gene on chromosome 16p13.3. Genomics. 1997 May 15;42(1):96-114. [PubMed Link Image]
  3. Borrow J, Stanton VP Jr, Andresen JM, Becher R, Behm FG, Chaganti RS, Civin CI, Disteche C, Dube I, Frischauf AM, Horsman D, Mitelman F, Volinia S, Watmore AE, Housman DE: The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein. Nat Genet. 1996 Sep;14(1):33-41. [PubMed Link Image]
  4. Panagopoulos I, Fioretos T, Isaksson M, Samuelsson U, Billstrom R, Strombeck B, Mitelman F, Johansson B: Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13). Hum Mol Genet. 2001 Feb 15;10(4):395-404. [PubMed Link Image]
  5. Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 1996 Jul 25;382(6589):319-24. [PubMed Link Image]
  6. Arany Z, Huang LE, Eckner R, Bhattacharya S, Jiang C, Goldberg MA, Bunn HF, Livingston DM: An essential role for p300/CBP in the cellular response to hypoxia. Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12969-73. [PubMed Link Image]
  7. Bex F, Yin MJ, Burny A, Gaynor RB: Differential transcriptional activation by human T-cell leukemia virus type 1 Tax mutants is mediated by distinct interactions with CREB binding protein and p300. Mol Cell Biol. 1998 Apr;18(4):2392-405. [PubMed Link Image]
  8. Zhang W, Bieker JJ: Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases. Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):9855-60. [PubMed Link Image]
  9. Johnston H, Kneer J, Chackalaparampil I, Yaciuk P, Chrivia J: Identification of a novel SNF2/SWI2 protein family member, SRCAP, which interacts with CREB-binding protein. J Biol Chem. 1999 Jun 4;274(23):16370-6. [PubMed Link Image]
  10. Doucas V, Tini M, Egan DA, Evans RM: Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling. Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):2627-32. [PubMed Link Image]
  11. Chen H, Lin RJ, Xie W, Wilpitz D, Evans RM: Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell. 1999 Sep 3;98(5):675-86. [PubMed Link Image]
  12. Mahajan MA, Samuels HH: A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein. Mol Cell Biol. 2000 Jul;20(14):5048-63. [PubMed Link Image]
  13. Hung HL, Kim AY, Hong W, Rakowski C, Blobel GA: Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-mediated acetylation. J Biol Chem. 2001 Apr 6;276(14):10715-21. Epub 2001 Jan 11. [PubMed Link Image]
  14. Yang T, Davis RJ, Chow CW: Requirement of two NFATc4 transactivation domains for CBP potentiation. J Biol Chem. 2001 Oct 26;276(43):39569-76. Epub 2001 Aug 20. [PubMed Link Image]
  15. Chakraborty S, Senyuk V, Sitailo S, Chi Y, Nucifora G: Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles. J Biol Chem. 2001 Nov 30;276(48):44936-43. Epub 2001 Sep 21. [PubMed Link Image]
  16. Scoggin KE, Ulloa A, Nyborg JK: The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to mediate transcriptional activation. Mol Cell Biol. 2001 Aug;21(16):5520-30. [PubMed Link Image]
  17. Zhang W, Nisbet JW, Albrecht B, Ding W, Kashanchi F, Bartoe JT, Lairmore MD: Human T-lymphotropic virus type 1 p30(II) regulates gene transcription by binding CREB binding protein/p300. J Virol. 2001 Oct;75(20):9885-95. [PubMed Link Image]
  18. Gizard F, Lavallee B, DeWitte F, Hum DW: A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression. J Biol Chem. 2001 Sep 7;276(36):33881-92. Epub 2001 May 10. [PubMed Link Image]
  19. Vadlamudi RK, Wang RA, Mazumdar A, Kim Y, Shin J, Sahin A, Kumar R: Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha. J Biol Chem. 2001 Oct 12;276(41):38272-9. Epub 2001 Jul 31. [PubMed Link Image]
  20. Yamamoto H, Kihara-Negishi F, Yamada T, Suzuki M, Nakano T, Oikawa T: Interaction between the hematopoietic Ets transcription factor Spi-B and the coactivator CREB-binding protein associated with negative cross-talk with c-Myb. Cell Growth Differ. 2002 Feb;13(2):69-75. [PubMed Link Image]
  21. Braganca J, Swingler T, Marques FI, Jones T, Eloranta JJ, Hurst HC, Shioda T, Bhattacharya S: Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2. J Biol Chem. 2002 Mar 8;277(10):8559-65. Epub 2001 Dec 14. [PubMed Link Image]
  22. Wu RC, Qin J, Hashimoto Y, Wong J, Xu J, Tsai SY, Tsai MJ, O'Malley BW: Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) Coactivator activity by I kappa B kinase. Mol Cell Biol. 2002 May;22(10):3549-61. [PubMed Link Image]
  23. Masumi A, Yamakawa Y, Fukazawa H, Ozato K, Komuro K: Interferon regulatory factor-2 regulates cell growth through its acetylation. J Biol Chem. 2003 Jul 11;278(28):25401-7. Epub 2003 May 7. [PubMed Link Image]
  24. Watanabe N, Wachi S, Fujita T: Identification and characterization of BCL-3-binding protein: implications for transcription and DNA repair or recombination. J Biol Chem. 2003 Jul 11;278(28):26102-10. Epub 2003 May 2. [PubMed Link Image]
  25. Wang H, Fang R, Cho JY, Libermann TA, Oettgen P: Positive and negative modulation of the transcriptional activity of the ETS factor ESE-1 through interaction with p300, CREB-binding protein, and Ku 70/86. J Biol Chem. 2004 Jun 11;279(24):25241-50. Epub 2004 Apr 8. [PubMed Link Image]
  26. van der Horst A, Tertoolen LG, de Vries-Smits LM, Frye RA, Medema RH, Burgering BM: FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1). J Biol Chem. 2004 Jul 9;279(28):28873-9. Epub 2004 May 4. [PubMed Link Image]
  27. Pradhan A, Liu Y: The calcium-responsive transactivator recruits CREB binding protein to nuclear bodies. Neurosci Lett. 2004 Nov 11;370(2-3):191-5. [PubMed Link Image]
  28. Aizawa H, Hu SC, Bobb K, Balakrishnan K, Ince G, Gurevich I, Cowan M, Ghosh A: Dendrite development regulated by CREST, a calcium-regulated transcriptional activator. Science. 2004 Jan 9;303(5655):197-202. [PubMed Link Image]
  29. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  30. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  31. Sarkar D, Park ES, Emdad L, Lee SG, Su ZZ, Fisher PB: Molecular basis of nuclear factor-kappaB activation by astrocyte elevated gene-1. Cancer Res. 2008 Mar 1;68(5):1478-84. [PubMed Link Image]
  32. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  33. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  34. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  35. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  36. Dames SA, Martinez-Yamout M, De Guzman RN, Dyson HJ, Wright PE: Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response. Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5271-6. [PubMed Link Image]
  37. Kitabayashi I, Aikawa Y, Nguyen LA, Yokoyama A, Ohki M: Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein. EMBO J. 2001 Dec 17;20(24):7184-96. [PubMed Link Image]
  38. Vendel AC, Lumb KJ: NMR mapping of the HIV-1 Tat interaction surface of the KIX domain of the human coactivator CBP. Biochemistry. 2004 Feb 3;43(4):904-8. [PubMed Link Image]
  39. Murata T, Kurokawa R, Krones A, Tatsumi K, Ishii M, Taki T, Masuno M, Ohashi H, Yanagisawa M, Rosenfeld MG, Glass CK, Hayashi Y: Defect of histone acetyltransferase activity of the nuclear transcriptional coactivator CBP in Rubinstein-Taybi syndrome. Hum Mol Genet. 2001 May 1;10(10):1071-6. [PubMed Link Image]
  40. Bartsch O, Locher K, Meinecke P, Kress W, Seemanova E, Wagner A, Ostermann K, Rodel G: Molecular studies in 10 cases of Rubinstein-Taybi syndrome, including a mild variant showing a missense mutation in codon 1175 of CREBBP. J Med Genet. 2002 Jul;39(7):496-501. [PubMed Link Image]
  41. Kalkhoven E, Roelfsema JH, Teunissen H, den Boer A, Ariyurek Y, Zantema A, Breuning MH, Hennekam RC, Peters DJ: Loss of CBP acetyltransferase activity by PHD finger mutations in Rubinstein-Taybi syndrome. Hum Mol Genet. 2003 Feb 15;12(4):441-50. [PubMed Link Image]
  42. Roelfsema JH, White SJ, Ariyurek Y, Bartholdi D, Niedrist D, Papadia F, Bacino CA, den Dunnen JT, van Ommen GJ, Breuning MH, Hennekam RC, Peters DJ: Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the CBP and EP300 genes cause disease. Am J Hum Genet. 2005 Apr;76(4):572-80. Epub 2005 Feb 10. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5351
Enzyme 3 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Enzyme 3 Synonyms
  1. E-NPP 1
  2. Membrane component chromosome 6 surface marker 1
  3. Phosphodiesterase I/nucleotide pyrophosphatase 1
  4. Plasma-cell membrane glycoprotein PC-1
  5. Alkaline phosphodiesterase I
  6. Nucleotide pyrophosphatase
  7. NPPase
Enzyme 3 Gene Name ENPP1
Enzyme 3 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED
Enzyme 3 Number of Residues 925
Enzyme 3 Molecular Weight 104923.6
Enzyme 3 Theoretical pI 7.14
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • ion binding
  • metal ion binding
  • molecular transducer activity
  • nucleic acid binding
  • pattern binding
  • polysaccharide binding
  • receptor activity
  • scavenger receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • immune response
  • immune system process
  • metabolic process
Component
Enzyme 3 General Function Involved in catalytic activity
Enzyme 3 Specific Function Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity
Enzyme 3 Pathways
Enzyme 3 Reactions
  • a dinucleotide + H2O = 2 mononucleotides [RN:R00056]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 77-97
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 170650661 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P22413 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ENPP1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2778 bp
ATGGAGCGCGACGGCTGCGCGGGGGGCGGGAGCCGCGGCGGCGAGGGCGGGCGCGCTCCC
CGGGAGGGCCCGGCGGGGAACGGCCGCGATCGGGGCCGCAGCCACGCTGCCGAGGCGCCC
GGGGACCCGCAGGCGGCCGCGTCCTTGCTGGCCCCTATGGACGTGGGGGAGGAGCCGCTG
GAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCCAACACCTATAAAGTACTCTCGCTG
GTATTGTCAGTATGTGTGTTAACAACAATACTTGGTTGTATATTTGGGTTGAAACCAAGC
TGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGTTTCGAGAGAACATTTGGGAACTGT
CGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGCTGTTTAGATTACCAGGAGACGTGC
ATAGAACCAGAACATATATGGACTTGCAACAAATTCAGGTGTGGTGAGAAAAGGTTGACC
AGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGACAAGGGCGACTGCTGCATCAACTAC
AGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAAGAACCATGTGAGAGCATTAATGAG
CCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACCCTCTTATTTTCTTTGGATGGATTC
AGGGCAGAATATTTACACACTTGGGGTGGACTTCTTCCTGTTATTAGCAAACTAAAAAAA
TGTGGAACATATACTAAAAACATGAGACCGGTATATCCAACAAAAACTTTCCCCAATCAC
TACAGCATTGTCACCGGATTGTATCCAGAATCTCATGGCATAATCGACAATAAAATGTAT
GATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGTAAAGAGAAATTTAATCCTGAGTGG
TACAAAGGAGAACCAATTTGGGTCACAGCTAAGTATCAAGGCCTCAAGTCTGGCACATTT
TTCTGGCCAGGATCAGATGTGGAAATTAACGGAATTTTCCCAGACATCTATAAAATGTAT
AATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCTGTTCTTCAGTGGCTACAGCTTCCT
AAAGATGAAAGACCACACTTTTACACTCTGTATTTAGAAGAACCAGATTCTTCAGGTCAT
TCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCCTTGCAGAGGGTTGATGGTATGGTT
GGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTGCACAGATGCCTGAACCTCATCCTT
ATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAGAAATACATATATCTGAATAAATAT
TTGGGGGATGTTAAAAATATTAAAGTTATCTATGGACCTGCAGCTCGATTGAGACCCTCT
GATGTCCCAGATAAATACTATTCATTTAACTATGAAGGCATTGCCCGAAATCTTTCTTGC
CGGGAACCAAACCAGCACTTCAAACCTTACCTGAAACATTTCTTACCTAAGCGTTTGCAC
TTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTCTATTTGGACCCTCAGTGGCAACTT
GCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGTGGATTTCATGGCTCTGACAATGTA
TTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGACCTGGATTCAAGCATGGCATTGAG
GCTGACACCTTTGAAAACATTGAAGTCTATAACTTAATGTGTGATTTACTGAATTTGACA
CCGGCTCCTAATAACGGAACTCATGGAAGTCTTAACCACCTTCTAAAGAATCCTGTTTAT
ACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTACAGTGCCCCTTCACAAGAAACCCC
AGAGATAACCTTGGCTGCTCATGTAACCCTTCGATTTTGCCGATTGAGGATTTTCAAACA
CAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATTAAGCATGAAACTTTACCCTATGGA
AGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGTCTTCTTTCCCAGCACCAGTTTATG
AGTGGATACAGCCAAGACATCTTAATGCCCCTTTGGACATCCTATACCGTGGACAGAAAT
GACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTGTACCAGGACTTTAGAATTCCTCTT
AGTCCTGTCCATAAATGTTCATTTTATAAAAATAACACCAAAGTGAGTTACGGGTTCCTC
TCCCCACCACAACTAAATAAAAATTCAAGTGGAATATATTCTGAAGCTTTGCTTACTACA
AATATAGTGCCAATGTACCAGAGTTTTCAAGTTATATGGCGCTACTTTCATGACACCCTA
CTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAATGTCGTCAGTGGTCCTGTGTTTGAC
TTTGATTATGATGGACGTTGTGATTCCTTAGAGAATCTGAGGCAAAAAAGAAGAGTCATC
CGTAACCAAGAAATTTTGATTCCAACTCACTTCTTTATTGTGCTAACAAGCTGTAAAGAT
ACATCTCAGACGCCTTTGCACTGTGAAAACCTAGACACCTTAGCTTTCATTTTGCCTCAC
AGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAGCATGACTCCTCATGGGTTGAAGAA
TTGTTAATGTTACACAGAGCACGGATCACAGATGTTGAGCACATCACTGGACTCAGCTTC
TATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTAAAGTTGAAAACACATTTGCCAACC
TTTAGCCAAGAAGACTGA
Enzyme 3 GenBank Gene ID NM_006208.2 Link Image
Enzyme 3 GeneCard ID ENPP1 Link Image
Enzyme 3 GenAtlas ID ENPP1 Link Image
Enzyme 3 HGNC ID HGNC:3356 Link Image
Enzyme 3 Chromosome Location 6
Enzyme 3 Locus 6q22-q23
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed Link Image]
  2. Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed Link Image]
  6. Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed Link Image]
  7. Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed Link Image]
  8. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed Link Image]
  9. Bello V, Goding JW, Greengrass V, Sali A, Dubljevic V, Lenoir C, Trugnan G, Maurice M: Characterization of a di-leucine-based signal in the cytoplasmic tail of the nucleotide-pyrophosphatase NPP1 that mediates basolateral targeting but not endocytosis. Mol Biol Cell. 2001 Oct;12(10):3004-15. [PubMed Link Image]
  10. Yano Y, Hayashi Y, Sano K, Nagano H, Nakaji M, Seo Y, Ninomiya T, Yoon S, Yokozaki H, Kasuga M: Expression and localization of ecto-nucleotide pyrophosphatase/phosphodiesterase I-1 (E-NPP1/PC-1) and -3 (E-NPP3/CD203c/PD-Ibeta/B10/gp130(RB13-6)) in inflammatory and neoplastic bile duct diseases. Cancer Lett. 2004 Apr 30;207(2):139-47. [PubMed Link Image]
  11. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  12. Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed Link Image]
  13. Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed Link Image]
  14. Rutsch F, Ruf N, Vaingankar S, Toliat MR, Suk A, Hohne W, Schauer G, Lehmann M, Roscioli T, Schnabel D, Epplen JT, Knisely A, Superti-Furga A, McGill J, Filippone M, Sinaiko AR, Vallance H, Hinrichs B, Smith W, Ferre M, Terkeltaub R, Nurnberg P: Mutations in ENPP1 are associated with 'idiopathic' infantile arterial calcification. Nat Genet. 2003 Aug;34(4):379-81. [PubMed Link Image]
  15. Cheng KS, Chen MR, Ruf N, Lin SP, Rutsch F: Generalized arterial calcification of infancy: different clinical courses in two affected siblings. Am J Med Genet A. 2005 Jul 15;136(2):210-3. [PubMed Link Image]
  16. Bacci S, Ludovico O, Prudente S, Zhang YY, Di Paola R, Mangiacotti D, Rauseo A, Nolan D, Duffy J, Fini G, Salvemini L, Amico C, Vigna C, Pellegrini F, Menzaghi C, Doria A, Trischitta V: The K121Q polymorphism of the ENPP1/PC-1 gene is associated with insulin resistance/atherogenic phenotypes, including earlier onset of type 2 diabetes and myocardial infarction. Diabetes. 2005 Oct;54(10):3021-5. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5781
Enzyme 4 Name Hormone-sensitive lipase
Enzyme 4 Synonyms
  1. HSL
Enzyme 4 Gene Name LIPE
Enzyme 4 Protein Sequence >Hormone-sensitive lipase
MEPGSKSVSRSDWQPEPHQRPITPLEPGPEKTPIAQPESKTLQGSNTQQKPASNQRPLTQ
QETPAQHDAESQKEPRAQQKSASQEEFLAPQKPAPQQSPYIQRVLLTQQEAASQQGPGLG
KESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAKPGAKREPSAPTESTSQET
PEQSDKQTTPVQGAKSKQGSLTELGFLTKLQELSIQRSALEWKALSEWVTDSESESDVGS
SSDTDSPATMGGMVAQGVKLGFKGKSGYKVMSGYSGTSPHEKTSARNHRHYQDTASRLIH
NMDLRTMTQSLVTLAEDNIAFFSSQGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAH
LFDLDPETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRTSHNLAELEAYLAALT
QLRALVYYAQRLLVTNRPGVLFFEGDEGLTADFLREYVTLHKGCFYGRCLGFQFTPAIRP
FLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWK
AFWNITEMEVLSSLANMASATVRVSRLLSLPPEAFEMPLTADPTLTVTISPPLAHTGPGP
VLVRLISYDLREGQDSEELSSLIKSNGQRSLELWPRPQQAPRSRSLIVHFHGGGFVAQTS
RSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGSTGERIC
LAGDSAGGNLCFTVALRAAAYGVRVPDGIMAAYPATMLQPAASPSRLLSLMDPLLPLSVL
SKCVSAYAGAKTEDHSNSDQKALGMMGLVRRDTALLLRDFRLGASSWLNSFLELSGRKSQ
KMSEPIAEPMRRSVSEAALAQPQGPLGTDSLKNLTLRDLSLRGNSETSSDTPEMSLSAET
LSPSTPSDVNFLLPPEDAGEEAEAKNELSPMDRGLGVRAAFPEGFHPRRSSQGATQMPLY
SSPIVKNPFMSPLLAPDSMLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVE
DLPHGFLTLAALCRETRQAAELCVERIRLVLTPPAGAGPSGETGAAGVDGGCGGRH
Enzyme 4 Number of Residues 1076
Enzyme 4 Molecular Weight 116596.7
Enzyme 4 Theoretical pI 6.68
Enzyme 4 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
Process
  • alcohol metabolic process
  • cholesterol metabolic process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • small molecule metabolic process
  • sterol metabolic process
Component
Enzyme 4 General Function Involved in hydrolase activity
Enzyme 4 Specific Function In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • (1) diacylglycerol + H2O = monoacylglycerol + a carboxylate [RN:R05209]
  • (2) triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
  • (3) monoacylglycerol + H2O = glycerol + a carboxylate [RN:R07293]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 47124456 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q05469 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name LIPS_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >3231 bp
ATGGAGCCAGGTTCTAAGTCAGTGTCTAGGTCAGACTGGCAACCTGAACCACACCAGAGG
CCTATAACCCCGCTAGAGCCTGGGCCAGAAAAGACACCCATAGCCCAGCCAGAATCGAAG
ACTCTGCAGGGATCCAATACCCAACAGAAGCCTGCTTCAAACCAAAGACCCCTCACCCAG
CAGGAGACCCCTGCACAACATGATGCTGAATCCCAGAAGGAACCTAGAGCCCAACAAAAA
TCTGCTTCACAAGAGGAATTTCTTGCCCCACAGAAGCCCGCACCACAGCAATCACCTTAC
ATCCAAAGGGTGCTGCTCACTCAACAGGAAGCTGCCTCCCAGCAGGGACCTGGGCTAGGA
AAAGAATCTATAACTCAACAGGAGCCAGCATTGAGACAAAGACATGTAGCCCAGCCAGGG
CCTGGGCCAGGAGAGCCACCTCCAGCTCAACAAGAAGCTGAATCAACACCTGCGGCCCAG
GCTAAACCTGGAGCCAAAAGGGAGCCATCTGCCCCGACTGAATCTACGTCCCAAGAGACA
CCTGAACAGTCAGACAAGCAAACAACGCCAGTCCAGGGAGCCAAATCCAAGCAGGGATCT
TTGACAGAGCTGGGATTTCTAACAAAACTTCAGGAACTATCCATACAGCGATCAGCCCTA
GAGTGGAAGGCACTTTCTGAGTGGGTCACAGATTCTGAGTCAGAATCAGATGTGGGATCA
TCTTCAGACACAGATTCTCCAGCCACGATGGGTGGAATGGTGGCCCAGGGAGTGAAGCTA
GGCTTCAAAGGAAAATCTGGTTATAAAGTGATGTCAGGATACAGTGGGACGTCGCCACAT
GAGAAAACCAGTGCTCGGAATCACAGACACTACCAGGATACAGCCTCAAGGCTCATCCAC
AACATGGACCTGCGCACAATGACACAGTCGCTGGTGACTCTGGCGGAGGACAACATAGCC
TTCTTCTCGAGCCAGGGTCCTGGGGAAACGGCCCAGCGGCTGTCAGGCGTTTTTGCCGGT
GTACGGGAGCAGGCGCTGGGGCTGGAGCCGGCCCTGGGCCGCCTGCTGGGTGTGGCGCAC
CTCTTTGACCTGGACCCAGAGACACCGGCCAACGGGTACCGCAGCCTAGTGCACACAGCC
CGCTGCTGCCTGGCGCACCTCCTGCACAAATCCCGCTATGTGGCCTCCAACCGCCGCAGC
ATCTTCTTCCGCACCAGCCACAACCTGGCCGAGCTGGAGGCCTACCTGGCTGCCCTCACC
CAGCTCCGCGCTCTGGTCTACTACGCCCAGCGCCTGCTGGTTACCAATCGGCCGGGGGTA
CTCTTCTTTGAGGGCGACGAGGGGCTCACCGCCGACTTCCTCCGGGAGTATGTCACGCTG
CATAAGGGATGCTTCTATGGCCGCTGCCTGGGCTTCCAGTTCACGCCTGCCATCCGGCCA
TTCCTGCAGACCATCTACATTGGGCTGGTGTCCTTCGGGGAGCACTACAAACGCAACGAG
ACAGGCCTCAGTGTGGCCGCCAGCTCTCTCTTCACCAGCGGCCGCTTTGCCATCGACCCC
GAGCTGCGTGGGGCTGAGTTTGAGCGGATCACACAGAACCTGGACGTGCACTTCTGGAAA
GCCTTCTGGAACATCACCGAGATGGAAGTGCTATCGTCTCTGGCCAACATGGCATCGGCC
ACCGTGAGGGTAAGCCGCCTGCTCAGCCTGCCACCCGAAGCCTTTGAGATGCCACTGACT
GCCGACCCCACGCTCACGGTCACCATCTCACCCCCACTGGCCCACACAGGCCCTGGGCCC
GTCCTCGTCAGGCTCATCTCCTGTGACCTGCGTGAAGGACAGGACAGTGAGGAGCTCAGC
AGCCTGATAAAGTCCAACGGCCAACGGAGCCTGGAGCTGTGGCCGCGCCCCCAGCAGGCA
CCCCGCTCGCGGTCCCTGATAGTGCACTTCCACGGCGGTGGCTTTGTGGCCCAGACCTCC
AGATCCCACGAGCCCTACCTCAAGAGCTGGGCCCAGGAGCTGGGCGCCCCCATCATCTCC
ATCGACTACTCCCTGGCCCCTGAGGCCCCCTTCCCCCGTGCGCTGGAGGAGTGCTTCTTC
GCCTACTGCTGGGCCATCAAGCACTGCGCCCTCCTTGGCTCAACAGGGGAACGAATCTGC
CTTGCGGGGGACAGTGCAGGCGGGAACCTCTGCTTCACCGTGGCTCTTCGGGCAGCAGCC
TACGGGGTGCGGGTGCCAGATGGCATCATGGCAGCCTACCCGGCCACAATGCTGCAGCCT
GCCGCCTCTCCCTCCCGCCTGCTGAGCCTCATGGACCCCTTGCTGCCCCTCAGTGTGCTC
TCCAAGTGTGTCAGCGCCTATGCTGGTGCAAAGACGGAGGACCACTCCAACTCAGACCAG
AAAGCCCTCGGCATGATGGGGCTGGTGCGGCGGGACACAGCCCTGCTCCTCCGAGACTTC
CGCCTGGGTGCCTCCTCATGGCTCAACTCCTTCCTGGAGTTAAGTGGGCGCAAGTCCCAG
AAGATGTCGGAGCCCATAGCAGAGCCGATGCGCCGCAGTGTGTCTGAAGCAGCACTGGCC
CAGCCCCAGGGCCCACTGGGCACGGATTCCCTCAAGAACCTGACCCTGAGGGACTTGAGC
CTGAGGGGAAACTCCGAGACGTCGTCGGACACCCCCGAGATGTCGCTGTCAGCTGAGACA
CTTAGCCCCTCCACACCCTCCGATGTCAACTTCTTATTACCACCTGAGGATGCAGGGGAA
GAGGCTGAGGCCAAAAATGAGCTGAGCCCCATGGACAGAGGCCTGGGCGTCCGTGCCGCC
TTCCCCGAGGGTTTCCACCCCCGACGCTCCAGCCAGGGTGCCACACAGATGCCCCTCTAC
TCCTCACCCATAGTCAAGAACCCCTTCATGTCGCCGCTGCTGGCACCCGACAGCATGCTC
AAGAGCCTGCCACCTGTGCACATCGTGGCGTGCGCGCTGGACCCCATGCTGGACGACTCG
GTCATGCTCGCGCGGCGACTGCGCAACCTGGGCCAGCCGGTGACGCTGCGCGTGGTGGAG
GACCTGCCGCACGGCTTCCTGACCCTAGCGGCGCTGTGCCGCGAGACGCGCCAGGCCGCA
GAGCTGTGCGTGGAGCGCATCCGCCTCGTCCTCACTCCTCCCGCCGGAGCCGGGCCGAGC
GGGGAGACGGGGGCTGCGGGGGTAGACGGGGGCTGCGGGGGGCGACACTAA
Enzyme 4 GenBank Gene ID BC070041 Link Image
Enzyme 4 GeneCard ID LIPE Link Image
Enzyme 4 GenAtlas ID LIPE Link Image
Enzyme 4 HGNC ID HGNC:6621 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 19q13.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Langin D, Laurell H, Holst LS, Belfrage P, Holm C: Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):4897-901. [PubMed Link Image]
  2. Holst LS, Langin D, Mulder H, Laurell H, Grober J, Bergh A, Mohrenweiser HW, Edgren G, Holm C: Molecular cloning, genomic organization, and expression of a testicular isoform of hormone-sensitive lipase. Genomics. 1996 Aug 1;35(3):441-7. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Aboulaich N, Ortegren U, Vener AV, Stralfors P: Association and insulin regulated translocation of hormone-sensitive lipase with PTRF. Biochem Biophys Res Commun. 2006 Nov 24;350(3):657-61. Epub 2006 Sep 28. [PubMed Link Image]
  5. Ortegren U, Yin L, Ost A, Karlsson H, Nystrom FH, Stralfors P: Separation and characterization of caveolae subclasses in the plasma membrane of primary adipocytes; segregation of specific proteins and functions. FEBS J. 2006 Jul;273(14):3381-92. Epub 2006 Jun 26. [PubMed Link Image]
  6. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  7. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5833
Enzyme 5 Name Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
Enzyme 5 Synonyms
  1. GMP-PDE gamma
Enzyme 5 Gene Name PDE6H
Enzyme 5 Protein Sequence >Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
MSDNTTLPAPASNQGPTTPRKGPPKFKQRQTRQFKSKPPKKGVKGFGDDIPGMEGLGTDI
TVICPWEAFSHLELHELAQFGII
Enzyme 5 Number of Residues 83
Enzyme 5 Molecular Weight 9074.4
Enzyme 5 Theoretical pI 9.98
Enzyme 5 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • GMP binding
  • binding
  • cGMP binding
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nucleoside binding
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • purine nucleoside binding
Process
  • multicellular organismal process
  • neurological system process
  • sensory perception
  • sensory perception of light stimulus
  • system process
  • visual perception
Component
Enzyme 5 General Function Involved in 3',5'-cyclic-nucleotide phosphodiesterase activity
Enzyme 5 Specific Function Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones
Enzyme 5 Pathways
Enzyme 5 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID Q13956 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name CNCG_HUMAN Link Image
Enzyme 5 PDB ID 1FQJ Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >252 bp
ATGAGTGACAACACTACTCTGCCTGCTCCAGCTTCAAACCAGGGTCCTACCACCCCACGC
AAAGGCCCTCCCAAGTTCAAGCAGAGGCAGACTCGCCAATTCAAGAGTAAACCTCCAAAG
AAAGGTGTGAAAGGATTTGGAGATGACATTCCAGGAATGGAGGGGCTAGGAACAGATATC
ACAGTGATTTGTCCATGGGAGGCATTCAGCCACCTGGAATTGCATGAGCTCGCTCAGTTT
GGGATTATCTGA
Enzyme 5 GenBank Gene ID D45399 Link Image
Enzyme 5 GeneCard ID PDE6H Link Image
Enzyme 5 GenAtlas ID PDE6H Link Image
Enzyme 5 HGNC ID HGNC:8790 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 12p13
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Shimizu-Matsumoto A, Itoh K, Inazawa J, Nishida K, Matsumoto Y, Kinoshita S, Matsubara K, Okubo K: Isolation and chromosomal localization of the human cone cGMP phosphodiesterase gamma cDNA (PDE6H). Genomics. 1996 Feb 15;32(1):121-4. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Piri N, Gao YQ, Danciger M, Mendoza E, Fishman GA, Farber DB: A substitution of G to C in the cone cGMP-phosphodiesterase gamma subunit gene found in a distinctive form of cone dystrophy. Ophthalmology. 2005 Jan;112(1):159-66. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5843
Enzyme 6 Name Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
Enzyme 6 Synonyms
  1. Cam-PDE 1A
  2. 61 kDa Cam-PDE
  3. hCam-1
Enzyme 6 Gene Name PDE1A
Enzyme 6 Protein Sequence >Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
MGSSATEIEELENTTFKYLTGEQTEKMWQRLKGILRCLVKQLERGDVNVVDLKKNIEYAA
SVLEAVYIDETRRLLDTEDELSDIQTDSVPSEVRDWLASTFTRKMGMTKKKPEEKPKFRS
IVHAVQAGIFVERMYRKTYHMVGLAYPAAVIVTLKDVDKWSFDVFALNEASGEHSLKFMI
YELFTRYDLINRFKIPVSCLITFAEALEVGYSKYKNPYHNLIHAADVTQTVHYIMLHTGI
MHWLTELEILAMVFAAAIHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLM
QEEEMNILINLSKDDWRDLRNLVIEMVLSTDMSGHFQQIKNIRNSLQQPEGIDRAKTMSL
ILHAADISHPAKSWKLHYRWTMALMEEFFLQGDKEAELGLPFSPLCDRKSTMVAQSQIGF
IDFIVEPTFSLLTDSTEKIVIPLIEEASKAETSSYVASSSTTIVGLHIADALRRSNTKGS
MSDGSYSPDYSLAAVDLKSFKNNLVDIIQQNKERWKELAAQEARTSSQKCEFIHQ
Enzyme 6 Number of Residues 535
Enzyme 6 Molecular Weight 61251.4
Enzyme 6 Theoretical pI 6.02
Enzyme 6 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 6 General Function Involved in catalytic activity
Enzyme 6 Specific Function Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a higher affinity for cGMP than for cAMP
Enzyme 6 Pathways
Enzyme 6 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 1151109 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P54750 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PDE1A_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1608 bp
ATGGGGTCTAGTGCCACAGAGATTGAAGAATTGGAAAACACCACTTTTAAGTATCTTACA
GGAGAACAGACTGAAAAAATGTGGCAGCGCCTGAAAGGAATACTAAGATGCTTGGTGAAG
CAGCTGGAAAGAGGTGATGTTAACGTCGTCGACTTAAAGAAGAATATTGAATATGCGGCA
TCTGTGCTGGAAGCAGTTTATATCGATGAAACAAGAAGACTTCTGGATACTGAAGATGAG
CTCAGTGACATTCAGACTGACTCAGTCCCATCTGAAGTCCGGGACTGGTTGGCTTCTACC
TTTACACGGAAAATGGGGATGACAAAAAAGAAACCTGAGGAAAAACCAAAATTTCGGAGC
ATTGTGCATGCTGTTCAAGCTGGAATTTTTGTGGAAAGAATGTACCGAAAAACATATCAT
ATGGTTGGTTTGGCATATCCAGCAGCTGTCATCGTAACATTAAAGGATGTTGATAAATGG
TCTTTCGATGTATTTGCCCTAAATGAAGCAAGTGGAGAGCATAGTCTGAAGTTTATGATT
TATGAACTGTTTACCAGATATGATCTTATCAACCGTTTCAAGATTCCTGTTTCTTGCCTA
ATCACCTTTGCAGAAGCTTTAGAAGTTGGTTACAGCAAGTACAAAAATCCATATCACAAT
TTGATTCATGCAGCTGATGTCACTCAAACTGTGCATTACATAATGCTTCATACAGGTATC
ATGCACTGGCTCACTGAACTGGAAATTTTAGCAATGGTCTTTGCTGCTGCCATTCATGAT
TATGAGCATACAGGGACAACAAACAACTTTCACATTCAGACAAGGTCAGATGTTGCCATT
TTGTATAATGATCGCTCTGTCCTTGAGAATCACCACGTGAGTGCAGCTTATCGACTTATG
CAAGAAGAAGAAATGAATATCTTGATAAATTTATCCAAAGATGACTGGAGGGATCTTCGG
AACCTAGTGATTGAAATGGTTTTATCTACAGACATGTCAGGTCACTTCCAGCAAATTAAA
AATATAAGAAACAGTTTGCAGCAGCCTGAAGGGATTGACAGAGCCAAAACCATGTCCCTG
ATTCTCCACGCAGCAGACATCAGCCACCCAGCCAAATCCTGGAAGCTGCATTATCGGTGG
ACCATGGCCCTAATGGAGGAGTTTTTCCTGCAGGGAGATAAAGAAGCTGAATTAGGGCTT
CCATTTTCCCCACTTTGTGATCGGAAGTCAACCATGGTGGCCCAGTCACAAATAGGTTTC
ATCGATTTCATAGTAGAGCCAACATTTTCTCTTCTGACAGACTCAACAGAGAAAATTGTT
ATTCCTCTTATAGAGGAAGCCTCAAAAGCCGAAACTTCTTCCTATGTGGCAAGCAGCTCA
ACCACCATTGTGGGGTTACACATTGCTGATGCACTAAGACGATCAAATACAAAAGGCTCC
ATGAGTGATGGGTCCTATTCCCCAGACTACTCCCTTGCAGCAGTGGACCTGAAGAGTTTC
AAGAACAACCTGGTGGACATCATTCAGCAGAACAAAGAGAGGTGGAAAGAGTTAGCTGCA
CAAGAAGCAAGAACCAGTTCACAGAAGTGTGAGTTTATTCATCAGTAA
Enzyme 6 GenBank Gene ID U40370 Link Image
Enzyme 6 GeneCard ID PDE1A Link Image
Enzyme 6 GenAtlas ID PDE1A Link Image
Enzyme 6 HGNC ID HGNC:8774 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 2q32.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Loughney K, Martins TJ, Harris EA, Sadhu K, Hicks JB, Sonnenburg WK, Beavo JA, Ferguson K: Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases. J Biol Chem. 1996 Jan 12;271(2):796-806. [PubMed Link Image]
  2. Michibata H, Yanaka N, Kanoh Y, Okumura K, Omori K: Human Ca2+/calmodulin-dependent phosphodiesterase PDE1A: novel splice variants, their specific expression, genomic organization, and chromosomal localization. Biochim Biophys Acta. 2001 Jan 26;1517(2):278-87. [PubMed Link Image]
  3. Fidock M, Miller M, Lanfear J: Isolation and differential tissue distribution of two human cDNAs encoding PDE1 splice variants. Cell Signal. 2002 Jan;14(1):53-60. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5847
Enzyme 7 Name High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name PDE8A
Enzyme 7 Protein Sequence >High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
MGCAPSIHISERLVAEDAPSPAAPPLSSGGPRLPQGQKTAALPRTRGAGLLESELRDGSG
KKVAVADVQFGPMRFHQDQLQVLLVFTKEDNQCNGFCRACEKAGFKCTVTKEAQAVLACF
LDKHHDIIIIDHRNPRQLDAEALCRSIRSSKLSENTVIVGVVRRVDREELSVMPFISAGF
TRRYVENPNIMACYNELLQLEFGEVRSQLKLRACNSVFTALENSEDAIEITSEDRFIQYA
NPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNI
QQNVKIIPVIGQGGKIRHYVSIIRVCNGNNKAEKISECVQSDTHTDNQTGKHKDRRKGSL
DVKAVASRATEVSSQRRHSSMARIHSMTIEAPITKVINIINAAQESSPMPVTEALDRVLE
ILRTTELYSPQFGAKDDDPHANDLVGGLMSDGLRRLSGNEYVLSTKNTQMVSSNIITPIS
LDDVPPRIARAMENEEYWDFDIFELEAATHNRPLIYLGLKMFARFGICEFLHCSESTLRS
WLQIIEANYHSSNPYHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDH
PGRTNSFLCNAGSELAILYNDTAVLESHHAALAFQLTTGDDKCNIFKNMERNDYRTLRQG
IIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKNQEVINTMLRTPENRTLIKRM
LIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPVVMPVFDRNTCSIPKSQIS
FIDYFITDMFDAWDAFVDLPDLMQHLDNNFKYWKGLDEMKLRNLRPPPE
Enzyme 7 Number of Residues 829
Enzyme 7 Molecular Weight 93303.1
Enzyme 7 Theoretical pI 6.03
Enzyme 7 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • molecular transducer activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • signal transducer activity
  • two-component response regulator activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • signal transduction
  • signal transmission
  • signaling process
  • two-component signal transduction system (phosphorelay)
Component
Enzyme 7 General Function Involved in catalytic activity
Enzyme 7 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development
Enzyme 7 Pathways
Enzyme 7 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID O60658 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PDE8A_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2490 bp
ATGGGCTGTGCCCCGAGCATCCACATTTCCGAGCGCCTGGTGGCCGAGGACGCGCCTAGC
CCCGCGGCACCGCCGCTGTCGTCCGGCGGGCCGCGCCTCCCGCAGGGCCAGAAGACGGCC
GCCTTGCCCCGGACCCGCGGCGCCGGCCTCTTGGAGTCGGAGCTTCGCGACGGCAGCGGC
AAGAAGGTAGCAGTAGCTGATGTGCAGTTTGGCCCCATGAGATTTCATCAAGATCAACTT
CAGGTACTTTTAGTGTTTACCAAAGAAGATAACCAATGTAATGGATTCTGCAGGGCATGT
GAAAAAGCAGGGTTTAAGTGTACAGTTACCAAGGAGGCTCAGGCTGTCCTTGCCTGTTTC
CTGGACAAACATCATGACATTATCATCATAGACCACAGAAATCCTCGACAGCTGGATGCA
GAGGCACTGTGCAGGTCTATCAGATCATCAAAACTCTCAGAAAACACAGTTATTGTTGGT
GTAGTACGCAGGGTGGATAGAGAAGAGTTGTCCGTAATGCCTTTCATTTCTGCTGGATTT
ACAAGGAGGTATGTAGAAAACCCCAACATCATGGCCTGCTACAATGAACTGCTCCAGCTG
GAGTTTGGAGAGGTGCGATCACAACTGAAACTCAGGGCTTGTAACTCAGTATTCACTGCA
TTAGAAAACAGTGAAGATGCAATTGAAATTACAAGCGAAGACCGTTTTATACAGTATGCA
AATCCTGCATTTGAAACAACAATGGGCTATCAGTCAGGTGAATTAATAGGGAAGGAGTTA
GGAGAAGTGCCTATAAATGAAAAAAAGGCTGACTTGCTCGATACTATAAATTCATGCATC
AGGATAGGCAAGGAGTGGCAAGGAATTTACTATGCAAAAAAGAAAAACGGAGATAATATA
CAACAAAATGTGAAGATAATACCTGTCATTGGACAGGGAGGAAAAATTAGACACTATGTG
TCCATTATCAGAGTGTGCAATGGCAACAATAAGGCTGAGAAAATATCCGAATGTGTTCAG
TCTGACACTCATACAGATAATCAGACAGGCAAACATAAAGACAGGAGAAAAGGCTCACTA
GACGTCAAAGCTGTTGCCTCCCGTGCAACTGAAGTTTCCAGCCAGAGACGACACTCTTCC
ATGGCCCGGATACATTCCATGACAATTGAGGCGCCCATCACCAAGGTAATCAATATTATC
AATGCTGCCCAGGAAAGTAGTCCCATGCCTGTGACAGAAGCCCTAGACCGTGTGCTGGAA
ATTCTAAGAACCACTGAGTTATATTCACCACAGTTTGGTGCTAAAGATGATGATCCCCAT
GCCAATGACCTTGTTGGGGGCTTAATGTCTGATGGTTTGCGAAGACTATCAGGGAATGAA
TATGTTCTTTCAACAAAAAACACTCAAATGGTTTCAAGCAATATAATCACTCCCATCTCC
CTTGATGATGTCCCACCACGGATAGCTCGGGCCATGGAAAATGAGGAATACTGGGACTTT
GATATTTTTGAACTGGAGGCTGCCACCCACAATAGGCCTTTGATTTATCTTGGTCTCAAA
ATGTTTGCTCGCTTTGGAATCTGTGAATTCTTACACTGCTCCGAGTCAACGCTAAGATCA
TGGTTACAAATTATCGAAGCCAATTATCATTCCTCCAATCCCTACCACAATTCTACACAT
TCTGCTGATGTGCTTCATGCCACTGCCTATTTTCTCTCCAAGGAGAGGATAAAGGAAACT
TTAGATCCAATTGATGAGGTCGCTGCACTCATCGCAGCCACCATTCATGATGTGGATCAC
CCTGGGAGAACCAACTCCTTCCTGTGTAATGCTGGAAGTGAGCTGGCCATTTTGTACAAT
GACACTGCTGTGCTGGAGAGCCACCATGCGGCCTTGGCCTTCCAGCTGACCACTGGAGAT
GATAAATGCAATATATTTAAAAACATGGAGAGGAATGATTATCGGACACTGCGCCAGGGG
ATTATCGACATGGTCTTAGCCACAGAAATGACAAAGCACTTTGAGCATGTCAACAAATTT
GTCAACAGCATCAACAAACCCTTGGCAACACTAGAAGAAAATGGGGAAACTGATAAAAAC
CAGGAAGTGATAAACACTATGCTTAGGACTCCAGAGAACCGGACCCTAATCAAACGAATG
CTGATTAAATGTGCTGATGTGTCCAATCCCTGCCGACCCCTGCAGTACTGCATCGAGTGG
GCTGCACGCATTTCGGAAGAATATTTTTCTCAGACTGATGAAGAGAAGCAGCAGGGCTTA
CCTGTGGTGATGCCAGTGTTTGACAGAAATACCTGCAGCATCCCCAAATCCCAAATCTCT
TTCATTGATTACTTCATCACAGACATGTTTGATGCTTGGGATGCCTTTGTAGACCTGCCT
GATTTAATGCAGCATCTTGACAACAACTTTAAATACTGGAAAGGACTGGACGAAATGAAG
CTGCGGAACCTCCGACCACCTCCTGAATAG
Enzyme 7 GenBank Gene ID AF388183 Link Image
Enzyme 7 GeneCard ID PDE8A Link Image
Enzyme 7 GenAtlas ID PDE8A Link Image
Enzyme 7 HGNC ID HGNC:8793 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 15q25.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Wang P, Wu P, Egan RW, Billah MM: Human phosphodiesterase 8A splice variants: cloning, gene organization, and tissue distribution. Gene. 2001 Dec 12;280(1-2):183-94. [PubMed Link Image]
  2. Glavas NA, Ostenson C, Schaefer JB, Vasta V, Beavo JA: T cell activation up-regulates cyclic nucleotide phosphodiesterases 8A1 and 7A3. Proc Natl Acad Sci U S A. 2001 May 22;98(11):6319-24. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Fisher DA, Smith JF, Pillar JS, St Denis SH, Cheng JB: Isolation and characterization of PDE8A, a novel human cAMP-specific phosphodiesterase. Biochem Biophys Res Commun. 1998 May 29;246(3):570-7. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Wang H, Yan Z, Yang S, Cai J, Robinson H, Ke H: Kinetic and structural studies of phosphodiesterase-8A and implication on the inhibitor selectivity. Biochemistry. 2008 Dec 2;47(48):12760-8. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5848
Enzyme 8 Name Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
Enzyme 8 Synonyms
  1. Cam-PDE 1B
  2. 63 kDa Cam-PDE
Enzyme 8 Gene Name PDE1B
Enzyme 8 Protein Sequence >Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
MELSPRSPPEMLEESDCPSPLELKSAPSKKMWIKLRSLLRYMVKQLENGEINIEELKKNL
EYTASLLEAVYIDETRQILDTEDELQELRSDAVPSEVRDWLASTFTQQARAKGRRAEEKP
KFRSIVHAVQAGIFVERMFRRTYTSVGPTYSTAVLNCLKNLDLWCFDVFSLNQAADDHAL
RTIVFELLTRHNLISRFKIPTVFLMSFLDALETGYGKYKNPYHNQIHAADVTQTVHCFLL
RTGMVHCLSEIELLAIIFAAAIHDYEHTGTTNSFHIQTKSECAIVYNDRSVLENHHISSV
FRLMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKTMKTALQQLERIDKPK
ALSLLLHAADISHPTKQWLVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQS
QIGFIDFIVEPTFSVLTDVAEKSVQPLADEDSKSKNQPSFQWRQPSLDVEVGDPNPDVVS
FRSTWVKRIQENKQKWKERAASGITNQMSIDELSPCEEEAPPSPAEDEHNQNGNLD
Enzyme 8 Number of Residues 536
Enzyme 8 Molecular Weight 61379.2
Enzyme 8 Theoretical pI 5.22
Enzyme 8 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 8 General Function Involved in catalytic activity
Enzyme 8 Specific Function Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a preference for cGMP as a substrate
Enzyme 8 Pathways
Enzyme 8 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID Q01064 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PDE1B_HUMAN Link Image
Enzyme 8 PDB ID 1TAZ Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1611 bp
ATGGAGCTGTCCCCCCGCAGTCCTCCGGAGATGCTGGAGGAGTCGGATTGCCCGTCACCC
CTGGAGCTGAAGTCAGCCCCCAGCAAGAAGATGTGGATTAAGCTTCGGTCTCTGCTGCGC
TACATGGTGAAGCAGTTGGAGAATGGGGAGATAAACATTGAGGAGCTGAAGAAAAATCTG
GAGTACACAGCTTCTCTGCTGGAAGCCGTCTACATAGATGAGACACGGCAAATCTTGGAC
ACGGAGGACGAGCTGCAGGAGCTGCGGTCAGATGCCGTGCCTTCGGAGGTGCGGGACTGG
CTGGCCTCCACCTTCACCCAGCAGGCCCGGGCCAAAGGCCGCCGAGCAGAGGAGAAGCCC
AAGTTCCGAAGCATTGTGCACGCTGTGCAGGCTGGGATCTTCGTGGAACGGATGTTCCGG
AGAACATACACCTCTGTGGGCCCCACTTACTCTACTGCGGTTCTCAACTGTCTCAAGAAC
CTGGATCTCTGGTGCTTTGATGTCTTTTCCTTGAACCAGGCAGCAGATGACCATGCCCTG
AGGACCATTGTTTTTGAGTTGCTGACTCGGCATAACCTCATCAGCCGCTTCAAGATTCCC
ACTGTGTTTTTGATGAGTTTCCTGGATGCCTTGGAGACAGGCTATGGGAAGTACAAGAAT
CCTTACCACAACCAGATCCACGCAGCCGATGTTACCCAGACAGTCCATTGCTTCTTGCTC
CGCACAGGGATGGTGCACTGCCTGTCGGAGATTGAGCTCCTGGCCATCATCTTTGCTGCA
GCTATCCATGATTATGAGCACACGGGCACTACCAACAGCTTCCACATCCAGACCAAGTCA
GAATGTGCCATCGTGTACAATGATCGTTCAGTGCTGGAGAATCACCACATCAGCTCTGTT
TTCCGATTGATGCAGGATGATGAGATGAACATTTTCATCAACCTCACCAAGGATGAGTTT
GTAGAACTCCGAGCCCTGGTCATTGAGATGGTGTTGGCCACAGACATGTCCTGCCATTTC
CAGCAAGTGAAGACCATGAAGACAGCCTTGCAACAGCTGGAGAGGATTGACAAGCCCAAG
GCCCTGTCTCTACTGCTCCATGCTGCTGACATCAGCCACCCAACCAAGCAGTGGTTGGTC
CACAGCCGTTGGACCAAGGCCCTCATGGAGGAATTCTTCCGTCAGGGTGACAAGGAGGCA
GAGTTGGGCCTGCCCTTTTCTCCACTCTGTGACCGCACTTCCACTCTAGTGGCACAGTCT
CAGATAGGGTTCATCGACTTCATTGTGGAGCCCACATTCTCTGTGCTGACTGACGTGGCA
GAGAAGAGTGTTCAGCCCCTGGCGGATGAGGACTCCAAGTCTAAAAACCAGCCCAGCTTT
CAGTGGCGCCAGCCCTCTCTGGATGTGGAAGTGGGAGACCCCAACCCTGATGTGGTCAGC
TTTCGTTCCACCTGGGTCAAGCGCATTCAGGAGAACAAGCAGAAATGGAAGGAACGGGCA
GCAAGTGGCATCACCAACCAGATGTCCATTGACGAGCTGTCCCCCTGTGAAGAAGAGGCC
CCCCCATCCCCTGCCGAAGATGAACACAACCAGAATGGGAATCTGGATTAG
Enzyme 8 GenBank Gene ID U56976 Link Image
Enzyme 8 GeneCard ID PDE1B Link Image
Enzyme 8 GenAtlas ID PDE1B Link Image
Enzyme 8 HGNC ID HGNC:8775 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 12q13
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Jiang X, Li J, Paskind M, Epstein PM: Inhibition of calmodulin-dependent phosphodiesterase induces apoptosis in human leukemic cells. Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):11236-41. [PubMed Link Image]
  2. Yu J, Wolda SL, Frazier AL, Florio VA, Martins TJ, Snyder PB, Harris EA, McCaw KN, Farrell CA, Steiner B, Bentley JK, Beavo JA, Ferguson K, Gelinas R: Identification and characterisation of a human calmodulin-stimulated phosphodiesterase PDE1B1. Cell Signal. 1997 Nov;9(7):519-29. [PubMed Link Image]
  3. Fidock M, Miller M, Lanfear J: Isolation and differential tissue distribution of two human cDNAs encoding PDE1 splice variants. Cell Signal. 2002 Jan;14(1):53-60. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Repaske DR, Swinnen JV, Jin SL, Van Wyk JJ, Conti M: A polymerase chain reaction strategy to identify and clone cyclic nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA encoding the 63-kDa calmodulin-dependent phosphodiesterase. J Biol Chem. 1992 Sep 15;267(26):18683-8. [PubMed Link Image]
  7. Zhang KY, Card GL, Suzuki Y, Artis DR, Fong D, Gillette S, Hsieh D, Neiman J, West BL, Zhang C, Milburn MV, Kim SH, Schlessinger J, Bollag G: A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases. Mol Cell. 2004 Jul 23;15(2):279-86. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5850
Enzyme 9 Name cGMP-inhibited 3',5'-cyclic phosphodiesterase B
Enzyme 9 Synonyms
  1. CGIPDE1
  2. CGIP1
  3. Cyclic GMP-inhibited phosphodiesterase B
  4. CGI-PDE B
Enzyme 9 Gene Name PDE3B
Enzyme 9 Protein Sequence >cGMP-inhibited 3',5'-cyclic phosphodiesterase B
MRRDERDAKAMRSLQPPDGAGSPPESLRNGYVKSCVSPLRQDPPRGFFFHLCRFCNVELR
PPPASPQQPRRCSPFCRARLSLGALAAFVLALLLGAEPESWAAGAAWLRTLLSVCSHSLS
PLFSIACAFFFLTCFLTRTKRGPGPGRSCGSWWLLALPACCYLGDFLVWQWWSWPWGDGD
AGSAAPHTPPEAAAGRLLLVLSCVGLLLTLAHPLRLRHCVLVLLLASFVWWVSFTSLGSL
PSALRPLLSGLVGGAGCLLALGLDHFFQIREAPLHPRLSSAAEEKVPVIRPRRRSSCVSL
GETAASYYGSCKIFRRPSLPCISREQMILWDWDLKQWYKPHYQNSGGGNGVDLSVLNEAR
NMVSDLLTDPSLPPQVISSLRSISSLMGAFSGSCRPKINPLTPFPGFYPCSEIEDPAEKG
DRKLNKGLNRNSLPTPQLRRSSGTSGLLPVEQSSRWDRNNGKRPHQEFGISSQGCYLNGP
FNSNLLTIPKQRSSSVSLTHHVGLRRAGVLSSLSPVNSSNHGPVSTGSLTNRSPIEFPDT
ADFLNKPSVILQRSLGNAPNTPDFYQQLRNSDSNLCNSCGHQMLKYVSTSESDGTDCCSG
KSGEEENIFSKESFKLMETQQEEETEKKDSRKLFQEGDKWLTEEAQSEQQTNIEQEVSLD
LILVEEYDSLIEKMSNWNFPIFELVEKMGEKSGRILSQVMYTLFQDTGLLEIFKIPTQQF
MNYFRALENGYRDIPYHNRIHATDVLHAVWYLTTRPVPGLQQIHNGCGTGNETDSDGRIN
HGRIAYISSKSCSNPDESYGCLSSNIPALELMALYVAAAMHDYDHPGRTNAFLVATNAPQ
AVLYNDRSVLENHHAASAWNLYLSRPEYNFLLHLDHVEFKRFRFLVIEAILATDLKKHFD
FLAEFNAKANDVNSNGIEWSNENDRLLVCQVCIKLADINGPAKVRDLHLKWTEGIVNEFY
EQGDEEANLGLPISPFMDRSSPQLAKLQESFITHIVGPLCNSYDAAGLLPGQWLEAEEDN
DTESGDDEDGEELDTEDEEMENNLNPKPPRRKSRRRIFCQLMHHLTENHKIWKEIVEEEE
KCKADGNKLQVENSSLPQADEIQVIEEADEEE
Enzyme 9 Number of Residues 1112
Enzyme 9 Molecular Weight 124332.1
Enzyme 9 Theoretical pI 5.75
Enzyme 9 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 9 General Function Involved in catalytic activity
Enzyme 9 Specific Function Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. May play a role in fat metabolism
Enzyme 9 Pathways
Enzyme 9 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • 88-108 117-137 152-172 192-212 220-240 247-267
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 1246755 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q13370 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PDE3B_HUMAN Link Image
Enzyme 9 PDB ID 1SOJ Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >3339 bp
ATGAGGAGGGACGAGCGAGACGCCAAAGCCATGCGGTCCCTGCAGCCGCCGGATGGGGCC
GGCTCGCCCCCCGAGAGTCTGAGGAACGGCTACGTGAAGAGCTGCGTGAGCCCCTTGCGG
CAGGACCCTCCGCGCGGCTTCTTCTTCCACCTCTGCCGCTTCTGCAACGTGGAGCTGCGG
CCGCCGCCGGCCTCTCCCCAGCAGCCGCGGCGCTGCTCCCCCTTCTGCCGGGCGCGCCTC
TCGCTGGGCGCCCTGGCTGTCTTTGTCCTCGCCCTGCTGCTGGGCGCGGAACCCGAGAGC
TGGGCTGCCGGGGCCGCCTGGCTGCGGACGCTGCTGAGCGTGTGTTCGCACAGCTTGAGC
CCCCTCTTCAGCATCGCCTGTGCCTTCTTCTTCCTCACCTGCTTCCTCACCCGGACCAAG
CGGGGACCCGGCCCGGGCCGGAGCTGCGGCTCCTGGTGGCTGCTGGCGCTGCCCGCCTGC
TGTTACCTGGGGGACTTCTTGGTGTGGCAGTGGTGGTCTTGGCCTTGGGGGGATGGCGAC
GCAGGGTCCGCGGCCCCGCACACGCCCCCGGAGGCGGCAGCGGGCAGGTTGCTGCTGGTG
CTGAGCTGCGTAGGGCTGCTGCTGACGCTCGCGCACCCGCTGCGGCTCCGGCACTGCGTT
CTGGTGCTGCTCCTGGCCAGCTTCGTCTGGTGGGTCTCCTTCACCAGCCTCGGGTCGCTG
CCCTCCGCCCTCAGGCCGCTGCTCTCCGGCCTGGTGGGGGGCGCTGGCTGCCTGCTGGCC
CTGGGGTTGGATCACTTCTTTCAAATCAGGGAAGCGCCTCTTCATCCTCGACTGTCCAGT
GCCGCCGAAGAAAAAGTGCCTGTGATCCGACCCCGGAGGAGGTCCAGCTGCGTGTCGTTA
GGAGAAACTGCAGCCAGTTACTATGGCAGTTGCAAAATATTCAGGAGACCGTCGTTGCCT
TGTATTTCCAGAGAACAGATGATTCTTTGGGATTGGGACTTAAAACAATGGTATAAGCCT
CATTATCAAAATTCTGGAGGTGGAAATGGAGTTGATCTTTCAGTGCTAAATGAGGCTCGC
AATATGGTGTCAGATCTTCTGACTGATCCAAGCCTTCCACCACAAGTCATTTCCTCTCTA
CGGAGTATTAGTAGCTTAATGGGTGCTTTCTCAGGTTCCTGTAGGCCAAAGATTAATCCT
CTCACACCATTTCCTGGATTTTACCCCTGTTCTGAAATAGAGGACCCAGCTGAGAAAGGG
GATAGAAAACTTAACAAGGGACTAAATAGGAATAGTTTGCCAACTCCACAGCTGAGGAGA
AGCTCAGGAACTTCAGGATTGCTACCTGTTGAACAGTCTTCAAGGTGGGATCGTAATAAT
GGCAAAAGGCCTCACCAAGAATTTGGCATTTCAAGTCAAGGATGCTATCTAAATGGGCCT
TTTAATTCAAATCTACTGACTATCCCGAAGCAAAGGTCATCTTCTGTATCACTGACTCAC
CATGTAGGTCTCAGAAGAGCTGGTGTTTTGTCCAGTCTGAGTCCTGTGAATTCTTCCAAC
CATGGACCAGTGTCTACTGGCTCTCTAACTAATCGATCACCCATAGAATTTCCTGATACT
GCTGATTTTCTTAATAAGCCAAGCGTTATCTTGCAGAGATCTCTGGGCAATGCACCTAAT
ACTCCAGATTTTTATCAGCAACTTAGAAATTCTGATAGCAATCTGTGTAACAGCTGTGGA
CATCAAATGCTGAAATATGTTTCAACATCTGAATCAGATGGTACAGATTGCTGCAGTGGA
AAATCAGGTGAAGAAGAAAACATTTTCTCGAAAGAATCATTCAAACTTATGGAAACTCAA
CAAGAAGAGGAAACAGAGAAGAAAGACAGCAGAAAATTATTTCAGGAAGGTGATAAGTGG
CTAACAGAAGAGGCACAGAGTGAACAGCAAACAAATATTGAACAGGAAGTATCACTGGAC
CTGATTTTAGTAGAAGAGTATGACTCATTAATAGAAAAGATGAGCAACTGGAATTTTCCA
ATTTTTGAACTTGTAGAAAAGATGGGAGAGAAATCAGGAAGGATTCTCAGTCAGGTTATG
TATACCTTATTTCAAGACACTGGTTTATTGGAAATATTTAAAATTCCCACTCAACAATTT
ATGAACTATTTTCGTGCATTAGAAAATGGCTATCGAGACATTCCTTATCACAATCGTATA
CATGCCACAGATGTGCTACATGCAGTTTGGTATCTGACAACGCGGCCAGTTCCTGGCTTA
CAGCAGATCCACAATGGTTGTGGAACAGGAAATGAAACAGATTCTGATGGTAGAATTAAC
CATGGGCGAATTGCTTATATTTCTTCGAAGAGCTGCTCTAATCCTGATGAGAGTTATGGC
TGCCTGTCTTCAAACATTCCTGCATTAGAATTGATGGCTCTATACGTGGCAGCTGCCATG
CATGATTATGATCACCCAGGGAGGACAAATGCATTTCTAGTGGCTACAAATGCCCCTCAG
GCAGTTTTATACAATGACAGATCTGTTCTGGAAAATCATCATGCTGCGTCAGCTTGGAAT
CTATATCTTTCTCGCCCAGAATACAACTTCCTTCTTCATCTTGATCATGTGGAATTCAAG
CGCTTTCGTTTTTTAGTCATTGAAGCAATCCTTGCTACGGATCTTAAAAAGCATTTTGAT
TTTCTCGCAGAATTCAATGCCAAGGCAAATGATGTAAATAGTAATGGCATAGAATGGAGT
AATGAAAATGATCGCCTCTTGGTATGCCAGGTGTGCATCAAACTGGCAGATATAAATGGC
CCAGCAAAAGTTCGAGACTTGCATTTGAAATGGACAGAAGGCATTGTCAATGAATTTTAT
GAGCAGGGAGATGAAGAAGCAAATCTTGGTCTGCCCATCAGTCCATTCATGGATCGTTCT
TCTCCTCAACTAGCAAAACTCCAAGAATCTTTTATCACCCACATAGTGGGTCCCCTGTGT
AACTCCTATGATGCTGCTGGTTTGCTACCAGGTCAGTGGTTAGAAGCAGAAGAGGATAAT
GATACTGAAAGTGGTGATGATGAAGACGGTGAAGAATTAGATACAGAAGATGAAGAAATG
GAAAACAATCTAAATCCAAAACCACCAAGAAGGAAAAGCAGACGGCGAATATTTTGTCAG
CTAATGCACCACCTCACTGAAAACCACAAGATATGGAAGGAAATCGTAGAGGAAGAAGAA
AAATGTAAAGCTGATGGGAATAAACTGCAGGTGGAGAATTCCTCCTTACCTCAAGCAGAT
GAGATTCAGGTAATTGAAGAGGCAGATGAAGAGGAATAG
Enzyme 9 GenBank Gene ID X95520 Link Image
Enzyme 9 GeneCard ID PDE3B Link Image
Enzyme 9 GenAtlas ID PDE3B Link Image
Enzyme 9 HGNC ID HGNC:8779 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 11p15.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Miki T, Taira M, Hockman S, Shimada F, Lieman J, Napolitano M, Ward D, Taira M, Makino H, Manganiello VC: Characterization of the cDNA and gene encoding human PDE3B, the cGIP1 isoform of the human cyclic GMP-inhibited cyclic nucleotide phosphodiesterase family. Genomics. 1996 Sep 15;36(3):476-85. [PubMed Link Image]
  2. Murata T, Taira M, Manganiello VC: Differential expression of cGMP-inhibited cyclic nucleotide phosphodiesterases in human hepatoma cell lines. FEBS Lett. 1996 Jul 15;390(1):29-33. [PubMed Link Image]
  3. Lobbert RW, Winterpacht A, Seipel B, Zabel BU: Molecular cloning and chromosomal assignment of the human homologue of the rat cGMP-inhibited phosphodiesterase 1 (PDE3A)--a gene involved in fat metabolism located at 11p 15.1. Genomics. 1996 Oct 15;37(2):211-8. [PubMed Link Image]
  4. Liu H, Tang JR, Choi YH, Napolitano M, Hockman S, Taira M, Degerman E, Manganiello VC: Importance of cAMP-response element-binding protein in regulation of expression of the murine cyclic nucleotide phosphodiesterase 3B (Pde3b) gene in differentiating 3T3-L1 preadipocytes. J Biol Chem. 2006 Jul 28;281(30):21096-113. Epub 2006 May 15. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Scapin G, Patel SB, Chung C, Varnerin JP, Edmondson SD, Mastracchio A, Parmee ER, Singh SB, Becker JW, Van der Ploeg LH, Tota MR: Crystal structure of human phosphodiesterase 3B: atomic basis for substrate and inhibitor specificity. Biochemistry. 2004 May 25;43(20):6091-100. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5862
Enzyme 10 Name High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A
Enzyme 10 Synonyms
  1. HCP1
  2. TM22
Enzyme 10 Gene Name PDE7A
Enzyme 10 Protein Sequence >High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A
MEVCYQLPVLPLDRPVPQHVLSRRGAISFSSSSALFGCPNPRQLSQRRGAISYDSSDQTA
LYIRMLGDVRVRSRAGFESERRGSHPYIDFRIFHSQSEIEVSVSARNIRRLLSFQRYLRS
SRFFRGTAVSNSLNILDDDYNGQAKCMLEKVGNWNFDIFLFDRLTNGNSLVSLTFHLFSL
HGLIEYFHLDMMKLRRFLVMIQEDYHSQNPYHNAVHAADVTQAMHCYLKEPKLANSVTPW
DILLSLIAAATHDLDHPGVNQPFLIKTNHYLATLYKNTSVLENHHWRSAVGLLRESGLFS
HLPLESRQQMETQIGALILATDISRQNEYLSLFRSHLDRGDLCLEDTRHRHLVLQMALKC
ADICNPCRTWELSKQWSEKVTEEFFHQGDIEKKYHLGVSPLCDRHTESIANIQIGFMTYL
VEPLFTEWARFSNTRLSQTMLGHVGLNKASWKGLQREQSSSEDTDAAFELNSQLLPQENR
LS
Enzyme 10 Number of Residues 482
Enzyme 10 Molecular Weight 55504.5
Enzyme 10 Theoretical pI 7.53
Enzyme 10 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 10 General Function Involved in 3',5'-cyclic-AMP phosphodiesterase activity
Enzyme 10 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May have a role in muscle signal transduction
Enzyme 10 Pathways
Enzyme 10 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
Enzyme 10 UniProtKB/Swiss-Prot ID Q13946 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PDE7A_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1449 bp
ATGGAAGTGTGTTACCAGCTGCCGGTACTGCCCCTGGACAGGCCGGTCCCCCAGCACGTC
CTCAGCCGCCGAGGAGCCATCAGCTTCAGCTCCAGCTCCGCTCTCTTCGGCTGCCCCAAT
CCCCGGCAGCTCTCTCAGAGGCGTGGAGCTATTTCCTATGACAGTTCTGATCAGACTGCA
TTATACATTCGTATGCTAGGAGATGTACGTGTAAGGAGCCGAGCAGGATTTGAATCAGAA
AGAAGAGGTTCTCACCCATATATTGATTTTCGTATTTTCCACTCTCAATCTGAAATTGAA
GTGTCTGTCTCTGCAAGGAATATCAGAAGGCTACTAAGTTTCCAGCGATATCTTAGATCT
TCACGCTTTTTTCGTGGTACTGCGGTTTCAAATTCCCTAAACATTTTAGATGATGATTAT
AATGGACAAGCCAAGTGTATGCTGGAAAAAGTTGGAAATTGGAATTTTGATATCTTTCTA
TTTGATAGACTAACAAATGGAAATAGTCTAGTAAGCTTAACCTTTCATTTATTTAGTCTT
CATGGATTAATTGAGTACTTCCATTTAGATATGATGAAACTTCGTAGATTTTTAGTTATG
ATTCAAGAAGATTACCACAGTCAAAATCCTTACCATAACGCAGTCCACGCTGCGGATGTT
ACTCAGGCCATGCACTGTTACTTAAAGGAACCTAAGCTTGCCAATTCTGTAACTCCTTGG
GATATCTTGCTGAGCTTAATTGCAGCTGCCACTCATGATCTGGATCATCCAGGTGTTAAT
CAACCTTTCCTTATTAAAACTAACCATTACTTGGCAACTTTATACAAGAATACCTCAGTA
CTGGAAAATCACCACTGGAGATCTGCAGTGGGCTTATTGAGAGAATCAGGCTTATTCTCA
CATCTGCCATTAGAAAGCAGGCAACAAATGGAGACACAGATAGGTGCTCTGATACTAGCC
ACAGACATCAGTCGCCAGAATGAGTATCTGTCTTTGTTTAGGTCCCATTTGGATAGAGGT
GATTTATGCCTAGAAGACACCAGACACAGACATTTGGTTTTACAGATGGCTTTGAAATGT
GCTGATATTTGTAACCCATGTCGGACGTGGGAATTAAGCAAGCAGTGGAGTGAAAAAGTA
ACGGAGGAATTCTTCCATCAAGGAGATATAGAAAAAAAATATCATTTGGGTGTGAGTCCA
CTTTGCGATCGTCACACTGAATCTATTGCCAACATCCAGATTGGTTTTATGACTTACCTA
GTGGAGCCTTTATTTACAGAATGGGCCAGGTTTTCCAATACAAGGCTATCCCAGACAATG
CTTGGACACGTGGGGCTGAATAAAGCCAGCTGGAAGGGACTGCAGAGAGAACAGTCGAGC
AGTGAGGACACTGATGCTGCATTTGAGTTGAACTCACAGTTATTACCTCAGGAAAATCGG
TTATCATAA
Enzyme 10 GenBank Gene ID L12052 Link Image
Enzyme 10 GeneCard ID PDE7A Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Michaeli T, Bloom TJ, Martins T, Loughney K, Ferguson K, Riggs M, Rodgers L, Beavo JA, Wigler M: Isolation and characterization of a previously undetected human cAMP phosphodiesterase by complementation of cAMP phosphodiesterase-deficient Saccharomyces cerevisiae. J Biol Chem. 1993 Jun 15;268(17):12925-32. [PubMed Link Image]
  2. Han P, Zhu X, Michaeli T: Alternative splicing of the high affinity cAMP-specific phosphodiesterase (PDE7A) mRNA in human skeletal muscle and heart. J Biol Chem. 1997 Jun 27;272(26):16152-7. [PubMed Link Image]
  3. Glavas NA, Ostenson C, Schaefer JB, Vasta V, Beavo JA: T cell activation up-regulates cyclic nucleotide phosphodiesterases 8A1 and 7A3. Proc Natl Acad Sci U S A. 2001 May 22;98(11):6319-24. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Asirvatham AL, Galligan SG, Schillace RV, Davey MP, Vasta V, Beavo JA, Carr DW: A-kinase anchoring proteins interact with phosphodiesterases in T lymphocyte cell lines. J Immunol. 2004 Oct 15;173(8):4806-14. [PubMed Link Image]
  8. Wang H, Liu Y, Chen Y, Robinson H, Ke H: Multiple elements jointly determine inhibitor selectivity of cyclic nucleotide phosphodiesterases 4 and 7. J Biol Chem. 2005 Sep 2;280(35):30949-55. Epub 2005 Jul 1. [PubMed Link Image]
  9. Castano T, Wang H, Campillo NE, Ballester S, Gonzalez-Garcia C, Hernandez J, Perez C, Cuenca J, Perez-Castillo A, Martinez A, Huertas O, Gelpi JL, Luque FJ, Ke H, Gil C: Synthesis, structural analysis, and biological evaluation of thioxoquinazoline derivatives as phosphodiesterase 7 inhibitors. ChemMedChem. 2009 May;4(5):866-76. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5872
Enzyme 11 Name cGMP-inhibited 3',5'-cyclic phosphodiesterase A
Enzyme 11 Synonyms
  1. Cyclic GMP-inhibited phosphodiesterase A
  2. CGI-PDE A
Enzyme 11 Gene Name PDE3A
Enzyme 11 Protein Sequence >cGMP-inhibited 3',5'-cyclic phosphodiesterase A
MAVPGDAARVRDKPVHSGVSQAPTAGRDCHHRADPASPRDSGCRGCWGDLVLQPLRSSRK
LSSALCAGSLSFLLALLVRLVRGEVGCDLEQCKEAAAAEEEEAAPGAEGGVFPGPRGGAP
GGGARLSPWLQPSALLFSLLCAFFWMGLYLLRAGVRLPLAVALLAACCGGEALVQIGLGV
GEDHLLSLPAAGVVLSCLAAATWLVLRLRLGVLMIALTSAVRTVSLISLERFKVAWRPYL
AYLAGVLGILLARYVEQILPQSAEAAPREHLGSQLIAGTKEDIPVFKRRRRSSSVVSAEM
SGCSSKSHRRTSLPCIPREQLMGHSEWDHKRGPRGSQSSGTSITVDIAVMGEAHGLITDL
LADPSLPPNVCTSLRAVSNLLSTQLTFQAIHKPRVNPVTSLSENYTCSDSEESSEKDKLA
IPKRLRRSLPPGLLRRVSSTWTTTTSATGLPTLEPAPVRRDRSTSIKLQEAPSSSPDSWN
NPVMMTLTKSRSFTSSYAISAANHVKAKKQSRPGALAKISPLSSPCSSPLQGTPASSLVS
KISAVQFPESADTTAKQSLGSHRALTYTQSAPDLSPQILTPPVICSSCGRPYSQGNPADE
PLERSGVATRTPSRTDDTAQVTSDYETNNNSDSSDIVQNEDETECLREPLRKASACSTYA
PETMMFLDKPILAPEPLVMDNLDSIMEQLNTWNFPIFDLVENIGRKCGRILSQVSYRLFE
DMGLFEAFKIPIREFMNYFHALEIGYRDIPYHNRIHATDVLHAVWYLTTQPIPGLSTVIN
DHGSTSDSDSDSGFTHGHMGYVFSKTYNVTDDKYGCLSGNIPALELMALYVAAAMHDYDH
PGRTNAFLVATSAPQAVLYNDRSVLENHHAAAAWNLFMSRPEYNFLINLDHVEFKHFRFL
VIEAILATDLKKHFDFVAKFNGKVNDDVGIDWTNENDRLLVCQMCIKLADINGPAKCKEL
HLQWTDGIVNEFYEQGDEEASLGLPISPFMDRSAPQLANLQESFISHIVGPLCNSYDSAG
LMPGKWVEDSDESGDTDDPEEEEEEAPAPNEEETCENNESPKKKTFKRRKIYCQITQHLL
QNHKMWKKVIEEEQRLAGIENQSLDQTPQSHSSEQIQAIKEEEEEKGKPRGEEIPTQKPD
Q
Enzyme 11 Number of Residues 1141
Enzyme 11 Molecular Weight 124978.1
Enzyme 11 Theoretical pI 5.87
Enzyme 11 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 11 General Function Involved in catalytic activity
Enzyme 11 Specific Function Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes
Enzyme 11 Pathways
Enzyme 11 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • 61-81 130-150 160-180 185-205 210-230 232-252
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 38201493 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q14432 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PDE3A_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >3426 bp
ATGGCAGTGCCCGGCGACGCTGCACGAGTCAGGGACAAGCCCGTCCACAGTGGGGTGAGT
CAAGCCCCCACGGCGGGCCGGGACTGCCACCATCGTGCGGACCCCGCATCGCCGCGGGAC
TCGGGCTGCCGTGGCTGCTGGGGAGACCTGGTGCTGCAGCCGCTCCGGAGCTCTCGGAAA
CTTTCCTCCGCGCTGTGCGCGGGCTCCCTATCCTTTCTGCTGGCGCTGCTGGTGAGGCTG
GTCCGCGGGGAGGTCGGCTGTGACCTGGAGCAGTGTAAGGAGGCGGCGGCGGCGGAGGAG
GAGGAAGCAGCCCCGGGAGCAGAAGGGGGCGTCTTCCCGGGGCCTCGGGGAGGTGCTCCC
GGGGGCGGTGCGCGGCTCAGCCCCTGGCTGCAGCCCTCGGCGCTGCTCTTCAGTCTCCTG
TGTGCCTTCTTCTGGATGGGCTTGTACCTCCTGCGCGCCGGGGTGCGCCTGCCTCTGGCT
GTCGCGCTGCTGGCCGCCTGCTGCGGGGGGGAAGCGCTCGTCCAGATTGGGCTGGGCGTC
GGGGAGGATCACTTACTCTCACTCCCCGCTGCGGGGGTGGTGCTCAGCTGCTTGGCCGCC
GCGACATGGCTGGTGCTGAGGCTGAGGCTGGGCGTCCTCATGATCGCCTTGACTAGCGCG
GTCAGGACCGTGTCCCTCATTTCCTTAGAGAGGTTCAAGGTCGCCTGGAGACCTTACCTG
GCGTACCTGGCCGGCGTGCTGGGGATCCTCTTGGCCAGGTACGTGGAACAAATCTTGCCG
CAGTCCGCGGAGGCGGCTCCAAGGGAGCATTTGGGGTCCCAGCTGATTGCTGGGACCAAG
GAAGATATCCCGGTGTTTAAGAGGAGGAGGCGGTCCAGCTCCGTCGTGTCCGCCGAGATG
TCCGGCTGCAGCAGCAAGTCCCATCGGAGGACCTCCCTGCCCTGTATACCGAGGGAACAG
CTCATGGGGCATTCAGAATGGGACCACAAACGAGGGCCAAGAGGATCACAGTCTTCAGGA
ACCAGTATTACTGTGGACATCGCCGTCATGGGCGAAGCCCACGGCCTCATTACCGACCTC
CTGGCAGACCCTTCTCTTCCACCAAACGTGTGCACATCCTTGAGAGCCGTGAGCAACTTG
CTCAGCACACAGCTCACCTTCCAGGCCATTCACAAGCCCAGAGTGAATCCCGTTACTTCG
CTCAGTGAAAACTATACCTGTTCTGACTCTGAAGAGAGCTCTGAAAAAGACAAGCTTGCT
ATTCCAAAGCGCCTGAGAAGGAGTTTGCCTCCTGGCTTGTTGAGACGAGTTTCTTCCACT
TGGACCACCACCACCTCGGCCACAGGTCTACCCACCTTGGAGCCTGCACCAGTACGGAGA
GACCGCAGCACCAGCATCAAACTGCAGGAAGCACCTTCATCCAGTCCTGATTCTTGGAAT
AATCCAGTGATGATGACCCTCACCAAAAGCAGATCCTTTACTTCATCCTATGCTATTTCT
GCAGCTAACCATGTAAAGGCTAAAAAGCAAAGTCGACCAGGTGCCCTCGCTAAAATTTCA
CCTCTTTCATCGCCCTGCTCCTCACCTCTCCAAGGGACTCCTGCCAGCAGCCTGGTCAGC
AAAATTTCTGCAGTGCAGTTTCCAGAATCTGCTGACACAACTGCCAAACAAAGCCTAGGT
TCTCACAGGGCCTTAACTTACACTCAGAGTGCCCCAGACCTATCCCCTCAAATCCTGACT
CCACCTGTTATATGTAGCAGCTGTGGCAGACCATATTCCCAAGGGAATCCTGCTGATGAG
CCCCTGGAGAGAAGTGGGGTAGCCACTCGGACACCAAGTCGAACAGATGACACTGCTCAA
GTTACCTCTGATTATGAAACCAATAACAACAGTGACAGCAGTGACATTGTACAGAATGAA
GATGAAACAGAGTGCCTGAGAGAGCCTCTGAGGAAAGCATCGGCTTGCAGCACCTATGCT
CCTGAGACCATGATGTTTCTGGACAAACCAATTCTTGCTCCCGAACCTCTTGTCATGGAT
AACCTGGACTCAATTATGGAGCAGCTAAATACTTGGAATTTTCCAATTTTTGATTTAGTG
GAAAATATAGGAAGAAAATGTGGCCGTATTCTTAGTCAGGTATCTTACAGACTTTTTGAA
GACATGGGCCTCTTTGAAGCTTTTAAAATTCCAATTAGGGAATTTATGAATTATTTTCAT
GCTTTGGAGATTGGATATAGGGATATTCCTTATCATAACAGAATCCATGCCACTGATGTT
TTACATGCTGTTTGGTATCTTACTACACAGCCTATTCCAGGCCTCTCAACTGTGATTAAT
GATCATGGTTCAACCAGTGATTCAGATTCTGACAGTGGATTTACACATGGACATATGGGA
TATGTATTCTCAAAAACGTATAATGTGACAGATGATAAATACGGATGTCTGTCTGGGAAT
ATCCCTGCCTTGGAGTTGATGGCGCTGTATGTGGCTGCAGCCATGCACGATTATGATCAT
CCAGGAAGGACTAATGCTTTCCTGGTTGCAACTAGTGCTCCTCAGGCGGTGCTATATAAC
GATCGTTCAGTTTTGGAGAATCATCACGCAGCTGCTGCATGGAATCTTTTCATGTCCCGG
CCAGAGTATAACTTCTTAATTAACCTTGACCATGTGGAATTTAAGCATTTCCGTTTCCTT
GTCATTGAAGCAATTTTGGCCACTGACCTGAAGAAACACTTTGACTTCGTAGCCAAATTT
AATGGCAAGGTAAATGATGATGTTGGAATAGATTGGACCAATGAAAATGATCGTCTACTG
GTTTGTCAAATGTGTATAAAGTTGGCTGATATCAATGGTCCAGCTAAATGTAAAGAACTC
CATCTTCAGTGGACAGATGGTATTGTCAATGAATTTTATGAACAGGGTGATGAAGAGGCC
AGCCTTGGATTACCCATAAGCCCCTTCATGGATCGTTCTGCTCCTCAGCTGGCCAACCTT
CAGGAATCCTTCATCTCTCACATTGTGGGGCCTCTGTGCAACTCCTATGATTCAGCAGGA
CTAATGCCTGGAAAATGGGTGGAAGACAGCGATGAGTCAGGAGATACTGATGACCCAGAA
GAAGAGGAGGAAGAAGCACCAGCACCAAATGAAGAGGAAACCTGTGAAAATAATGAATCT
CCAAAAAAGAAGACTTTCAAAAGGAGAAAAATCTACTGCCAAATAACTCAGCACCTCTTA
CAGAACCACAAGATGTGGAAGAAAGTCATTGAAGAGGAGCAACGGTTGGCAGGCATAGAA
AATCAATCCCTGGACCAGACCCCTCAGTCGCACTCTTCAGAACAGATCCAGGCTATCAAG
GAAGAAGAAGAAGAGAAAGGGAAACCAAGAGGCGAGGAGATACCAACCCAAAAGCCAGAC
CAGTGA
Enzyme 11 GenBank Gene ID M91667 Link Image
Enzyme 11 GeneCard ID PDE3A Link Image
Enzyme 11 GenAtlas ID PDE3A Link Image
Enzyme 11 HGNC ID HGNC:8778 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 12p12
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Meacci E, Taira M, Moos M Jr, Smith CJ, Movsesian MA, Degerman E, Belfrage P, Manganiello V: Molecular cloning and expression of human myocardial cGMP-inhibited cAMP phosphodiesterase. Proc Natl Acad Sci U S A. 1992 May 1;89(9):3721-5. [PubMed Link Image]
  2. Cheung PP, Xu H, McLaughlin MM, Ghazaleh FA, Livi GP, Colman RW: Human platelet cGI-PDE: expression in yeast and localization of the catalytic domain by deletion mutagenesis. Blood. 1996 Aug 15;88(4):1321-9. [PubMed Link Image]
  3. Kuthe A, Eckel H, Stief CG, Uckert S, Forssmann WG, Jonas U, Magert HJ: Molecular biological characterization of phosphodiesterase 3A from human corpus cavernosum. Chem Biol Interact. 1999 May 14;119-120:593-8. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Degerman E, Moos M Jr, Rascon A, Vasta V, Meacci E, Smith CJ, Lindgren S, Andersson KE, Belfrage P, Manganiello V: Single-step affinity purification, partial structure and properties of human platelet cGMP inhibited cAMP phosphodiesterase. Biochim Biophys Acta. 1994 Apr 13;1205(2):189-98. [PubMed Link Image]
  6. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  7. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  8. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5876
Enzyme 12 Name cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name PDE10A
Enzyme 12 Protein Sequence >cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
MRIEERKSQHLTGLTDEKVKAYLSLHPQVLDEFVSESVSAETVEKWLKRKNNKSEDESAP
KEVSRYQDTNMQGVVYELNSYIEQRLDTGGDNQLLLYELSSIIKIATKADGFALYFLGEC
NNSLCIFTPPGIKEGKPRLIPAGPITQGTTVSAYVAKSRKTLLVEDILGDERFPRGTGLE
SGTRIQSVLCLPIVTAIGDLIGILELYRHWGKEAFCLSHQEVATANLAWASVAIHQVQVC
RGLAKQTELNDFLLDVSKTYFDNIVAIDSLLEHIMIYAKNLVNADRCALFQVDHKNKELY
SDLFDIGEEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDAYADPRFNREVDLYT
GYTTRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHR
IRHSECIYRVTMEKLSYHSICTSEEWQGLMQFTLPVRLCKEIELFHFDIGPFENMWPGIF
VYMVHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAILQNNHTLFTD
LERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTVSILQLEGHNI
FSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLNNQSHRDRVIGLMM
TACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFY
NAVAIPCYTTLTQILPPTEPLLKACRDNLSQWEKVIRGEETATWISSPSVAQKAAASED
Enzyme 12 Number of Residues 779
Enzyme 12 Molecular Weight 88411.7
Enzyme 12 Theoretical pI 6.57
Enzyme 12 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 12 General Function Involved in catalytic activity
Enzyme 12 Specific Function Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate
Enzyme 12 Pathways
Enzyme 12 Reactions
  • guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID Q9Y233 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name PDE10_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >2340 bp
ATGAGGATAGAAGAGAGGAAATCCCAACATTTAACAGGTTTGACAGATGAAAAAGTGAAG
GCATATCTTTCTCTTCACCCCCAGGTATTAGATGAATTTGTATCTGAAAGTGTTAGTGCA
GAGACAGTAGAGAAATGGCTGAAGAGGAAGAACAACAAATCAGAAGATGAATCAGCTCCT
AAGGAAGTCAGCAGGTACCAAGATACGAATATGCAGGGAGTTGTATATGAACTAAACAGC
TATATAGAACAACGGTTGGACACAGGAGGAGACAACCAGCTACTCCTCTATGAACTGAGC
AGCATCATTAAAATAGCCACAAAAGCCGATGGATTTGCACTGTATTTCCTTGGAGAGTGC
AATAATAGCCTGTGTATATTCACGCCACCTGGGATAAAGGAAGGAAAACCCCGCCTCATC
CCTGCTGGGCCCATCACTCAGGGCACCACCGTCTCTGCTTATGTGGCCAAGTCCAGGAAA
ACACTGCTAGTAGAAGACATCCTTGGAGATGAACGATTTCCAAGAGGTACTGGACTGGAA
TCAGGGACTCGTATCCAGTCTGTTCTTTGCTTACCAATTGTCACTGCAATTGGTGACTTG
ATTGGTATTCTCGAGCTGTATCGGCACTGGGGCAAAGAAGCCTTCTGTCTTAGTCACCAG
GAGGTTGCAACAGCAAATCTTGCCTGGGCTTCAGTAGCAATACATCAGGTGCAGGTATGC
AGAGGCCTTGCCAAACAGACAGAATTGAATGACTTCCTACTCGACGTATCAAAAACATAT
TTTGATAACATAGTTGCAATAGATTCTCTACTTGAACACATAATGATATATGCAAAAAAC
CTGGTGAATGCCGATCGTTGTGCGCTTTTCCAGGTGGACCATAAGAACAAGGAGTTATAT
TCAGACCTTTTTGATATTGGAGAGGAAAAGGAAGGAAAACCTGTCTTCAAGAAGACCAAA
GAGATAAGATTTTCAATTGAGAAAGGAATTGCTGGCCAAGTAGCAAGAACAGGGGAAGTC
CTGAACATTCCAGATGCCTATGCAGACCCACGCTTTAACAGAGAAGTAGACTTGTACACA
GGCTACACCACGCGGAACATCCTGTGCATGCCCATCGTCAGCCGAGGCAGCGTGATAGGT
GTGGTGCAGATGGTCAACAAAATCAGTGGCAGTGCCTTCTCTAAAACAGATGAAAACAAC
TTCAAAATGTTTGCCGTCTTTTGTGCTTTAGCCTTACACTGTGCTAATATGTATCATAGA
ATTCGCCACTCAGAGTGCATTTACCGGGTAACGATGGAAAAGCTGTCCTACCATAGCATT
TGTACTTCAGAAGAGTGGCAAGGTCTCATGCAATTCACCCTTCCCGTGCGTCTCTGCAAA
GAAATTGAATTATTCCACTTTGACATTGGTCCTTTTGAAAACATGTGGCCTGGAATTTTT
GTCTACATGGTTCATCGGTCCTGTGGGACATCCTGCTTTGAGCTTGAAAAGTTGTGTCGT
TTTATTATGTCTGTGAAGAAGAACTATCGGCGGGTTCCTTATCACAACTGGAAGCATGCG
GTCACTGTAGCACACTGCATGTATGCCATACTTCAGAACAATCACACGCTTTTCACAGAC
CTTGAGCGCAAAGGACTGCTGATTGCGTGTCTGTGTCATGACCTGGACCACAGGGGCTTC
AGTAACAGCTACCTGCAGAAGTTCGACCACCCTCTGGCCGCTCTCTACTCCACTTCCACC
ATGGAGCAGCACCACTTCTCCCAGACTGTGTCCATCCTTCAGTTGGAAGGGCACAATATC
TTCTCCACTCTGAGCTCCAGTGAATATGAGCAGGTGCTTGAGATCATCCGCAAAGCCATC
ATTGCCACAGACCTTGCTTTATACTTTGGAAACAGGAAGCAGTTGGAAGAGATGTACCAG
ACCGGATCACTAAACCTTAATAATCAATCACATAGAGACCGTGTAATTGGTTTGATGATG
ACTGCCTGTGACCTTTGTTCTGTGACAAAACTGTGGCCCGTTACAAAATTGACGGCAAAT
GATATATATGCAGAATTCTGGGCTGAGGGTGATGAAATGAAGAAATTGGGAATACAGCCT
ATTCCTATGATGGACAGAGACAAGAAGGATGAAGTCCCCCAAGGCCAGCTTGGGTTCTAC
AATGCCGTGGCCATTCCCTGCTATACAACCCTTACCCAGATCCTCCCTCCCACGGAGCCT
CTTCTGAAAGCATGCAGGGATAATCTCAGTCAGTGGGAGAAGGTGATTCGAGGGGAGGAG
ACTGCAACCTGGATTTCATCCCCATCCGTGGCTCAGAAGGCAGCTGCATCTGAAGATTGA
Enzyme 12 GenBank Gene ID AB020593 Link Image
Enzyme 12 GeneCard ID PDE10A Link Image
Enzyme 12 GenAtlas ID PDE10A Link Image
Enzyme 12 HGNC ID HGNC:8772 Link Image
Enzyme 12 Chromosome Location 6
Enzyme 12 Locus 6q26
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Fujishige K, Kotera J, Michibata H, Yuasa K, Takebayashi S, Okumura K, Omori K: Cloning and characterization of a novel human phosphodiesterase that hydrolyzes both cAMP and cGMP (PDE10A). J Biol Chem. 1999 Jun 25;274(26):18438-45. [PubMed Link Image]
  2. Loughney K, Snyder PB, Uher L, Rosman GJ, Ferguson K, Florio VA: Isolation and characterization of PDE10A, a novel human 3', 5'-cyclic nucleotide phosphodiesterase. Gene. 1999 Jun 24;234(1):109-17. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Fujishige K, Kotera J, Yuasa K, Omori K: The human phosphodiesterase PDE10A gene genomic organization and evolutionary relatedness with other PDEs containing GAF domains. Eur J Biochem. 2000 Oct;267(19):5943-51. [PubMed Link Image]
  6. Gross-Langenhoff M, Hofbauer K, Weber J, Schultz A, Schultz JE: cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10 and cGMP for the tandem GAF domain of phosphodiesterase 11. J Biol Chem. 2006 Feb 3;281(5):2841-6. Epub 2005 Dec 5. [PubMed Link Image]
  7. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  8. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  9. Wang H, Liu Y, Hou J, Zheng M, Robinson H, Ke H: Structural insight into substrate specificity of phosphodiesterase 10. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5782-7. Epub 2007 Mar 26. [PubMed Link Image]
  10. Handa N, Mizohata E, Kishishita S, Toyama M, Morita S, Uchikubo-Kamo T, Akasaka R, Omori K, Kotera J, Terada T, Shirouzu M, Yokoyama S: Crystal structure of the GAF-B domain from human phosphodiesterase 10A complexed with its ligand, cAMP. J Biol Chem. 2008 Jul 11;283(28):19657-64. Epub 2008 May 13. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5877
Enzyme 13 Name Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
Enzyme 13 Synonyms
  1. Cam-PDE 1C
  2. hCam-3
Enzyme 13 Gene Name PDE1C
Enzyme 13 Protein Sequence >Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
MESPTKEIEEFESNSLKYLQPEQIEKIWLRLRGLRKYKKTSQRLRSLVKQLERGEASVVD
LKKNLEYAATVLESVYIDETRRLLDTEDELSDIQSDAVPSEVRDWLASTFTRQMGMMLRR
SDEKPRFKSIVHAVQAGIFVERMYRRTSNMVGLSYPPAVIEALKDVDKWSFDVFSLNEAS
GDHALKFIFYELLTRYDLISRFKIPISALVSFVEALEVGYSKHKNPYHNLMHAADVTQTV
HYLLYKTGVANWLTELEIFAIIFSAAIHDYEHTGTTNNFHIQTRSDPAILYNDRSVLENH
HLSAAYRLLQDDEEMNILINLSKDDWREFRTLVIEMVMATDMSCHFQQIKAMKTALQQPE
AIEKPKALSLMLHTADISHPAKAWDLHHRWTMSLLEEFFRQGDREAELGLPFSPLCDRKS
TMVAQSQVGFIDFIVEPTFTVLTDMTEKIVSPLIDETSQTGGTGQRRSSLNSISSSDAKR
SGVKTSGSEGSAPINNSVISVDYKSFKATWTEVVHINRERWRAKVPKEEKAKKEAEEKAR
LAAEEQQKEMEAKSQAEEGASGKAEKKTSGETKNQVNGTRANKSDNPRGKNSKAEKSSGE
QQQNGDFKDGKNKTDKKDHSNIGNDSKKTDGTKQRSHGSPAPSTSSTCRLTLPVIKPPLR
HFKRPAYASSSYAPSVSKKTDEHPARYKMLDQRIKMKKIQNISHNWNRK
Enzyme 13 Number of Residues 709
Enzyme 13 Molecular Weight 80759.7
Enzyme 13 Theoretical pI 9.31
Enzyme 13 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 13 General Function Involved in catalytic activity
Enzyme 13 Specific Function Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a high affinity for both cAMP and cGMP
Enzyme 13 Pathways
Enzyme 13 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 193786355 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q14123 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name PDE1C_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >2130 bp
ATGGAGTCGCCAACCAAGGAGATTGAAGAATTTGAGAGCAACTCTCTGAAATACCTGCAA
CCGGAACAGATCGAGAAAATCTGGCTTCGGCTCCGCGGGCTGAGGAAATATAAGAAAACG
TCCCAGAGATTACGGTCTTTGGTCAAACAATTAGAGAGAGGGGAAGCTTCAGTGGTAGAT
CTTAAGAAGAATTTGGAATATGCAGCCACAGTGCTTGAATCTGTGTATATTGATGAAACA
AGGAGACTCCTGGATACAGAGGATGAGCTCAGTGACATTCAGTCAGATGCTGTGCCTTCT
GAGGTCCGAGACTGGCTGGCCTCCACCTTCACGCGGCAGATGGGGATGATGCTCAGGAGG
AGCGACGAGAAGCCCCGGTTCAAGAGCATCGTTCACGCAGTGCAGGCTGGGATATTTGTG
GAGAGAATGTATAGACGGACATCAAACATGGTTGGACTGAGCTATCCACCAGCTGTTATT
GAGGCATTAAAGGATGTGGACAAGTGGTCCTTTGACGTCTTTTCCCTCAATGAGGCCAGT
GGGGATCATGCACTGAAATTTATTTTCTATGAACTACTCACACGTTATGATCTGATCAGC
CGTTTCAAGATCCCCATTTCTGCACTTGTCTCATTTGTGGAGGCCCTGGAAGTGGGATAC
AGCAAGCACAAAAATCCTTACCATAACTTAATGCACGCTGCCGATGTTACACAGACAGTG
CATTACCTCCTCTATAAGACAGGAGTGGCGAACTGGCTGACGGAGCTGGAGATCTTTGCT
ATAATCTTCTCAGCTGCCATCCATGACTACGAGCATACCGGAACCACCAACAATTTCCAC
ATTCAGACTCGGTCTGATCCAGCTATTCTGTATAATGACAGATCTGTACTGGAGAATCAC
CATTTAAGTGCAGCTTATCGCCTTCTGCAAGATGACGAGGAAATGAATATTTTGATTAAC
CTCTCAAAGGATGACTGGAGGGAGTTTCGAACCTTGGTAATTGAAATGGTGATGGCCACA
GATATGTCTTGTCACTTCCAACAAATCAAAGCAATGAAGACTGCTCTGCAGCAGCCAGAA
GCCATTGAAAAGCCAAAAGCCTTATCCCTTATGCTGCATACAGCAGATATTAGCCATCCA
GCAAAAGCATGGGACCTCCATCATCGCTGGACAATGTCACTCCTGGAGGAGTTCTTCAGA
CAGGGTGACAGAGAAGCAGAGCTGGGGCTGCCTTTTTCTCCTCTGTGTGACCGAAAGTCC
ACTATGGTTGCTCAGTCACAAGTAGGTTTCATTGATTTCATCGTGGAACCCACCTTCACT
GTGCTTACGGACATGACCGAGAAGATTGTGAGTCCATTAATCGATGAAACCTCTCAAACT
GGTGGGACAGGACAGAGGCGTTCGAGTTTGAATAGCATCAGCTCGTCAGATGCCAAGCGA
TCAGGTGTCAAGACCTCTGGTTCAGAGGGAAGTGCCCCGATCAACAATTCTGTCATCTCC
GTTGACTATAAGAGCTTTAAAGCTACTTGGACGGAAGTGGTGCACATCAATCGGGAGAGA
TGGAGGGCCAAGGTACCCAAAGAGGAGAAGGCCAAGAAGGAAGCAGAGGAAAAGGCTCGC
CTGGCCGCAGAGGAGCAGCAAAAGGAAATGGAAGCCAAAAGCCAGGCTGAAGAAGGCGCA
TCCGGCAAAGCTGAGAAAAAGACGTCTGGAGAAACTAAGAATCAAGTCAATGGAACACGG
GCAAACAAAAGTGACAACCCTCGTGGGAAAAATTCCAAAGCCGAGAAGTCATCAGGAGAA
CAGCAACAGAATGGTGACTTCAAAGATGGTAAAAATAAGACAGACAAGAAGGATCACTCT
AACATCGGAAATGATTCAAAGAAAACAGATGGCACAAAACAGCGTTCTCACGGCTCACCA
GCCCCAAGCACCAGCTCCACGTGTCGCCTTACGTTGCCAGTCATCAAGCCTCCTTTGCGT
CATTTTAAACGCCCTGCTTACGCATCTAGCTCCTATGCACCTTCAGTCTCAAAGAAAACT
GATGAGCATCCTGCAAGGTACAAGATGCTGGATCAGAGGATCAAAATGAAAAAGATTCAG
AACATCTCACATAACTGGAACAGAAAATAG
Enzyme 13 GenBank Gene ID AK056170 Link Image
Enzyme 13 GeneCard ID PDE1C Link Image
Enzyme 13 GenAtlas ID PDE1C Link Image
Enzyme 13 HGNC ID HGNC:8776 Link Image
Enzyme 13 Chromosome Location 7
Enzyme 13 Locus 7p14.3
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Loughney K, Martins TJ, Harris EA, Sadhu K, Hicks JB, Sonnenburg WK, Beavo JA, Ferguson K: Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases. J Biol Chem. 1996 Jan 12;271(2):796-806. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5881
Enzyme 14 Name cAMP-specific 3',5'-cyclic phosphodiesterase 4B
Enzyme 14 Synonyms
  1. DPDE4
  2. PDE32
Enzyme 14 Gene Name PDE4B
Enzyme 14 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 4B
MKKSRSVMTVMADDNVKDYFECSLSKSYSSSSNTLGIDLWRGRRCCSGNLQLPPLSQRQS
ERARTPEGDGISRPTTLPLTTLPSIAITTVSQECFDVENGPSPGRSPLDPQASSSAGLVL
HATFPGHSQRRESFLYRSDSDYDLSPKAMSRNSSLPSEQHGDDLIVTPFAQVLASLRSVR
NNFTILTNLHGTSNKRSPAASQPPVSRVNPQEESYQKLAMETLEELDWCLDQLETIQTYR
SVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQNDVEIPSPTQKDREKKK
KQQLMTQISGVKKLMHSSSLNNTSISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSH
NRPLTCIMYAIFQERDLLKTFRISSDTFITYMMTLEDHYHSDVAYHNSLHAADVAQSTHV
LLSTPALDAVFTDLEILAAIFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHL
AVGFKLLQEEHCDIFMNLTKKQRQTLRKMVIDMVLATDMSKHMSLLADLKTMVETKKVTS
SGVLLLDNYTDRIQVLRNMVHCADLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEI
SPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILDTLEDNRNWYQSMIPQSP
SPPLDEQNRDCQGLMEKFQFELTLDEEDSEGPEKEGEGHSYFSSTKTLCVIDPENRDSLG
ETDIDIATEDKSPVDT
Enzyme 14 Number of Residues 736
Enzyme 14 Molecular Weight 83342.7
Enzyme 14 Theoretical pI 4.89
Enzyme 14 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 14 General Function Involved in catalytic activity
Enzyme 14 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in mediating central nervous system effects of therapeutic agents ranging from antidepressants to antiasthmatic and anti-inflammatory agents
Enzyme 14 Pathways
Enzyme 14 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
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 Q07343 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name PDE4B_HUMAN Link Image
Enzyme 14 PDB ID 1TB5 Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >2211 bp
ATGAAGAAAAGCAGGAGTGTGATGACGGTGATGGCTGATGATAATGTTAAAGATTATTTT
GAATGTAGCTTGAGTAAATCCTACAGTTCTTCCAGTAACACACTTGGGATCGACCTCTGG
AGAGGGAGAAGGTGTTGCTCAGGAAACTTACAGTTACCACCACTGTCTCAAAGACAGAGT
GAAAGGGCAAGGACTCCTGAGGGAGATGGTATTTCCAGGCCGACCACACTGCCTTTGACA
ACGCTTCCAAGCATTGCTATTACAACTGTAAGCCAGGAGTGCTTTGATGTGGAAAATGGC
CCTTCCCCAGGTCGGAGTCCACTGGATCCCCAGGCCAGCTCTTCCGCTGGGCTGGTACTT
CACGCCACCTTTCCTGGGCACAGCCAGCGCAGAGAGTCATTTCTCTACAGATCAGACAGC
GACTATGACTTGTCACCAAAGGCGATGTCGAGAAACTCTTCTCTTCCAAGCGAGCAACAC
GGCGATGACTTGATTGTAACTCCTTTTGCCCAGGTCCTTGCCAGCTTGCGAAGTGTGAGA
AACAACTTCACTATACTGACAAACCTTCATGGTACATCTAACAAGAGGTCCCCAGCTGCT
AGTCAGCCTCCTGTCTCCAGAGTCAACCCACAAGAAGAATCTTATCAAAAATTAGCAATG
GAAACGCTGGAGGAATTAGACTGGTGTTTAGACCAGCTAGAGACCATACAGACCTACCGG
TCTGTCAGTGAGATGGCTTCTAACAAGTTCAAAAGAATGCTGAACCGGGAGCTGACACAC
CTCTCAGAGATGAGCCGATCAGGGAACCAGGTGTCTGAATACATTTCAAATACTTTCTTA
GACAAGCAGAATGATGTGGAGATCCCATCTCCTACCCAGAAAGACAGGGAGAAAAAGAAA
AAGCAGCAGCTCATGACCCAGATAAGTGGAGTGAAGAAATTAATGCATAGTTCAAGCCTA
AACAATACAAGCATCTCACGCTTTGGAGTCAACACTGAAAATGAAGATCACCTGGCCAAG
GAGCTGGAAGACCTGAACAAATGGGGTCTTAACATCTTTAATGTGGCTGGATATTCTCAC
AATAGACCCCTAACATGCATCATGTATGCTATATTCCAGGAAAGAGACCTCCTAAAGACA
TTCAGAATCTCATCTGACACATTTATAACCTACATGATGACTTTAGAAGACCATTACCAT
TCTGACGTGGCATATCACAACAGCCTGCACGCTGCTGATGTAGCCCAGTCGACCCATGTT
CTCCTTTCTACACCAGCATTAGACGCTGTCTTCACAGATTTGGAGATCCTGGCTGCCATT
TTTGCAGCTGCCATCCATGACGTTGATCATCCTGGAGTCTCCAATCAGTTTCTCATCAAC
ACAAATTCAGAACTTGCTTTGATGTATAATGATGAATCTGTGTTGGAAAATCATCACCTT
GCTGTGGGTTTCAAACTGCTGCAAGAAGAACACTGTGACATCTTCATGAATCTCACCAAG
AAGCAGCGTCAGACACTCAGGAAGATGGTTATTGACATGGTGTTAGCAACTGATATGTCT
AAACATATGAGCCTGCTGGCAGACCTGAAGACAATGGTAGAAACGAAGAAAGTTACAAGT
TCAGGCGTTCTTCTCCTAGACAACTATACCGATCGCATTCAGGTCCTTCGCAACATGGTA
CACTGTGCAGACCTGAGCAACCCCACCAAGTCCTTGGAATTGTATCGGCAATGGACAGAC
CGCATCATGGAGGAATTTTTCCAGCAGGGAGACAAAGAGCGGGAGAGGGGAATGGAAATT
AGCCCAATGTGTGATAAACACACAGCTTCTGTGGAAAAATCCCAGGTTGGTTTCATCGAC
TACATTGTCCATCCATTGTGGGAGACATGGGCAGATTTGGTACAGCCTGATGCTCAGGAC
ATTCTCGATACCTTAGAAGATAACAGGAACTGGTATCAGAGCATGATACCTCAAAGTCCC
TCACCACCACTGGACGAGCAGAACAGGGACTGCCAGGGTCTGATGGAGAAGTTTCAGTTT
GAACTGACTCTCGATGAGGAAGATTCTGAAGGACCTGAGAAGGAGGGAGAGGGACACAGC
TATTTCAGCAGCACAAAGACGCTTTGTGTGATTGATCCAGAAAACAGAGATTCCCTGGGA
GAGACTGACATAGACATTGCAACAGAAGACAAGTCCCCCGTGGATACATAA
Enzyme 14 GenBank Gene ID L20966 Link Image
Enzyme 14 GeneCard ID PDE4B Link Image
Enzyme 14 GenAtlas ID PDE4B Link Image
Enzyme 14 HGNC ID HGNC:8781 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 1p31
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed Link Image]
  2. Huston E, Lumb S, Russell A, Catterall C, Ross AH, Steele MR, Bolger GB, Perry MJ, Owens RJ, Houslay MD: Molecular cloning and transient expression in COS7 cells of a novel human PDE4B cAMP-specific phosphodiesterase, HSPDE4B3. Biochem J. 1997 Dec 1;328 ( Pt 2):549-58. [PubMed Link Image]
  3. McLaughlin MM, Cieslinski LB, Burman M, Torphy TJ, Livi GP: A low-Km, rolipram-sensitive, cAMP-specific phosphodiesterase from human brain. Cloning and expression of cDNA, biochemical characterization of recombinant protein, and tissue distribution of mRNA. J Biol Chem. 1993 Mar 25;268(9):6470-6. [PubMed Link Image]
  4. Xu RX, Hassell AM, Vanderwall D, Lambert MH, Holmes WD, Luther MA, Rocque WJ, Milburn MV, Zhao Y, Ke H, Nolte RT: Atomic structure of PDE4: insights into phosphodiesterase mechanism and specificity. Science. 2000 Jun 9;288(5472):1822-5. [PubMed Link Image]
  5. Xu RX, Rocque WJ, Lambert MH, Vanderwall DE, Luther MA, Nolte RT: Crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and rolipram. J Mol Biol. 2004 Mar 19;337(2):355-65. [PubMed Link Image]
  6. Zhang KY, Card GL, Suzuki Y, Artis DR, Fong D, Gillette S, Hsieh D, Neiman J, West BL, Zhang C, Milburn MV, Kim SH, Schlessinger J, Bollag G: A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases. Mol Cell. 2004 Jul 23;15(2):279-86. [PubMed Link Image]
  7. Card GL, England BP, Suzuki Y, Fong D, Powell B, Lee B, Luu C, Tabrizizad M, Gillette S, Ibrahim PN, Artis DR, Bollag G, Milburn MV, Kim SH, Schlessinger J, Zhang KY: Structural basis for the activity of drugs that inhibit phosphodiesterases. Structure. 2004 Dec;12(12):2233-47. [PubMed Link Image]
  8. Card GL, Blasdel L, England BP, Zhang C, Suzuki Y, Gillette S, Fong D, Ibrahim PN, Artis DR, Bollag G, Milburn MV, Kim SH, Schlessinger J, Zhang KY: A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design. Nat Biotechnol. 2005 Feb;23(2):201-7. Epub 2005 Jan 30. [PubMed Link Image]
  9. Wang H, Peng MS, Chen Y, Geng J, Robinson H, Houslay MD, Cai J, Ke H: Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors. Biochem J. 2007 Dec 1;408(2):193-201. [PubMed Link Image]
  10. Hamblin JN, Angell TD, Ballantine SP, Cook CM, Cooper AW, Dawson J, Delves CJ, Jones PS, Lindvall M, Lucas FS, Mitchell CJ, Neu MY, Ranshaw LE, Solanke YE, Somers DO, Wiseman JO: Pyrazolopyridines as a novel structural class of potent and selective PDE4 inhibitors. Bioorg Med Chem Lett. 2008 Jul 15;18(14):4237-41. Epub 2008 May 17. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5884
Enzyme 15 Name cAMP-specific 3',5'-cyclic phosphodiesterase 7B
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name PDE7B
Enzyme 15 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 7B
MSCLMVERCGEILFENPDQNAKCVCMLGDIRLRGQTGVRAERRGSYPFIDFRLLNSTTYS
GEIGTKKKVKRLLSFQRYFHASRLLRGIIPQAPLHLLDEDYLGQARHMLSKVGMWDFDIF
LFDRLTNGNSLVTLLCHLFNTHGLIHHFKLDMVTLHRFLVMVQEDYHSQNPYHNAVHAAD
VTQAMHCYLKEPKLASFLTPLDIMLGLLAAAAHDVDHPGVNQPFLIKTNHHLANLYQNMS
VLENHHWRSTIGMLRESRLLAHLPKEMTQDIEQQLGSLILATDINRQNEFLTRLKAHLHN
KDLRLEDAQDRHFMLQIALKCADICNPCRIWEMSKQWSERVCEEFYRQGELEQKFELEIS
PLCNQQKDSIPSIQIGFMSYIVEPLFREWAHFTGNSTLSENMLGHLAHNKAQWKSLLPRQ
HRSRGSSGSGPDHDHAGQGTESEEQEGDSP
Enzyme 15 Number of Residues 450
Enzyme 15 Molecular Weight 51834.9
Enzyme 15 Theoretical pI 7.03
Enzyme 15 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 15 General Function Involved in catalytic activity
Enzyme 15 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in the control of cAMP-mediated neural activity and cAMP metabolism in the brain
Enzyme 15 Pathways
Enzyme 15 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 8439497 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q9NP56 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name PDE7B_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1353 bp
ATGTCTTGTTTAATGGTTGAGAGGTGTGGCGAAATCTTGTTTGAGAACCCCGATCAGAAT
GCCAAATGTGTTTGCATGCTGGGAGATATACGACTAAGGGGTCAGACGGGGGTTCGTGCT
GAACGCCGTGGCTCCTACCCATTCATTGACTTCCGCCTACTTAACAGTACAACATACTCA
GGGGAGATTGGCACCAAGAAAAAGGTGAAAAGACTATTAAGCTTTCAAAGATACTTCCAT
GCATCAAGGCTGCTTCGTGGAATTATACCACAAGCCCCTCTGCACCTGCTGGATGAAGAC
TACCTTGGACAAGCAAGGCATATGCTCTCCAAAGTGGGAATGTGGGATTTTGACATTTTC
TTGTTTGATCGCTTGACAAATGGAAACAGCCTGGTAACACTGTTGTGCCACCTCTTCAAT
ACCCATGGACTCATTCACCATTTCAAGTTAGATATGGTGACCTTACACCGATTTTTAGTC
ATGGTTCAAGAAGATTACCACAGCCAAAACCCGTATCACAATGCTGTTCACGCAGCCGAC
GTCACCCAGGCCATGCACTGCTACCTGAAAGAGCCAAAGCTTGCCAGCTTCCTCACGCCT
CTGGACATCATGCTTGGACTGCTGGCTGCAGCAGCACACGATGTGGACCACCCAGGGGTG
AACCAGCCATTTTTGATAAAAACTAACCACCATCTTGCAAACCTATATCAGAATATGTCT
GTGCTGGAGAATCATCACTGGCGATCTACAATTGGCATGCTTCGAGAATCAAGGCTTCTT
GCTCATTTGCCAAAGGAAATGACACAGGATATTGAACAGCAGCTGGGCTCCTTGATCTTG
GCAACAGACATCAACAGGCAGAATGAATTTTTGACCAGATTGAAAGCTCACCTCCACAAT
AAAGACTTAAGACTGGAGGATGCACAGGACAGGCACTTTATGCTTCAGATCGCCTTGAAG
TGTGCTGACATTTGCAATCCTTGTAGAATCTGGGAGATGAGCAAGCAGTGGAGTGAAAGG
GTCTGTGAAGAATTCTACAGGCAAGGTGAACTTGAACAGAAATTTGAACTGGAAATCAGT
CCTCTTTGTAATCAACAGAAAGATTCCATCCCTAGTATACAAATTGGTTTCATGAGCTAC
ATCGTGGAGCCGCTCTTCCGGGAATGGGCCCATTTCACGGGTAACAGCACCCTGTCGGAG
AACATGCTGGGCCACCTCGCACACAACAAGGCCCAGTGGAAGAGCCTGTTGCCCAGGCAG
CACAGAAGCAGGGGCAGCAGTGGCAGCGGGCCTGACCACGACCACGCAGGCCAAGGGACT
GAGAGCGAGGAGCAGGAAGGCGACAGCCCCTAG
Enzyme 15 GenBank Gene ID AB038040 Link Image
Enzyme 15 GeneCard ID PDE7B Link Image
Enzyme 15 GenAtlas ID PDE7B Link Image
Enzyme 15 HGNC ID HGNC:8792 Link Image
Enzyme 15 Chromosome Location 6
Enzyme 15 Locus 6q23-q24
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Sasaki T, Kotera J, Yuasa K, Omori K: Identification of human PDE7B, a cAMP-specific phosphodiesterase. Biochem Biophys Res Commun. 2000 May 19;271(3):575-83. [PubMed Link Image]
  2. Gardner C, Robas N, Cawkill D, Fidock M: Cloning and characterization of the human and mouse PDE7B, a novel cAMP-specific cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun. 2000 May 27;272(1):186-92. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  6. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5888
Enzyme 16 Name High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name PDE9A
Enzyme 16 Protein Sequence >High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAM
VSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRRE
GAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANH
LAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDV
PTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLF
CVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYN
NTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLI
LATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCL
LEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIML
QPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA
Enzyme 16 Number of Residues 593
Enzyme 16 Molecular Weight 68491.9
Enzyme 16 Theoretical pI 6.10
Enzyme 16 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 16 General Function Involved in catalytic activity
Enzyme 16 Specific Function Hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions
  • guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID O76083 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name PDE9A_HUMAN Link Image
Enzyme 16 PDB ID 1TBM Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1782 bp
ATGGGATCCGGCTCCTCCAGCTACCGGCCCAAGGCCATCTACCTGGACATCGATGGACGC
ATTCAGAAGGTAATCTTCAGCAAGTACTGCAACTCCAGCGACATCATGGACCTGTTCTGC
ATCGCCACCGGCCTGCCTCGGAACACGACCATCTCCCTGCTGACCACCGACGACGCCATG
GTCTCCATCGACCCCACCATGCCCGCGAATTCAGAACGCACTCCGTACAAAGTGAGACCT
GTGGCCATCAAGCAACTCTCCGCTGGTGTCGAGGACAAGAGAACCACAAGCCGTGGCCAG
TCTGCTGAGAGACCACTGAGGGACAGACGGGTTGTGGGCCTGGAGCAGCCCCGGAGGGAA
GGAGCATTTGAAAGTGGACAGGTAGAGCCCAGGCCCAGAGAGCCCCAGGGCTGCTACCAG
GAAGGCCAGCGCATCCCTCCAGAGAGAGAAGAATTAATCCAGAGCGTGCTGGCGCAGGTT
GCAGAGCAGTTCTCAAGAGCATTCAAAATCAATGAACTGAAAGCTGAAGTTGCAAATCAC
TTGGCTGTCCTAGAGAAACGCGTGGAATTGGAAGGACTAAAAGTGGTGGAGATTGAGAAA
TGCAAGAGTGACATTAAGAAGATGAGGGAGGAGCTGGCGGCCAGAAGCAGCAGGACCAAC
TGCCCCTGTAAGTACAGTTTTTTGGATAACCACAAGAAGTTGACTCCTCGACGCGATGTT
CCCACTTACCCCAAGTACCTGCTCTCTCCAGAGACCATCGAGGCCCTGCGGAAGCCGACC
TTTGACGTCTGGCTTTGGGAGCCCAATGAGATGCTGAGCTGCCTGGAGCACATGTACCAC
GACCTCGGGCTGGTCAGGGACTTCAGCATCAACCCTGTCACCCTCAGGAGGTGGCTGTTC
TGTGTCCACGACAACTACAGAAACAACCCCTTCCACAACTTCCGGCACTGCTTCTGCGTG
GCCCAGATGATGTACAGCATGGTCTGGCTCTGCAGTCTCCAGGAGAAGTTCTCACAAACG
GATATCCTGATCCTAATGACAGCGGCCATCTGCCACGATCTGGACCATCCCGGCTACAAC
AACACGTACCAGATCAATGCCCGCACAGAGCTGGCGGTCCGCTACAATGACATCTCACCG
CTGGAGAACCACCACTGCGCCGTGGCCTTCCAGATCCTCGCCGAGCCTGAGTGCAACATC
TTCTCCAACATCCCACCTGATGGGTTCAAGCAGATCCGACAGGGAATGATCACATTAATC
TTGGCCACTGACATGGCAAGACATGCAGAAATTATGGATTCTTTCAAAGAGAAAATGGAG
AATTTTGACTACAGCAACGAGGAGCACATGACCCTGCTGAAGATGATTTTGATAAAATGC
TGTGATATCTCTAACGAGGTCCGTCCAATGGAAGTCGCAGAGCCTTGGGTGGACTGTTTA
TTAGAGGAATATTTTATGCAGAGCGACCGTGAGAAGTCAGAAGGCCTTCCTGTGGCACCG
TTCATGGACCGAGACAAAGTGACCAAGGCCACAGCCCAGATTGGGTTCATCAAGTTTGTC
CTGATCCCAATGTTTGAAACAGTGACCAAGCTCTTCCCCATGGTTGAGGAGATCATGCTG
CAGCCACTTTGGGAATCCCGAGATCGCTACGAGGAGCTGAAGCGGATAGATGACGCCATG
AAAGAGTTACAGAAGAAGACTGACAGCTTGACGTCTGGGGCCACCGAGAAGTCCAGAGAG
AGAAGCAGAGATGTGAAAAACAGTGAAGGAGACTGTGCCTGA
Enzyme 16 GenBank Gene ID AF048837 Link Image
Enzyme 16 GeneCard ID PDE9A Link Image
Enzyme 16 GenAtlas ID PDE9A Link Image
Enzyme 16 HGNC ID HGNC:8795 Link Image
Enzyme 16 Chromosome Location 2
Enzyme 16 Locus 21q22.3
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Fisher DA, Smith JF, Pillar JS, St Denis SH, Cheng JB: Isolation and characterization of PDE9A, a novel human cGMP-specific phosphodiesterase. J Biol Chem. 1998 Jun 19;273(25):15559-64. [PubMed Link Image]
  2. Guipponi M, Scott HS, Kudoh J, Kawasaki K, Shibuya K, Shintani A, Asakawa S, Chen H, Lalioti MD, Rossier C, Minoshima S, Shimizu N, Antonarakis SE: Identification and characterization of a novel cyclic nucleotide phosphodiesterase gene (PDE9A) that maps to 21q22.3: alternative splicing of mRNA transcripts, genomic structure and sequence. Hum Genet. 1998 Oct;103(4):386-92. [PubMed Link Image]
  3. Rentero C, Monfort A, Puigdomenech P: Identification and distribution of different mRNA variants produced by differential splicing in the human phosphodiesterase 9A gene. Biochem Biophys Res Commun. 2003 Feb 14;301(3):686-92. [PubMed Link Image]
  4. Wang P, Wu P, Egan RW, Billah MM: Identification and characterization of a new human type 9 cGMP-specific phosphodiesterase splice variant (PDE9A5). Differential tissue distribution and subcellular localization of PDE9A variants. Gene. 2003 Sep 18;314:15-27. [PubMed Link Image]
  5. Rentero C, Puigdomenech P: Specific use of start codons and cellular localization of splice variants of human phosphodiesterase 9A gene. BMC Mol Biol. 2006 Nov 8;7:39. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed Link Image]
  10. Huai Q, Wang H, Zhang W, Colman RW, Robinson H, Ke H: Crystal structure of phosphodiesterase 9 shows orientation variation of inhibitor 3-isobutyl-1-methylxanthine binding. Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9624-9. Epub 2004 Jun 21. [PubMed Link Image]
  11. Liu S, Mansour MN, Dillman KS, Perez JR, Danley DE, Aeed PA, Simons SP, Lemotte PK, Menniti FS: Structural basis for the catalytic mechanism of human phosphodiesterase 9. Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13309-14. Epub 2008 Aug 29. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5889
Enzyme 17 Name cGMP-dependent 3',5'-cyclic phosphodiesterase
Enzyme 17 Synonyms
  1. Cyclic GMP-stimulated phosphodiesterase
  2. CGS-PDE
  3. cGSPDE
Enzyme 17 Gene Name PDE2A
Enzyme 17 Protein Sequence >cGMP-dependent 3',5'-cyclic phosphodiesterase
MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQDALLSLGSVIDI
SGLQRAVKEALSAVLPRVETVYTYLLDGESQLVCEDPPHELPQEGKVREAIISQKRLGCN
GLGFSDLPGKPLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAV
EKHTLVALRRVQVLQQRGPREAPRAVQNPPEGTAEDQKGGAAYTDRDRKILQLCGELYDL
DASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPLTGCLGQVV
EDKKSIQLKDLTSEDVQQLQSMLGCELQAMLCVPVISRATDQVVALACAFNKLEGDLFTD
EDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITE
ARNLSNAEICSVFLLDQNELVAKVFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPD
AYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELVNKINGPWFSKFDEDLATAF
SIYCGISIAHSLLYKKVNEAQYRSHLANEMMMYHMKVSDDEYTKLLHDGIQPVAAIDSNF
ASFTYTPRSLPEDDTSMAILSMLQDMNFINNYKIDCPTLARFCLMVKKGYRDPPYHNWMH
AFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYS
SEGSVMERHHFAQAIAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDL
QKMAEVGYDRNNKQHHRLLLCLLMTSCDLSDQTKGWKTTRKIAELIYKEFFSQGDLEKAM
GNRPMEMMDREKAYIPELQISFMEHIAMPIYKLLQDLFPKAAELYERVASNREHWTKVSH
KFTIRGLPSNNSLDFLDEEYEVPDLDGTRAPINGCCSLDAE
Enzyme 17 Number of Residues 941
Enzyme 17 Molecular Weight 105715.8
Enzyme 17 Theoretical pI 5.08
Enzyme 17 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 17 General Function Involved in catalytic activity
Enzyme 17 Specific Function Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes
Enzyme 17 Pathways
Enzyme 17 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 2108052 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID O00408 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name PDE2A_HUMAN Link Image
Enzyme 17 PDB ID 1MC0 Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >2826 bp
ATGGGGCAGGCATGCGGCCACTCCATCCTCTGCAGGAGCCAGCAGTACCCGGCAGCGCGA
CCGGCTGAGCCGCGGGGCCAGCAGGTCTTCCTCAAGCCGGACGAGCCGCCGCCGCCGCCG
CAGCCATGCGCCGACAGCCTGCAGGACGCCTTGCTGAGTCTGGGCTCTGTCATCGACATT
TCAGGCCTGCAACGTGCTGTCAAGGAGGCCCTGTCAGCTGTGCTCCCCCGAGTGGAAACT
GTCTACACCTACCTACTGGATGGTGAGTCCCAGCTGGTGTGTGAGGACCCCCCACATGAG
CTGCCCCAGGAGGGGAAAGTCCGGGAGGCTATCATCTCCCAGAAGCGGCTGGGCTGCAAT
GGGCTGGGCTTCTCAGACCTGCCAGGGAAGCCCTTGGCCAGGCTGGTGGCTCCACTGGCT
CCTGATACCCAAGTGCTGGTCATGCCGCTAGCGGACAAGGAGGCTGGGGCCGTGGCAGCT
GTCATCTTGGTGCACTGTGGCCAGCTGAGTGATAATGAGGAATGGAGCCTGCAGGCGGTG
GAGAAGCATACCCTGGTCGCCCTGCGGAGGGTGCAGGTCCTGCAGCAGCGCGGGCCCAGG
GAGGCTCCCCGAGCCGTCCAGAACCCCCCGGAGGGGACGGCGGAAGACCAGAAGGGCGGG
GCGGCGTACACCGACCGCGACCGCAAGATCCTCCAACTGTGCGGGGAACTCTACGACCTG
GATGCCTCTTCCCTGCAGCTCAAAGTGCTCCAATACCTGCAGCAGGAGACCCGGGCATCC
CGCTGCTGCCTCCTGCTGGTGTCGGAGGACAATCTCCAGCTTTCTTGCAAGGTCATCGGA
GACAAAGTGCTCGGGGAAGAGGTCAGCTTTCCCTTGACAGGATGCCTGGGCCAGGTGGTG
GAAGACAAGAAGTCCATCCAGCTGAAGGACCTCACCTCCGAGGATGTACAACAGCTGCAG
AGCATGTTGGGCTGTGAGCTGCAGGCCATGCTCTGTGTCCCTGTCATCAGCCGGGCCACT
GACCAGGTGGTGGCCTTGGCCTGCGCCTTCAACAAGCTAGAAGGAGACTTGTTCACCGAC
GAGGACGAGCATGTGATCCAGCACTGCTTCCACTACACCAGCACCGTGCTCACCAGCACC
CTGGCCTTCCAGAAGGAACAGAAACTCAAGTGTGAGTGCCAGGCTCTTCTCCAAGTGGCA
AAGAACCTCTTCACCCACCTGGATGACGTCTCTGTCCTGCTCCAGGAGATCATCACGGAG
GCCAGAAACCTCAGCAACGCAGAGATCTGCTCTGTGTTCCTGCTGGATCAGAATGAGCTG
GTGGCCAAGGTGTTCGACGGGGGCGTGGTGGATGATGAGAGCTATGAGATCCGCATCCCG
GCCGATCAGGGCATCGCGGGACACGTGGCGACCACGGGCCAGATCCTGAACATCCCTGAC
GCATATGCCCATCCGCTTTTCTACCGCGGCGTGGACGACAGCACCGGCTTCCGCACGCGC
AACATCCTCTGCTTCCCCATCAAGAACGAGAACCAGGAGGTCATCGGTGTGGCCGAGCTG
GTGAACAAGATCAATGGGCCATGGTTCAGCAAGTTCGACGAGGACCTGGCGACGGCCTTC
TCCATCTACTGCGGCATCAGCATCGCCCATTCTCTCCTATACAAAAAAGTGAATGAGGCT
CAGTATCGCAGCCACCTGGCCAATGAGATGATGATGTACCACATGAAGGTCTCCGACGAT
GAGTATACCAAACTTCTCCATGATGGGATCCAGCCTGTGGCTGCCATTGACTCCAATTTT
GCAAGTTTCACCTATACCCCTCGTTCCCTGCCCGAGGATGACACGTCCATGGCCATCCTG
AGCATGCTGCAGGACATGAATTTCATCAACAACTACAAAATTGACTGCCCGACCCTGGCC
CGGTTCTGTTTGATGGTGAAGAAGGGCTACCGGGATCCCCCCTACCACAACTGGATGCAC
GCCTTTTCTGTCTCCCACTTCTGCTACCTGCTCTACAAGAACCTGGAGCTCACCAACTAC
CTCGAGGACATCGAGATCTTTGCCTTGTTTATTTCCTGCATGTGTCATGACCTGGACCAC
AGAGGCACAAACAACTCTTTCCAGGTGGCCTCGAAATCTGTGCTGGCTGCGCTCTACAGC
TCTGAGGGCTCCGTCATGGAGAGGCACCACTTTGCTCAGGCCATCGCCATCCTCAACACC
CACGGCTGCAACATCTTTGATCATTTCTCCCGGAAGGACTATCAGCGCATGCTGGATCTG
ATGCGGGACATCATCTTGGCCACAGACCTGGCCCACCATCTCCGCATCTTCAAGGACCTC
CAGAAGATGGCTGAGGTGGGCTACGACCGAAACAACAAGCAGCACCACAGACTTCTCCTC
TGCCTCCTCATGACCTCCTGTGACCTCTCTGACCAGACCAAGGGCTGGAAGACTACGAGA
AAGATCGCGGAGCTGATCTACAAAGAATTCTTCTCCCAGGGAGACCTGGAGAAGGCCATG
GGCAACAGGCCGATGGAGATGATGGACCGGGAGAAGGCCTATATCCCTGAGCTGCAAATC
AGCTTCATGGAGCACATTGCAATGCCCATCTACAAGCTGTTGCAGGACCTGTTCCCCAAA
GCGGCAGAGCTGTACGAGCGCGTGGCCTCCAACCGTGAGCACTGGACCAAGGTGTCCCAC
AAGTTCACCATCCGCGGCCTCCCAAGTAACAACTCGCTGGACTTCCTGGATGAGGAGTAC
GAGGTGCCTGATCTGGATGGCACTAGGGCCCCCATCAATGGCTGCTGCAGCCTTGATGCT
GAGTGA
Enzyme 17 GenBank Gene ID U67733 Link Image
Enzyme 17 GeneCard ID PDE2A Link Image
Enzyme 17 GenAtlas ID PDE2A Link Image
Enzyme 17 HGNC ID HGNC:8777 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 11q13.4
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Rosman GJ, Martins TJ, Sonnenburg WK, Beavo JA, Ferguson K, Loughney K: Isolation and characterization of human cDNAs encoding a cGMP-stimulated 3',5'-cyclic nucleotide phosphodiesterase. Gene. 1997 May 20;191(1):89-95. [PubMed Link Image]
  2. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  3. Iffland A, Kohls D, Low S, Luan J, Zhang Y, Kothe M, Cao Q, Kamath AV, Ding YH, Ellenberger T: Structural determinants for inhibitor specificity and selectivity in PDE2A using the wheat germ in vitro translation system. Biochemistry. 2005 Jun 14;44(23):8312-25. [PubMed Link Image]
  4. Pandit J, Forman MD, Fennell KF, Dillman KS, Menniti FS: Mechanism for the allosteric regulation of phosphodiesterase 2A deduced from the X-ray structure of a near full-length construct. Proc Natl Acad Sci U S A. 2009 Oct 27;106(43):18225-30. Epub 2009 Oct 14. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5902
Enzyme 18 Name High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B
Enzyme 18 Synonyms
  1. HsPDE8B
  2. Cell proliferation-inducing gene 22 protein
Enzyme 18 Gene Name PDE8B
Enzyme 18 Protein Sequence >High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B
MGCAPSIHVSQSGVIYCRDSDESSSPRQTTSVSQGPAAPLPGLFVQTDAADAIPPSRASG
PPSVARVRRARTELGSGSSAGSAAPAATTSRGRRRHCCSSAEAETQTCYTSVKQVSSAEV
RIGPMRLTQDPIQVLLIFAKEDSQSDGFWWACDRAGYRCNIARTPESALECFLDKHHEII
VIDHRQTQNFDAEAVCRSIRATNPSEHTVILAVVSRVSDDHEEASVLPLLHAGFNRRFME
NSSIIACYNELIQIEHGEVRSQFKLRACNSVFTALDHCHEAIEITSDDHVIQYVNPAFER
MMGYHKGELLGKELADLPKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVK
ITPVIGQGGKIRHFVSLKKLCCTTDNNKQIHKIHRDSGDNSQTEPHSFRYKNRRKESIDV
KSISSRGSDAPSLQNRRYPSMARIHSMTIEAPITKVINIINAAQENSPVTVAEALDRVLE
ILRTTELYSPQLGTKDEDPHTSDLVGGLMTDGLRRLSGNEYVFTKNVHQSHSHLAMPITI
NDVPPCISQLLDNEESWDFNIFELEAITHKRPLVYLGLKVFSRFGVCEFLNCSETTLRAW
FQVIEANYHSSNAYHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHP
GRTNSFLCNAGSELAVLYNDTAVLESHHTALAFQLTVKDTKCNIFKNIDRNHYRTLRQAI
IDMVLATEMTKHFEHVNKFVNSINKPMAAEIEGSDCECNPAGKNFPENQILIKRMMIKCA
DVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPVVMPVFDRNTCSIPKSQISFIDYF
ITDMFDAWDAFAHLPALMQHLADNYKHWKTLDDLKCKSLRLPSDS
Enzyme 18 Number of Residues 885
Enzyme 18 Molecular Weight 98977.9
Enzyme 18 Theoretical pI 6.81
Enzyme 18 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • molecular transducer activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • signal transducer activity
  • two-component response regulator activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • signal transduction
  • signal transmission
  • signaling process
  • two-component signal transduction system (phosphorelay)
Component
Enzyme 18 General Function Involved in catalytic activity
Enzyme 18 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in specific signaling in the thyroid gland
Enzyme 18 Pathways
Enzyme 18 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 27372873 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID O95263 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PDE8B_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >2658 bp
ATGGGCTGCGCCCCCAGCATCCATGTCTCGCAGAGCGGCGTGATCTACTGCCGGGACTCG
GACGAGTCCAGCTCGCCCCGCCAGACCACCAGCGTGTCGCAGGGCCCGGCGGCACCCCTG
CCCGGCCTCTTCGTCCAGACCGACGCCGCCGACGCCATCCCCCCGAGCCGCGCGTCGGGA
CCCCCCAGCGTAGCCCGCGTCCGCAGGGCCCGCACCGAGCTGGGCAGCGGTAGCAGCGCG
GGTTCCGCAGCCCCCGCCGCGACCACCAGCAGGGGCCGGAGGCGCCACTGCTGCAGCAGC
GCCGAGGCCGAGACTCAGACCTGCTACACCAGCGTGAAGCAGGTGTCTTCTGCGGAGGTG
CGCATCGGGCCCATGAGACTGACGCAGGACCCTATTCAGGTTTTGCTGATCTTTGCAAAG
GAAGATAGTCAGAGCGATGGCTTCTGGTGGGCCTGCGACAGAGCTGGTTATAGATGCAAT
ATTGCTCGGACTCCAGAGTCAGCCCTTGAATGCTTTCTTGATAAGCATCATGAAATTATT
GTAATTGATCATAGACAAACTCAGAACTTCGATGCAGAAGCAGTGTGCAGGTCGATCCGG
GCCACAAATCCCTCCGAGCACACGGTGATCCTCGCAGTGGTTTCGCGAGTATCGGATGAC
CATGAAGAGGCGTCAGTCCTTCCTCTTCTCCACGCAGGCTTCAACAGGAGATTTATGGAG
AATAGCAGCATAATTGCTTGCTATAATGAACTGATTCAAATAGAACATGGGGAAGTTCGC
TCCCAGTTCAAATTACGGGCCTGTAATTCAGTGTTTACAGCATTAGATCACTGTCATGAA
GCCATAGAAATAACAAGCGATGACCACGTGATTCAGTATGTCAACCCAGCCTTCGAAAGG
ATGATGGGCTACCACAAAGGTGAGCTCCTGGGAAAAGAACTCGCTGATCTGCCCAAAAGC
GATAAGAACCGGGCAGACCTTCTCGACACCATCAATACATGCATCAAGAAGGGAAAGGAG
TGGCAGGGGGTTTACTATGCCAGACGGAAATCCGGGGACAGCATCCAACAGCACGTGAAG
ATCACCCCAGTGATTGGCCAAGGAGGGAAAATTAGGCATTTTGTCTCGCTCAAGAAACTG
TGTTGTACCACTGACAATAATAAGCAGATTCACAAGATTCATCGTGATTCAGGAGACAAT
TCTCAGACAGAGCCTCATTCATTCAGATATAAGAACAGGAGGAAAGAGTCCATTGACGTG
AAATCGATATCATCTCGAGGCAGTGATGCACCAAGCCTGCAGAATCGTCGCTATCCGTCC
ATGGCGAGGATCCACTCCATGACCATCGAGGCTCCCATCACAAAGGTTATAAATATAATC
AATGCAGCCCAAGAAAACAGCCCAGTCACAGTAGCGGAAGCCTTGGACAGAGTTCTAGAG
ATTTTACGGACCACAGAACTGTACTCCCCTCAGCTGGGTACCAAAGATGAAGATCCCCAC
ACCAGTGATCTTGTTGGAGGCCTGATGACTGACGGCTTGAGAAGACTGTCAGGAAACGAG
TATGTGTTTACTAAGAATGTGCACCAGAGTCACAGTCACCTTGCAATGCCAATAACCATC
AATGATGTTCCCCCTTGTATCTCTCAATTACTTGATAATGAGGAGAGTTGGGACTTCAAC
ATCTTTGAATTGGAAGCCATTACGCATAAAAGGCCATTGGTTTATCTGGGCTTAAAGGTC
TTCTCTCGGTTTGGAGTATGTGAGTTTTTAAACTGTTCTGAAACCACTCTTCGGGCCTGG
TTCCAAGTGATCGAAGCCAACTACCACTCTTCCAATGCCTACCACAACTCCACCCATGCT
GCCGACGTCCTGCACGCCACCGCTTTCTTTCTTGGAAAGGAAAGAGTAAAGGGAAGCCTC
GATCAGTTGGATGAGGTGGCAGCCCTCATTGCTGCCACAGTCCATGACGTGGATCACCCG
GGAAGGACCAACTCTTTCCTCTGCAATGCAGGCAGTGAGCTTGCTGTGCTCTACAATGAC
ACTGCTGTTCTGGAGAGTCACCACACCGCCCTGGCCTTCCAGCTCACGGTCAAGGACACC
AAATGCAACATTTTCAAGAATATTGACAGGAACCATTATCGAACGCTGCGCCAGGCTATT
ATTGACATGGTTTTGGCAACAGAGATGACAAAACACTTTGAACATGTGAATAAGTTTGTG
AACAGCATCAACAAGCCAATGGCAGCTGAGATTGAAGGCAGCGACTGTGAATGCAACCCT
GCTGGGAAGAACTTCCCTGAAAACCAAATCCTGATCAAACGCATGATGATTAAGTGTGCT
GACGTGGCCAACCCATGCCGCCCCTTGGACCTGTGCATTGAATGGGCTGGGAGGATCTCT
GAGGAGTATTTTGCACAGACTGATGAAGAGAAGAGACAGGGACTACCTGTGGTGATGCCA
GTGTTTGACCGGAATACCTGTAGCATCCCCAAGTCTCAGATCTCTTTCATTGACTACTTC
ATAACAGACATGTTTGATGCTTGGGATGCCTTTGCACATCTGCCAGCCCTGATGCAACAT
TTGGCTGACAACTACAAACACTGGAAGACACTAGATGACCTAAAGTGCAAAAGTTTGAGG
CTTCCATCTGACAGCTAA
Enzyme 18 GenBank Gene ID AB085824 Link Image
Enzyme 18 GeneCard ID PDE8B Link Image
Enzyme 18 GenAtlas ID PDE8B Link Image
Enzyme 18 HGNC ID HGNC:8794 Link Image
Enzyme 18 Chromosome Location 5
Enzyme 18 Locus 5q13.3
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Hayashi M, Shimada Y, Nishimura Y, Hama T, Tanaka T: Genomic organization, chromosomal localization, and alternative splicing of the human phosphodiesterase 8B gene. Biochem Biophys Res Commun. 2002 Oct 11;297(5):1253-8. [PubMed Link Image]
  2. Gamanuma M, Yuasa K, Sasaki T, Sakurai N, Kotera J, Omori K: Comparison of enzymatic characterization and gene organization of cyclic nucleotide phosphodiesterase 8 family in humans. Cell Signal. 2003 Jun;15(6):565-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Hayashi M, Matsushima K, Ohashi H, Tsunoda H, Murase S, Kawarada Y, Tanaka T: Molecular cloning and characterization of human PDE8B, a novel thyroid-specific isozyme of 3',5'-cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun. 1998 Sep 29;250(3):751-6. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5903
Enzyme 19 Name cAMP-specific 3',5'-cyclic phosphodiesterase 4C
Enzyme 19 Synonyms
  1. DPDE1
  2. PDE21
Enzyme 19 Gene Name PDE4C
Enzyme 19 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 4C
MENLGVGEGAEACSRLSRSRGRHSMTRAPKHLWRQPRRPIRIQQRFYSDPDKSAGCRERD
LSPRPELRKSRLSWPVSSCRRFDLENGLSCGRRALDPQSSPGLGRIMQAPVPHSQRRESF
LYRSDSDYELSPKAMSRNSSVASDLHGEDMIVTPFAQVLASLRTVRSNVAALARQQCLGA
AKQGPVGNPSSSNQLPPAEDTGQKLALETLDELDWCLDQLETLQTRHSVGEMASNKFKRI
LNRELTHLSETSRSGNQVSEYISRTFLDQQTEVELPKVTAEEAPQPMSRISGLHGLCHSA
SLSSATVPRFGVQTDQEEQLAKELEDTNKWGLDVFKVAELSGNRPLTAIIFSIFQERDLL
KTFQIPADTLATYLLMLEGHYHANVAYHNSLHAADVAQSTHVLLATPALEAVFTDLEILA
ALFASAIHDVDHPGVSNQFLINTNSELALMYNDASVLENHHLAVGFKLLQAENCDIFQNL
SAKQRLSLRRMVIDMVLATDMSKHMNLLADLKTMVETKKVTSLGVLLLDNYSDRIQVLQN
LVHCADLSNPTKPLPLYRQWTDRIMAEFFQQGDRERESGLDISPMCDKHTASVEKSQVGF
IDYIAHPLWETWADLVHPDAQDLLDTLEDNREWYQSKIPRSPSDLTNPERDGPDRFQFEL
TLEEAEEEDEEEEEEGEETALAKEALELPDTELLSPEAGPDPGDLPLDNQRT
Enzyme 19 Number of Residues 712
Enzyme 19 Molecular Weight 79900.8
Enzyme 19 Theoretical pI 4.84
Enzyme 19 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 19 General Function Involved in catalytic activity
Enzyme 19 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes
Enzyme 19 Pathways
Enzyme 19 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 115529445 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q08493 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name PDE4C_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >2139 bp
ATGGAGAACCTGGGGGTCGGCGAAGGGGCAGAGGCTTGCAGCAGGTTGAGTCGCTCTCGC
GGCCGCCACAGCATGACCAGAGCCCCGAAGCACCTGTGGCGGCAACCCCGGCGCCCCATC
CGCATCCAACAGCGCTTCTATTCGGATCCGGACAAGTCCGCGGGCTGCCGCGAGAGGGAC
CTGAGCCCGCGGCCGGAGCTCAGGAAGTCGCGGCTCTCCTGGCCCGTTTCCTCCTGCAGG
CGCTTTGACCTGGAAAATGGGCTCTCGTGTGGGAGGAGGGCCCTGGACCCTCAGTCCAGC
CCTGGCCTGGGCCGGATTATGCAGGCTCCAGTCCCGCACAGCCAGCGGCGCGAGTCCTTC
CTGTACCGCTCAGATAGCGACTATGAACTCTCGCCCAAGGCCATGTCTCGGAACTCCTCT
GTGGCCAGCGACCTACATGGAGAGGACATGATTGTGACGCCCTTTGCCCAGGTCCTGGCC
AGTCTGCGGACCGTTCGGAGCAACGTGGCGGCCCTTGCCCGCCAGCAATGCCTAGGAGCA
GCCAAGCAGGGACCCGTCGGAAACCCTTCATCCAGCAATCAGCTCCCTCCTGCAGAGGAC
ACGGGGCAGAAGCTGGCATTGGAGACGCTAGACGAGCTGGACTGGTGCCTGGATCAGTTG
GAGACGCTGCAGACCCGGCACTCGGTGGGGGAGATGGCCTCCAACAAGTTCAAGCGGATC
CTGAACCGGGAGTTGACCCACCTGTCCGAAACCAGCCGCTCCGGGAACCAGGTGTCCGAG
TACATCTCCCGGACCTTCCTGGACCAGCAGACCGAGGTGGAGCTGCCCAAGGTGACCGCT
GAGGAGGCCCCACAGCCCATGTCCCGGATCAGTGGCCTACATGGGCTCTGCCACAGTGCC
AGCCTCTCCTCAGCCACTGTCCCACGCTTTGGGGTCCAGACTGACCAGGAGGAGCAACTG
GCCAAGGAGCTAGAAGACACCAACAAGTGGGGACTTGATGTGTTCAAGGTGGCGGAGCTA
AGTGGGAACCGGCCCCTCACAGCTATCATATTCAGCATTTTTCAGGAGCGGGACCTGCTG
AAGACATTCCAGATCCCAGCAGACACACTGGCCACCTACCTGCTGATGCTGGAAGGTCAC
TACCACGCCAATGTGGCCTACCACAACAGCCTACATGCCGCCGACGTGGCCCAGTCCACG
CATGTGCTGCTGGCTACGCCCGCCCTCGAGGCTGTGTTCACAGACTTGGAAATCCTGGCT
GCCCTCTTTGCAAGCGCCATCCACGACGTGGACCATCCTGGGGTCTCCAACCAGTTTCTG
ATTAACACCAACTCAGAGCTGGCGCTTATGTACAACGACGCCTCGGTGCTGGAGAACCAT
CACCTGGCTGTGGGCTTCAAGCTGCTGCAGGCAGAGAACTGCGATATCTTCCAGAACCTC
AGCGCCAAGCAGCGACTGAGTCTGCGCAGGATGGTCATTGACATGGTGCTGGCCACAGAC
ATGTCCAAACACATGAACCTCCTGGCCGACCTCAAGACCATGGTGGAGACCAAGAAGGTG
ACAAGCCTCGGTGTCCTCCTCCTGGACAACTATTCCGACCGAATCCAGGTCTTGCAGAAC
CTGGTGCACTGTGCTGATCTGAGCAACCCCACCAAGCCGCTGCCCCTGTACCGCCAGTGG
ACGGACCGCATCATGGCCGAGTTCTTCCAGCAGGGAGACCGCGAGCGTGAGTCGGGCCTG
GACATCAGTCCCATGTGTGACAAGCATACGGCCTCAGTGGAGAAGTCCCAGGTGGGTTTC
ATTGACTACATTGCTCACCCACTGTGGGAGACTTGGGCTGACCTGGTCCACCCAGATGCA
CAGGACCTGCTGGACACGCTGGAGGACAATCGAGAGTGGTACCAGAGCAAGATCCCCCGA
AGTCCCTCAGACCTCACCAACCCCGAGCGGGACGGGCCTGACAGATTCCAGTTTGAACTG
ACTCTGGAGGAGGCAGAGGAAGAGGATGAGGAGGAAGAAGAGGAGGGGGAAGAGACAGCT
TTAGCCAAAGAGGCCTTGGAGTTGCCTGACACTGAACTCCTGTCCCCTGAAGCCGGCCCA
GACCCTGGGGACTTACCCCTCGACAACCAGAGGACTTAG
Enzyme 19 GenBank Gene ID NM_000923.3 Link Image
Enzyme 19 GeneCard ID PDE4C Link Image
Enzyme 19 GenAtlas ID PDE4C Link Image
Enzyme 19 HGNC ID HGNC:8782 Link Image
Enzyme 19 Chromosome Location 1
Enzyme 19 Locus 19p13.11
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Engels P, Sullivan M, Muller T, Lubbert H: Molecular cloning and functional expression in yeast of a human cAMP-specific phosphodiesterase subtype (PDE IV-C). FEBS Lett. 1995 Jan 30;358(3):305-10. [PubMed Link Image]
  2. Sullivan M, Olsen AS, Houslay MD: Genomic organisation of the human cyclic AMP-specific phosphodiesterase PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and JUND. Cell Signal. 1999 Oct;11(10):735-42. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  5. Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed Link Image]
  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  7. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  8. Wang H, Peng MS, Chen Y, Geng J, Robinson H, Houslay MD, Cai J, Ke H: Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors. Biochem J. 2007 Dec 1;408(2):193-201. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5908
Enzyme 20 Name cAMP-specific 3',5'-cyclic phosphodiesterase 4D
Enzyme 20 Synonyms
  1. DPDE3
  2. PDE43
Enzyme 20 Gene Name PDE4D
Enzyme 20 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 4D
MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQYPLRQPQFRLLHPHHHLPPP
PPPSPQPQPQCPLQPPPPPPLPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRA
MDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPMTSPGSGLILQA
NFVHSQRRESFLYRSDSDYDLSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNF
AALTNLQDRAPSKRSPMCNQPSINKATITEEAYQKLASETLEELDWCLDQLETLQTRHSV
SEMASNKFKRMLNRELTHLSEMSRSGNQVSEFISNTFLDKQHEVEIPSPTQKEKEKKKRP
MSQISGVKKLMHSSSLTNSSIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPL
TVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLST
PALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGF
KLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVL
LLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMC
DKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAP
DDPEEGRQGQTEKFQFELTLEEDGESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPL
DEQVEEEAVGEEEESQPEACVIDDRSPDT
Enzyme 20 Number of Residues 809
Enzyme 20 Molecular Weight 91114.1
Enzyme 20 Theoretical pI 5.25
Enzyme 20 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 20 General Function Involved in catalytic activity
Enzyme 20 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes
Enzyme 20 Pathways
Enzyme 20 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 157277988 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q08499 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name PDE4D_HUMAN Link Image
Enzyme 20 PDB ID 1PTW Link Image
Enzyme 20 PDB File Show
Enzyme 20 3D Structure
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >2430 bp
ATGGAGGCAGAGGGCAGCAGCGCGCCGGCCCGGGCGGGCAGCGGAGAGGGCAGCGACAGC
GCCGGCGGGGCCACGCTCAAAGCCCCCAAGCATCTCTGGAGGCACGAGCAGCACCACCAG
TACCCGCTCCGGCAGCCCCAGTTCCGCCTCCTGCATCCCCATCACCACCTGCCCCCGCCG
CCGCCACCCTCGCCCCAGCCCCAGCCCCAGTGTCCGCTACAGCCGCCGCCGCCGCCCCCC
CTGCCGCCGCCCCCGCCGCCGCCCGGGGCTGCCCGCGGCCGCTACGCCTCGAGCGGGGCC
ACCGGCCGCGTCCGGCATCGCGGCTACTCGGACACCGAGCGCTACCTGTACTGTCGCGCC
ATGGACCGCACCTCCTACGCGGTGGAGACCGGCCACCGGCCCGGCCTGAAGAAATCCAGG
ATGTCCTGGCCCTCCTCGTTCCAGGGACTCAGGCGTTTTGATGTGGACAATGGCACATCT
GCGGGACGGAGTCCCTTGGATCCCATGACCAGCCCAGGATCCGGGCTAATTCTCCAAGCA
AATTTTGTCCACAGTCAACGACGGGAGTCCTTCCTGTATCGATCCGACAGCGATTATGAC
CTCTCTCCAAAGTCTATGTCCCGGAACTCCTCCATTGCCAGTGATATACACGGAGATGAC
TTGATTGTGACTCCATTTGCTCAGGTCTTGGCCAGTCTGCGAACTGTACGAAACAACTTT
GCTGCATTAACTAATTTGCAAGATCGAGCACCTAGCAAAAGATCACCCATGTGCAACCAA
CCATCCATCAACAAAGCCACCATAACAGAGGAGGCCTACCAGAAACTGGCCAGCGAGACC
CTGGAGGAGCTGGACTGGTGTCTGGACCAGCTAGAGACCCTACAGACCAGGCACTCCGTC
AGTGAGATGGCCTCCAACAAGTTTAAAAGGATGCTTAATCGGGAGCTCACCCATCTCTCT
GAAATGAGTCGGTCTGGAAATCAAGTGTCAGAGTTTATATCAAACACATTCTTAGATAAG
CAACATGAAGTGGAAATTCCTTCTCCAACTCAGAAGGAAAAGGAGAAAAAGAAAAGACCA
ATGTCTCAGATCAGTGGAGTCAAGAAATTGATGCACAGCTCTAGTCTGACTAATTCAAGT
ATCCCAAGGTTTGGAGTTAAAACTGAACAAGAAGATGTCCTTGCCAAGGAACTAGAAGAT
GTGAACAAATGGGGTCTTCATGTTTTCAGAATAGCAGAGTTGTCTGGTAACCGGCCCTTG
ACTGTTATCATGCACACCATTTTTCAGGAACGGGATTTATTAAAAACATTTAAAATTCCA
GTAGATACTTTAATTACATATCTTATGACTCTCGAAGACCATTACCATGCTGATGTGGCC
TATCACAACAATATCCATGCTGCAGATGTTGTCCAGTCTACTCATGTGCTATTATCTACA
CCTGCTTTGGAGGCTGTGTTTACAGATTTGGAGATTCTTGCAGCAATTTTTGCCAGTGCA
ATACATGATGTAGATCATCCTGGTGTGTCCAATCAATTTCTGATCAATACAAACTCTGAA
CTTGCCTTGATGTACAATGATTCCTCAGTCTTAGAGAACCATCATTTGGCTGTGGGCTTT
AAATTGCTTCAGGAAGAAAACTGTGACATTTTCCAGAATTTGACCAAAAAACAAAGACAA
TCTTTAAGGAAAATGGTCATTGACATCGTACTTGCAACAGATATGTCAAAACACATGAAT
CTACTGGCTGATTTGAAGACTATGGTTGAAACTAAGAAAGTGACAAGCTCTGGAGTTCTT
CTTCTTGATAATTATTCCGATAGGATTCAGGTTCTTCAGAATATGGTGCACTGTGCAGAT
CTGAGCAACCCAACAAAGCCTCTCCAGCTGTACCGCCAGTGGACGGACCGGATAATGGAG
GAGTTCTTCCGCCAAGGAGACCGAGAGAGGGAACGTGGCATGGAGATAAGCCCCATGTGT
GACAAGCACAATGCTTCCGTGGAAAAATCACAGGTGGGCTTCATAGACTATATTGTTCAT
CCCCTCTGGGAGACATGGGCAGACCTCGTCCACCCTGACGCCCAGGATATTTTGGACACT
TTGGAGGACAATCGTGAATGGTACCAGAGCACAATCCCTCAGAGCCCCTCTCCTGCACCT
GATGACCCAGAGGAGGGCCGGCAGGGTCAAACTGAGAAATTCCAGTTTGAACTAACTTTA
GAGGAAGATGGTGAGTCAGACACGGAAAAGGACAGTGGCAGTCAAGTGGAAGAAGACACT
AGCTGCAGTGACTCCAAGACTCTTTGTACTCAAGACTCAGAGTCTACTGAAATTCCCCTT
GATGAACAGGTTGAAGAGGAGGCAGTAGGGGAAGAAGAGGAAAGCCAGCCTGAAGCCTGT
GTCATAGATGATCGTTCTCCTGACACGTAA
Enzyme 20 GenBank Gene ID NM_001104631.1 Link Image
Enzyme 20 GeneCard ID PDE4D Link Image
Enzyme 20 GenAtlas ID PDE4D Link Image
Enzyme 20 HGNC ID HGNC:8783 Link Image
Enzyme 20 Chromosome Location 5
Enzyme 20 Locus 5q12
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed Link Image]
  2. Nemoz G, Zhang R, Sette C, Conti M: Identification of cyclic AMP-phosphodiesterase variants from the PDE4D gene expressed in human peripheral mononuclear cells. FEBS Lett. 1996 Apr 8;384(1):97-102. [PubMed Link Image]
  3. Baecker PA, Obernolte R, Bach C, Yee C, Shelton ER: Isolation of a cDNA encoding a human rolipram-sensitive cyclic AMP phosphodiesterase (PDE IVD). Gene. 1994 Jan 28;138(1-2):253-6. [PubMed Link Image]
  4. Bolger GB, Erdogan S, Jones RE, Loughney K, Scotland G, Hoffmann R, Wilkinson I, Farrell C, Houslay MD: Characterization of five different proteins produced by alternatively spliced mRNAs from the human cAMP-specific phosphodiesterase PDE4D gene. Biochem J. 1997 Dec 1;328 ( Pt 2):539-48. [PubMed Link Image]
  5. Miro X, Casacuberta JM, Gutierrez-Lopez MD, de Landazuri MO, Puigdomenech P: Phosphodiesterases 4D and 7A splice variants in the response of HUVEC cells to TNF-alpha(1). Biochem Biophys Res Commun. 2000 Aug 2;274(2):415-21. [PubMed Link Image]
  6. Wang D, Deng C, Bugaj-Gaweda B, Kwan M, Gunwaldsen C, Leonard C, Xin X, Hu Y, Unterbeck A, De Vivo M: Cloning and characterization of novel PDE4D isoforms PDE4D6 and PDE4D7. Cell Signal. 2003 Sep;15(9):883-91. [PubMed Link Image]
  7. Gretarsdottir S, Thorleifsson G, Reynisdottir ST, Manolescu A, Jonsdottir S, Jonsdottir T, Gudmundsdottir T, Bjarnadottir SM, Einarsson OB, Gudjonsdottir HM, Hawkins M, Gudmundsson G, Gudmundsdottir H, Andrason H, Gudmundsdottir AS, Sigurdardottir M, Chou TT, Nahmias J, Goss S, Sveinbjornsdottir S, Valdimarsson EM, Jakobsson F, Agnarsson U, Gudnason V, Thorgeirsson G, Fingerle J, Gurney M, Gudbjartsson D, Frigge ML, Kong A, Stefansson K, Gulcher JR: The gene encoding phosphodiesterase 4D confers risk of ischemic stroke. Nat Genet. 2003 Oct;35(2):131-8. Epub 2003 Sep 21. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Bolger GB, McCahill A, Yarwood SJ, Steele MR, Warwicker J, Houslay MD: Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5. BMC Biochem. 2002 Aug 23;3:24. [PubMed Link Image]
  10. Bolger GB, McCahill A, Huston E, Cheung YF, McSorley T, Baillie GS, Houslay MD: The unique amino-terminal region of the PDE4D5 cAMP phosphodiesterase isoform confers preferential interaction with beta-arrestins. J Biol Chem. 2003 Dec 5;278(49):49230-8. Epub 2003 Sep 18. [PubMed Link Image]
  11. Richter W, Conti M: The oligomerization state determines regulatory properties and inhibitor sensitivity of type 4 cAMP-specific phosphodiesterases. J Biol Chem. 2004 Jul 16;279(29):30338-48. Epub 2004 May 6. [PubMed Link Image]
  12. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  13. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  14. Rosand J, Bayley N, Rost N, de Bakker PI: Many hypotheses but no replication for the association between PDE4D and stroke. Nat Genet. 2006 Oct;38(10):1091-2; author reply 1092-3. [PubMed Link Image]
  15. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  16. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  17. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  18. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  19. Lee ME, Markowitz J, Lee JO, Lee H: Crystal structure of phosphodiesterase 4D and inhibitor complex(1). FEBS Lett. 2002 Oct 23;530(1-3):53-8. [PubMed Link Image]
  20. Huai Q, Colicelli J, Ke H: The crystal structure of AMP-bound PDE4 suggests a mechanism for phosphodiesterase catalysis. Biochemistry. 2003 Nov 18;42(45):13220-6. [PubMed Link Image]
  21. Huai Q, Wang H, Sun Y, Kim HY, Liu Y, Ke H: Three-dimensional structures of PDE4D in complex with roliprams and implication on inhibitor selectivity. Structure. 2003 Jul;11(7):865-73. [PubMed Link Image]
  22. Huai Q, Liu Y, Francis SH, Corbin JD, Ke H: Crystal structures of phosphodiesterases 4 and 5 in complex with inhibitor 3-isobutyl-1-methylxanthine suggest a conformation determinant of inhibitor selectivity. J Biol Chem. 2004 Mar 26;279(13):13095-101. Epub 2003 Dec 10. [PubMed Link Image]
  23. Xu RX, Rocque WJ, Lambert MH, Vanderwall DE, Luther MA, Nolte RT: Crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and rolipram. J Mol Biol. 2004 Mar 19;337(2):355-65. [PubMed Link Image]
  24. Zhang KY, Card GL, Suzuki Y, Artis DR, Fong D, Gillette S, Hsieh D, Neiman J, West BL, Zhang C, Milburn MV, Kim SH, Schlessinger J, Bollag G: A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases. Mol Cell. 2004 Jul 23;15(2):279-86. [PubMed Link Image]
  25. Card GL, England BP, Suzuki Y, Fong D, Powell B, Lee B, Luu C, Tabrizizad M, Gillette S, Ibrahim PN, Artis DR, Bollag G, Milburn MV, Kim SH, Schlessinger J, Zhang KY: Structural basis for the activity of drugs that inhibit phosphodiesterases. Structure. 2004 Dec;12(12):2233-47. [PubMed Link Image]
  26. Card GL, Blasdel L, England BP, Zhang C, Suzuki Y, Gillette S, Fong D, Ibrahim PN, Artis DR, Bollag G, Milburn MV, Kim SH, Schlessinger J, Zhang KY: A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design. Nat Biotechnol. 2005 Feb;23(2):201-7. Epub 2005 Jan 30. [PubMed Link Image]
  27. Huai Q, Sun Y, Wang H, Macdonald D, Aspiotis R, Robinson H, Huang Z, Ke H: Enantiomer discrimination illustrated by the high resolution crystal structures of type 4 phosphodiesterase. J Med Chem. 2006 Mar 23;49(6):1867-73. [PubMed Link Image]
  28. Wang H, Peng MS, Chen Y, Geng J, Robinson H, Houslay MD, Cai J, Ke H: Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors. Biochem J. 2007 Dec 1;408(2):193-201. [PubMed Link Image]
  29. Smith KJ, Baillie GS, Hyde EI, Li X, Houslay TM, McCahill A, Dunlop AJ, Bolger GB, Klussmann E, Adams DR, Houslay MD: 1H NMR structural and functional characterisation of a cAMP-specific phosphodiesterase-4D5 (PDE4D5) N-terminal region peptide that disrupts PDE4D5 interaction with the signalling scaffold proteins, beta-arrestin and RACK1. Cell Signal. 2007 Dec;19(12):2612-24. Epub 2007 Sep 1. [PubMed Link Image]
  30. Wang H, Robinson H, Ke H: The molecular basis for different recognition of substrates by phosphodiesterase families 4 and 10. J Mol Biol. 2007 Aug 10;371(2):302-7. Epub 2007 May 26. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5909
Enzyme 21 Name Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
Enzyme 21 Synonyms
  1. GMP-PDE gamma
Enzyme 21 Gene Name PDE6G
Enzyme 21 Protein Sequence >Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
MNLEPPKAEFRSATRVAGGPVTPRKGPPKFKQRQTRQFKSKPPKKGVQGFGDDIPGMEGL
GTDITVICPWEAFNHLELHELAQYGII
Enzyme 21 Number of Residues 87
Enzyme 21 Molecular Weight 9643.1
Enzyme 21 Theoretical pI 10.16
Enzyme 21 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • GMP binding
  • binding
  • cGMP binding
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nucleoside binding
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • purine nucleoside binding
Process
  • multicellular organismal process
  • neurological system process
  • sensory perception
  • sensory perception of light stimulus
  • system process
  • visual perception
Component
Enzyme 21 General Function Involved in 3',5'-cyclic-nucleotide phosphodiesterase activity
Enzyme 21 Specific Function Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones
Enzyme 21 Pathways
Enzyme 21 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein Not Available
Enzyme 21 UniProtKB/Swiss-Prot ID P18545 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name CNRG_HUMAN Link Image
Enzyme 21 PDB ID 1FQJ Link Image
Enzyme 21 PDB File Show
Enzyme 21 3D Structure
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >264 bp
ATGAACCTGGAACCGCCCAAGGCTGAGTTCCGGTCAGCCACCAGGGTGGCCGGGGGACCT
GTCACCCCCAGGAAAGGGCCCCCTAAATTTAAGCAGCGACAGACCAGGCAGTTCAAGAGC
AAGCCCCCAAAGAAAGGCGTTCAAGGGTTTGGGGACGACATCCCTGGAATGGAAGGCCTG
GGAACAGACATCACAGTCATCTGCCCTTGGGAGGCCTTCAACCACCTGGAGCTGCACGAG
CTGGCCCAATATGGCATCATCTAG
Enzyme 21 GenBank Gene ID M36476 Link Image
Enzyme 21 GeneCard ID PDE6G Link Image
Enzyme 21 GenAtlas ID PDE6G Link Image
Enzyme 21 HGNC ID HGNC:8789 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 17q25
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Tuteja N, Danciger M, Klisak I, Tuteja R, Inana G, Mohandas T, Sparkes RS, Farber DB: Isolation and characterization of cDNA encoding the gamma-subunit of cGMP phosphodiesterase in human retina. Gene. 1990 Apr 16;88(2):227-32. [PubMed Link Image]
  2. Piriev NI, Purishko VA, Khramtsov NV, Lipkin VM: [The organization of the gamma-subunit gene of human photoreceptor cyclic GMP phosphodiesterase] Dokl Akad Nauk SSSR. 1990;315(1):229-31. [PubMed Link Image]
  3. Hahn LB, Berson EL, Dryja TP: Evaluation of the gene encoding the gamma subunit of rod phosphodiesterase in retinitis pigmentosa. Invest Ophthalmol Vis Sci. 1994 Mar;35(3):1077-82. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5913
Enzyme 22 Name Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
Enzyme 22 Synonyms
  1. GMP-PDE delta
  2. Protein p17
Enzyme 22 Gene Name PDE6D
Enzyme 22 Protein Sequence >Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
MSAKDERAREILRGFKLNWMNLRDAETGKILWQGTEDLSVPGVEHEARVPKKILKCKAVS
RELNFSSTEQMEKFRLEQKVYFKGQCLEEWFFEFGFVIPNSTNTWQSLIEAAPESQMMPA
SVLTGNVIIETKFFDDDLLVSTSRVRLFYV
Enzyme 22 Number of Residues 150
Enzyme 22 Molecular Weight 17419.9
Enzyme 22 Theoretical pI 5.35
Enzyme 22 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • binding
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • protein binding
Process
  • multicellular organismal process
  • neurological system process
  • sensory perception
  • sensory perception of light stimulus
  • system process
  • visual perception
Component
Enzyme 22 General Function Involved in 3',5'-cyclic-nucleotide phosphodiesterase activity
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 2655094 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID O43924 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name PDE6D_HUMAN Link Image
Enzyme 22 PDB ID 1KSG Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >453 bp
ATGTCAGCCAAGGACGAGCGGGCCAGGGAGATCCTGAGGGGCTTCAAACTAAATTGGATG
AACCTTCGGGATGCTGAGACAGGGAAGATACTCTGGCAAGGAACAGAAGACCTGTCTGTC
CCTGGTGTGGAGCATGAAGCCCGTGTTCCCAAGAAAATCCTCAAGTGCAAGGCAGTGTCT
CGAGAACTTAATTTTTCTTCGACAGAACAAATGGAAAAATTCCGCCTGGAACAAAAAGTT
TACTTCAAAGGGCAATGCCTAGAAGAATGGTTCTTCGAGTTTGGCTTTGTGATCCCTAAC
TCCACAAATACCTGGCAGTCCTTGATAGAGGCAGCACCCGAGTCCCAGATGATGCCAGCA
AGCGTCTTAACTGGGAACGTTATCATAGAAACAAAGTTTTTTGACGACGATCTTCTTGTA
AGCACATCCAGAGTGAGACTTTTCTATGTTTGA
Enzyme 22 GenBank Gene ID AF022912 Link Image
Enzyme 22 GeneCard ID PDE6D Link Image
Enzyme 22 GenAtlas ID PDE6D Link Image
Enzyme 22 HGNC ID HGNC:8788 Link Image
Enzyme 22 Chromosome Location 2
Enzyme 22 Locus 2q35-q36
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Li N, Florio SK, Pettenati MJ, Rao PN, Beavo JA, Baehr W: Characterization of human and mouse rod cGMP phosphodiesterase delta subunit (PDE6D) and chromosomal localization of the human gene. Genomics. 1998 Apr 1;49(1):76-82. [PubMed Link Image]
  2. Ershova G, Derre J, Chetelin S, Nancy V, Berger R, Kaplan J, Munnich A, de Gunzburg J: cDNA sequence, genomic organization and mapping of PDE6D, the human gene encoding the delta subunit of the cGMP phosphodiesterase of retinal rod cells to chromosome 2q36. Cytogenet Cell Genet. 1997;79(1-2):139-41. [PubMed Link Image]
  3. Lorenz B, Migliaccio C, Lichtner P, Meyer C, Strom TM, D'Urso M, Becker J, Ciccodicola A, Meitinger T: Cloning and gene structure of the rod cGMP phosphodiesterase delta subunit gene (PDED) in man and mouse. Eur J Hum Genet. 1998 May-Jun;6(3):283-90. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Linari M, Hanzal-Bayer M, Becker J: The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner. FEBS Lett. 1999 Sep 10;458(1):55-9. [PubMed Link Image]
  6. Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC: The complex of Arl2-GTP and PDE delta: from structure to function. EMBO J. 2002 May 1;21(9):2095-106. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5922
Enzyme 23 Name cAMP-specific 3',5'-cyclic phosphodiesterase 4A
Enzyme 23 Synonyms
  1. DPDE2
  2. PDE46
Enzyme 23 Gene Name PDE4A
Enzyme 23 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 4A
MEPPTVPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYSDSAERAERERQ
PHRPIERADAMDTSDRPGLRTTRMSWPSSFHGTGTGSGGAGGGSSRRFEAENGPTPSPGR
SPLDSQASPGLVLHAGAATSQRRESFLYRSDSDYDMSPKTMSRNSSVTSEAHAEDLIVTP
FAQVLASLRSVRSNFSLLTNVPVPSNKRSPLGGPTPVCKATLSEETCQQLARETLEELDW
CLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISTTFLDKQNEVEI
PSPTMKEREKQQAPRPRPSQPPPPPVPHLQPMSQITGLKKLMHSNSLNNSNIPRFGVKTD
QEELLAQELENLNKWGLNIFCVSDYAGGRSLTCIMYMIFQERDLLKKFRIPVDTMVTYML
TLEDHYHADVAYHNSLHAADVLQSTHVLLATPALDAVFTDLEILAALFAAAIHDVDHPGV
SNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEDNCDIFQNLSKRQRQSLRKMVIDM
VLATDMSKHMTLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLRNMVHCADLSNPTKPLE
LYRQWTDRIMAEFFQQGDRERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADL
VHPDAQEILDTLEDNRDWYYSAIRQSPSPPPEEESRGPGHPPLPDKFQFELTLEEEEEEE
ISMAQIPCTAQEALTAQGLSGVEEALDATIAWEASPAQESLEVMAQEASLEAELEAVYLT
QQAQSTGSAPVAPDEFSSREEFVVAVSHSSPSALALQSPLLPAWRTLSVSEHAPGLPGLP
STAAEVEAQREHQAAKRACSACAGTFGEDTSALPAPGGGGSGGDPT
Enzyme 23 Number of Residues 886
Enzyme 23 Molecular Weight 98142.2
Enzyme 23 Theoretical pI 4.87
Enzyme 23 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 23 General Function Involved in 3',5'-cyclic-nucleotide phosphodiesterase activity
Enzyme 23 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes
Enzyme 23 Pathways
Enzyme 23 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein Not Available
Enzyme 23 UniProtKB/Swiss-Prot ID P27815 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name PDE4A_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >2661 bp
ATGGAACCCCCGACCGTCCCCTCGGAAAGGAGCCTGTCTCTGTCACTGCCCGGGCCCCGG
GAGGGCCAGGCCACCCTGAAGCCTCCCCCGCAGCACCTGTGGCGGCAGCCTCGGACCCCC
ATCCGTATCCAGCAGCGCGGCTACTCCGACAGCGCGGAGCGCGCCGAGCGGGAGCGGCAG
CCGCACCGGCCCATAGAGCGCGCCGATGCCATGGACACCAGCGACCGGCCCGGCCTGCGC
ACGACCCGCATGTCCTGGCCCTCGTCCTTCCATGGCACTGGCACCGGCAGCGGCGGCGCG
GGCGGAGGCAGCAGCAGGCGCTTCGAGGCAGAGAATGGGCCGACACCATCTCCTGGCCGC
AGCCCCCTGGACTCGCAGGCGAGCCCAGGACTCGTGCTGCACGCCGGGGCGGCCACCAGC
CAGCGCCGGGAGTCCTTCCTGTACCGCTCAGACAGCGACTATGACATGTCACCCAAGACC
ATGTCCCGGAACTCATCGGTCACCAGCGAGGCGCACGCTGAAGACCTCATCGTAACACCA
TTTGCTCAGGTGCTGGCCAGCCTCCGGAGCGTCCGTAGCAACTTCTCACTCCTGACCAAT
GTGCCCGTTCCCAGTAACAAGCGGTCCCCGCTGGGCGGCCCCACCCCTGTCTGCAAGGCC
ACGCTGTCAGAAGAAACGTGTCAGCAGTTGGCCCGGGAGACTCTGGAGGAGCTGGACTGG
TGTCTGGAGCAGCTGGAGACCATGCAGACCTATCGCTCTGTCAGCGAGATGGCCTCGCAC
AAGTTCAAAAGGATGTTGAACCGTGAGCTCACACACCTGTCAGAAATGAGCAGGTCCGGA
AACCAGGTCTCAGAGTACATTTCCACAACATTCCTGGACAAACAGAATGAAGTGGAGATC
CCATCACCCACGATGAAGGAACGAGAAAAACAGCAAGCGCCGCGACCAAGACCCTCCCAG
CCGCCCCCGCCCCCTGTACCACACTTACAGCCCATGTCCCAAATCACAGGGTTGAAAAAG
TTGATGCATAGTAACAGCCTGAACAACTCTAACATTCCCCGATTTGGGGTGAAGACCGAT
CAAGAAGAGCTCCTGGCCCAAGAACTGGAGAACCTGAACAAGTGGGGCCTGAACATCTTT
TGCGTGTCGGATTACGCTGGAGGCCGCTCACTCACCTGCATCATGTACATGATATTCCAG
GAGCGGGACCTGCTGAAGAAATTCCGCATCCCGGTGGACACGATGGTGACATACATGCTG
ACGCTGGAGGATCACTACCACGCTGACGTGGCCTACCATAACAGCCTGCACGCAGCTGAC
GTGCTGCAGTCCACCCACGTACTGCTGGCCACGCCTGCACTAGATGCAGTGTTCACGGAC
CTGGAGATTCTCGCCGCCCTCTTCGCGGCTGCCATCCACGATGTGGATCACCCTGGGGTC
TCCAACCAGTTCCTCATCAACACCAATTCGGAGCTGGCGCTCATGTACAACGATGAGTCG
GTGCTCGAGAATCACCACCTGGCCGTGGGCTTCAAGCTGCTGCAGGAGGACAACTGCGAC
ATCTTCCAGAACCTCAGCAAGCGCCAGCGGCAGAGCCTACGCAAGATGGTCATCGACATG
GTGCTGGCCACGGACATGTCCAAGCACATGACCCTCCTGGCTGACCTGAAGACCATGGTG
GAGACCAAGAAAGTGACCAGCTCAGGGGTCCTCCTGCTAGATAACTACTCCGACCGCATC
CAGGTCCTCCGGAACATGGTGCACTGTGCCGACCTCAGCAACCCCACCAAGCCGCTGGAG
CTGTACCGCCAGTGGACAGACCGCATCATGGCCGAGTTCTTCCAGCAGGGTGACCGAGAG
CGCGAGCGTGGCATGGAAATCAGCCCCATGTGTGACAAGCACACTGCCTCCGTGGAGAAG
TCTCAGGTGGGTTTTATTGACTACATTGTGCACCCATTGTGGGAGACCTGGGCGGACCTT
GTCCACCCAGATGCCCAGGAGATCTTGGACACTTTGGAGGACAACCGGGACTGGTACTAC
AGCGCCATCCGGCAGAGCCCATCTCCGCCACCCGAGGAGGAGTCAAGGGGGCCAGGCCAC
CCACCCCTGCCTGACAAGTTCCAGTTTGAGCTGACGCTGGAGGAGGAAGAGGAGGAAGAA
ATATCAATGGCCCAGATACCGTGCACAGCCCAAGAGGCATTGACTGCGCAGGGATTGTCA
GGAGTCGAGGAAGCTCTGGATGCAACCATAGCCTGGGAGGCATCCCCGGCCCAGGAGTCG
TTGGAAGTTATGGCACAGGAAGCATCCCTGGAGGCCGAGCTGGAGGCAGTGTATTTGACA
CAGCAGGCACAGTCCACAGGCAGTGCACCTGTGGCTCCGGATGAGTTCTCGTCCCGGGAG
GAATTCGTGGTTGCTGTAAGCCACAGCAGCCCCTCTGCCCTGGCTCTTCAAAGCCCCCTT
CTCCCTGCTTGGAGGACCCTGTCTGTTTCAGAGCATGCCCCGGGCCTCCCGGGCCTCCCC
TCCACGGCGGCCGAGGTGGAGGCCCAACGAGAGCACCAGGCTGCCAAGAGGGCTTGCAGT
GCCTGCGCAGGGACATTTGGGGAGGACACATCCGCACTCCCAGCTCCTGGTGGCGGGGGG
TCAGGTGGAGACCCTACCTGA
Enzyme 23 GenBank Gene ID L20965 Link Image
Enzyme 23 GeneCard ID PDE4A Link Image
Enzyme 23 GenAtlas ID PDE4A Link Image
Enzyme 23 HGNC ID HGNC:8780 Link Image
Enzyme 23 Chromosome Location 1
Enzyme 23 Locus 19p13.2
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed Link Image]
  2. Sullivan M, Egerton M, Shakur Y, Marquardsen A, Houslay MD: Molecular cloning and expression, in both COS-1 cells and S. cerevisiae, of a human cytosolic type-IVA, cyclic AMP specific phosphodiesterase (hPDE-IVA-h6.1). Cell Signal. 1994 Sep;6(7):793-812. [PubMed Link Image]
  3. Horton YM, Sullivan M, Houslay MD: Molecular cloning of a novel splice variant of human type IVA (PDE-IVA) cyclic AMP phosphodiesterase and localization of the gene to the p13.2-q12 region of human chromosome 19 [corrected] Biochem J. 1995 Jun 1;308 ( Pt 2):683-91. [PubMed Link Image]
  4. Sullivan M, Rena G, Begg F, Gordon L, Olsen AS, Houslay MD: Identification and characterization of the human homologue of the short PDE4A cAMP-specific phosphodiesterase RD1 (PDE4A1) by analysis of the human HSPDE4A gene locus located at chromosome 19p13.2. Biochem J. 1998 Aug 1;333 ( Pt 3):693-703. [PubMed Link Image]
  5. Rena G, Begg F, Ross A, MacKenzie C, McPhee I, Campbell L, Huston E, Sullivan M, Houslay MD: Molecular cloning, genomic positioning, promoter identification, and characterization of the novel cyclic amp-specific phosphodiesterase PDE4A10. Mol Pharmacol. 2001 May;59(5):996-1011. [PubMed Link Image]
  6. Wallace DA, Johnston LA, Huston E, MacMaster D, Houslay TM, Cheung YF, Campbell L, Millen JE, Smith RA, Gall I, Knowles RG, Sullivan M, Houslay MD: Identification and characterization of PDE4A11, a novel, widely expressed long isoform encoded by the human PDE4A cAMP phosphodiesterase gene. Mol Pharmacol. 2005 Jun;67(6):1920-34. Epub 2005 Feb 28. [PubMed Link Image]
  7. Mackenzie KF, Topping EC, Bugaj-Gaweda B, Deng C, Cheung YF, Olsen AE, Stockard CR, High Mitchell L, Baillie GS, Grizzle WE, De Vivo M, Houslay MD, Wang D, Bolger GB: Human PDE4A8, a novel brain-expressed PDE4 cAMP-specific phosphodiesterase that has undergone rapid evolutionary change. Biochem J. 2008 Apr 15;411(2):361-9. [PubMed Link Image]
  8. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  9. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  10. Livi GP, Kmetz P, McHale MM, Cieslinski LB, Sathe GM, Taylor DP, Davis RL, Torphy TJ, Balcarek JM: Cloning and expression of cDNA for a human low-Km, rolipram-sensitive cyclic AMP phosphodiesterase. Mol Cell Biol. 1990 Jun;10(6):2678-86. [PubMed Link Image]
  11. Lario PI, Bobechko B, Bateman K, Kelly J, Vrielink A, Huang Z: Purification and characterization of the human PDE4A catalytic domain (PDE4A330-723) expressed in Sf9 cells. Arch Biochem Biophys. 2001 Oct 1;394(1):54-60. [PubMed Link Image]
  12. Hillman RT, Green RE, Brenner SE: An unappreciated role for RNA surveillance. Genome Biol. 2004;5(2):R8. Epub 2004 Feb 2. [PubMed Link Image]
  13. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  14. Wang H, Peng MS, Chen Y, Geng J, Robinson H, Houslay MD, Cai J, Ke H: Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors. Biochem J. 2007 Dec 1;408(2):193-201. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5927
Enzyme 24 Name cGMP-specific 3',5'-cyclic phosphodiesterase
Enzyme 24 Synonyms
  1. cGMP-binding cGMP-specific phosphodiesterase
  2. CGB-PDE
Enzyme 24 Gene Name PDE5A
Enzyme 24 Protein Sequence >cGMP-specific 3',5'-cyclic phosphodiesterase
MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAE
RVHTIPVCKEGIRGHTESCSCPLQQSPRADNSVPGTPTRKISASEFDRPLRPIVVKDSEG
TVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLI
SADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPL
NIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDE
KDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIIS
FMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTME
PLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGK
VKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETREL
QSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWIL
SVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGV
NNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAI
LATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAE
LVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCF
PLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN
Enzyme 24 Number of Residues 875
Enzyme 24 Molecular Weight 100012.2
Enzyme 24 Theoretical pI 6.00
Enzyme 24 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 24 General Function Involved in catalytic activity
Enzyme 24 Specific Function Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'- GMP
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions
  • guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein Not Available
Enzyme 24 UniProtKB/Swiss-Prot ID O76074 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PDE5A_HUMAN Link Image
Enzyme 24 PDB ID 1T9R Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >2628 bp
ATGGAGCGGGCCGGCCCCAGCTTCGGGCAGCAGCGACAGCAGCAGCAGCCCCAGCAGCAG
AAGCAGCAGCAGAGGGATCAGGACTCGGTCGAAGCATGGCTGGACGATCACTGGGACTTT
ACCTTCTCATACTTTGTTAGAAAAGCCACCAGAGAAATGGTCAATGCATGGTTTGCTGAG
AGAGTTCACACCATCCCTGTGTGCAAGGAAGGTATCAGAGGCCACACCGAATCTTGCTCT
TGTCCCTTGCAGCAGAGTCCTCGTGCAGATAACAGTGTCCCTGGAACACCAACCAGGAAA
ATCTCTGCCTCTGAATTTGACCGGCCTCTTAGACCCATTGTTGTCAAGGATTCTGAGGGA
ACTGTGAGCTTCCTCTCTGACTCAGAAAAGAAGGAACAGATGCCTCTAACCCCTCCAAGG
TTTGATCATGATGAAGGGGACCAGTGCTCAAGACTCTTGGAATTAGTGAAGGATATTTCT
AGTCATTTGGATGTCACAGCCTTATGTCACAAAATTTTCTTGCATATCCATGGACTGATA
TCTGCTGACCGCTATTCCCTGTTCCTTGTCTGTGAAGACAGCTCCAATGACAAGTTTCTT
ATCAGCCGCCTCTTTGATGTTGCTGAAGGTTCAACACTGGAAGAAGTTTCAAATAACTGT
ATCCGCTTAGAATGGAACAAAGGCATTGTGGGACATGTGGCAGCGCTTGGTGAGCCCTTG
AACATCAAAGATGCATATGAGGATCCTCGGTTCAATGCAGAAGTTGACCAAATTACAGGC
TACAAGACACAAAGCATTCTTTGTATGCCAATTAAGAATCATAGGGAAGAGGTTGTTGGT
GTAGCCCAGGCCATCAACAAGAAATCAGGAAACGGTGGGACATTTACTGAAAAAGATGAA
AAGGACTTTGCTGCTTATTTGGCATTTTGTGGTATTGTTCTTCATAATGCTCAGCTCTAT
GAGACTTCACTGCTGGAGAACAAGAGAAATCAGGTGCTGCTTGACCTTGCTAGTTTAATT
TTTGAAGAACAACAATCATTAGAAGTAATTTTGAAGAAAATAGCTGCCACTATTATCTCT
TTCATGCAAGTGCAGAAATGCACCATTTTCATAGTGGATGAAGATTGCTCCGATTCTTTT
TCTAGTGTGTTTCACATGGAGTGTGAGGAATTAGAAAAATCATCTGATACATTAACAAGG
GAACATGATGCAAACAAAATCAATTACATGTATGCTCAGTATGTCAAAAATACTATGGAA
CCACTTAATATCCCAGATGTCAGTAAGGATAAAAGATTTCCCTGGACAACTGAAAATACA
GGAAATGTAAACCAGCAGTGCATTAGAAGTTTGCTTTGTACACCTATAAAAAATGGAAAG
AAGAATAAAGTTATAGGGGTTTGCCAACTTGTTAATAAGATGGAGGAGAATACTGGCAAG
GTTAAGCCTTTCAACCGAAATGACGAACAGTTTCTGGAAGCTTTTGTCATCTTTTGTGGC
TTGGGGATCCAGAACACGCAGATGTATGAAGCAGTGGAGAGAGCCATGGCCAAGCAAATG
GTCACATTGGAGGTTCTGTCGTATCATGCTTCAGCAGCAGAGGAAGAAACAAGAGAGCTA
CAGTCGTTAGCGGCTGCTGTGGTGCCATCTGCCCAGACCCTTAAAATTACTGACTTTAGC
TTCAGTGACTTTGAGCTGTCTGATCTGGAAACAGCACTGTGTACAATTCGGATGTTTACT
GACCTCAACCTTGTGCAGAACTTCCAGATGAAACATGAGGTTCTTTGCAGATGGATTTTA
AGTGTTAAGAAGAATTATCGGAAGAATGTTGCCTATCATAATTGGAGACATGCCTTTAAT
ACAGCTCAGTGCATGTTTGCTGCTCTAAAAGCAGGCAAAATTCAGAACAAGCTGACTGAC
CTGGAGATACTTGCATTGCTGATTGCTGCACTAAGCCACGATTTGGATCACCGTGGTGTG
AATAACTCTTACATACAGCGAAGTGAACATCCACTTGCCCAGCTTTACTGCCATTCAATC
ATGGAACACCATCATTTTGACCAGTGCCTGATGATTCTTAATAGTCCAGGCAATCAGATT
CTCAGTGGCCTCTCCATTGAAGAATATAAGACCACGTTGAAAATAATCAAGCAAGCTATT
TTAGCTACAGACCTAGCACTGTACATTAAGAGGCGAGGAGAATTTTTTGAACTTATAAGA
AAAAATCAATTCAATTTGGAAGATCCTCATCAAAAGGAGTTGTTTTTGGCAATGCTGATG
ACAGCTTGTGATCTTTCTGCAATTACAAAACCCTGGCCTATTCAACAACGGATAGCAGAA
CTTGTAGCAACTGAATTTTTTGATCAAGGAGACAGAGAGAGAAAAGAACTCAACATAGAA
CCCACTGATCTAATGAACAGGGAGAAGAAAAACAAAATCCCAAGTATGCAAGTTGGGTTC
ATAGATGCCATCTGCTTGCAACTGTATGAGGCCCTGACCCACGTGTCAGAGGACTGTTTC
CCTTTGCTAGATGGCTGCAGAAAGAACAGGCAGAAATGGCAGGCCCTTGCAGAACAGCAG
GAGAAGATGCTGATTAATGGGGAAAGCGGCCAGGCCAAGCGGAACTGA
Enzyme 24 GenBank Gene ID AF043731 Link Image
Enzyme 24 GeneCard ID PDE5A Link Image
Enzyme 24 GenAtlas ID PDE5A Link Image
Enzyme 24 HGNC ID HGNC:8784 Link Image
Enzyme 24 Chromosome Location 4
Enzyme 24 Locus 4q27
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Loughney K, Hill TR, Florio VA, Uher L, Rosman GJ, Wolda SL, Jones BA, Howard ML, McAllister-Lucas LM, Sonnenburg WK, Francis SH, Corbin JD, Beavo JA, Ferguson K: Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-binding, cGMP-specific 3',5'-cyclic nucleotide phosphodiesterase. Gene. 1998 Aug 17;216(1):139-47. [PubMed Link Image]
  2. Yanaka N, Kotera J, Ohtsuka A, Akatsuka H, Imai Y, Michibata H, Fujishige K, Kawai E, Takebayashi S, Okumura K, Omori K: Expression, structure and chromosomal localization of the human cGMP-binding cGMP-specific phosphodiesterase PDE5A gene. Eur J Biochem. 1998 Jul 15;255(2):391-9. [PubMed Link Image]
  3. Stacey P, Rulten S, Dapling A, Phillips SC: Molecular cloning and expression of human cGMP-binding cGMP-specific phosphodiesterase (PDE5). Biochem Biophys Res Commun. 1998 Jun 18;247(2):249-54. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Zhou L, Thompson WJ, Potter DE: Multiple cyclic nucleotide phosphodiesterases in human trabecular meshwork cells. Invest Ophthalmol Vis Sci. 1999 Jul;40(8):1745-52. [PubMed Link Image]
  7. Sung BJ, Hwang KY, Jeon YH, Lee JI, Heo YS, Kim JH, Moon J, Yoon JM, Hyun YL, Kim E, Eum SJ, Park SY, Lee JO, Lee TG, Ro S, Cho JM: Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules. Nature. 2003 Sep 4;425(6953):98-102. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5977
Enzyme 25 Name Adenylate cyclase type 7
Enzyme 25 Synonyms
  1. ATP pyrophosphate-lyase 7
  2. Adenylate cyclase type VII
  3. Adenylyl cyclase 7
Enzyme 25 Gene Name ADCY7
Enzyme 25 Protein Sequence >Adenylate cyclase type 7
MPAKGRYFLNEGEEGPDQDALYEKYQLTSQHGPLLLTLLLVAATACVALIIIAFSQGDPS
RHQAILGMAFLVLAVFAALSVLMYVECLLRRWLRALALLTWACLVALGYVLVFDAWTKAA
CAWEQVPFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVLGSLMGGFTTPSVRVGLQL
LANAVIFLCGNLTGAFHKHQMQDASRDLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAH
ISMGMKLAIIERLKEHGDRRCMPDNNFHSLYVKRHQNVSILYADIVGFTQLASDCSPKEL
VVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQAIKQ
VREATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEAT
LKHLDKAYEVEDGHGQQRDPYLKEMNIRTYLVIDPRSQQPPPPSQHLPRPKGDAALKMRA
SVRMTRYLESWGAARPFAHLNHRESVSSGETHVPNGRRPKSVPQRHRRTPDRSMSPKGRS
EDDSYDDEMLSAIEGLSSTRPCCSKSDDFYTFGSIFLEKGFEREYRLAPIPRARHDFACA
SLIFVCILLVHVLLMPRTAALGVSFGLVACVLGLVLGLCFATKFSRCCPARGTLCTISER
VETQPLLRLTLAVLTIGSLLTVAIINLPLMPFQVPELPVGNETGLLAASSKTRALCEPLP
YYTCSCVLGFIACSVFLRMSLEPKVVLLTVALVAYLVLFNLSPCWQWDCCGQGLGNLTKP
NGTTSGTPSCSWKDLKTMTNFYLVLFYITLLTLSRQIDYYCRLDCLWKKKFKKEHEEFET
MENVNRLLLENVLPAHVAAHFIGDKLNEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKE
GLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSVASGHENQELERQHAH
IGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVAS
RMESTGELGKIQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFVCTDTAKFQGLGLN
Enzyme 25 Number of Residues 1080
Enzyme 25 Molecular Weight 120307.2
Enzyme 25 Theoretical pI 8.16
Enzyme 25 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 25 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 25 Specific Function This is a membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 25 Pathways
Enzyme 25 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • 34-54 63-83 95-117 122-142 147-167 176-196 595-615 620-640 669-688 718-737 746-773 794-814
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 116496681 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P51828 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name ADCY7_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >3243 bp
ATGCCAGCCAAGGGGCGCTACTTCCTCAACGAGGGCGAGGAGGGCCCTGACCAAGATGCG
CTCTACGAGAAGTACCAGCTCACCAGCCAGCATGGGCCGCTGCTGCTCACGCTCCTGCTG
GTGGCCGCCACTGCCTGCGTGGCCCTCATCATCATTGCCTTCAGCCAGGGGGACCCCTCC
AGACACCAGGCCATTCTGGGCATGGCGTTCCTGGTGCTGGCGGTGTTTGCGGCCCTCTCT
GTGCTGATGTACGTCGAGTGTCTCCTGCGGCGCTGGCTCAGGGCCTTGGCGCTGCTCACC
TGGGCCTGCTTGGTGGCGCTGGGCTATGTGCTGGTGTTCGACGCATGGACAAAGGCGGCC
TGTGCGTGGGAGCAGGTGCCCTTCTTCCTGTTCATTGTCTTCGTGGTGTACACACTACTG
CCCTTCAGCATGCGGGGCGCTGTCGCCGTTGGGGCCGTCTCCACTGCCTCCCACCTCCTG
GTGCTCGGTTCTTTGATGGGAGGCTTCACGACACCCAGTGTCCGGGTGGGGCTGCAGCTG
CTGGCCAACGCAGTCATCTTCCTGTGTGGGAACCTGACAGGCGCCTTCCACAAGCACCAA
ATGCAGGATGCGTCCCGGGACCTCTTCACCTACACTGTGAAGTGCATCCAGATCCGCCGG
AAGCTGCGCATCGAGAAGCGCCAGCAGGAGAACCTGCTGCTGTCAGTGCTTCCGGCCCAC
ATCTCCATGGGCATGAAGCTGGCCATCATCGAACGGCTCAAGGAGCATGGTGACCGTCGC
TGCATGCCTGACAACAACTTCCACAGCCTCTACGTCAAGAGGCACCAGAATGTCAGCATC
CTCTATGCGGACATCGTGGGCTTCACGCAGCTGGCCAGCGACTGTTCTCCCAAGGAGCTG
GTGGTGGTGCTGAATGAGCTCTTTGGCAAGTTCGACCAGATCGCCAAGGCCAACGAGTGC
ATGCGAATCAAGATCCTCGGCGACTGCTACTACTGTGTATCGGGCCTGCCCGTGTCGCTG
CCTACCCACGCCCGGAACTGCGTGAAGATGGGGCTGGACATGTGCCAGGCCATCAAGCAG
GTGCGGGAGGCCACGGGCGTGGACATCAACATGCGTGTGGGCATACACTCGGGGAATGTG
CTGTGCGGGGTCATCGGGCTGCGCAAGTGGCAGTATGACGTGTGGTCCCACGACGTGTCC
CTGGCCAACCGGATGGAGGCAGCCGGAGTACCCGGCCGGGTGCACATCACGGAGGCCACG
CTAAAGCACCTGGACAAGGCGTACGAGGTGGAGGATGGGCACGGGCAGCAGCGGGACCCC
TACCTCAAGGAGATGAACATCCGCACCTACCTGGTCATCGACCCCCGGAGCCAGCAGCCA
CCCCCGCCCAGCCAACACCTCCCCAGGCCCAAGGGGGACGCGGCCCTGAAGATGCGGGCG
TCAGTGCGCATGACCCGGTACCTCGAGTCCTGGGGGGCGGCACGGCCCTTTGCACATCTC
AACCACCGTGAGAGCGTGAGCAGTGGTGAGACCCACGTCCCCAACGGGCGGAGGCCTAAG
AGCGTTCCCCAGCGCCACCGCCGGACCCCAGACAGAAGCATGTCCCCCAAGGGGCGGTCG
GAGGATGACTCGTACGATGACGAGATGCTGTCAGCCATTGAGGGGCTCAGCTCCACGAGG
CCCTGCTGCTCCAAGTCCGATGACTTCTACACCTTTGGGTCCATCTTCCTGGAGAAGGGC
TTTGAGCGCGAGTACCGCCTGGCACCCATCCCCCGGGCCCGCCACGACTTTGCCTGCGCC
AGCCTGATCTTCGTCTGCATCCTGCTCGTCCATGTCCTGCTCATGCCCAGGACGGCGGCA
CTGGGTGTGTCCTTCGGGCTGGTGGCCTGTGTACTGGGGCTGGTGCTGGGCCTGTGCTTT
GCCACCAAGTTCTCGAGGTGCTGCCCAGCTCGGGGGACGCTCTGCACTATCTCTGAGAGG
GTGGAGACACAGCCCCTGCTGAGGCTGACCCTGGCCGTCCTGACCATCGGCAGCCTGCTC
ACTGTGGCCATCATCAACCTGCCCCTGATGCCTTTCCAAGTTCCAGAGCTGCCTGTTGGC
AATGAGACAGGCCTACTGGCCGCGAGCAGCAAGACAAGAGCCCTGTGTGAGCCCCTCCCG
TACTACACCTGCAGCTGTGTCCTGGGCTTCATCGCCTGCTCGGTCTTCCTGAGGATGAGC
CTGGAGCCAAAGGTTGTGCTGCTGACAGTGGCCCTGGTGGCCTACCTGGTGCTCTTCAAC
CTCTCCCCATGCTGGCAGTGGGACTGCTGCGGCCAAGGCCTGGGCAACCTCACCAAGCCC
AACGGCACCACCAGTGGCACCCCTAGCTGTTCCTGGAAGGACCTGAAGACCATGACCAAT
TTCTACCTGGTCCTGTTCTACATCACCCTGCTTACACTCTCCAGACAGATTGACTATTAC
TGCCGCTTGGACTGCCTATGGAAGAAGAAGTTCAAGAAGGAGCACGAGGAGTTTGAGACC
ATGGAGAACGTGAACCGCCTTCTTCTGGAGAACGTCCTGCCAGCCCACGTGGCTGCCCAC
TTTATCGGTGACAAGTTAAACGAGGACTGGTACCATCAGTCCTATGACTGCGTCTGTGTC
ATGTTTGCCTCCGTGCCGGACTTCAAAGTGTTCTACACAGAGTGCGATGTCAACAAAGAA
GGGCTGGAGTGCCTACGCCTGCTCAATGAGATCATTGCCGACTTCGACGAGCTCCTACTG
AAGCCCAAGTTCAGCGGCGTGGAGAAGATCAAGACCATCGGCAGCACGTACATGGCAGCT
GCAGGGCTCAGCGTCGCCTCAGGGCACGAGAACCAGGAGCTGGAGCGGCAGCATGCCCAC
ATTGGTGTCATGGTGGAGTTCAGCATCGCCCTGATGAGTAAGCTGGACGGCATCAACAGG
CACTCCTTCAACTCCTTCCGCCTCCGCGTCGGCATAAACCATGGGCCTGTGATTGCTGGA
GTGATTGGGGCCCGAAAACCTCAGTATGACATCTGGGGAAACACTGTCAATGTGGCCAGC
CGAATGGAAAGCACTGGAGAACTTGGGAAAATCCAGGTTACCGAGGAGACCTGCACCATC
CTCCAGGGCCTCGGGTACTCTTGTGAATGCCGTGGCCTGATCAACGTCAAAGGCAAAGGC
GAGCTGAGGACTTACTTTGTCTGTACGGACACTGCCAAGTTTCAGGGGCTGGGGCTGAAC
TGA
Enzyme 25 GenBank Gene ID BC126271 Link Image
Enzyme 25 GeneCard ID ADCY7 Link Image
Enzyme 25 GenAtlas ID ADCY7 Link Image
Enzyme 25 HGNC ID HGNC:238 Link Image
Enzyme 25 Chromosome Location 1
Enzyme 25 Locus 16q12.1
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5978
Enzyme 26 Name Adenylate cyclase type 4
Enzyme 26 Synonyms
  1. ATP pyrophosphate-lyase 4
  2. Adenylate cyclase type IV
  3. Adenylyl cyclase 4
Enzyme 26 Gene Name ADCY4
Enzyme 26 Protein Sequence >Adenylate cyclase type 4
MARLFSPRPPPSEDLFYETYYSLSQQYPLLLLLLGIVLCALAALLAVAWASGRELTSDPS
FLTTVLCALGGFSLLLGLASREQRLQRWTRPLSGLVWVALLALGHAFLFTGGVVSAWDQV
SYFLFVIFTAYAMLPLGMRDAAVAGLASSLSHLLVLGLYLGPQPDSRPALLPQLAANAVL
FLCGNVAGVYHKALMERALRATFREALSSLHSRRRLDTEKKHQEHLLLSILPAYLAREMK
AEIMARLQAGQGSRPESTNNFHSLYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNE
LFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIRKLRAATG
VDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAG
AYAVEDAGMEHRDPYLRELGEPTYLVIDPRAEEEDEKGTAGGLLSSLEGLKMRPSLLMTR
YLESWGAAKPFAHLSHGDSPVSTSTPLPEKTLASFSTQWSLDRSRTPRGLDDELDTGDAK
FFQVIEQLNSQKQWKQSKDFNPLTLYFREKEMEKEYRLSAIPAFKYYEACTFLVFLSNFI
IQMLVTNRPPALAITYSITFLLFLLILFVCFSEDLMRCVLKGPKMLHWLPALSGLVATRP
GLRIALGTATILLVFAMAITSLFFFPTSSDCPFQAPNVSSMISNLSWELPGSLPLISVPY
SMHCCTLGFLSCSLFLHMSFELKLLLLLLWLAASCSLFLHSHAWLSECLIVRLYLGPLDS
RPGVLKEPKLMGAISFFIFFFTLLVLARQNEYYCRLDFLWKKKLRQEREETETMENLTRL
LLENVLPAHVAPQFIGQNRRNEDLYHQSYECVCVLFASVPDFKEFYSESNINHEGLECLR
LLNEIIADFDELLSKPKFSGVEKIKTIGSTYMAATGLNATSGQDAQQDAERSCSHLGTMV
EFAVALGSKLDVINKHSFNNFRLRVGLNHGPVVAGVIGAQKPQYDIWGNTVNVASRMEST
GVLGKIQVTEETAWALQSLGYTCYSRGVIKVKGKGQLCTYFLNTDLTRTGPPSATLG
Enzyme 26 Number of Residues 1077
Enzyme 26 Molecular Weight 119792.9
Enzyme 26 Theoretical pI 7.50
Enzyme 26 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 26 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 26 Specific Function This is a membrane-bound, calmodulin-insensitive adenylyl cyclase
Enzyme 26 Pathways
Enzyme 26 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • 29-50 61-80 94-117 120-138 141-162 170-190 586-607 611-633 664-687 715-736 744-764 791-807
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 22212709 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q8NFM4 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name ADCY4_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >3234 bp
ATGGCCCGCCTCTTCAGCCCCCGGCCGCCCCCCAGCGAAGACCTCTTCTACGAGACCTAC
TACAGCCTGAGCCAGCAGTACCCGCTGCTGCTGCTGCTGCTGGGGATCGTGCTCTGTGCG
CTCGCGGCGCTGCTCGCAGTGGCCTGGGCCAGCGGCAGGGAGCTGACCTCAGACCCGAGC
TTCCTGACCACTGTGCTGTGCGCGCTGGGCGGCTTCTCGCTGCTGCTGGGCCTCGCTTCC
CGGGAGCAGCGACTGCAGCGCTGGACGCGTCCCCTGTCCGGCTTGGTATGGGTCGCGCTG
CTAGCGCTAGGCCACGCCTTCCTGTTCACCGGGGGCGTGGTGAGCGCCTGGGACCAGGTG
TCCTATTTTCTCTTCGTCATCTTCACGGCGTATGCCATGCTGCCCTTGGGCATGCGGGAC
GCCGCCGTCGCGGGCCTCGCCTCCTCACTCTCGCATCTGCTGGTCCTCGGGCTGTATCTT
GGGCCACAGCCGGACTCACGGCCTGCACTGCTGCCGCAGTTGGCAGCAAACGCAGTGCTG
TTCCTGTGCGGGAACGTGGCAGGAGTGTACCACAAGGCGCTGATGGAGCGCGCCCTGCGG
GCCACGTTCCGGGAGGCACTCAGCTCCCTGCACTCACGCCGGCGGCTGGACACCGAGAAG
AAGCACCAGGAACACCTTCTCTTGTCCATCCTTCCTGCCTACCTGGCCCGAGAGATGAAG
GCAGAGATCATGGCACGGCTGCAGGCAGGACAGGGGTCACGGCCAGAGAGCACTAACAAT
TTCCACAGCCTCTATGTCAAGAGGCACCAGGGAGTCAGCGTGCTGTATGCTGACATCGTG
GGCTTCACGCGGCTGGCCAGCGAGTGTTCCCCTAAGGAGCTGGTGCTCATGCTCAATGAG
CTCTTTGGCAAGTTCGACCAGATTGCCAAGGAGCATGAATGCATGCGGATCAAGATCCTG
GGGGACTGTTACTACTGTGTCTCTGGGCTGCCACTCTCACTGCCAGACCATGCCATCAAC
TGCGTGCGCATGGGCCTGGACATGTGCCGGGCCATCAGGAAACTGCGGGCAGCCACTGGC
GTGGACATCAACATGCGTGTGGGCGTGCACTCAGGCAGCGTACTGTGTGGAGTCATCGGG
CTGCAGAAGTGGCAGTACGACGTTTGGTCACATGATGTCACACTGGCTAACCACATGGAG
GCAGGCGGTGTACCAGGGCGAGTGCACATCACAGGGGCTACCCTGGCCCTGCTGGCAGGG
GCTTATGCTGTGGAGGACGCAGGCATGGAGCATCGGGACCCCTACCTTCGGGAGCTAGGG
GAGCCTACCTATCTGGTCATCGATCCACGGGCAGAGGAGGAGGATGAGAAGGGCACTGCA
GGAGGCTTGCTGTCCTCGCTTGAGGGCCTCAAGATGCGTCCATCACTGCTGATGACCCGT
TACCTGGAGTCCTGGGGCGCAGCCAAGCCTTTTGCCCACCTGAGCCACGGAGACAGCCCT
GTGTCCACCTCCACCCCTCTCCCGGAGAAGACCCTGGCTTCCTTCAGCACCCAGTGGAGC
CTGGATCGGAGCCGTACCCCCCGGGGACTAGATGATGAACTGGACACCGGGGATGCCAAG
TTCTTCCAGGTCATTGAGCAGCTCAACTCGCAGAAACAGTGGAAGCAGTCGAAGGACTTC
AACCCACTGACACTGTACTTCAGAGAGAAGGAGATGGAGAAAGAGTACCGACTCTCTGCA
ATCCCCGCCTTCAAATACTATGAAGCCTGCACCTTCCTGGTTTTTCTCTCCAACTTCATC
ATCCAGATGCTAGTGACAAACAGGCCCCCAGCTCTGGCCATCACGTATAGCATCACCTTC
CTCCTCTTCCTCCTCATCCTTTTTGTCTGCTTCTCAGAGGACCTGATGAGGTGTGTCCTG
AAAGGCCCCAAGATGCTGCACTGGCTGCCTGCACTGTCTGGCCTGGTGGCCACACGACCA
GGACTGAGAATAGCCTTGGGCACCGCCACCATCCTCCTTGTCTTTGCCATGGCCATTACC
AGCCTGTTCTTCTTCCCAACATCATCAGACTGCCCTTTCCAAGCTCCCAATGTGTCCTCC
ATGATTTCCAACCTCTCCTGGGAGCTCCCTGGGTCTCTGCCTCTCATCAGTGTCCCATAC
TCCATGCACTGCTGCACGCTGGGCTTCCTCTCCTGCTCCCTCTTTCTGCACATGAGCTTC
GAGCTGAAGCTGCTGCTGCTCCTGCTGTGGCTGGCGGCATCCTGCTCCCTCTTCCTGCAC
TCCCATGCCTGGCTGTCGGAATGCCTCATCGTCCGCCTCTATCTGGGCCCCTTGGACTCC
AGGCCCGGAGTGCTGAAGGAGCCCAAACTGATGGGTGCTATCTCCTTCTTCATCTTCTTC
TTCACCCTCCTTGTCCTGGCTCGCCAGAATGAGTACTACTGCCGCCTGGACTTCCTGTGG
AAGAAGAAGCTGAGGCAGGAGAGGGAGGAGACAGAGACGATGGAGAACCTGACTCGGCTG
CTCTTGGAGAACGTGCTCCCTGCACACGTGGCCCCCCAGTTCATTGGCCAGAACCGGCGC
AACGAGGATCTCTACCACCAGTCCTATGAATGCGTTTGTGTCCTCTTCGCCTCAGTCCCA
GACTTCAAGGAGTTCTACTCTGAATCCAACATCAATCATGAGGGCCTAGAGTGTCTGAGG
CTGCTCAATGAGATAATTGCTGATTTTGATGAGCTGCTCTCCAAGCCCAAGTTCAGTGGG
GTGGAGAAGATCAAGACCATCGGCAGCACCTACATGGCAGCCACAGGCTTAAATGCCACC
TCTGGACAGGATGCACAACAGGATGCTGAACGGAGCTGCAGCCACCTTGGCACTATGGTG
GAATTTGCCGTGGCCCTGGGGTCTAAGCTGGACGTCATCAACAAGCATTCATTCAACAAC
TTCCGCCTGCGAGTGGGGTTGAACCATGGACCCGTAGTAGCTGGAGTTATTGGGGCCCAG
AAGCCGCAATATGACATTTGGGGCAACACAGTGAACGTGGCCAGCCGCATGGAGAGTACA
GGAGTCCTTGGCAAAATCCAAGTGACTGAGGAGACAGCATGGGCCCTACAGTCCCTGGGC
TACACCTGCTACAGCCGGGGTGTCATCAAGGTGAAAGGCAAAGGGCAGCTCTGCACCTAC
TTCCTGAACACAGACTTGACACGAACTGGACCTCCTTCAGCTACCCTAGGCTGA
Enzyme 26 GenBank Gene ID AF497516 Link Image
Enzyme 26 GeneCard ID ADCY4 Link Image
Enzyme 26 GenAtlas ID ADCY4 Link Image
Enzyme 26 HGNC ID HGNC:235 Link Image
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 14q12
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Ludwig MG, Seuwen K: Characterization of the human adenylyl cyclase gene family: cDNA, gene structure, and tissue distribution of the nine isoforms. J Recept Signal Transduct Res. 2002 Feb-Nov;22(1-4):79-110. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 5979
Enzyme 27 Name Adenylate cyclase type 6
Enzyme 27 Synonyms
  1. ATP pyrophosphate-lyase 6
  2. Adenylate cyclase type VI
  3. Adenylyl cyclase 6
  4. Ca(2+)-inhibitable adenylyl cyclase
Enzyme 27 Gene Name ADCY6
Enzyme 27 Protein Sequence >Adenylate cyclase type 6
MSWFSGLLVPKVDERKTAWGERNGQKRSRRRGTRAGGFCTPRYMSCLRDAEPPSPTPAGP
PRCPWQDDAFIRRGGPGKGKELGLRAVALGFEDTEVTTTAGGTAEVAPDAVPRSGRSCWR
RLVQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLTAVLLAFHAAPARPQPAY
VALLACAAALFVGLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAADPRSPSAGLW
CPVFFVYIAYTLLPIRMRAAVLSGLGLSTLHLILAWQLNRGDAFLWKQLGANVLLFLCTN
VIGICTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINT
KKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHC
LRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRV
HCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNGDYEVEPGRGGERNA
YLKEQHIETFLILGASQKRKEEKAMLAKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFR
QMGIDDSSKDNRGTQDALNPEDEVDEFLSRAIDARSIDQLRKDHVRRFLLTFQREDLEKK
YSRKVDPRFGAYVACALLVFCFICFIQLLIFPHSTLMLGIYASIFLLLLITVLICAVYSC
GSLFPKALQRLSRSIVRSRAHSTAVGIFSVLLVFTSAIANMFTCNHTPIRSCAARMLNLT
PADITACHLQQLNYSLGLDAPLCEGTMPTCSFPEYFIGNMLLSLLASSVFLHISSIGKLA
MIFVLGLIYLVLLLLGPPATIFDNYDLLLGVHGLASSNETFDGLDCPAAGRVALKYMTPV
ILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHF
LARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIIS
EERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNN
FQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKG
YQLECRGVVKVKGKGEMTTYFLNGGPSS
Enzyme 27 Number of Residues 1168
Enzyme 27 Molecular Weight 130614.1
Enzyme 27 Theoretical pI 8.27
Enzyme 27 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 27 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 27 Specific Function Membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 27 Pathways
Enzyme 27 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • 152-168 181-197 214-230 239-255 259-275 289-305 674-691 702-718 743-759 820-836 839-855 897-913
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein Not Available
Enzyme 27 UniProtKB/Swiss-Prot ID O43306 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name ADCY6_HUMAN Link Image
Enzyme 27 PDB ID 1U0H Link Image
Enzyme 27 PDB File Show
Enzyme 27 3D Structure
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >3507 bp
ATGTCATGGTTTAGTGGCCTCCTGGTCCCTAAAGTGGATGAACGGAAAACAGCCTGGGGC
GAACGCAATGGGCAGAAGCGTTCGCGGCGCCGTGGCACTCGGGCAGGTGGCTTCTGCACG
CCCCGCTATATGAGCTGCCTCCGGGATGCAGAGCCACCCAGCCCCACCCCTGCCGGCCCC
CCTCGGTGCCCCTGGCAGGATGACGCCTTCATCCGGAGGGGCGGCCCAGGCAAGGGCAAG
GAGCTGGGGCTGCGGGCAGTGGCCCTGGGCTTCGAGGATACCGAGGTGACAACGACAGCG
GGCGGGACGGCTGAGGTGGCGCCCGACGCGGTGCCCAGGAGTGGGCGATCCTGCTGGCGC
CGTCTGGTGCAGGTGTTCCAGTCGAAGCAGTTCCGTTCGGCCAAGCTGGAGCGCCTGTAC
CAGCGGTACTTCTTCCAGATGAACCAGAGCAGCCTGACGCTGCTGATGGCGGTGCTGGTG
CTGCTCACAGCGGTGCTGCTGGCTTTCCACGCCGCACCCGCCCGCCCTCAGCCTGCCTAT
GTGGCACTGTTGGCCTGTGCCGCCGCCCTGTTCGTGGGGCTCATGGTGGTGTGTAACCGG
CATAGCTTCCGCCAGGACTCCATGTGGGTGGTGAGCTACGTGGTGCTGGGCATCCTGGCG
GCAGTGCAGGTCGGGGGCGCTCTCGCAGCAGACCCGCGCAGCCCCTCTGCGGGCCTCTGG
TGCCCTGTGTTCTTTGTCTACATCGCCTACACGCTCCTCCCCATCCGCATGCGGGCTGCC
GTCCTCAGCGGCCTGGGCCTCTCCACCTTGCATTTGATCTTGGCCTGGCAACTTAACCGT
GGTGATGCCTTCCTCTGGAAGCAGCTCGGTGCCAATGTGCTGCTGTTCCTCTGCACCAAC
GTCATTGGCATCTGCACACACTATCCAGCAGAGGTGTCTCAGCGCCAGGCCTTTCAGGAG
ACCCGCGGTTACATCCAGGCCCGGCTCCACCTGCAGCATGAGAATCGGCAGCAGGAGCGG
CTGCTGCTGTCGGTATTGCCCCAGCACGTTGCCATGGAGATGAAAGAAGACATCAACACA
AAAAAAGAAGACATGATGTTCCACAAGATCTACATACAGAAGCATGACAATGTCAGCATC
CTGTTTGCAGACATTGAGGGCTTCACCAGCCTGGCATCCCAGTGCACTGCGCAGGAGCTG
GTCATGACCCTGAATGAGCTCTTTGCCCGGTTTGACAAGCTGGCTGCGGAGAATCACTGC
CTGAGGATCAAGATCTTGGGGGACTGTTACTACTGTGTGTCAGGGCTGCCGGAGGCCCGG
GCCGACCATGCCCACTGCTGTGTGGAGATGGGGGTAGACATGATTGAGGCCATCTCGCTG
GTACGTGAGGTGACAGGTGTGAATGTGAACATGCGCGTGGGCATCCACAGCGGGCGCGTG
CACTGCGGCGTCCTTGGCTTGCGGAAATGGCAGTTCGATGTGTGGTCCAATGATGTGACC
CTGGCCAACCACATGGAGGCAGGAGGCCGGGCTGGCCGCATCCACATCACTCGGGCAACA
CTGCAGTACCTGAACGGGGACTACGAGGTGGAGCCAGGCCGTGGTGGCGAGCGCAACGCG
TACCTCAAGGAGCAGCACATTGAGACTTTCCTCATCCTGGGCGCCAGCCAGAAACGGAAA
GAGGAGAAGGCCATGCTGGCCAAGCTGCAGCGGACTCGGGCCAACTCCATGGAAGGGCTG
ATGCCGCGCTGGGTTCCTGATCGTGCCTTCTCCCGGACCAAGGACTCCAAGGCCTTCCGC
CAGATGGGCATTGATGATTCCAGCAAAGACAACCGGGGCACCCAAGATGCCCTGAACCCT
GAGGATGAGGTGGATGAGTTCCTGAGCCGTGCCATCGATGCCCGCAGCATTGATCAGCTG
CGGAAGGACCATGTGCGCCGGTTTCTGCTCACCTTCCAGAGAGAGGATCTTGAGAAGAAG
TACTCCCGGAAGGTGGATCCCCGCTTCGGAGCCTACGTTGCCTGTGCCCTGTTGGTCTTC
TGCTTCATCTGCTTCATCCAGCTTCTCATCTTCCCACACTCCACCCTGATGCTTGGGATC
TATGCCAGCATCTTCCTGCTGCTGCTAATCACCGTGCTGATCTGTGCTGTGTACTCCTGT
GGTTCTCTGTTCCCTAAGGCCCTGCAACGTCTGTCCCGCAGCATTGTCCGCTCACGGGCA
CATAGCACCGCAGTTGGCATCTTTTCCGTCCTGCTTGTGTTTACTTCTGCCATTGCCAAC
ATGTTCACCTGTAACCACACCCCCATACGGAGCTGTGCAGCCCGGATGCTGAATTTAACA
CCTGCTGACATCACTGCCTGCCACCTGCAGCAGCTCAATTACTCTCTGGGCCTGGATGCT
CCCCTGTGTGAGGGCACCATGCCCACCTGCAGCTTTCCTGAGTACTTCATCGGGAACATG
CTGCTGAGTCTCTTGGCCAGCTCTGTCTTCCTGCACATCAGCAGCATCGGGAAGTTGGCC
ATGATCTTTGTCTTGGGGCTCATCTATTTGGTGCTGCTTCTGCTGGGTCCCCCAGCCACC
ATCTTTGACAACTATGACCTACTGCTTGGCGTCCATGGCTTGGCTTCTTCCAATGAGACC
TTTGATGGGCTGGACTGTCCAGCTGCAGGGAGGGTGGCCCTCAAATATATGACCCCTGTG
ATTCTGCTGGTGTTTGCGCTGGCGCTGTATCTGCATGCTCAGCAGGTGGAGTCGACTGCC
CGCCTAGACTTCCTCTGGAAACTACAGGCAACAGGGGAGAAGGAGGAGATGGAGGAGCTA
CAGGCATACAACCGGAGGCTGCTGCATAACATTCTGCCCAAGGACGTGGCGGCCCACTTC
CTGGCCCGGGAGCGCCGCAATGATGAACTCTACTATCAGTCGTGTGAGTGTGTGGCTGTT
ATGTTTGCCTCCATTGCCAACTTCTCTGAGTTCTATGTGGAGCTGGAGGCAAACAATGAG
GGTGTCGAGTGCCTGCGGCTGCTCAACGAGATCATCGCTGACTTTGATGAGATTATCAGC
GAGGAGCGGTTCCGGCAGCTGGAAAAGATCAAGACGATTGGTAGCACCTACATGGCTGCC
TCAGGGCTGAACGCCAGCACCTACGATCAGGTGGGCCGCTCCCACATCACTGCCCTGGCT
GACTACGCCATGCGGCTCATGGAGCAGATGAAGCACATCAATGAGCACTCCTTCAACAAT
TTCCAGATGAAGATTGGGCTGAACATGGGCCCAGTCGTGGCAGGTGTCATCGGGGCTCGG
AAGCCACAGTATGACATCTGGGGGAACACAGTGAATGTCTCTAGTCGTATGGACAGCACG
GGGGTCCCCGACCGAATCCAGGTGACCACGGACCTGTACCAGGTTCTAGCTGCCAAGGGC
TACCAGCTGGAGTGTCGAGGGGTGGTCAAGGTGAAGGGCAAGGGGGAGATGACCACCTAC
TTCCTCAATGGGGGCCCCAGCAGTTAA
Enzyme 27 GenBank Gene ID AF250226 Link Image
Enzyme 27 GeneCard ID ADCY6 Link Image
Enzyme 27 GenAtlas ID ADCY6 Link Image
Enzyme 27 HGNC ID HGNC:237 Link Image
Enzyme 27 Chromosome Location 1
Enzyme 27 Locus 12q12-q13
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Wicker R, Catalan AG, Cailleux A, Starenki D, Stengel D, Sarasin A, Suarez HG: Cloning and expression of human adenylyl cyclase type VI in normal thyroid tissues. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):279-83. [PubMed Link Image]
  2. Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1997 Oct 31;4(5):307-13. [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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [PubMed Link Image]
  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  7. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 5980
Enzyme 28 Name Adenylate cyclase type 5
Enzyme 28 Synonyms
  1. ATP pyrophosphate-lyase 5
  2. Adenylate cyclase type V
  3. Adenylyl cyclase 5
Enzyme 28 Gene Name ADCY5
Enzyme 28 Protein Sequence >Adenylate cyclase type 5
MSGSKSVSPPGYAAQKTAAPAPRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGA
VTPQQQQRLASRWRSDDDDDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRR
GAASGGSTRAPPAGGGGGSAAAAASAGGTEVRPRSVEVGLEERRGKGRAADELEAGAVEG
GEGSGDGGSSADSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQS
SLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGL
ACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSAL
HLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLH
SQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTS
LASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEM
GMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGK
AGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMN
RQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFL
GRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQI
TIVPHSIFMLSFYLTCSLLLTLVVFVSVIYSCVKLFPSPLQTLSRKIVRSKMNSTLVGVF
TITLVFLAAFVNMFTCNSRDLLGCLAQEHNISASQVNACHVAESAVNYSLGDEQGFCGSP
WPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADL
LVTANAIDFFNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKL
QATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANF
SEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTY
DKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWG
NTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPL
S
Enzyme 28 Number of Residues 1261
Enzyme 28 Molecular Weight 138906.4
Enzyme 28 Theoretical pI 7.25
Enzyme 28 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 28 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 28 Specific Function This is a membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 28 Pathways
Enzyme 28 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • 196-216 242-262 268-288 299-319 325-345 374-394 770-790 792-812 836-856 910-930 935-955 984-1004
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 34486092 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID O95622 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name ADCY5_HUMAN Link Image
Enzyme 28 PDB ID 1U0H Link Image
Enzyme 28 PDB File Show
Enzyme 28 3D Structure
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >3786 bp
ATGTCCGGCTCCAAAAGCGTGAGCCCCCCGGGCTACGCGGCGCAGAAGACTGCGGCGCCG
GCGCCCCGGGGAGGCCCCGAACACCGCTCTGCGTGGGGCGAGGCCGATTCCCGCGCGAAT
GGCTACCCCCATGCCCCCGGGGGCTCTGCCCGCGGCTCCACCAAGAAACCCGGGGGGGCG
GTGACCCCGCAGCAGCAGCAGCGCCTGGCCAGCCGCTGGCGCAGCGACGACGACGACGAT
CCTCCGCTGAGCGGTGACGACCCCCTGGCCGGGGGCTTCGGCTTCAGCTTCCGCTCCAAG
TCCGCCTGGCAGGAGCGCGGCGGCGACGACTGCGGTCGCGGCAGCCGCCGGCAGCGGCGG
GGCGCGGCCAGCGGGGGCAGCACCCGGGCGCCCCCTGCGGGCGGCGGCGGCGGCTCGGCG
GCGGCGGCTGCCTCGGCGGGCGGGACGGAGGTGCGCCCTCGCTCGGTGGAGGTGGGTCTG
GAGGAGCGGCGGGGCAAGGGGCGCGCGGCCGACGAGCTGGAGGCCGGCGCCGTCGAGGGC
GGCGAGGGGTCCGGGGATGGCGGCAGCTCGGCGGACTCGGGCTCGGGCGCGGGGCCCGGC
GCGGTGCTGTCCCTGGGCGCCTGCTGCCTGGCGTTGCTGCAGATATTCCGCTCCAAGAAG
TTCCCGTCGGACAAACTGGAGCGGCTGTACCAGCGCTACTTCTTCCGCCTGAACCAGAGC
AGCCTCACCATGCTCATGGCCGTGCTGGTGCTCGTGTGCCTGGTCATGTTGGCCTTCCAC
GCGGCGCGGCCCCCGCTCCAGCTGCCCTACCTGGCCGTGCTGGCGGCCGCCGTCGGCGTG
ATCCTCATCATGGCTGTGCTTTGCAACCGCGCCGCCTTCCACCAGGACCACATGGGCCTG
GCCTGCTATGCGCTCATCGCCGTGGTGCTGGCCGTCCAGGTGGTGGGCCTGCTGCTGCCG
CAGCCACGCAGCGCCTCTGAGGGCATCTGGTGGACCGTGTTCTTCATCTACACCATCTAC
ACGCTGCTGCCCGTGCGCATGCGGGCCGCAGTGCTCAGCGGGGTGCTCCTGTCCGCCCTC
CACCTGGCCATCGCCCTGCGCACCAACGCCCAGGACCAGTTCCTGCTGAAGCAGCTTGTC
TCCAATGTTCTCATTTTCTCCTGCACCAACATCGTGGGTGTCTGCACCCACTATCCGGCT
GAGGTCTCCCAGAGACAGGCTTTCCAGGAGACCCGAGAGTGCATCCAGGCGCGGCTCCAC
TCGCAGCGGGAGAACCAGCAGCAGGAACGGCTCCTGCTGTCTGTCCTTCCCCGTCATGTT
GCCATGGAGATGAAAGCAGACATCAACGCCAAGCAGGAGGATATGATGTTCCATAAGATT
TACATCCAGAAACATGACAACGTGAGCATCCTGTTTGCTGACATCGAGGGCTTCACCAGC
CTGGCGTCCCAGTGCACTGCACAGGAACTGGTCATGACCCTCAACGAGCTCTTCGCCCGC
TTTGACAAGCTGGCCGCAGAGAATCACTGTTTACGTATTAAGATCCTTGGGGATTGTTAT
TACTGCGTCTCGGGGCTGCCTGAAGCAAGGGCTGACCACGCCCACTGCTGTGTGGAGATG
GGCATGGACATGATCGAGGCCATCTCGTTGGTCCGGGAGGTGACAGGGGTGAACGTGAAC
ATGCGTGTGGGAATTCACAGCGGGCGAGTACACTGCGGTGTCCTTGGTCTCAGGAAGTGG
CAGTTCGACGTCTGGTCTAACGATGTCACGCTAGCCAACCACATGGAGGCTGGCGGCAAG
GCAGGACGCATCCACATCACCAAGGCTACACTCAACTACCTGAATGGGGACTACGAGGTG
GAGCCAGGCTGTGGGGGCGAGCGCAACGCCTACCTCAAGGAGCACAGTATCGAGACCTTC
CTCATCCTGCGCTGCACCCAGAAGCGGAAAGAAGAGAAGGCCATGATCGCCAAGATGAAC
CGCCAGAGAACCAACTCCATCGGGCACAACCCACCACACTGGGGGGCTGAGCGCCCCTTC
TACAACCACCTGGGTGGCAACCAGGTGTCCAAGGAGATGAAGCGGATGGGCTTTGAAGAC
CCCAAGGACAAGAACGCCCAGGAGAGTGCGAACCCTGAGGATGAAGTGGATGAGTTTCTG
GGCCGTGCCATTGACGCCAGGAGCATTGATAGGCTTCGGTCTGAGCACGTCCGCAAGTTC
CTCCTGACCTTCAGGGAGCCTGACTTAGAGAAGAAGTACTCCAAGCAGGTAGACGACCGA
TTTGGTGCCTATGTGGCGTGTGCCTCGCTCGTCTTCCTCTTCATCTGCTTTGTCCAGATC
ACCATCGTGCCCCACTCCATATTCATGCTCAGCTTCTACCTGACCTGTTCCCTGCTGCTG
ACCTTGGTGGTGTTTGTGTCTGTGATCTACTCCTGCGTAAAGCTCTTCCCCTCCCCACTG
CAGACCCTCTCCAGGAAGATCGTGCGGTCCAAGATGAACAGCACCCTGGTTGGGGTGTTC
ACCATCACCCTGGTGTTCCTGGCGGCTTTTGTCAACATGTTCACGTGCAACTCCAGGGAC
CTGCTGGGCTGCTTGGCACAGGAGCACAACATCAGCGCGAGCCAGGTCAACGCGTGTCAC
GTGGCGGAGTCGGCCGTCAACTACAGCCTGGGCGATGAGCAGGGCTTCTGTGGCAGCCCC
TGGCCCAACTGCAACTTCCCCGAGTACTTCACCTACAGCGTGCTGCTCAGCCTGCTGGCC
TGCTCCGTGTTCCTGCAGATCAGCTGCATCGGGAAGCTGGTGCTCATGCTGGCCATCGAG
CTCATCTACGTGCTCATCGTGGAGGTGCCAGGTGTCACGCTCTTCGACAACGCCGACCTG
CTGGTCACCGCCAACGCCATAGACTTCTTCAACAACGGGACCTCCCAGTGCCCTGAGCAT
GCAACCAAGGTGGCATTGAAGGTGGTGACGCCCATCATCATCTCAGTCTTTGTGCTGGCC
CTGTACCTGCACGCCCAGCAGGTGGAGTCCACTGCCCGCCTCGACTTCCTCTGGAAACTG
CAGGCCACAGAGGAGAAAGAGGAGATGGAGGAGCTGCAGGCCTACAACCGGCGGCTGCTG
CACAACATCCTGCCCAAGGACGTGGCCGCTCACTTCCTGGCCCGCGAGCGGCGCAATGAT
GAGCTCTACTATCAGTCCTGTGAGTGTGTGGCGGTCATGTTCGCCTCCATCGCCAACTTC
TCCGAGTTCTACGTTGAGCTGGAGGCCAACAACGAGGGTGTCGAGTGCCTGCGGCTACTC
AATGAGATCATCGCTGACTTTGATGAGATCATCAGCGAGGATCGGTTCCGGCAGCTGGAG
AAGATCAAGACCATCGGCAGCACCTACATGGCTGCCTCCGGCCTCAACGACTCTACCTAC
GACAAGGTGGGCAAGACCCACATCAAGGCACTGGCCGACTTTGCCATGAAGCTGATGGAC
CAGATGAAGTACATCAATGAGCACTCCTTCAACAACTTCCAGATGAAGATCGGGCTCAAC
ATCGGCCCCGTGGTGGCCGGGGTGATAGGGGCACGAAAGCCTCAGTACGACATCTGGGGC
AATACCGTGAACGTGGCCAGCCGCATGGACAGCACCGGTGTACCCGACCGCATCCAGGTC
ACCACAGACATGTACCAGGTGCTGGCTGCCAACACGTACCAGCTGGAGTGCCGGGGCGTG
GTCAAGGTCAAGGGCAAAGGCGAGATGATGACCTACTTCCTCAATGGAGGGCCCCCGCTC
AGTTAG
Enzyme 28 GenBank Gene ID NM_183357.1 Link Image
Enzyme 28 GeneCard ID ADCY5 Link Image
Enzyme 28 GenAtlas ID ADCY5 Link Image
Enzyme 28 HGNC ID HGNC:236 Link Image
Enzyme 28 Chromosome Location 3
Enzyme 28 Locus 3q13.2-q21
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  2. Ludwig MG, Seuwen K: Characterization of the human adenylyl cyclase gene family: cDNA, gene structure, and tissue distribution of the nine isoforms. J Recept Signal Transduct Res. 2002 Feb-Nov;22(1-4):79-110. [PubMed Link Image]
  3. Raimundo S, Giray J, Volff JN, Schwab M, Altenbuchner J, Ratge D, Wisser H: Cloning and sequence of partial cDNAs encoding the human type V and VI adenylyl cyclases and subsequent RNA-quantification in various tissues. Clin Chim Acta. 1999 Jul;285(1-2):155-61. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 5981
Enzyme 29 Name Adenylate cyclase type 8
Enzyme 29 Synonyms
  1. ATP pyrophosphate-lyase 8
  2. Adenylate cyclase type VIII
  3. Adenylyl cyclase 8
  4. Ca(2+)/calmodulin-activated adenylyl cyclase
Enzyme 29 Gene Name ADCY8
Enzyme 29 Protein Sequence >Adenylate cyclase type 8
MELSDVRCLTGSEELYTIHPTPPAGDGRSASRPQRLLWQTAVRHITEQRFIHGHRGGSGS
GSGGSGKASDPAGGGPNHHAPQLSGDSALPLYSLGPGERAHSTCGTKVFPERSGSGSASG
SGGGGDLGFLHLDCAPSNSDFFLNGGYSYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRK
SEVVMNVLDVLTKLTLLVLHLSLASAPMDPLKGILLGFFTGIEVVICALVVVRKDTTSHT
YLQYSGVVTWVAMTTQILAAGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLGTS
LLQVILQVVIPRLAVISINQVVAQAVLFMCMNTAGIFISYLSDRAQRQAFLETRRCVEAR
LRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDEHLQHQFHRIYIHRYENVSILFADV
KGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRQDHAH
CCVEMGLSMIKTIRYVRSRTKHDVDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKL
ESGGIPGRIHISKATLDCLNGDYNVEEGHGKERNEFLRKHNIETYLIKQPEDSLLSLPED
IVKESVSSSDRRNSGATFTEGSWSPELPFDNIVGKQNTLAALTRNSINLLPNHLAQALHV
QSGPEEINKRIEHTIDLRSGDKLRREHIKPFSLMFKDSSLEHKYSQMRDEVFKSNLVCAF
IVLLFITAIQSLLPSSRVMPMTIQFSILIMLHSALVLITTAEDYKCLPLILRKTCCWINE
TYLARNVIIFASILINFLGAILNILWCDFDKSIPLKNLTFNSSAVFTDICSYPEYFVFTG
VLAMVTCAVFLRLNSVLKLAVLLIMIAIYALLTETVYAGLFLRYDNLNHSGEDFLGTKEV
SLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMKELREHNENMLRNILPSHVA
RHFLEKDRDNEELYSQSYDAVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDE
LLGEDRFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWGHLCALADFSLALTESIQEINKH
SFNNFELRIGISHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSGRIQVPEETYLIL
KDQGFAFDYRGEIYVKGISEQEGKIKTYFLLGRVQPNPFILPPRRLPGQYSLAAVVLGLV
QSLNRQRQKQLLNENNNTGIIKGHYNRRTLLSPSGTEPGAQAEGTDKSDLP
Enzyme 29 Number of Residues 1251
Enzyme 29 Molecular Weight 140120.8
Enzyme 29 Theoretical pI 6.99
Enzyme 29 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 29 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 29 Specific Function This is a membrane-bound, calcium-stimulable adenylyl cyclase. May be involved in learning, in memory and in drug dependence
Enzyme 29 Pathways
Enzyme 29 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • 183-203 212-232 247-267 274-294 296-316 321-341 716-736 738-758 787-807 831-851 861-881 894-914
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 516263 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P40145 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name ADCY8_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >3756 bp
ATGGAGCTCTCCGATGTGCGCTGCCTTACAGGCAGCGAGGAACTCTACACCATCCACCCG
ACGCCCCCGGCCGGCGACGGCAGGAGCGCCTCCCGGCCGCAGCGGCTGCTGTGGCAGACG
GCGGTGCGACACATCACGGAGCAGCGCTTCATTCACGGGCACCGGGGAGGCAGCGGCAGC
GGGAGTGGAGGCTCGGGCAAAGCCTCGGACCCTGCGGGCGGCGGCCCCAACCACCACGCG
CCGCAGCTGTCAGGCGACTCGGCGCTGCCCCTCTACTCGCTGGGCCCGGGAGAGCGAGCG
CACAGCACCTGCGGCACCAAAGTCTTCCCGGAACGCAGCGGGAGCGGCAGTGCCAGCGGC
AGCGGAGGCGGGGGCGACCTGGGCTTCCTGCACCTTGACTGTGCCCCTAGCAACTCGGAT
TTCTTTCTTAATGGGGGCTATAGCTACCGAGGGGTCATTTTCCCCACCCTGCGCAACTCC
TTCAAATCTCGGGATTTGGAACGCCTCTACCAGCGCTATTTCTTGGGCCAAAGGCGCAAA
TCGGAAGTGGTGATGAACGTGCTGGACGTGCTGACCAAACTCACTCTCTTGGTCCTACAC
TTGAGCCTGGCCTCGGCCCCCATGGACCCGCTCAAGGGCATCCTGCTGGGCTTCTTCACC
GGCATTGAGGTAGTGATCTGCGCCCTGGTGGTGGTCAGGAAGGACACCACCTCCCACACG
TACCTGCAGTACAGCGGCGTGGTCACCTGGGTGGCCATGACCACCCAGATCCTGGCAGCA
GGCCTCGGCTACGGGCTCCTGGGCGACGGCATAGGCTACGTGCTCTTCACGCTCTTCGCC
ACCTACAGTATGCTGCCGCTGCCGCTCACCTGGGCCATCCTGGCCGGCCTGGGCACCTCG
CTGCTGCAGGTCATCCTCCAAGTGGTCATACCCCGGCTGGCGGTCATTTCCATCAACCAG
GTTGTGGCCCAGGCAGTGCTATTCATGTGTATGAACACAGCTGGAATCTTCATCAGTTAC
CTGTCAGACCGGGCCCAGCGCCAAGCTTTCCTGGAGACTCGGAGGTGTGTGGAGGCCAGG
CTGCGCCTGGAGACAGAGAACCAAAGACAGGAGCGGCTCGTGCTTTCTGTGCTCCCCCGG
TTTGTTGTCCTGGAAATGATCAACGACATGACCAATGTGGAAGATGAGCACCTGCAGCAC
CAGTTCCATCGGATCTACATCCATCGCTATGAGAACGTCAGTATTCTTTTTGCAGATGTT
AAAGGATTTACCAACCTCTCCACGACCTTGTCTGCTCAGGAGCTGGTCAGGATGCTCAAC
GAGCTCTTTGCCAGATTTGATCGACTGGCCCATGAGCATCACTGCCTTCGTATTAAAATC
CTGGGGGACTGCTACTACTGCGTGTCTGGACTTCCTGAGCCCCGCCAGGACCATGCCCAC
TGCTGTGTTGAAATGGGTCTCAGCATGATCAAAACCATCAGGTATGTGCGGTCAAGGACA
AAACACGATGTTGACATGAGGATTGGAATCCACTCCGGCTCGGTGCTGTGCGGTGTTTTG
GGACTACGGAAGTGGCAGTTTGATGTCTGGTCTTGGGATGTGGATATTGCAAACAAACTC
GAATCTGGAGGAATCCCCGGGAGGATTCACATTTCCAAAGCCACGCTGGACTGTCTCAAC
GGTGACTATAACGTGGAAGAGGGCCATGGTAAAGAGAGGAATGAATTCCTGAGGAAGCAT
AATATCGAAACTTACTTAATTAAGCAGCCTGAGGACAGTCTGCTGTCCTTGCCTGAAGAT
ATCGTCAAGGAGTCAGTGAGCTCCTCAGACCGGAGAAACAGTGGGGCCACATTCACTGAA
GGATCCTGGAGCCCTGAACTGCCCTTTGATAATATCGTGGGGAAACAGAATACTCTGGCT
GCCCTAACAAGAAATTCAATAAATCTGCTTCCAAACCATCTTGCACAAGCTTTGCATGTC
CAGTCTGGGCCTGAGGAAATTAACAAGAGAATAGAACATACCATCGACTTGCGGAGTGGC
GATAAATTGAGAAGAGAGCATATCAAGCCATTCTCACTGATGTTTAAAGACTCCAGCCTG
GAGCACAAGTATTCTCAAATGAGGGATGAAGTGTTCAAGTCAAACTTGGTCTGTGCATTT
ATCGTTCTTCTATTTATCACGGCAATACAAAGTTTGCTTCCTTCTTCAAGAGTGATGCCA
ATGACCATCCAGTTCTCCATTCTGATTATGCTGCACTCGGCTCTGGTCCTCATCACCACA
GCAGAGGATTATAAATGTTTGCCCCTCATCCTCCGGAAAACTTGCTGTTGGATTAATGAG
ACCTATTTGGCCCGGAACGTCATCATCTTTGCATCCATTTTGATTAATTTCCTGGGTGCC
ATCTTAAATATCCTGTGGTGTGATTTTGACAAGTCGATACCCTTGAAGAACCTGACTTTC
AATTCCTCAGCTGTGTTTACAGATATCTGCTCCTACCCAGAGTACTTTGTCTTCACGGGG
GTGTTGGCCATGGTGACCTGTGCAGTTTTCCTCCGGCTGAACTCCGTCCTGAAGCTGGCA
GTGCTGCTGATCATGATTGCCATCTATGCCCTGCTCACTGAGACCGTCTACGCAGGCCTC
TTTCTGCGTTATGACAACCTCAACCACAGTGGAGAAGATTTCCTGGGGACCAAGGAGGTA
TCACTGCTACTGATGGCCATGTTCCTCCTGGCTGTGTTCTACCATGGACAGCAGCTGGAG
TACACAGCCCGCCTGGACTTCCTTTGGCGAGTACAGGCCAAAGAGGAGATCAATGAGATG
AAGGAGCTGAGGGAACACAATGAGAACATGCTCCGGAATATCTTACCCAGCCATGTGGCC
CGCCATTTCCTAGAGAAGGACCGAGACAATGAGGAGCTGTATTCTCAATCCTATGATGCT
GTTGGGGTGATGTTTGCCTCCATCCCAGGATTTGCGGACTTTTACTCTCAGACTGAAATG
AATAACCAGGGAGTGGAATGCCTGCGCTTGCTCAATGAGATCATTGCTGACTTCGATGAG
TTGCTTGGTGAAGACCGATTTCAAGACATTGAAAAGATTAAGACCATTGGCAGCACCTAC
ATGGCCGTGTCAGGCCTGTCACCTGAAAAACAGCAATGTGAAGACAAGTGGGGACATTTG
TGTGCTCTGGCTGACTTCTCACTCGCCCTGACAGAAAGCATACAGGAGATCAACAAGCAT
TCATTCAACAATTTTGAACTCCGGATTGGCATCAGCCACGGCTCAGTGGTAGCTGGCGTT
ATCGGCGCTAAGAAACCACAGTATGACATTTGGGGCAAAACTGTGAACCTGGCAAGCCGA
ATGGACAGCACGGGGGTTAGTGGCCGGATCCAAGTCCCAGAGGAGACCTATCTCATCCTG
AAGGACCAGGGCTTTGCCTTTGATTACCGAGGGGAGATCTATGTGAAGGGTATCAGTGAA
CAGGAAGGAAAAATCAAAACGTACTTTCTTCTGGGAAGAGTCCAACCCAACCCATTCATC
TTGCCCCCAAGAAGACTGCCTGGGCAGTACTCCCTGGCCGCGGTTGTCCTGGGACTTGTC
CAGTCCCTCAATAGGCAAAGGCAGAAGCAGCTACTCAATGAGAACAACAACACAGGAATC
ATCAAGGGTCATTACAACCGGCGGACTTTGTTGTCACCCAGCGGCACAGAGCCTGGAGCC
CAGGCTGAAGGCACCGACAAATCTGATTTGCCATAA
Enzyme 29 GenBank Gene ID Z35309 Link Image
Enzyme 29 GeneCard ID ADCY8 Link Image
Enzyme 29 GenAtlas ID ADCY8 Link Image
Enzyme 29 HGNC ID HGNC:239 Link Image
Enzyme 29 Chromosome Location 8
Enzyme 29 Locus 8q24
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Defer N, Marinx O, Stengel D, Danisova A, Iourgenko V, Matsuoka I, Caput D, Hanoune J: Molecular cloning of the human type VIII adenylyl cyclase. FEBS Lett. 1994 Aug 29;351(1):109-13. [PubMed Link Image]
  2. Parma J, Stengel D, Gannage MH, Poyard M, Barouki R, Hanoune J: Sequence of a human brain adenylyl cyclase partial cDNA: evidence for a consensus cyclase specific domain. Biochem Biophys Res Commun. 1991 Aug 30;179(1):455-62. [PubMed Link Image]
  3. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 5982
Enzyme 30 Name Adenylate cyclase type 9
Enzyme 30 Synonyms
  1. ATP pyrophosphate-lyase 9
  2. Adenylate cyclase type IX
  3. Adenylyl cyclase 9
Enzyme 30 Gene Name ADCY9
Enzyme 30 Protein Sequence >Adenylate cyclase type 9
MASPPHQQLLHHHSTEVSCDSSGDSNSVRVKINPKQLSSNSHPKHCKYSISSSCSSSGDS
GGVPRRVGGGGRLRRQKKLPQLFERASSRWWDPKFDSVNLEEACLERCFPQTQRRFRYAL
FYIGFACLLWSIYFAVHMRSRLIVMVAPALCFLLVCVGFFLFTFTKLYARHYAWTSLALT
LLVFALTLAAQFQVLTPVSGRGDSSNLTATARPTDTCLSQVGSFSMCIEVLFLLYTVMHL
PLYLSLCLGVAYSVLFETFGYHFRDEACFPSPGAGALHWELLSRGLLHGCIHAIGVHLFV
MSQVRSRSTFLKVGQSIMHGKDLEVEKALKERMIHSVMPRIIADDLMKQGDEESENSVKR
HATSSPKNRKKKSSIQKAPIAFRPFKMQQIEEVSILFADIVGFTKMSANKSAHALVGLLN
DLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIKAIEQFCQEK
KEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLD
DRYEMEDGKVIERLGQSVVADQLKGLKTYLISGQRAKESRCSCAEALLSGFEVIDGSQVS
SGPRGQGTASSGNVSDLAQTVKTFDNLKTCPSCGITFAPKSEAGAEGGAPQNGCQDEHKN
STKASGGPNPKTQNGLLSPPQEEKLTNSQTSLCEILQEKGRWAGVSLDQSALLPLRFKNI
REKTDAHFVDVIKEDSLMKDYFFKPPINQFSLNFLDQELERSYRTSYQEEVIKNSPVKTF
ASPTFSSLLDVFLSTTVFLTLSTTCFLKYEAATVPPPPAALAVFSAALLLEVLSLAVSIR
MVFFLEDVMACTKRLLEWIAGWLPRHCIGAILVSLPALAVYSHVTSEYETNIHFPVFTGS
AALIAVVHYCNFCQLSSWMRSSLATVVGAGPLLLLYVSLCPDSSVLTSPLDAVQNFSSER
NPCNSSVPRDLRRPASLIGQEVVLVFFLLLLLVWFLNREFEVSYRLHYHGDVEADLHRTK
IQSMRDQADWLLRNIIPYHVAEQLKVSQTYSKNHDSGGVIFASIVNFSEFYEENYEGGKE
CYRVLNELIGDFDELLSKPDYSSIEKIKTIGATYMAASGLNTAQAQDGSHPQEHLQILFE
FAKEMMRVVDDFNNNMLWFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTT
GVECRIQVSEESYRVLSKMGYDFDYRGTVNVKGKGQMKTYLYPKCTDHRVIPQHQLSISP
DIRVQVDGSIGRSPTDEIANLVPSVQYVDKTSLGSDSSTQAKDAHLSPKRPWKEPVKAEE
RGRFGKAIEKDDCDETGIEEANELTKLNVSKSV
Enzyme 30 Number of Residues 1353
Enzyme 30 Molecular Weight 150699.4
Enzyme 30 Theoretical pI 7.35
Enzyme 30 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
Enzyme 30 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 30 Specific Function May play a fundamental role in situations where fine interplay between intracellular calcium and cAMP determines the cellular function. May be a physiologically relevant docking site for calcineurin
Enzyme 30 Pathways
Enzyme 30 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • 118-138 142-162 172-192 216-235 242-259 281-301 787-807 819-839 868-888 892-912 921-941 976-996
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 50959205 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID O60503 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name ADCY9_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >4062 bp
ATGGCTTCCCCACCCCACCAGCAGCTGCTGCATCACCACAGCACCGAGGTGAGCTGCGAC
TCCAGCGGGGACAGCAACAGCGTGCGCGTCAAGATCAACCCCAAGCAGCTGTCCTCCAAC
AGCCACCCCAAGCACTGCAAATACAGCATCTCCTCTAGCTGCAGCAGCTCTGGGGACTCC
GGGGGCGTCCCCCGGCGAGTGGGCGGCGGAGGCCGGCTGCGCAGGCAGAAGAAGCTGCCC
CAGCTGTTCGAGAGGGCCTCCAGCCGCTGGTGGGACCCCAAGTTCGACTCGGTGAACCTG
GAGGAGGCCTGCCTGGAGCGCTGCTTCCCGCAGACCCAGCGCCGGTTCCGGTATGCGCTC
TTCTACATCGGCTTCGCCTGCCTTCTGTGGAGCATCTATTTTGCGGTCCACATGAGATCC
AGACTGATCGTCATGGTCGCCCCCGCGCTGTGCTTCCTCCTGGTGTGTGTGGGCTTCTTT
CTGTTTACCTTCACCAAGCTGTACGCCCGGCATTACGCGTGGACCTCGCTGGCTCTCACC
CTGCTGGTGTTCGCCCTGACCCTGGCTGCGCAGTTCCAGGTCTTGACGCCTGTCTCAGGA
CGCGGCGACAGCTCCAACCTTACGGCCACAGCCCGGCCCACAGATACTTGCTTATCTCAA
GTGGGGAGCTTCTCCATGTGCATCGAAGTGCTCTTTTTGCTCTATACCGTCATGCACTTA
CCTTTGTACCTGAGTTTGTGTCTGGGGGTGGCCTACTCTGTCCTTTTCGAGACCTTTGGC
TACCATTTCCGGGATGAAGCCTGCTTCCCCTCGCCCGGAGCCGGGGCCCTGCACTGGGAG
CTGCTGAGCAGGGGGCTGCTCCACGGCTGCATCCACGCCATCGGGGTCCACCTGTTCGTC
ATGTCCCAGGTGAGGTCCAGGAGCACCTTCCTCAAGGTGGGGCAATCCATTATGCACGGG
AAGGACCTGGAAGTGGAAAAAGCCCTCAAAGAGAGGATGATTCATTCCGTGATGCCAAGA
ATCATAGCCGATGACTTAATGAAGCAGGGAGATGAGGAGAGTGAGAATTCTGTCAAGAGG
CATGCCACCTCGAGCCCCAAGAACAGGAAGAAAAAGTCTTCCATCCAAAAAGCTCCTATA
GCCTTCCGCCCTTTTAAGATGCAGCAGATCGAAGAAGTCAGTATTTTATTTGCAGATATC
GTGGGCTTCACCAAGATGAGTGCCAACAAGTCTGCCCACGCCCTGGTGGGTCTCCTGAAC
GATCTGTTCGGTCGCTTCGACCGCCTGTGTGAGGAGACCAAGTGTGAGAAAATCAGCACC
CTGGGAGACTGTTACTACTGCGTGGCGGGCTGTCCCGAGCCCCGGGCCGACCATGCCTAC
TGCTGCATCGAGATGGGCCTGGGCATGATCAAGGCCATCGAGCAGTTCTGCCAGGAGAAG
AAGGAGATGGTGAACATGAGAGTCGGGGTGCACACGGGCACCGTCCTTTGCGGCATCCTG
GGCATGAGGAGGTTTAAATTTGACGTGTGGTCCAACGATGTGAACCTGGCCAATCTCATG
GAGCAGCTGGGAGTGGCCGGCAAAGTTCACATTTCTGAGGCCACCGCAAAATACTTAGAT
GACCGGTACGAAATGGAAGATGGGAAAGTTATTGAACGGCTGGGCCAGAGCGTGGTTGCT
GACCAGTTGAAAGGTTTGAAGACATACCTGATATCGGGTCAGAGAGCCAAGGAGTCTCGC
TGCAGCTGTGCAGAGGCCTTGCTTTCTGGCTTTGAGGTCATTGACGGCTCACAGGTGTCC
TCAGGCCCTAGGGGACAGGGGACAGCGTCATCAGGGAATGTCAGTGACTTGGCGCAGACT
GTCAAAACCTTTGATAACCTTAAGACCTGCCCTTCGTGCGGAATCACATTTGCTCCCAAA
TCTGAAGCCGGCGCCGAGGGAGGAGCACCTCAAAACGGCTGCCAAGACGAGCATAAAAAC
AGCACCAAGGCTTCTGGAGGACCTAATCCCAAAACTCAGAACGGGCTCCTCAGCCCTCCC
CAAGAGGAGAAGCTCACCAACAGTCAGACTTCTCTGTGTGAGATCTTGCAGGAGAAGGGA
AGGTGGGCAGGGGTGAGCCTGGACCAGTCGGCTCTCCTTCCGCTGAGGTTCAAGAACATC
CGGGAGAAAACGGACGCCCACTTTGTGGACGTTATCAAAGAAGACAGCCTGATGAAAGAT
TACTTTTTTAAGCCGCCCATTAATCAGTTCAGCCTGAACTTCCTGGATCAGGAGCTGGAG
CGATCCTACAGGACCAGCTATCAGGAAGAGGTCATAAAGAACTCCCCCGTGAAGACGTTT
GCTAGTCCCACCTTCAGCTCCCTCCTGGATGTGTTTCTGTCGACCACAGTGTTTCTGACG
CTGTCCACCACCTGCTTCCTGAAGTACGAGGCGGCCACCGTGCCTCCCCCGCCCGCCGCC
CTGGCGGTCTTCAGTGCAGCCCTGCTGCTGGAGGTGCTGTCCCTCGCGGTGTCCATCAGG
ATGGTGTTCTTCCTGGAGGACGTCATGGCCTGCACCAAGCGCCTGCTGGAGTGGATCGCC
GGCTGGCTACCACGTCACTGCATCGGGGCCATCCTGGTGTCGCTTCCCGCACTGGCCGTC
TACTCCCATGTCACCTCCGAATATGAGACCAACATACACTTCCCAGTGTTCACAGGCTCG
GCCGCGCTGATTGCCGTCGTGCACTACTGTAACTTCTGCCAGCTCAGCTCCTGGATGAGG
TCCTCCCTCGCCACCGTCGTGGGGGCCGGGCCGCTGCTCCTGCTCTACGTCTCCCTGTGC
CCAGACAGTTCTGTATTAACTTCGCCCCTTGACGCAGTACAGAATTTCAGTTCCGAGAGG
AACCCGTGCAATAGTTCGGTGCCGCGTGACCTCCGGCGGCCCGCCAGCCTCATCGGCCAG
GAGGTGGTTCTCGTCTTCTTTCTCCTGCTCTTGTTGGTCTGGTTCCTGAATCGCGAATTT
GAAGTCAGCTACCGCCTCCACTACCACGGAGACGTGGAAGCGGATCTTCACCGCACCAAG
ATCCAGAGCATGCGGGACCAGGCAGACTGGCTGCTGAGGAACATCATCCCCTACCACGTG
GCTGAGCAGCTGAAGGTGTCCCAGACCTACTCCAAGAACCATGACAGCGGAGGGGTGATC
TTCGCCAGCATCGTCAACTTCAGCGAGTTCTACGAGGAGAACTACGAGGGCGGCAAGGAG
TGCTACCGGGTCCTCAACGAGCTCATCGGGGACTTTGACGAGCTCCTAAGCAAGCCGGAC
TACAGCAGCATCGAGAAGATCAAGACCATCGGAGCCACGTACATGGCGGCGTCAGGGCTG
AACACCGCGCAGGCCCAGGACGGCAGCCACCCGCAGGAGCACCTGCAGATCCTGTTCGAG
TTCGCCAAGGAGATGATGCGCGTGGTGGACGACTTCAACAACAACATGCTGTGGTTCAAC
TTCAAGCTCCGCGTCGGCTTCAACCATGGGCCCCTCACGGCCGGGGTCATCGGCACCACC
AAGCTGCTGTACGACATCTGGGGAGACACCGTCAACATCGCCAGCAGGATGGACACCACC
GGCGTGGAGTGCCGCATCCAGGTGAGCGAAGAGAGCTACCGCGTCTTGAGCAAGATGGGC
TATGACTTCGACTACAGAGGGACCGTGAATGTCAAGGGGAAAGGCCAGATGAAGACCTAC
CTGTACCCAAAGTGCACGGATCACAGGGTCATCCCACAGCACCAGCTGTCCATCTCCCCA
GACATCCGCGTCCAGGTGGATGGCAGCATCGGACGGTCTCCCACAGACGAGATTGCCAAC
CTGGTGCCTTCTGTCCAGTATGTGGACAAGACATCTCTGGGTTCTGACAGCAGCACGCAG
GCCAAGGATGCCCACCTGTCCCCCAAGAGACCGTGGAAGGAGCCCGTCAAAGCCGAAGAA
AGGGGTCGATTTGGCAAAGCCATAGAGAAAGACGACTGTGACGAAACAGGAATAGAAGAA
GCCAACGAACTCACCAAGCTCAACGTTTCAAAGAGTGTGTGA
Enzyme 30 GenBank Gene ID NM_001116.3 Link Image
Enzyme 30 GeneCard ID ADCY9 Link Image
Enzyme 30 GenAtlas ID ADCY9 Link Image
Enzyme 30 HGNC ID HGNC:240 Link Image
Enzyme 30 Chromosome Location 1
Enzyme 30 Locus 16p13.3
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Hacker BM, Tomlinson JE, Wayman GA, Sultana R, Chan G, Villacres E, Disteche C, Storm DR: Cloning, chromosomal mapping, and regulatory properties of the human type 9 adenylyl cyclase (ADCY9). Genomics. 1998 May 15;50(1):97-104. [PubMed Link Image]
  2. Small KM, Brown KM, Theiss CT, Seman CA, Weiss ST, Liggett SB: An Ile to Met polymorphism in the catalytic domain of adenylyl cyclase type 9 confers reduced beta2-adrenergic receptor stimulation. Pharmacogenetics. 2003 Sep;13(9):535-41. [PubMed Link Image]
  3. Tantisira KG, Small KM, Litonjua AA, Weiss ST, Liggett SB: Molecular properties and pharmacogenetics of a polymorphism of adenylyl cyclase type 9 in asthma: interaction between beta-agonist and corticosteroid pathways. Hum Mol Genet. 2005 Jun 15;14(12):1671-7. Epub 2005 May 6. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  5. 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]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 5983
Enzyme 31 Name Adenylate cyclase type 3
Enzyme 31 Synonyms
  1. ATP pyrophosphate-lyase 3
  2. Adenylate cyclase type III
  3. AC-III
  4. Adenylate cyclase, olfactive type
  5. Adenylyl cyclase 3
  6. AC3
Enzyme 31 Gene Name ADCY3
Enzyme 31 Protein Sequence >Adenylate cyclase type 3
MPRNQGFSEPEYSAEYSAEYSVSLPSDPDRGVGRTHEISVRNSGSCLCLPRFMRLTFVPE
SLENLYQTYFKRQRHETLLVLVVFAALFDCYVVVMCAVVFSSDKLASLAVAGIGLVLDII
LFVLCKKGLLPDRVTRRVLPYVLWLLITAQIFSYLGLNFARAHAASDTVGWQVFFVFSFF
ITLPLSLSPIVIISVVSCVVHTLVLGVTVAQQQQEELKGMQLLREILANVFLYLCAIAVG
IMSYYMADRKHRKAFLEARQSLEVKMNLEEQSQQQENLMLSILPKHVADEMLKDMKKDES
QKDQQQFNTMYMYRHENVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQ
LRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVEAISYVREKTKTGVDMRVGVHTGTV
LGGVLGQKRWQYDVWSTDVTVANKMEAGGIPGRVHISQSTMDCLKGEFDVEPGDGGSRCD
YLEEKGIETYLIIASKPEVKKTATQNGLNGSALPNGAPASSKSSSPALIETKEPNGSAHS
SGSTSEKPEEQDAQADNPSFPNPRRRLRLQDLADRVVDASEDEHELNQLLNEALLERESA
QVVKKRNTFLLSMRFMDPEMETRYSVEKEKQSGAAFSCSCVVLLCTALVEILIDPWLMTN
YVTFMVGEILLLILTICSLAAIFPRAFPKKLVAFSTWIDRTRWARNTWAMLAIFILVMAN
VVDMLSCLQYYTGPSNATAGMETEGSCLENPKYYNYVAVLSLIATIMLVQVSHMVKLTLM
LLVAGAVATINLYAWRPVFDEYDHKRFREHDLPMVALEQMQGFNPGLNGTDRLPLVPSKY
SMTVMVFLMMLSFYYFSRHVEKLARTLFLWKIEVHDQKERVYEMRRWNEALVTNMLPEHV
ARHFLGSKKRDEELYSQTYDEIGVMFASLPNFADFYTEESINNGGIECLRFLNEIISDFD
SLLDNPKFRVITKIKTIGSTYMAASGVTPDVNTNGFASSNKEDKSERERWQHLADLADFA
LAMKDTLTNINNQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASRMESTGVM
GNIQVVEETQVILREYGFRFVRRGPIFVKGKGELLTFFLKGRDKLATFPNGPSVTLPHQV
VDNS
Enzyme 31 Number of Residues 1144
Enzyme 31 Molecular Weight 128958.9
Enzyme 31 Theoretical pI 6.55
Enzyme 31 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
Enzyme 31 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 31 Specific Function Mediates odorant detection (possibly) via modulation of intracellular cAMP concentration
Enzyme 31 Pathways
Enzyme 31 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • 80-100 105-125 139-159 173-193 226-246 381-401 633-653 664-684 708-728 754-774 775-795 833-853
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 148536830 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID O60266 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name ADCY3_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >3435 bp
ATGCCGAGGAACCAGGGCTTCTCCGAGCCCGAATACTCGGCCGAGTACTCAGCCGAGTAC
TCCGTCAGCCTGCCCTCCGACCCTGACCGCGGGGTGGGCCGGACCCATGAAATCTCGGTC
CGGAACTCGGGCTCCTGCCTGTGCCTGCCTCGCTTCATGCGGCTGACTTTCGTGCCGGAG
TCCTTGGAGAACCTCTACCAGACCTACTTCAAAAGGCAGCGCCACGAGACCCTGCTGGTG
CTGGTGGTCTTTGCAGCCCTCTTTGACTGCTACGTGGTGGTCATGTGTGCTGTGGTCTTC
TCCAGCGACAAGCTGGCTTCCCTCGCCGTGGCTGGAATTGGACTGGTGTTGGACATCATC
CTCTTCGTGCTCTGCAAAAAGGGGCTGCTCCCGGACCGGGTCACCCGCAGAGTGCTGCCC
TACGTGCTGTGGCTGCTCATAACCGCCCAGATCTTCTCCTACCTGGGCCTGAACTTCGCG
CGTGCCCACGCGGCTAGTGACACGGTGGGCTGGCAGGTCTTCTTTGTCTTCTCCTTCTTC
ATCACGCTGCCCCTCAGCCTCAGCCCCATCGTGATCATCTCCGTGGTCTCCTGTGTGGTG
CACACGTTGGTCCTGGGGGTCACCGTGGCCCAGCAGCAGCAGGAGGAGCTCAAGGGGATG
CAGCTGCTGCGGGAGATCCTGGCCAACGTCTTCCTCTACCTGTGCGCCATCGCTGTGGGC
ATCATGTCCTACTACATGGCTGACCGCAAGCACCGCAAGGCCTTCCTGGAGGCCCGCCAG
TCGCTGGAGGTGAAGATGAACCTGGAAGAGCAGAGCCAGCAGCAGGAGAACCTCATGCTT
TCCATCCTGCCCAAGCACGTGGCTGACGAGATGCTGAAAGACATGAAGAAAGACGAGAGC
CAGAAGGACCAGCAGCAGTTCAACACCATGTACATGTACCGTCACGAGAACGTCAGCATC
CTCTTTGCCGACATCGTGGGCTTTACCCAGCTGTCTTCTGCCTGCAGTGCCCAGGAGCTT
GTGAAGCTGCTCAACGAGCTCTTTGCCCGCTTTGACAAGCTGGCAGCTAAATACCACCAG
CTGCGGATTAAGATCCTGGGCGACTGCTACTACTGCATCTGCGGCTTGCCCGACTACCGG
GAGGACCACGCCGTCTGCTCCATCCTCATGGGGCTGGCCATGGTGGAGGCCATCTCGTAT
GTGCGGGAGAAGACCAAGACTGGGGTGGACATGCGTGTGGGGGTGCACACGGGCACCGTG
CTGGGGGGCGTCCTGGGCCAGAAGCGCTGGCAGTACGACGTGTGGTCGACTGATGTCACT
GTAGCCAACAAGATGGAGGCCGGCGGCATCCCTGGGCGCGTGCACATCTCCCAGAGCACC
ATGGACTGCCTGAAAGGGGAGTTTGATGTGGAGCCAGGCGATGGGGGCAGCCGCTGTGAT
TACCTAGAAGAGAAGGGTATTGAAACCTACCTCATCATTGCCTCCAAGCCAGAGGTGAAG
AAAACAGCCACCCAGAATGGCCTCAATGGCTCGGCCCTGCCCAATGGAGCACCAGCTTCC
TCAAAGTCCAGCTCCCCTGCCCTCATTGAGACCAAGGAGCCCAACGGGAGTGCCCACAGC
AGTGGGTCCACGTCGGAGAAGCCCGAGGAGCAGGATGCCCAGGCCGACAACCCCTCATTC
CCCAACCCACGCCGGAGGCTGCGCCTGCAGGACCTGGCTGACCGAGTGGTGGATGCCTCT
GAAGATGAGCACGAGCTCAACCAGCTGCTCAACGAGGCCCTGCTTGAGCGAGAGTCCGCC
CAAGTAGTAAAGAAGAGAAACACCTTCCTCTTGTCCATGCGGTTCATGGACCCCGAGATG
GAAACCCGCTACTCGGTGGAGAAGGAGAAGCAGAGTGGGGCTGCCTTCAGCTGCTCCTGC
GTCGTCCTGCTCTGCACGGCCCTGGTCGAGATACTCATCGACCCCTGGCTAATGACAAAC
TATGTGACCTTCATGGTGGGGGAGATTCTGCTCCTCATCCTGACCATCTGCTCCCTGGCT
GCCATCTTTCCCCGGGCCTTTCCTAAGAAGCTTGTGGCCTTCTCAACTTGGATTGACCGG
ACCCGCTGGGCCAGGAACACCTGGGCCATGCTCGCCATCTTCATCCTGGTGATGGCAAAT
GTCGTGGACATGCTCAGCTGTCTCCAGTACTACACGGGACCCAGCAATGCAACGGCAGGG
ATGGAAACGGAGGGCAGCTGCCTGGAGAACCCCAAGTATTACAACTATGTGGCCGTGCTG
TCCCTCATCGCCACCATCATGCTGGTGCAGGTCAGCCACATGGTGAAGCTCACGCTCATG
CTGCTCGTCGCAGGCGCCGTGGCCACCATCAACCTCTATGCCTGGCGTCCCGTCTTTGAT
GAATACGACCACAAGCGTTTTCGGGAGCACGACTTACCTATGGTGGCCTTAGAGCAGATG
CAAGGATTCAACCCTGGGCTCAATGGCACTGACAGGCTGCCCCTGGTGCCTTCCAAGTAC
TCTATGACGGTGATGGTGTTCCTCATGATGCTCAGCTTCTACTACTTCTCCCGCCACGTA
GAAAAACTGGCACGGACACTTTTCTTGTGGAAGATTGAGGTCCACGACCAGAAGGAACGT
GTCTATGAGATGCGACGCTGGAACGAGGCCTTGGTCACCAACATGTTGCCTGAGCACGTG
GCACGCCATTTCCTGGGGTCCAAGAAGAGAGATGAGGAGCTGTATAGCCAGACGTATGAT
GAGATTGGAGTCATGTTTGCCTCCCTGCCCAACTTTGCTGACTTCTACACAGAGGAGAGC
ATCAACAATGGTGGTATTGAGTGTCTGCGTTTCCTCAATGAAATCATCTCAGATTTTGAC
TCTCTCCTGGACAATCCCAAGTTCCGGGTGATCACCAAGATCAAAACCATTGGCAGCACG
TATATGGCGGCTTCAGGAGTCACCCCCGATGTCAACACCAATGGCTTTGCCAGCTCCAAC
AAGGAAGACAAGTCCGAGAGAGAGCGCTGGCAGCACCTGGCTGACCTGGCCGACTTCGCG
CTGGCCATGAAGGATACGCTCACCAACATCAACAACCAGTCCTTCAATAACTTCATGCTG
CGCATAGGCATGAACAAAGGCGGGGTTCTGGCTGGGGTCATCGGAGCCCGGAAACCACAC
TACGACATCTGGGGCAATACAGTCAATGTAGCCAGCAGGATGGAGTCCACGGGGGTCATG
GGCAACATTCAGGTGGTAGAAGAAACCCAAGTCATCCTCCGAGAGTACGGCTTCCGCTTT
GTGAGGCGAGGCCCCATCTTTGTGAAGGGGAAGGGGGAGCTGCTGACCTTCTTCTTGAAG
GGGCGGGATAAGCTAGCCACCTTCCCCAATGGCCCCTCTGTCACACTGCCCCACCAGGTG
GTGGACAACTCCTGA
Enzyme 31 GenBank Gene ID NM_004036.3 Link Image
Enzyme 31 GeneCard ID ADCY3 Link Image
Enzyme 31 GenAtlas ID ADCY3 Link Image
Enzyme 31 HGNC ID HGNC:234 Link Image
Enzyme 31 Chromosome Location 2
Enzyme 31 Locus 2p23.3
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Yang B, He B, Abdel-Halim SM, Tibell A, Brendel MD, Bretzel RG, Efendic S, Hillert J: Molecular cloning of a full-length cDNA for human type 3 adenylyl cyclase and its expression in human islets. Biochem Biophys Res Commun. 1999 Jan 27;254(3):548-51. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  5. Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 5984
Enzyme 32 Name Adenylate cyclase type 1
Enzyme 32 Synonyms
  1. ATP pyrophosphate-lyase 1
  2. Adenylate cyclase type I
  3. Adenylyl cyclase 1
  4. Ca(2+)/calmodulin-activated adenylyl cyclase
Enzyme 32 Gene Name ADCY1
Enzyme 32 Protein Sequence >Adenylate cyclase type 1
MAGAPRGGGGGGGGAGEPGGAERAAGTSRRRGLRACDEEFACPELEALFRGYTLRLEQAA
TLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCVLFLALLVVTNVRSLQVPQLQ
QVGQLALLFSLTFALLCCPFALGGPARGSAGAAGGPATAEQGVWQLLLVTFVSYALLPVR
SLLAIGFGLVVAASHLLVTATLVPAKRPRLWRTLGANALLFVGVNMYGVFVRILTERSQR
KAFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHD
NVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGL
TQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWS
NDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGYGHERNSFLKTHNIETFFIVPSH
RRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALR
TASEKLRNRSSFSTNVVYTTPGTRVNRYISRLLEARQTELEMADLNFFTLKYKHVEREQK
YHQLQDEYFTSAVVLTLILAALFGLVYLLIFPQSVVVLLLLVFCICFLVACVLYLHITRV
QCFPGCLTIQIRTVLCIFIVVLIYSVAQGCVVGCLPWAWSSKPNSSLVVLSSGGQRTALP
TLPCESTHHALLCCLVGTLPLAIFFRVSSLPKMILLSGLTTSYILVLELSGYTRTGGGAV
SGRSYEPIVAILLFSCALALHARQVDIRLRLDYLWAAQAEEEREDMEKVKLDNRRILFNL
LPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEI
IADFDELMEKDFYKDIEKIKTIGSTYMAAVGLAPTSGTKAKKSISSHLSTLADFAIEMFD
VLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQV
TEEVHRLLRRCPYHFVCRGKVSVKGKGEMLTYFLEGRTDGNGSQIRSLGLDRKMCPFGRA
GLQGRRPPVCPMPGVSVRAGLPPHSPGQYLPSAAAGKEA
Enzyme 32 Number of Residues 1119
Enzyme 32 Molecular Weight 123438.8
Enzyme 32 Theoretical pI 8.49
Enzyme 32 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
Enzyme 32 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 32 Specific Function This is a calmodulin-sensitive adenylyl cyclase. May be involved in regulatory processes in the central nervous system. It may play a role in memory acquisition and learning
Enzyme 32 Pathways
Enzyme 32 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • 64-84 88-108 125-145 158-178 183-203 214-234 611-631 635-655 674-694 725-745 753-773 775-794
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 31083193 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q08828 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name ADCY1_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >3360 bp
ATGGCGGGGGCGCCGCGCGGCGGAGGCGGCGGCGGAGGCGGCGCGGGCGAGCCCGGGGGC
GCCGAGCGGGCGGCCGGGACAAGCCGCCGGCGCGGGCTCCGGGCGTGCGACGAGGAGTTC
GCTTGCCCAGAGCTGGAGGCGCTGTTCCGCGGCTACACGCTGCGGCTGGAGCAGGCGGCC
ACGCTGAAGGCGCTGGCCGTTCTCAGCCTGCTGGCGGGCGCGCTGGCGCTGGCCGAGCTG
CTGGGCGCGCCGGGGCCCGCGCCCGGCCTGGCCAAGGGCTCACACCCGGTGCACTGCGTC
CTCTTCCTGGCGCTGCTCGTGGTAACCAACGTCCGGTCCCTGCAGGTGCCCCAGCTGCAG
CAGGTCGGCCAGCTGGCGCTGCTCTTCAGCCTCACCTTCGCGCTGCTCTGCTGTCCTTTC
GCGCTGGGCGGCCCCGCCCGGGGTTCCGCCGGGGCCGCTGGGGGGCCAGCGACCGCCGAA
CAAGGGGTTTGGCAGCTCCTTTTGGTCACCTTCGTGTCCTATGCCTTGCTGCCCGTGCGC
AGCCTGCTGGCCATAGGCTTTGGGCTCGTGGTGGCTGCGTCGCACTTGCTGGTCACAGCC
ACCTTGGTCCCCGCCAAGCGCCCACGTCTCTGGAGGACGCTCGGTGCCAATGCCTTGCTC
TTCGTCGGTGTGAACATGTATGGGGTCTTTGTGCGGATTCTGACTGAGCGTTCACAGAGG
AAGGCGTTCCTGCAGGCCCGGAGCTGCATTGAGGACCGACTGAGGCTGGAGGATGAGAAC
GAGAAGCAGGAGCGGCTCCTCATGAGCCTCCTGCCCCGGAACGTTGCCATGGAGATGAAG
GAGGACTTCCTGAAGCCCCCTGAGAGGATTTTCCACAAGATTTACATCCAGAGGCACGAC
AATGTGAGCATCCTGTTTGCTGACATCGTGGGTTTCACGGGCTTGGCATCCCAGTGCACA
GCCCAGGAGCTGGTGAAACTCCTCAATGAGCTCTTCGGCAAGTTCGATGAATTAGCCACG
GAGAACCACTGTCGCCGCATCAAGATTCTCGGGGACTGCTACTACTGCGTGTCGGGCCTC
ACCCAGCCCAAGACTGACCATGCCCACTGCTGTGTGGAGATGGGACTCGACATGATTGAT
ACCATCACATCTGTGGCTGAAGCCACCGAGGTGGATCTGAACATGCGTGTGGGTCTGCAC
ACGGGCAGGGTCCTCTGTGGTGTCCTGGGCTTGCGCAAGTGGCAGTACGACGTGTGGTCC
AATGATGTGACCTTGGCCAATGTCATGGAAGCCGCTGGCCTGCCAGGGAAGGTTCATATC
ACAAAGACGACCCTAGCGTGCTTGAATGGGGACTACGAGGTAGAACCGGGTTACGGACAT
GAGAGGAACAGTTTCTTGAAAACTCATAACATCGAAACCTTTTTTATTGTGCCATCCCAT
CGCCGAAAGATATTTCCAGGCCTGATTCTCTCAGATATAAAACCGGCCAAAAGGATGAAG
TTCAAGACTGTCTGCTACCTGCTGGTGCAGCTCATGCACTGCCGGAAAATGTTCAAGGCC
GAGATCCCCTTCTCCAATGTCATGACCTGCGAGGACGATGACAAGCGGAGGGCATTAAGA
ACAGCCTCGGAAAAACTCAGAAACCGCTCATCTTTTTCTACCAACGTTGTCTACACCACC
CCGGGCACTCGCGTCAACAGGTACATCAGCCGCCTCTTAGAAGCCCGCCAGACAGAGCTG
GAGATGGCAGACCTGAACTTCTTTACCCTGAAGTACAAACATGTCGAACGGGAGCAAAAG
TACCACCAGCTTCAGGACGAGTATTTCACCAGCGCCGTTGTCCTCACCCTCATCCTGGCT
GCCTTATTTGGCCTTGTCTACCTTCTAATATTCCCACAGAGTGTGGTCGTCCTGCTCCTG
CTAGTATTCTGCATCTGCTTCCTGGTGGCCTGTGTCCTGTACCTGCACATCACCCGGGTC
CAGTGTTTTCCAGGGTGCCTGACGATTCAGATTCGCACTGTCCTGTGTATTTTCATAGTG
GTCTTAATCTACTCAGTAGCCCAAGGTTGTGTGGTGGGCTGCCTGCCTTGGGCCTGGAGC
TCCAAGCCCAACAGTTCCCTGGTGGTCCTTTCGTCTGGGGGCCAGCGCACAGCCCTGCCC
ACCCTGCCCTGCGAGTCTACACACCATGCCCTGCTCTGCTGCCTGGTGGGCACCCTCCCG
CTAGCCATATTTTTCCGGGTGTCCTCCTTGCCAAAAATGATCCTGCTCTCCGGGCTCACC
ACGTCCTACATCCTCGTTCTGGAGCTCAGCGGATACACCAGGACTGGGGGTGGTGCCGTC
TCCGGGCGCAGCTACGAGCCGATTGTGGCCATCCTGCTCTTCTCCTGTGCGCTGGCCCTG
CATGCCAGGCAGGTGGACATCAGGCTGAGGCTGGACTACCTCTGGGCCGCACAGGCAGAG
GAGGAGCGAGAGGACATGGAGAAGGTGAAGCTGGACAACAGGCGCATCCTCTTCAACCTC
CTGCCGGCCCACGTCGCCCAGCACTTCCTCATGTCCAACCCTCGGAACATGGACCTCTAC
TACCAGTCCTACTCCCAGGTGGGCGTCATGTTTGCCTCCATCCCCAACTTCAATGACTTC
TACATCGAGCTGGACGGCAACAACATGGGGGTGGAGTGTCTGCGGCTTCTCAACGAGATC
ATCGCCGACTTTGACGAGCTCATGGAAAAAGACTTTTACAAGGACATAGAGAAGATCAAG
ACCATCGGGAGCACCTACATGGCCGCTGTGGGGCTAGCGCCCACCTCGGGGACCAAGGCT
AAGAAGTCCATCTCCTCCCACCTGAGCACGCTGGCGGACTTTGCCATTGAGATGTTTGAC
GTTCTGGATGAAATCAACTACCAGTCTTACAACGACTTTGTCCTCCGAGTTGGCATCAAT
GTTGGCCCTGTGGTGGCTGGAGTGATTGGCGCTCGCAGGCCCCAGTACGACATCTGGGGA
AACACAGTCAACGTGGCCAGTCGGATGGATAGCACAGGGGTCCAGGGCAGAATCCAGGTG
ACTGAGGAAGTCCACCGGCTGCTGAGAAGGTGCCCCTACCACTTTGTGTGCCGAGGCAAA
GTCAGTGTCAAGGGCAAAGGCGAGATGTTGACATACTTTCTAGAAGGCAGGACTGATGGA
AACGGCTCCCAAATCAGGTCCCTGGGCTTGGATCGGAAAATGTGTCCATTTGGGAGAGCT
GGCCTTCAGGGCAGACGTCCCCCCGTGTGCCCCATGCCTGGCGTCTCAGTCAGGGCTGGG
CTCCCTCCACACTCCCCAGGCCAGTACCTGCCCTCTGCAGCAGCTGGGAAGGAGGCTTAG
Enzyme 32 GenBank Gene ID NM_021116.2 Link Image
Enzyme 32 GeneCard ID ADCY1 Link Image
Enzyme 32 GenAtlas ID ADCY1 Link Image
Enzyme 32 HGNC ID HGNC:232 Link Image
Enzyme 32 Chromosome Location 7
Enzyme 32 Locus 7p13-p12
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  2. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  3. Villacres EC, Xia Z, Bookbinder LH, Edelhoff S, Disteche CM, Storm DR: Cloning, chromosomal mapping, and expression of human fetal brain type I adenylyl cyclase. Genomics. 1993 May;16(2):473-8. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 6209
Enzyme 33 Name Adenylate cyclase type 2
Enzyme 33 Synonyms
  1. ATP pyrophosphate-lyase 2
  2. Adenylate cyclase type II
  3. Adenylyl cyclase 2
Enzyme 33 Gene Name ADCY2
Enzyme 33 Protein Sequence >Adenylate cyclase type 2
MWQEAMRRRRYLRDRSEEAAGGGDGLPRSRDWLYESYYCMSQQHPLIVFLLLIVMGSCLA
LLAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRLFSLVIWICLVAM
GYLFMCFGGTVSPWDQVSFFLFIIFVVYTMLPFNMRDAIIASVLTSSSHTIVLSVCLSAT
PGGKEHLVWQILANVIIFICGNLAGAYHKHLMELALQQTYQDTCNCIKSRIKLEFEKRQQ
ERLLLSLLPAHIAMEMKAEIIQRLQGPKAGQMENTNNFHNLYVKRHTNVSILYADIVGFT
RLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVK
MGLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGG
VPGRVHISSVTLEHLNGAYKVEEGDGDIRDPYLKQHLVKTYFVINPKGERRSPQHLFRPR
HTLDGAKMRASVRMTRYLESWGAAKPFAHLHHRDSMTTENGKISTTDVPMGQHNFQNRTL
RTKSQKKRFEEELNERMIQAIDGINAQKQWLKSEDIQRISLLFYNKVLEKEYRATALPAF
KYYVTCACLIFFCIFIVQILVLPKTSVLGISFGAAFLLLAFILFVCFAGQLLQCSKKASP
LLMWLLKSSGIIANRPWPRISLTIITTAIILMMAVFNMFFLSDSEETIPPTANTTNTSFS
ASNNQVAILRAQNLFFLPYFIYSCILGLISCSVFLRVNYELKMLIMMVALVGYNTILLHT
HAHVLGDYSQVLFERPGIWKDLKTMGSVSLSIFFITLLVLGRQNEYYCRLDFLWKNKFKK
EREEIETMENLNRVLLENVLPAHVAEHFLARSLKNEELYHQSYDCVCVMFASIPDFKEFY
TESDVNKEGLECLRLLNEIIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAVPSQEHS
QEPERQYMHIGTMVEFAFALVGKLDAINKHSFNDFKLRVGINHGPVIAGVIGAQKPQYDI
WGNTVNVASRMDSTGVLDKIQVTEETSLVLQTLGYTCTCRGIINVKGKGDLKTYFVNTEM
SRSLSQSNVAS
Enzyme 33 Number of Residues 1091
Enzyme 33 Molecular Weight 123602.2
Enzyme 33 Theoretical pI 8.15
Enzyme 33 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 33 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 33 Specific Function This is a membrane-bound, calmodulin-insensitive adenylyl cyclase
Enzyme 33 Pathways
Enzyme 33 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • 46-66 76-96 108-128 133-153 159-179 187-207 602-622 628-652 680-701 734-755 763-780 801-821
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 115387102 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q08462 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name ADCY2_HUMAN Link Image
Enzyme 33 PDB ID 1AB8 Link Image
Enzyme 33 PDB File Show
Enzyme 33 3D Structure
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >3276 bp
ATGTGGCAGGAGGCGATGCGGCGCCGCCGCTACCTGCGGGACCGCTCCGAGGAGGCGGCG
GGCGGCGGAGACGGGCTGCCGCGGTCCCGGGACTGGCTCTACGAGTCCTACTACTGCATG
AGCCAGCAGCACCCGCTCATCGTCTTCCTGCTGCTCATCGTCATGGGCTCCTGCCTCGCC
CTGCTCGCCGTCTTCTTCGCGCTCGGGCTGGAAGTTGAAGACCATGTGGCGTTTCTAATA
ACAGTTCCAACTGCCCTGGCGATTTTCTTTGCGATATTTATCCTGGTCTGCATCGAGTCT
GTGTTTAAGAAGCTGCTGCGCCTCTTCTCGTTGGTGATATGGATATGCCTTGTTGCCATG
GGATACCTGTTCATGTGTTTTGGAGGCACCGTCTCTCCCTGGGACCAGGTATCGTTCTTC
CTCTTCATCATCTTCGTGGTGTACACCATGCTGCCCTTCAACATGCGAGACGCCATCATT
GCCAGCGTCCTCACCTCCTCCTCCCACACCATCGTGCTTAGCGTCTGCCTGTCTGCAACA
CCGGGAGGCAAGGAGCACCTGGTCTGGCAGATCCTGGCCAATGTGATCATTTTCATCTGT
GGGAACCTGGCGGGAGCCTACCATAAGCACCTCATGGAACTCGCTCTTCAGCAAACATAT
CAGGACACCTGTAATTGCATCAAGTCGCGGATCAAGTTGGAATTTGAAAAACGTCAACAG
GAGCGGCTTCTGCTCTCCCTGCTGCCGGCCCACATCGCCATGGAGATGAAAGCGGAGATC
ATCCAGAGGCTGCAGGGCCCCAAGGCGGGCCAGATGGAGAACACAAATAACTTCCACAAC
CTGTATGTGAAGCGGCATACAAACGTGAGCATCTTATACGCTGACATCGTTGGCTTTACC
CGGCTGGCAAGTGACTGCTCCCCGGGAGAACTAGTCCACATGCTGAATGAGCTCTTTGGA
AAGTTTGATCAAATTGCAAAGGAGAATGAATGCATGAGAATTAAAATTTTAGGAGACTGC
TACTACTGTGTATCTGGACTCCCTATATCTCTCCCTAACCATGCCAAGAACTGTGTGAAA
ATGGGGCTGGACATGTGTGAAGCCATAAAGAAAGTGAGGGATGCTACTGGAGTTGATATC
AACATGCGCGTGGGCGTGCATTCTGGGAATGTCCTGTGTGGCGTGATTGGTCTGCAGAAG
TGGCAATATGATGTGTGGTCACATGATGTGACCTTGGCCAACCACATGGAAGCTGGAGGG
GTCCCTGGACGTGTTCACATTTCTTCTGTCACCCTGGAGCACTTGAATGGCGCTTATAAA
GTGGAGGAGGGAGATGGTGACATTAGGGACCCATATTTAAAACAGCACCTGGTGAAAACC
TACTTTGTGATCAACCCCAAGGGAGAACGACGGAGCCCCCAGCATCTCTTCAGACCTCGC
CACACCCTTGATGGAGCCAAAATGAGGGCCTCGGTCCGCATGACCCGGTACTTGGAGTCC
TGGGGGGCAGCCAAGCCCTTTGCACACCTACATCACAGGGACAGCATGACCACAGAGAAC
GGCAAGATCAGCACCACGGATGTACCCATGGGTCAGCATAATTTTCAAAATCGCACCTTA
AGAACCAAGTCACAAAAGAAGAGATTTGAAGAAGAATTGAATGAAAGGATGATTCAAGCA
ATTGATGGGATTAATGCACAGAAGCAATGGCTCAAGTCTGAAGACATTCAGAGAATCTCA
CTGCTTTTCTATAACAAAGTACTAGAAAAAGAGTACCGGGCCACGGCACTGCCAGCGTTC
AAGTATTATGTGACTTGTGCCTGTCTCATATTCTTCTGCATCTTCATTGTGCAGATTCTC
GTGCTGCCAAAAACGTCCGTCCTGGGCATCTCCTTTGGGGCTGCGTTTCTCTTGCTGGCC
TTCATCCTCTTCGTCTGCTTTGCTGGACAGCTTCTGCAATGCAGCAAAAAAGCCTCTCCC
CTGCTCATGTGGCTTTTGAAGTCCTCGGGCATCATTGCCAACCGCCCCTGGCCACGGATC
TCTCTCACGATCATCACCACAGCCATCATATTAATGATGGCCGTGTTCAACATGTTTTTC
CTGAGTGACTCAGAGGAAACAATCCCTCCAACTGCCAACACAACAAACACAAGCTTTTCA
GCCTCAAATAATCAGGTGGCGATTCTGCGTGCGCAGAATTTATTTTTCCTCCCGTACTTT
ATCTACAGCTGCATTCTGGGACTGATATCCTGTTCCGTGTTCCTGCGGGTAAACTATGAG
CTGAAGATGTTGATCATGATGGTGGCCTTGGTGGGCTACAACACCATCCTACTCCACACC
CACGCCCACGTCCTGGGCGACTACAGCCAGGTCTTATTTGAGAGACCAGGCATTTGGAAA
GACCTGAAGACCATGGGCTCTGTGTCTCTCTCTATATTCTTCATCACACTGCTTGTTCTG
GGTAGACAGAATGAATATTACTGTAGGTTAGACTTCTTATGGAAGAACAAATTCAAAAAA
GAGCGGGAGGAGATAGAGACCATGGAGAACCTGAACCGCGTGCTGCTGGAGAACGTGCTT
CCCGCGCACGTGGCTGAGCACTTCCTGGCCAGGAGCCTGAAGAATGAGGAGCTATACCAC
CAGTCCTATGACTGCGTCTGCGTCATGTTTGCCTCCATTCCGGATTTCAAAGAATTTTAT
ACAGAATCCGACGTGAACAAGGAGGGCTTGGAATGCCTTCGGCTCCTGAACGAGATCATC
GCTGACTTTGATGATCTTCTTTCCAAGCCAAAATTCAGTGGAGTTGAAAAGATTAAGACC
ATTGGCAGCACATACATGGCAGCAACAGGTCTGAGCGCTGTGCCCAGCCAGGAGCACTCC
CAGGAGCCCGAGCGGCAGTACATGCACATTGGCACCATGGTGGAGTTTGCTTTTGCCCTG
GTAGGGAAGCTGGATGCCATCAACAAGCACTCCTTCAACGACTTCAAATTGCGAGTGGGT
ATTAACCATGGACCTGTGATAGCTGGTGTGATTGGAGCTCAGAAGCCACAATATGATATC
TGGGGCAACACTGTCAATGTGGCCAGTAGGATGGACAGCACCGGAGTCCTGGACAAAATA
CAGGTTACCGAGGAGACGAGCCTCGTCCTGCAGACCCTCGGATACACGTGCACCTGTCGA
GGAATAATCAACGTGAAAGGAAAGGGGGACCTGAAGACGTACTTTGTAAACACAGAAATG
TCAAGGTCCCTTTCCCAGAGCAACGTGGCATCCTGA
Enzyme 33 GenBank Gene ID NM_020546.2 Link Image
Enzyme 33 GeneCard ID ADCY2 Link Image
Enzyme 33 GenAtlas ID ADCY2 Link Image
Enzyme 33 HGNC ID HGNC:233 Link Image
Enzyme 33 Chromosome Location 5
Enzyme 33 Locus 5p15.3
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed Link Image]
  3. Stengel D, Parma J, Gannage MH, Roeckel N, Mattei MG, Barouki R, Hanoune J: Different chromosomal localization of two adenylyl cyclase genes expressed in human brain. Hum Genet. 1992 Sep-Oct;90(1-2):126-30. [PubMed Link Image]
  4. Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 6332
Enzyme 34 Name Steroid 17-alpha-hydroxylase/17,20 lyase
Enzyme 34 Synonyms
  1. CYPXVII
  2. Cytochrome P450 17A1
  3. Cytochrome P450-C17
  4. Cytochrome P450c17
  5. Steroid 17-alpha-monooxygenase
Enzyme 34 Gene Name CYP17A1
Enzyme 34 Protein Sequence >Steroid 17-alpha-hydroxylase/17,20 lyase
MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKY
GPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAH
WQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVIS
LICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRN
DLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIF
GAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREV
LRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNP
AGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIP
KVVFLIDSFKVKIKVRQAWREAQAEGST
Enzyme 34 Number of Residues 508
Enzyme 34 Molecular Weight 57370.0
Enzyme 34 Theoretical pI 8.87
Enzyme 34 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 34 General Function Involved in monooxygenase activity
Enzyme 34 Specific Function Conversion of pregnenolone and progesterone to their 17- alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved in sexual development during fetal life and at puberty
Enzyme 34 Pathways
Enzyme 34 Reactions
  • a steroid + AH2 + O2 = a 17alpha-hydroxysteroid + A + H2O [RN:R02131]
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein Not Available
Enzyme 34 UniProtKB/Swiss-Prot ID P05093 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name CP17A_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1527 bp
ATGTGGGAGCTCGTGGCTCTCTTGCTGCTTACCCTAGCTTATTTGTTTTGGCCCAAGAGA
AGGTGCCCTGGTGCCAAGTACCCCAAGAGCCTCCTGTCCCTGCCCCTGGTGGGCAGCCTG
CCATTCCTCCCCAGACATGGCCATATGCATAACAACTTCTTCAAGCTGCAGAAAAAATAT
GGCCCCATCTATTCTGTTCGTATGGGCACCAAGACTACAGTGATTGTCGGCCACCACCAG
CTGGCCAAGGAGGTGCTTATTAAGAAGGGCAAGGACTTCTCTGGGCGGCCTCAAATGGCA
ACTCTAGACATCGCGTCCAACAACCGTAAGGGTATCGCCTTCGCTGACTCTGGCGCACAC
TGGCAGCTGCATCGAAGGCTGGCGATGGCCACCTTTGCCCTGTTCAAGGATGGCGATCAG
AAGCTGGAGAAGATCATTTGTCAGGAAATCAGTACATTGTGTGATATGCTGGCCACCCAC
AACGGACAGTCCATAGACATCTCCTTTCCTGTCTTCGTGGCGGTAACCAATGTCATCTCC
TTGATCTGCTTCAATACCTCCTACAAGAATGGGGACCCTGAGTTGAATGTCATACAGAAT
TACAATGAAGGCATCATAGACAACCTGAGCAAAGACAGCCTGGTGGACCTAGTCCCCTGG
TTGAAGATTTTCCCCAACAAAACCCTGGAAAAATTAAAGAGCCATGTTAAAATACGAAAT
GATCTGCTGAATAAAATACTTGAAAATTACAAGGAGAAATTCCGGAGTGACTCTATCACC
AACATGCTGGACACACTGATGCAAGCCAAGATGAACTCAGATAATGGCAATGCTGGCCCA
GATCAAGATTCAGAGCTGCTTTCAGATAACCACATTCTCACCACCATAGGGGACATCTTT
GGGGCTGGCGTGGAGACCACCACCTCTGTGGTTAAATGGACCCTGGCCTTCCTGCTGCAC
AATCCTCAGGTGAAGAAGAAGCTCTACGAGGAGATTGACCAGAATGTGGGTTTCAGCCGC
ACACCAACTATCAGTGACCGTAACCGTCTCCTCCTGCTGGAGGCCACCATCCGAGAGGTG
CTTCGCCTCAGGCCCGTGGCCCCTATGCTCATCCCCCACAAGGCCAACGTTGACTCCAGC
ATCGGTGAGTTTGCTGTGGACAAGGGCACAGAAGTTATCATCAATCTGTGGGCGCTGCAT
CACAATGAGAAGGAGTGGCACCAGCCGGATCAGTTCATGCCTGAGCGTTTCTTGAATCCA
GCGGGGACCCAGCTCATCTCACCGTCAGTAAGCTATTTGCCCTTCGGAGCAGGACCTCGC
TCCTGTATAGGTGAGATCCTGGCCCGCCAGGAGCTCTTCCTCATCATGGCCTGGCTGCTG
CAGAGGTTCGACCTGGAGGTGCCAGATGATGGGCAGCTGCCCTCCCTGGAAGGCATCCCC
AAGGTGGTCTTTCTGATCGACTCTTTCAAAGTGAAGATCAAGGTGCGCCAGGCCTGGAGG
GAAGCCCAGGCTGAGGGTAGCACCTAA
Enzyme 34 GenBank Gene ID M14564 Link Image
Enzyme 34 GeneCard ID CYP17A1 Link Image
Enzyme 34 GenAtlas ID CYP17A1 Link Image
Enzyme 34 HGNC ID HGNC:2593 Link Image
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 10q24.3
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Chung BC, Picado-Leonard J, Haniu M, Bienkowski M, Hall PF, Shively JE, Miller WL: Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues. Proc Natl Acad Sci U S A. 1987 Jan;84(2):407-11. [PubMed Link Image]
  2. Picado-Leonard J, Miller WL: Cloning and sequence of the human gene for P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): similarity with the gene for P450c21. DNA. 1987 Oct;6(5):439-48. [PubMed Link Image]
  3. Bradshaw KD, Waterman MR, Couch RT, Simpson ER, Zuber MX: Characterization of complementary deoxyribonucleic acid for human adrenocortical 17 alpha-hydroxylase: a probe for analysis of 17 alpha-hydroxylase deficiency. Mol Endocrinol. 1987 May;1(5):348-54. [PubMed Link Image]
  4. Brentano ST, Picado-Leonard J, Mellon SH, Moore CC, Miller WL: Tissue-specific, cyclic adenosine 3',5'-monophosphate-induced, and phorbol ester-repressed transcription from the human P450c17 promoter in mouse cells. Mol Endocrinol. 1990 Dec;4(12):1972-9. [PubMed Link Image]
  5. Kagimoto M, Winter JS, Kagimoto K, Simpson ER, Waterman MR: Structural characterization of normal and mutant human steroid 17 alpha-hydroxylase genes: molecular basis of one example of combined 17 alpha-hydroxylase/17,20 lyase deficiency. Mol Endocrinol. 1988 Jun;2(6):564-70. [PubMed Link Image]
  6. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Auchus RJ, Miller WL: Molecular modeling of human P450c17 (17alpha-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations. Mol Endocrinol. 1999 Jul;13(7):1169-82. [PubMed Link Image]
  9. Yanase T, Kagimoto M, Suzuki S, Hashiba K, Simpson ER, Waterman MR: Deletion of a phenylalanine in the N-terminal region of human cytochrome P-450(17 alpha) results in partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1989 Oct 25;264(30):18076-82. [PubMed Link Image]
  10. Lin D, Harikrishna JA, Moore CC, Jones KL, Miller WL: Missense mutation serine106----proline causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1991 Aug 25;266(24):15992-8. [PubMed Link Image]
  11. Yanase T, Waterman MR, Zachmann M, Winter JS, Simpson ER, Kagimoto M: Molecular basis of apparent isolated 17,20-lyase deficiency: compound heterozygous mutations in the C-terminal region (Arg(496)----Cys, Gln(461)----Stop) actually cause combined 17 alpha-hydroxylase/17,20-lyase deficiency. Biochim Biophys Acta. 1992 Aug 25;1139(4):275-9. [PubMed Link Image]
  12. Ahlgren R, Yanase T, Simpson ER, Winter JS, Waterman MR: Compound heterozygous mutations (Arg 239----stop, Pro 342----Thr) in the CYP17 (P45017 alpha) gene lead to ambiguous external genitalia in a male patient with partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Clin Endocrinol Metab. 1992 Mar;74(3):667-72. [PubMed Link Image]
  13. Imai T, Globerman H, Gertner JM, Kagawa N, Waterman MR: Expression and purification of functional human 17 alpha-hydroxylase/17,20-lyase (P450c17) in Escherichia coli. Use of this system for study of a novel form of combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1993 Sep 15;268(26):19681-9. [PubMed Link Image]
  14. Monno S, Ogawa H, Date T, Fujioka M, Miller WL, Kobayashi M: Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1993 Dec 5;268(34):25811-7. [PubMed Link Image]
  15. Fardella CE, Zhang LH, Mahachoklertwattana P, Lin D, Miller WL: Deletion of amino acids Asp487-Ser488-Phe489 in human cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1993 Aug;77(2):489-93. [PubMed Link Image]
  16. Fardella CE, Hum DW, Homoki J, Miller WL: Point mutation of Arg440 to His in cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1994 Jul;79(1):160-4. [PubMed Link Image]
  17. Laflamme N, Leblanc JF, Mailloux J, Faure N, Labrie F, Simard J: Mutation R96W in cytochrome P450c17 gene causes combined 17 alpha-hydroxylase/17-20-lyase deficiency in two French Canadian patients. J Clin Endocrinol Metab. 1996 Jan;81(1):264-8. [PubMed Link Image]
  18. Biason-Lauber A, Kempken B, Werder E, Forest MG, Einaudi S, Ranke MB, Matsuo N, Brunelli V, Schonle EJ, Zachmann M: 17alpha-hydroxylase/17,20-lyase deficiency as a model to study enzymatic activity regulation: role of phosphorylation. J Clin Endocrinol Metab. 2000 Mar;85(3):1226-31. [PubMed Link Image]
  19. Gupta MK, Geller DH, Auchus RJ: Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency. J Clin Endocrinol Metab. 2001 Sep;86(9):4416-23. [PubMed Link Image]
  20. Di Cerbo A, Biason-Lauber A, Savino M, Piemontese MR, Di Giorgio A, Perona M, Savoia A: Combined 17alpha-Hydroxylase/17,20-lyase deficiency caused by Phe93Cys mutation in the CYP17 gene. J Clin Endocrinol Metab. 2002 Feb;87(2):898-905. [PubMed Link Image]
  21. Van Den Akker EL, Koper JW, Boehmer AL, Themmen AP, Verhoef-Post M, Timmerman MA, Otten BJ, Drop SL, De Jong FH: Differential inhibition of 17alpha-hydroxylase and 17,20-lyase activities by three novel missense CYP17 mutations identified in patients with P450c17 deficiency. J Clin Endocrinol Metab. 2002 Dec;87(12):5714-21. [PubMed Link Image]
  22. Martin RM, Lin CJ, Costa EM, de Oliveira ML, Carrilho A, Villar H, Longui CA, Mendonca BB: P450c17 deficiency in Brazilian patients: biochemical diagnosis through progesterone levels confirmed by CYP17 genotyping. J Clin Endocrinol Metab. 2003 Dec;88(12):5739-46. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 6413
Enzyme 35 Name Cyclic nucleotide-gated cation channel alpha-3
Enzyme 35 Synonyms
  1. Cone photoreceptor cGMP-gated channel subunit alpha
  2. Cyclic nucleotide-gated channel alpha-3
  3. CNG channel alpha-3
  4. CNG-3
  5. CNG3
Enzyme 35 Gene Name CNGA3
Enzyme 35 Protein Sequence >Cyclic nucleotide-gated cation channel alpha-3
MAKINTQYSHPSRTHLKVKTSDRDLNRAENGLSRAHSSSEETSSVLQPGIAMETRGLADS
GQGSFTGQGIARLSRLIFLLRRWAARHVHHQDQGPDSFPDRFRGAELKEVSSQESNAQAN
VGSQEPADRGRSAWPLAKCNTNTSNNTEEEKKTKKKDAIVVDPSSNLYYRWLTAIALPVF
YNWYLLICRACFDELQSEYLMLWLVLDYSADVLYVLDVLVRARTGFLEQGLMVSDTNRLW
QHYKTTTQFKLDVLSLVPTDLAYLKVGTNYPEVRFNRLLKFSRLFEFFDRTETRTNYPNM
FRIGNLVLYILIIIHWNACIYFAISKFIGFGTDSWVYPNISIPEHGRLSRKYIYSLYWST
LTLTTIGETPPPVKDEEYLFVVVDFLVGVLIFATIVGNVGSMISNMNASRAEFQAKIDSI
KQYMQFRKVTKDLETRVIRWFDYLWANKKTVDEKEVLKSLPDKLKAEIAINVHLDTLKKV
RIFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGKEMYIINEGKLAVVADDGVTQFVV
LSDGSYFGEISILNIKGSKSGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPEAKKALEE
KGRQILMKDNLIDEELARAGADPKDLEEKVEQLGSSLDTLQTRFARLLAEYNATQMKMKQ
RLSQLESQVKGGGDKPLADGEVPGDATKTEDKQQ
Enzyme 35 Number of Residues 694
Enzyme 35 Molecular Weight 78837.4
Enzyme 35 Theoretical pI 7.80
Enzyme 35 GO Classification
Function
  • ion channel activity
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 35 General Function Involved in ion channel activity
Enzyme 35 Specific Function Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of cone photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficacy of the channel when coexpressed with CNGB3. Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • 171-192 305-325 378-397
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 62988794 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q16281 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name CNGA3_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >2085 bp
ATGGCCAAGATCAACACCCAATACTCCCACCCCTCCAGGACCCACCTCAAGGTAAAGACC
TCAGACCGAGATCTCAATCGCGCTGAAAATGGCCTCAGCAGAGCCCACTCGTCAAGTGAG
GAGACATCGTCAGTGCTGCAGCCGGGGATCGCCATGGAGACCAGAGGACTGGCTGACTCC
GGGCAGGGCTCCTTCACCGGCCAGGGGATCGCCAGGCTGTCGCGCCTCATCTTCTTGCTG
CGCAGGTGGGCTGCCAGGCATGTGCACCACCAGGACCAGGGACCGGACTCTTTTCCTGAT
CGTTTCCGTGGAGCCGAGCTTAAGGAGGTGTCCAGCCAAGAAAGCAATGCCCAGGCAAAT
GTGGGCAGCCAGGAGCCAGCAGACAGAGGGAGAAGCGCCTGGCCCCTGGCCAAATGCAAC
ACTAACACCAGCAACAACACGGAGGAGGAGAAGAAGACGAAAAAGAAGGATGCGATCGTG
GTGGACCCGTCCAGCAACCTGTACTACCGCTGGCTGACCGCCATCGCCCTGCCTGTCTTC
TATAACTGGTATCTGCTTATTTGCAGGGCCTGTTTCGATGAGCTGCAGTCCGAGTACCTG
ATGCTGTGGCTGGTCCTGGACTACTCGGCAGATGTCCTGTATGTCTTGGATGTGCTTGTA
CGAGCTCGGACAGGTTTTCTCGAGCAAGGCTTAATGGTCAGTGATACCAACAGGCTGTGG
CAGCATTACAAGACGACCACGCAGTTCAAGCTGGATGTGTTGTCCCTGGTCCCCACCGAC
CTGGCTTACTTAAAGGTGGGCACAAACTACCCAGAAGTGAGGTTCAACCGCCTACTGAAG
TTTTCCCGGCTCTTTGAATTCTTTGACCGCACAGAGACAAGGACCAACTACCCCAATATG
TTCAGGATTGGGAACTTGGTCTTGTACATTCTCATCATCATCCACTGGAATGCCTGCATC
TACTTTGCCATTTCCAAGTTCATTGGTTTTGGGACAGACTCCTGGGTCTACCCAAACATC
TCAATCCCAGAGCATGGGCGCCTCTCCAGGAAGTACATTTACAGTCTCTACTGGTCCACC
TTGACCCTTACCACCATTGGTGAGACCCCACCCCCCGTGAAAGATGAGGAGTATCTCTTT
GTGGTCGTAGACTTCTTGGTGGGTGTTCTGATTTTTGCCACCATTGTGGGCAATGTGGGC
TCCATGATCTCGAATATGAATGCCTCACGGGCAGAGTTCCAGGCCAAGATTGATTCCATC
AAGCAGTACATGCAGTTCCGCAAGGTCACCAAGGACTTGGAGACGCGGGTTATCCGGTGG
TTTGACTACCTGTGGGCCAACAAGAAGACGGTGGATGAGAAGGAGGTGCTCAAGAGCCTC
CCAGACAAGCTGAAGGCTGAGATCGCCATCAACGTGCACCTGGACACGCTGAAGAAGGTT
CGCATCTTCCAGGACTGTGAGGCAGGGCTGCTGGTGGAGCTGGTGCTGAAGCTGCGACCC
ACTGTGTTCAGCCCTGGGGATTATATCTGCAAGAAGGGAGATATTGGGAAGGAGATGTAC
ATCATCAACGAGGGCAAGCTGGCCGTGGTGGCTGATGATGGGGTCACCCAGTTCGTGGTC
CTCAGCGATGGCAGCTACTTCGGGGAGATCAGCATTCTGAACATCAAGGGGAGCAAGTCG
GGGAACCGCAGGACGGCCAACATCCGCAGCATTGGCTACTCAGACCTGTTCTGCCTCTCA
AAGGACGATCTCATGGAGGCCCTCACCGAGTACCCCGAAGCCAAGAAGGCCCTGGAGGAG
AAAGGACGGCAGATCCTGATGAAAGACAACCTGATCGATGAGGAGCTGGCCAGGGCGGGC
GCGGACCCCAAGGACCTTGAGGAGAAAGTGGAGCAGCTGGGGTCCTCCCTGGACACCCTG
CAGACCAGGTTTGCACGCCTCCTGGCTGAGTACAACGCCACCCAGATGAAGATGAAGCAG
CGTCTCAGCCAACTGGAAAGCCAGGTGAAGGGTGGTGGGGACAAGCCCCTGGCTGATGGG
GAAGTTCCCGGGGATGCTACAAAAACAGAGGACAAACAACAGTGA
Enzyme 35 GenBank Gene ID AC092675 Link Image
Enzyme 35 GeneCard ID CNGA3 Link Image
Enzyme 35 GenAtlas ID CNGA3 Link Image
Enzyme 35 HGNC ID HGNC:2150 Link Image
Enzyme 35 Chromosome Location 2
Enzyme 35 Locus 2q11.2
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Wissinger B, Muller F, Weyand I, Schuffenhauer S, Thanos S, Kaupp UB, Zrenner E: Cloning, chromosomal localization and functional expression of the gene encoding the alpha-subunit of the cGMP-gated channel in human cone photoreceptors. Eur J Neurosci. 1997 Dec;9(12):2512-21. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Distler M, Biel M, Flockerzi V, Hofmann F: Expression of cyclic nucleotide-gated cation channels in non-sensory tissues and cells. Neuropharmacology. 1994 Nov;33(11):1275-82. [PubMed Link Image]
  5. Sundin OH, Yang JM, Li Y, Zhu D, Hurd JN, Mitchell TN, Silva ED, Maumenee IH: Genetic basis of total colourblindness among the Pingelapese islanders. Nat Genet. 2000 Jul;25(3):289-93. [PubMed Link Image]
  6. Peng C, Rich ED, Varnum MD: Subunit configuration of heteromeric cone cyclic nucleotide-gated channels. Neuron. 2004 May 13;42(3):401-10. [PubMed Link Image]
  7. Kohl S, Marx T, Giddings I, Jagle H, Jacobson SG, Apfelstedt-Sylla E, Zrenner E, Sharpe LT, Wissinger B: Total colourblindness is caused by mutations in the gene encoding the alpha-subunit of the cone photoreceptor cGMP-gated cation channel. Nat Genet. 1998 Jul;19(3):257-9. [PubMed Link Image]
  8. Wissinger B, Gamer D, Jagle H, Giorda R, Marx T, Mayer S, Tippmann S, Broghammer M, Jurklies B, Rosenberg T, Jacobson SG, Sener EC, Tatlipinar S, Hoyng CB, Castellan C, Bitoun P, Andreasson S, Rudolph G, Kellner U, Lorenz B, Wolff G, Verellen-Dumoulin C, Schwartz M, Cremers FP, Apfelstedt-Sylla E, Zrenner E, Salati R, Sharpe LT, Kohl S: CNGA3 mutations in hereditary cone photoreceptor disorders. Am J Hum Genet. 2001 Oct;69(4):722-37. Epub 2001 Aug 30. [PubMed Link Image]
  9. Johnson S, Michaelides M, Aligianis IA, Ainsworth JR, Mollon JD, Maher ER, Moore AT, Hunt DM: Achromatopsia caused by novel mutations in both CNGA3 and CNGB3. J Med Genet. 2004 Feb;41(2):e20. [PubMed Link Image]
  10. Liu C, Varnum MD: Functional consequences of progressive cone dystrophy-associated mutations in the human cone photoreceptor cyclic nucleotide-gated channel CNGA3 subunit. Am J Physiol Cell Physiol. 2005 Jul;289(1):C187-98. Epub 2005 Mar 2. [PubMed Link Image]
  11. Nishiguchi KM, Sandberg MA, Gorji N, Berson EL, Dryja TP: Cone cGMP-gated channel mutations and clinical findings in patients with achromatopsia, macular degeneration, and other hereditary cone diseases. Hum Mutat. 2005 Mar;25(3):248-58. [PubMed Link Image]
  12. Reuter P, Koeppen K, Ladewig T, Kohl S, Baumann B, Wissinger B: Mutations in CNGA3 impair trafficking or function of cone cyclic nucleotide-gated channels, resulting in achromatopsia. Hum Mutat. 2008 Oct;29(10):1228-36. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 6416
Enzyme 36 Name Cyclic nucleotide-gated cation channel beta-3
Enzyme 36 Synonyms
  1. Cone photoreceptor cGMP-gated channel subunit beta
  2. Cyclic nucleotide-gated cation channel modulatory subunit
  3. Cyclic nucleotide-gated channel beta-3
  4. CNG channel beta-3
Enzyme 36 Gene Name CNGB3
Enzyme 36 Protein Sequence >Cyclic nucleotide-gated cation channel beta-3
MFKSLTKVNKVKPIGENNENEQSSRRNEEGSHPSNQSQQTTAQEENKGEEKSLKTKSTPV
TSEEPHTNIQDKLSKKNSSGDLTTNPDPQNAAEPTGTVPEQKEMDPGKEGPNSPQNKPPA
APVINEYADAQLHNLVKRMRQRTALYKKKLVEGDLSSPEASPQTAKPTAVPPVKESDDKP
TEHYYRLLWFKVKKMPLTEYLKRIKLPNSIDSYTDRLYLLWLLLVTLAYNWNCWFIPLRL
VFPYQTADNIHYWLIADIICDIIYLYDMLFIQPRLQFVRGGDIIVDSNELRKHYRTSTKF
QLDVASIIPFDICYLFFGFNPMFRANRMLKYTSFFEFNHHLESIMDKAYIYRVIRTTGYL
LFILHINACVYYWASNYEGIGTTRWVYDGEGNEYLRCYYWAVRTLITIGGLPEPQTLFEI
VFQLLNFFSGVFVFSSLIGQMRDVIGAATANQNYFRACMDDTIAYMNNYSIPKLVQKRVR
TWYEYTWDSQRMLDESDLLKTLPTTVQLALAIDVNFSIISKVDLFKGCDTQMIYDMLLRL
KSVLYLPGDFVCKKGEIGKEMYIIKHGEVQVLGGPDGTKVLVTLKAGSVFGEISLLAAGG
GNRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILMKKARVLLKQKAKTAEATPPRK
DLALLFPPKEETPKLFKTLLGGTGKASLARLLKLKREQAAQKKENSEGGEEEGKENEDKQ
KENEDKQKENEDKGKENEDKDKGREPEEKPLDRPECTASPIAVEEEPHSVRRTVLPRGTS
RQSLIISMAPSAEGGEEVLTIEVKEKAKQ
Enzyme 36 Number of Residues 809
Enzyme 36 Molecular Weight 92248.8
Enzyme 36 Theoretical pI 8.11
Enzyme 36 GO Classification
Function
  • ion channel activity
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 36 General Function Involved in ion channel activity
Enzyme 36 Specific Function Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cGMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficiency of the channel when coexpressed with CNGA3. Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • 217-237 251-271 303-323 360-380 418-438 505-525
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 116642889 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q9NQW8 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name CNGB3_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >2430 bp
ATGTTTAAATCGCTGACAAAAGTCAACAAGGTGAAGCCTATAGGAGAGAACAATGAGAAT
GAACAAAGTTCTCGTCGGAATGAAGAAGGCTCTCACCCAAGTAATCAGTCTCAGCAAACC
ACAGCACAGGAAGAAAACAAAGGTGAAGAGAAATCTCTCAAAACCAAGTCAACTCCAGTC
ACGTCTGAAGAGCCACACACCAACATACAAGACAAACTCTCCAAGAAAAATTCCTCTGGA
GATCTGACCACAAACCCTGACCCTCAAAATGCAGCAGAACCAACTGGAACAGTGCCAGAG
CAGAAGGAAATGGACCCCGGGAAAGAAGGTCCAAACAGCCCACAAAACAAACCGCCTGCA
GCTCCTGTTATAAATGAGTATGCCGATGCCCAGCTACACAACCTGGTGAAAAGAATGCGT
CAAAGAACAGCCCTCTACAAGAAAAAGTTGGTAGAGGGAGATCTCTCCTCACCCGAAGCC
AGCCCACAAACTGCAAAGCCCACGGCTGTACCACCAGTAAAAGAAAGCGATGATAAGCCA
ACAGAACATTACTACAGGCTGTTGTGGTTCAAAGTCAAAAAGATGCCTTTAACAGAGTAC
TTAAAGCGAATTAAACTTCCAAACAGCATAGATTCATACACAGATCGACTCTATCTCCTG
TGGCTCTTGCTTGTCACTCTTGCCTATAACTGGAACTGCTGTTTTATACCACTGCGCCTC
GTCTTCCCATATCAAACCGCAGACAACATACACTACTGGCTTATTGCGGACATCATATGT
GATATCATCTACCTTTATGATATGCTATTTATCCAGCCCAGACTCCAGTTTGTAAGAGGA
GGAGACATAATAGTGGATTCAAATGAGCTAAGGAAACACTACAGGACTTCTACAAAATTT
CAGTTGGATGTCGCATCAATAATACCATTTGATATTTGCTACCTCTTCTTTGGGTTTAAT
CCAATGTTTAGAGCAAATAGGATGTTAAAGTACACTTCATTTTTTGAATTTAATCATCAC
CTAGAGTCTATAATGGACAAAGCATATATCTACAGAGTTATTCGAACAACTGGATACTTG
CTGTTTATTCTGCACATTAATGCCTGTGTTTATTACTGGGCTTCAAACTATGAAGGAATT
GGCACTACTAGATGGGTGTATGATGGGGAAGGAAACGAGTATCTGAGATGTTATTATTGG
GCAGTTCGAACTTTAATTACCATTGGTGGCCTTCCAGAACCACAAACTTTATTTGAAATT
GTTTTTCAACTCTTGAATTTTTTTTCTGGAGTTTTTGTGTTCTCCAGTTTAATTGGTCAG
ATGAGAGATGTGATTGGAGCAGCTACAGCCAATCAGAACTACTTCCGCGCCTGCATGGAT
GACACCATTGCCTACATGAACAATTACTCCATTCCTAAACTTGTGCAAAAGCGAGTTCGG
ACTTGGTATGAATATACATGGGACTCTCAAAGAATGCTAGATGAGTCTGATTTGCTTAAG
ACCCTACCAACTACGGTCCAGTTAGCCCTCGCCATTGATGTGAACTTCAGCATCATCAGC
AAAGTCGACTTGTTCAAGGGTTGTGATACACAGATGATTTATGACATGTTGCTAAGATTG
AAATCCGTTCTCTATTTGCCTGGTGACTTTGTCTGCAAAAAGGGAGAAATTGGCAAGGAA
ATGTATATCATCAAGCATGGAGAAGTCCAAGTTCTTGGAGGCCCTGATGGTACTAAAGTT
CTGGTTACTCTGAAAGCTGGGTCGGTGTTTGGAGAAATCAGCCTTCTAGCAGCAGGAGGA
GGAAACCGTCGAACTGCCAATGTGGTGGCCCACGGGTTTGCCAATCTTTTAACTCTAGAC
AAAAAGACCCTCCAAGAAATTCTAGTGCATTATCCAGATTCTGAAAGGATCCTCATGAAG
AAAGCCAGAGTGCTTTTAAAGCAGAAGGCTAAGACCGCAGAAGCAACCCCTCCAAGAAAA
GATCTTGCCCTCCTCTTCCCACCGAAAGAAGAGACACCCAAACTGTTTAAAACTCTCCTA
GGAGGCACAGGAAAAGCAAGTCTTGCAAGACTACTCAAATTGAAGCGAGAGCAAGCAGCT
CAGAAGAAAGAAAATTCTGAAGGAGGAGAGGAAGAAGGAAAAGAAAATGAAGATAAACAA
AAAGAAAATGAAGATAAACAAAAAGAAAATGAAGATAAAGGAAAAGAAAATGAAGATAAA
GATAAAGGAAGAGAGCCAGAAGAGAAGCCACTGGACAGACCTGAATGTACAGCAAGTCCT
ATTGCAGTGGAGGAAGAACCCCACTCAGTTAGAAGGACAGTTTTACCCAGAGGGACTTCT
CGTCAATCACTCATTATCAGCATGGCTCCTTCTGCTGAGGGCGGAGAAGAGGTTCTTACT
ATTGAAGTCAAAGAAAAGGCTAAGCAATAA
Enzyme 36 GenBank Gene ID NM_019098.4 Link Image
Enzyme 36 GeneCard ID CNGB3 Link Image
Enzyme 36 GenAtlas ID CNGB3 Link Image
Enzyme 36 HGNC ID HGNC:2153 Link Image
Enzyme 36 Chromosome Location 8
Enzyme 36 Locus 8q21.3
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Kohl S, Baumann B, Broghammer M, Jagle H, Sieving P, Kellner U, Spegal R, Anastasi M, Zrenner E, Sharpe LT, Wissinger B: Mutations in the CNGB3 gene encoding the beta-subunit of the cone photoreceptor cGMP-gated channel are responsible for achromatopsia (ACHM3) linked to chromosome 8q21. Hum Mol Genet. 2000 Sep 1;9(14):2107-16. [PubMed Link Image]
  2. Sundin OH, Yang JM, Li Y, Zhu D, Hurd JN, Mitchell TN, Silva ED, Maumenee IH: Genetic basis of total colourblindness among the Pingelapese islanders. Nat Genet. 2000 Jul;25(3):289-93. [PubMed Link Image]
  3. Rojas CV, Maria LS, Santos JL, Cortes F, Alliende MA: A frameshift insertion in the cone cyclic nucleotide gated cation channel causes complete achromatopsia in a consanguineous family from a rural isolate. Eur J Hum Genet. 2002 Oct;10(10):638-42. [PubMed Link Image]
  4. Johnson S, Michaelides M, Aligianis IA, Ainsworth JR, Mollon JD, Maher ER, Moore AT, Hunt DM: Achromatopsia caused by novel mutations in both CNGA3 and CNGB3. J Med Genet. 2004 Feb;41(2):e20. [PubMed Link Image]
  5. Kohl S, Varsanyi B, Antunes GA, Baumann B, Hoyng CB, Jagle H, Rosenberg T, Kellner U, Lorenz B, Salati R, Jurklies B, Farkas A, Andreasson S, Weleber RG, Jacobson SG, Rudolph G, Castellan C, Dollfus H, Legius E, Anastasi M, Bitoun P, Lev D, Sieving PA, Munier FL, Zrenner E, Sharpe LT, Cremers FP, Wissinger B: CNGB3 mutations account for 50% of all cases with autosomal recessive achromatopsia. Eur J Hum Genet. 2005 Mar;13(3):302-8. [PubMed Link Image]
  6. Nishiguchi KM, Sandberg MA, Gorji N, Berson EL, Dryja TP: Cone cGMP-gated channel mutations and clinical findings in patients with achromatopsia, macular degeneration, and other hereditary cone diseases. Hum Mutat. 2005 Mar;25(3):248-58. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 6417
Enzyme 37 Name Rap guanine nucleotide exchange factor 2
Enzyme 37 Synonyms
  1. Neural RAP guanine nucleotide exchange protein
  2. nRap GEP
  3. PDZ domain-containing guanine nucleotide exchange factor 1
  4. PDZ-GEF1
  5. RA-GEF
Enzyme 37 Gene Name RAPGEF2
Enzyme 37 Protein Sequence >Rap guanine nucleotide exchange factor 2
MKPLAIPANHGVMGQQEKHSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLS
DIYQATESEAGDMDLSGLPETAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTD
DDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAGTIVLNDGEELDSWSVILNGS
VEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEK
NMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLL
TYRTFLSSPMEVGKKLLEWFNDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENN
LEREKMGGHLRLLNIACAAKAKRRLMTLTKPSREAPLPFILLGGSEKGFGIFVDSVDSGS
KATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEE
KRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKT
RISILPQKPYNDIGIGQSQDDSIVGLRQTKHIPTALPVSGTLSSSNPDLLQSHHRILDFS
ATPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIREFAVTATPDQYSLCEVSVTPE
GVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVE
VATQLSMRNFELFRNIEPTEYIDDLFKLRSKTSCANLKRFEEVINQETFWVASEILRETN
QLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDL
QDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFLHEGNDSKVDGLVNFEKLRMI
AKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSTNATVLDVAQTGGHKKRVRRSS
FLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATNTLPKNPGDKKPVKSE
TSPVAPRAGSQQKAQSLPQPQQQPPPAHKINQGLQVPAVSLYPSRKKVPVKDLPPFGINS
PQALKKILSLSEEGSLERHKKQAEDTISNASSQLSSPPTSPQSSPRKGYTLAPSGTVDNF
SDSGHSEISSRSSIVSNSSFDSVPVSLHDERRQRHSVSIVETNLGMGRMERRTMIEPDQY
SLGSYAPMSEGRGLYATATVISSPSTEELSQDQGDRASLDAADSGRGSWTSCSSGSHDNI
QTIQHQRSWETLPFGHTHFDYSGDPAGLWASSSHMDQIMFSDHSTKYNRQNQSRESLEQA
QSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSIEAESSSLTSVTTEETKPVPMPAHIAV
ASSTTKGLIARKEGRYREPPPTPPGYIGIPITDFPEGHSHPARKPPDYNVALQRSRMVAR
SSDTAGPSSVQQPHGHPTSSRPVNKPQWHKPNESDPRLAPYQSQGFSTEEDEDEQVSAV
Enzyme 37 Number of Residues 1499
Enzyme 37 Molecular Weight 167415.5
Enzyme 37 Theoretical pI 6.64
Enzyme 37 GO Classification
Function
  • GTPase regulator activity
  • binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • protein binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 37 General Function Involved in protein binding
Enzyme 37 Specific Function Guanine nucleotide exchange factor (GEF) for Rap1A, Rap1B and Rap2B GTPases. Does not interact with cAMP or cGMP
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 7657261 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q9Y4G8 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name RPGF2_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >4500 bp
ATGAAACCACTAGCAATCCCAGCTAACCATGGAGTTATGGGCCAGCAGGAGAAACACTCA
CTTCCTGCAGATTTCACAAAACTGCATCTTACTGACAGTCTCCACCCACAGGTGACCCAC
GTTTCTTCTAGCCATTCAGGATGTAGTATCACTAGTGATTCTGGGAGCAGCAGTCTTTCT
GATATCTACCAGGCCACAGAAAGCGAGGCTGGTGATATGGACCTGAGTGGGTTGCCAGAA
ACAGCAGTGGATTCCGAAGACGACGACGATGAAGAAGACATTGAGAGAGCATCAGATCCT
CTGATGAGCAGGGACATTGTGAGAGACTGCCTAGAGAAGGACCCAATTGACCGGACAGAT
GATGACATTGAACAACTCTTGGAATTTATGCACCAGTTGCCTGCTTTTGCCAATATGACA
ATGTCAGTGAGGCGAGAACTCTGTGCTGTGATGGTGTTCGCAGTGGTGGAAAGAGCAGGG
ACCATAGTGTTAAATGATGGTGAAGAGCTGGACTCCTGGTCAGTGATTCTCAATGGATCT
GTGGAAGTGACTTATCCAGATGGAAAAGCAGAAATACTGTGCATGGGAAATAGTTTTGGT
GTCTCTCCTACCATGGACAAAGAATACATGAAAGGAGTGATGAGAACAAAGGTGGATGAC
TGCCAGTTTGTCTGCATAGCCCAGCAAGATTACTGCCGTATTCTCAATCAAGTAGAAAAG
AACATGCAAAAAGTTGAAGAGGAAGGAGAGATTGTTATGGTGAAAGAACACCGAGAACTT
GATCGAACTGGAACAAGAAAGGGACACATTGTCATCAAGGGTACCTCAGAAAGGTTAACA
ATGCATTTGGTGGAAGAGCATTCAGTAGTAGATCCAACATTCATAGAAGACTTTCTGTTG
ACCTATAGGACTTTTCTTTCTAGCCCAATGGAAGTGGGCAAAAAGTTATTGGAGTGGTTT
AATGACCCGAGCCTCAGGGATAAGGTTACACGGGTAGTATTATTGTGGGTAAATAATCAC
TTCAATGACTTTGAAGGAGATCCTGCAATGACTCGATTTTTAGAAGAATTTGAAAACAAT
CTGGAAAGAGAGAAAATGGGTGGACACCTAAGGCTGTTGAATATCGCGTGTGCTGCTAAA
GCAAAAAGAAGATTGATGACGTTAACAAAACCATCCCGAGAAGCTCCTTTGCCTTTTATC
TTACTTGGAGGCTCTGAGAAGGGATTTGGAATCTTTGTTGACAGTGTAGATTCAGGTAGC
AAAGCAACTGAAGCAGGCTTGAAACGGGGGGATCAGATATTAGAAGTAAATGGCCAAAAC
TTTGAAAACATTCAGCTGTCAAAAGCTATGGAAATTCTTAGAAATAACACACATTTATCT
ATCACTGTGAAAACCAATTTATTTGTATTTAAAGAACTTCTAACAAGATTGTCAGAAGAG
AAAAGAAATGGTGCCCCCCACCTTCCTAAAATTGGTGACATTAAAAAGGCCAGTCGCTAC
TCCATTCCAGATCTTGCTGTAGATGTAGAACAGGTGATAGGACTTGAAAAAGTGAACAAA
AAAAGTAAAGCCAACACTGTGGGAGGAAGGAACAAGCTGAAAAAGATACTCGACAAGACT
CGGATCAGTATCTTGCCACAGAAACCATACAATGATATTGGGATTGGTCAGTCTCAAGAT
GACAGCATAGTAGGATTAAGGCAGACAAAGCACATCCCAACTGCATTGCCTGTCAGTGGA
ACCTTATCATCCAGTAATCCTGATTTATTGCAGTCACATCATCGCATTTTAGACTTCAGT
GCTACTCCTGACTTGCCAGATCAAGTGCTAAGGGTTTTTAAGGCTGATCAGCAAAGCCGC
TACATCATGATCAGTAAGGACACTACAGCAAAGGAAGTGGTCATTCAGGCTATCAGGGAG
TTTGCTGTTACTGCCACCCCGGATCAATATTCACTATGTGAGGTCTCTGTCACACCTGAG
GGAGTAATCAAACAAAGAAGACTTCCAGATCAGCTTTCCAAACTTGCAGACAGAATACAA
CTGAGTGGAAGGTATTATCTGAAAAACAACATGGAAACAGAAACTCTTTGTTCAGATGAA
GATGCTCAGGAGTTGTTGAGAGAGAGTCAAATTTCCCTCCTTCAGCTCAGCACTGTGGAA
GTTGCAACACAGCTCTCTATGCGAAATTTTGAACTCTTTCGCAACATTGAACCTACTGAA
TATATAGATGATTTATTTAAACTCAGATCAAAAACCAGCTGTGCCAACCTGAAGAGATTT
GAAGAAGTCATTAACCAGGAAACATTTTGGGTAGCATCTGAAATTCTCAGAGAAACAAAC
CAGCTGAAGAGGATGAAGATCATTAAGCATTTCATCAAGATAGCACTGCACTGTAGGGAA
TGCAAGAATTTTAACTCAATGTTTGCAATCATCAGTGGCCTAAACCTGGCACCAGTGGCA
AGACTGCGAACGACCTGGGAGAAACTTCCCAATAAATACGAAAAACTATTTCAAGATCTC
CAAGACCTGTTTGATCCTTCCAGAAACATGGCAAAATATCGTAATGTTCTCAATAGTCAA
AATCTACAACCTCCCATAATCCCTCTATTCCCAGTTATCAAAAAGGATCTCACCTTCCTT
CACGAAGGAAATGACTCAAAAGTAGACGGGCTGGTCAATTTTGAGAAGCTAAGGATGATT
GCAAAAGAAATTCGTCACGTTGGCCGAATGGCTTCAGTGAACATGGACCCTGCCCTCATG
TTCAGGACTCGGAAGAAGAAATGGCGGAGTTTGGGGTCTCTCAGCCAGGGTAGTACAAAT
GCAACAGTGCTAGATGTTGCTCAGACAGGTGGTCATAAAAAGCGGGTACGTCGTAGTTCC
TTTCTCAATGCCAAAAAGCTTTATGAAGATGCCCAAATGGCTCGAAAAGTGAAGCAGTAC
CTTTCCAATTTGGAGCTAGAAATGGACGAGGAGAGTCTTCAGACATTATCTCTGCAGTGT
GAGCCAGCAACCAACACATTGCCTAAGAATCCTGGTGACAAAAAGCCTGTCAAATCCGAG
ACCTCTCCAGTAGCTCCAAGGGCAGGGTCACAACAGAAAGCTCAGTCCCTGCCACAGCCC
CAGCAGCAGCCACCACCAGCACATAAAATCAACCAGGGACTACAGGTTCCCGCCGTGTCC
CTTTATCCTTCACGGAAGAAAGTGCCCGTAAAGGATCTCCCACCTTTTGGCATAAACTCT
CCACAAGCTTTAAAAAAAATTCTTTCTTTGTCTGAAGAAGGAAGTTTGGAACGTCACAAG
AAACAGGCTGAAGATACAATATCAAATGCATCTTCGCAGCTTTCTTCTCCTCCTACTTCT
CCACAGAGTTCTCCAAGGAAAGGCTATACTTTGGCTCCCAGTGGTACTGTGGATAATTTT
TCAGATTCTGGTCACAGTGAAATTTCTTCACGATCCAGTATTGTTAGCAATTCGTCTTTT
GACTCAGTGCCAGTCTCACTGCACGATGAGAGGCGCCAGAGGCATTCTGTCAGCATCGTG
GAAACAAACCTAGGGATGGGCAGGATGGAGAGGCGGACCATGATTGAACCTGATCAGTAT
AGCTTGGGGTCCTATGCACCAATGTCCGAGGGCCGAGGCTTATATGCTACAGCTACAGTA
ATTTCTTCTCCAAGCACAGAGGAACTTTCCCAGGATCAGGGGGATCGCGCGTCACTTGAT
GCTGCTGACAGTGGCCGTGGGAGCTGGACGTCATGCTCAAGTGGCTCCCATGATAATATA
CAGACGATCCAGCACCAGAGAAGCTGGGAGACTCTTCCATTCGGGCATACTCACTTTGAT
TATTCAGGGGATCCTGCAGGTTTATGGGCATCAAGCAGCCATATGGACCAAATTATGTTT
TCTGATCATAGCACAAAGTATAACAGGCAAAATCAAAGTAGAGAGAGCCTTGAACAAGCC
CAGTCCCGAGCAAGCTGGGCGTCTTCCACAGGTTACTGGGGAGAAGACTCAGAAGGTGAC
ACAGGCACAATAAAGCGGAGGGGTGGAAAGGATGTTTCCATTGAAGCCGAAAGCAGTAGC
CTAACGTCTGTGACTACGGAAGAAACCAAGCCTGTCCCCATGCCTGCCCACATAGCTGTG
GCATCAAGTACTACAAAGGGGCTCATTGCACGAAAGGAGGGCAGGTATCGAGAGCCCCCG
CCCACCCCTCCCGGCTACATTGGAATTCCCATTACTGACTTTCCAGAAGGGCACTCCCAT
CCAGCCAGGAAACCGCCGGACTACAACGTGGCCCTTCAGAGATCGCGGATGGTCGCACGA
TCCTCCGACACAGCTGGGCCTTCATCCGTACAGCAGCCACATGGGCATCCCACCAGCAGC
AGGCCTGTGAACAAACCTCAGTGGCATAAACCGAACGAGTCTGACCCGCGCCTCGCCCCC
TATCAGTCCCAAGGGTTTTCCACCGAGGAGGATGAAGATGAACAAGTTTCTGCTGTTTGA
Enzyme 37 GenBank Gene ID NM_014247.2 Link Image
Enzyme 37 GeneCard ID RAPGEF2 Link Image
Enzyme 37 GenAtlas ID RAPGEF2 Link Image
Enzyme 37 HGNC ID HGNC:16854 Link Image
Enzyme 37 Chromosome Location 4
Enzyme 37 Locus 4q32.1
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  2. Ohtsuka T, Hata Y, Ide N, Yasuda T, Inoue E, Inoue T, Mizoguchi A, Takai Y: nRap GEP: a novel neural GDP/GTP exchange protein for rap1 small G protein that interacts with synaptic scaffolding molecule (S-SCAM). Biochem Biophys Res Commun. 1999 Nov;265(1):38-44. [PubMed Link Image]
  3. de Rooij J, Boenink NM, van Triest M, Cool RH, Wittinghofer A, Bos JL: PDZ-GEF1, a guanine nucleotide exchange factor specific for Rap1 and Rap2. J Biol Chem. 1999 Dec 31;274(53):38125-30. [PubMed Link Image]
  4. Rebhun JF, Castro AF, Quilliam LA: Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction. J Biol Chem. 2000 Nov 10;275(45):34901-8. [PubMed Link Image]
  5. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  6. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 6420
Enzyme 38 Name Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
Enzyme 38 Synonyms
  1. Brain cyclic nucleotide-gated channel 1
  2. BCNG-1
Enzyme 38 Gene Name HCN1
Enzyme 38 Protein Sequence >Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
MEGGGKPNSSSNSRDDGNSVFPAKASATGAGPAAAEKRLGTPPGGGGAGAKEHGNSVCFK
VDGGGGGGGGGGGGEEPAGGFEDAEGPRRQYGFMQRQFTSMLQPGVNKFSLRMFGSQKAV
EKEQERVKTAGFWIIHPYSDFRFYWDLIMLIMMVGNLVIIPVGITFFTEQTTTPWIIFNV
ASDTVFLLDLIMNFRTGTVNEDSSEIILDPKVIKMNYLKSWFVVDFISSIPVDYIFLIVE
KGMDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFN
LIGMMLLLCHWDGCLQFLVPLLQDFPPDCWVSLNEMVNDSWGKQYSYALFKAMSHMLCIG
YGAQAPVSMSDLWITMLSMIVGATCYAMFVGHATALIQSLDSSRRQYQEKYKQVEQYMSF
HKLPADMRQKIHDYYEHRYQGKIFDEENILNELNDPLREEIVNFNCRKLVATMPLFANAD
PNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVITKSSKEMKLTDGSYFGE
ICLLTKGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSI
LLQKFQKDLNTGVFNNQENEILKQIVKHDREMVQAIAPINYPQMTTLNSTSSTTTPTSRM
RTQSPPVYTATSLSHSNLHSPSPSTQTPQPSAILSPCSYTTAVCSPPVQSPLAARTFHYA
SPTASQLSLMQQQPQQQVQQSQPPQTQPQQPSPQPQTPGSSTPKNEVHKSTQALHNTNLT
REVRPLSASQPSLPHEVSTLISRPHPTVGESLASIPQPVTAVPGTGLQAGGRSTVPQRVT
LFRQMSSGAIPPNRGVPPAPPPPAAALPRESSSVLNTDPDAEKPRFASNL
Enzyme 38 Number of Residues 890
Enzyme 38 Molecular Weight 98795.3
Enzyme 38 Theoretical pI 8.54
Enzyme 38 GO Classification
Function
  • cation channel activity
  • ion channel activity
  • ion transmembrane transporter activity
  • potassium channel activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
  • voltage-gated potassium channel activity
Process
  • cation transport
  • establishment of localization
  • ion transport
  • monovalent inorganic cation transport
  • potassium ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 38 General Function Involved in ion channel activity
Enzyme 38 Specific Function Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Activated by cAMP, and at 10-100 times higher concentrations, also by cGMP. May mediate responses to sour stimuli
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • 147-167 174-194 220-240 249-269 301-321 372-392
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 116325989 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID O60741 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name HCN1_HUMAN Link Image
Enzyme 38 PDB ID 1Q3E Link Image
Enzyme 38 PDB File Show
Enzyme 38 3D Structure
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >2673 bp
ATGGAAGGAGGCGGCAAGCCCAACTCTTCGTCTAACAGCCGGGACGATGGCAACAGCGTC
TTCCCCGCCAAGGCGTCCGCGACGGGCGCGGGGCCGGCCGCGGCCGAGAAGCGCCTGGGC
ACCCCGCCGGGGGGCGGCGGGGCCGGCGCGAAGGAGCACGGCAACTCCGTGTGCTTCAAG
GTGGACGGCGGTGGCGGCGGTGGCGGCGGCGGCGGCGGCGGCGAGGAGCCGGCGGGGGGC
TTCGAAGACGCCGAGGGGCCCCGGCGGCAGTACGGCTTCATGCAGAGGCAGTTCACCTCC
ATGCTGCAGCCCGGGGTCAACAAATTCTCCCTCCGCATGTTTGGGAGCCAGAAGGCGGTG
GAAAAGGAGCAGGAAAGGGTTAAAACTGCAGGCTTCTGGATTATCCACCCTTACAGTGAT
TTCAGGTTTTACTGGGATTTAATAATGCTTATAATGATGGTTGGAAATCTAGTCATCATA
CCAGTTGGAATCACATTCTTTACAGAGCAAACAACAACACCATGGATTATTTTCAATGTG
GCATCAGATACAGTTTTCCTATTGGACCTGATCATGAATTTTAGGACTGGGACTGTCAAT
GAAGACAGTTCTGAAATCATCCTGGACCCCAAAGTGATCAAGATGAATTATTTAAAAAGC
TGGTTTGTGGTTGACTTCATCTCATCCATCCCAGTGGATTATATCTTTCTTATTGTAGAA
AAAGGAATGGATTCTGAAGTTTACAAGACAGCCAGGGCACTTCGCATTGTGAGGTTTACA
AAAATTCTCAGTCTCTTGCGTTTATTACGACTTTCAAGGTTAATTAGATACATACATCAA
TGGGAAGAGATATTCCACATGACATATGATCTCGCCAGTGCAGTGGTGAGAATTTTTAAT
CTCATCGGCATGATGCTGCTCCTGTGCCACTGGGATGGTTGTCTTCAGTTCTTAGTACCA
CTACTGCAGGACTTCCCACCAGATTGCTGGGTGTCTTTAAATGAAATGGTTAATGATTCT
TGGGGAAAGCAGTATTCATACGCACTCTTCAAAGCTATGAGTCACATGCTGTGCATTGGG
TATGGAGCCCAAGCCCCAGTCAGCATGTCTGACCTCTGGATTACCATGCTGAGCATGATC
GTCGGGGCCACCTGCTATGCCATGTTTGTCGGCCATGCCACCGCTTTAATCCAGTCTCTG
GATTCTTCGAGGCGGCAGTATCAAGAGAAGTATAAGCAAGTGGAACAATACATGTCATTC
CATAAGTTACCAGCTGATATGCGTCAGAAGATACATGATTACTATGAACACAGATACCAA
GGCAAAATCTTTGATGAGGAAAATATTCTCAATGAACTCAATGATCCTCTGAGAGAGGAG
ATAGTCAACTTCAACTGTCGGAAACTGGTGGCTACAATGCCTTTATTTGCTAATGCGGAT
CCTAATTTTGTGACTGCCATGCTGAGCAAGTTGAGATTTGAGGTGTTTCAACCTGGAGAT
TATATCATACGAGAAGGAGCCGTGGGTAAAAAAATGTATTTCATTCAACACGGTGTTGCT
GGTGTCATTACAAAATCCAGTAAAGAAATGAAGCTGACAGATGGCTCTTACTTTGGAGAG
ATTTGCCTGCTGACCAAAGGACGTCGTACTGCCAGTGTTCGAGCTGATACATATTGTCGT
CTTTACTCACTTTCCGTGGACAATTTCAACGAGGTCCTGGAGGAATATCCAATGATGAGG
AGAGCCTTTGAGACAGTTGCCATTGACCGACTAGATCGAATAGGAAAGAAAAATTCAATT
CTTCTGCAAAAGTTCCAGAAGGATCTGAACACTGGTGTTTTCAACAATCAGGAGAACGAA
ATCCTCAAGCAGATTGTGAAACATGACAGGGAGATGGTGCAGGCAATCGCTCCCATCAAT
TATCCTCAAATGACAACCCTGAATTCCACATCGTCTACTACGACCCCGACCTCCCGCATG
AGGACACAATCTCCACCGGTGTACACAGCGACCAGCCTGTCTCACAGCAACCTGCACTCC
CCCAGTCCCAGCACACAGACCCCCCAGCCATCAGCCATCCTGTCACCCTGCTCCTACACC
ACCGCGGTCTGCAGCCCTCCTGTACAGAGCCCTCTGGCCGCTCGAACTTTCCACTATGCC
TCCCCCACCGCCTCCCAGCTGTCACTCATGCAACAGCAGCCGCAGCAGCAGGTACAGCAG
TCCCAGCCGCCGCAGACTCAGCCACAGCAGCCGTCCCCGCAGCCACAGACACCTGGCAGC
TCCACGCCGAAAAATGAAGTGCACAAGAGCACGCAGGCGCTTCACAACACCAACCTGACC
CGGGAAGTCAGGCCACTCTCCGCCTCGCAGCCCTCGCTGCCCCATGAGGTGTCCACTCTG
ATTTCCAGACCTCATCCCACTGTGGGCGAGTCCCTGGCCTCCATCCCTCAACCCGTGACG
GCGGTCCCCGGAACGGGCCTTCAGGCAGGGGGCAGGAGCACTGTCCCGCAGCGCGTCACC
CTCTTCCGACAGATGTCGTCGGGAGCCATCCCCCCGAACCGAGGAGTCCCTCCAGCACCC
CCTCCACCAGCAGCTGCTCTTCCAAGAGAATCTTCCTCAGTCTTAAACACAGACCCAGAC
GCAGAAAAGCCACGATTTGCTTCAAATTTATGA
Enzyme 38 GenBank Gene ID NM_021072.2 Link Image
Enzyme 38 GeneCard ID HCN1 Link Image
Enzyme 38 GenAtlas ID HCN1 Link Image
Enzyme 38 HGNC ID HGNC:4845 Link Image
Enzyme 38 Chromosome Location 5
Enzyme 38 Locus 5p12
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
  2. Santoro B, Liu DT, Yao H, Bartsch D, Kandel ER, Siegelbaum SA, Tibbs GR: Identification of a gene encoding a hyperpolarization-activated pacemaker channel of brain. Cell. 1998 May 29;93(5):717-29. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 6503
Enzyme 39 Name cAMP-dependent protein kinase catalytic subunit gamma
Enzyme 39 Synonyms
  1. PKA C-gamma
Enzyme 39 Gene Name PRKACG
Enzyme 39 Protein Sequence >cAMP-dependent protein kinase catalytic subunit gamma
MGNAPAKKDTEQEESVNEFLAKARGDFLYRWGNPAQNTASSDQFERLRTLGMGSFGRVML
VRHQETGGHYAMKILNKQKVVKMKQVEHILNEKRILQAIDFPFLVKLQFSFKDNSYLYLV
MEYVPGGEMFSRLQRVGRFSEPHACFYAAQVVLAVQYLHSLDLIHRDLKPENLLIDQQGY
LQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAVGFPPFY
ADQPIQIYEKIVSGRVRFPSKLSSDLKHLLRSLLQVDLTKRFGNLRNGVGDIKNHKWFAT
TSWIAIYEKKVEAPFIPKYTGPGDASNFDDYEEEELRISINEKCAKEFSEF
Enzyme 39 Number of Residues 351
Enzyme 39 Molecular Weight 40434.2
Enzyme 39 Theoretical pI 8.89
Enzyme 39 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
Enzyme 39 General Function Involved in protein serine/threonine kinase activity
Enzyme 39 Specific Function Phosphorylates a large number of substrates in the cytoplasm and the nucleus
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 3115220 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID P22612 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name KAPCG_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >1056 bp
ATGGGCAACGCCCCCGCCAAGAAGGACACCGAGCAGGAGGAGAGCGTGAACGAGTTCCTA
GCCAAAGCCAGAGGAGATTTCCTCTACAGATGGGGAAACCCCGCTCAAAACACCGCCAGC
TCGGATCAGTTCGAACGGCTCAGGACGCTGGGCATGGGCTCCTTCGGGCGGGTGATGCTG
GTGAGGCACCAGGAGACCGGCGGCCACTACGCCATGAAGATCCTCAACAAGCAGAAGGTG
GTGAAGATGAAGCAGGTCGAGCACATACTGAACGAGAAGCGCATCCTGCAGGCGATCGAC
TTTCCGTTCCTCGTCAAGCTCCAGTTCTCCTTTAAGGACAACTCCTACCTGTACCTGGTG
ATGGAGTACGTGCCGGGTGGGGAGATGTTCTCCCGCCTACAGCGCGTCGGAAGGTTTAGC
GAGCCCCATGCCTGTTTCTATGCCGCCCAGGTCGTCCTGGCCGTCCAGTACCTACACTCG
CTCGACCTCATCCACCGCGACCTGAAGCCCGAGAATCTCCTCATCGACCAGCAGGGCTAC
CTGCAGGTGACGGACTTCGGTTTCGCCAAGCGCGTGAAGGGCCGCACTTGGACCTTGTGC
GGGACCCCAGAGTACCTGGCCCCCGAGATCATCCTGAGCAAAGGCTACAACAAGGCCGTG
GACTGGTGGGCCCTAGGGGTGCTCATCTATGAGATGGCCGTGGGCTTCCCACCCTTCTAC
GCCGACCAGCCCATCCAGATCTACGAGAAGATCGTCTCTGGGAGGGTGCGGTTTCCCTCC
AAACTCAGCTCTGACCTCAAGCATCTGCTGCGGAGCCTGCTGCAGGTGGACCTCACCAAG
CGCTTCGGAAACCTCAGGAACGGGGTTGGCGACATCAAGAACCACAAGTGGTTCGCCACA
ACCAGCTGGATCGCCATCTATGAGAAGAAGGTGGAAGCTCCCTTCATCCCGAAGTACACA
GGCCCTGGGGATGCCAGTAACTTTGACGACTACGAGGAGGAAGAGCTCCGGATCTCCATC
AATGAGAAGTGTGCCAAGGAGTTTTCTGAGTTTTAG
Enzyme 39 GenBank Gene ID AJ001597 Link Image
Enzyme 39 GeneCard ID PRKACG Link Image
Enzyme 39 GenAtlas ID PRKACG Link Image
Enzyme 39 HGNC ID HGNC:9382 Link Image
Enzyme 39 Chromosome Location 9
Enzyme 39 Locus 9q13
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Beebe SJ, Oyen O, Sandberg M, Froysa A, Hansson V, Jahnsen T: Molecular cloning of a tissue-specific protein kinase (C gamma) from human testis--representing a third isoform for the catalytic subunit of cAMP-dependent protein kinase. Mol Endocrinol. 1990 Mar;4(3):465-75. [PubMed Link Image]
  2. Reinton N, Haugen TB, Orstavik S, Skalhegg BS, Hansson V, Jahnsen T, Tasken K: The gene encoding the C gamma catalytic subunit of cAMP-dependent protein kinase is a transcribed retroposon. Genomics. 1998 Apr 15;49(2):290-7. [PubMed Link Image]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 6648
Enzyme 40 Name cAMP-dependent protein kinase catalytic subunit alpha
Enzyme 40 Synonyms
  1. PKA C-alpha
Enzyme 40 Gene Name PRKACA
Enzyme 40 Protein Sequence >cAMP-dependent protein kinase catalytic subunit alpha
MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVML
VKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMV
MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGY
IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF
ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFAT
TDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
Enzyme 40 Number of Residues 351
Enzyme 40 Molecular Weight 40589.4
Enzyme 40 Theoretical pI 9.22
Enzyme 40 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
Enzyme 40 General Function Involved in protein serine/threonine kinase activity
Enzyme 40 Specific Function Phosphorylates a large number of substrates in the cytoplasm and the nucleus
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 35479 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID P17612 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name KAPCA_HUMAN Link Image
Enzyme 40 PDB ID 1CTP Link Image
Enzyme 40 PDB File Show
Enzyme 40 3D Structure
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >1056 bp
ATGGGCAACGCCGCCGCCGCCAAGAAGGGCAGCGAGCAGGAGAGCGTGAAAGAATTCTTA
GCCAAAGCCAAAGAAGATTTTCTTAAAAAATGGGAAAGTCCCGCTCAGAACACAGCCCAC
TTGGATCAGTTTGAACGAATCAAGACCCTCGGCACGGGCTCCTTCGGGCGGGTGATGCTG
GTGAAACACAAGGAGACCGGGAACCACTATGCCATGAAGATCCTCGACAAACAGAAGGTG
GTGAAACTGAAACAGATCGAACACACCCTGAATGAAAAGCGCATCCTGCAAGCTGTCAAC
TTTCCGTTCCTCGTCAAACTCGAGTTCTCCTTCAAGGACAACTCAAACTTATACATGGTC
ATGGAGTACGTGCCCGGCGGGGAGATGTTCTCACACCTACGGCGGATCGGAAGGTTCAGT
GAGCCCCATGCCCGTTTCTACGCGGCCCAGATCGTCCTGACCTTTGAGTATCTGCACTCG
CTGGATCTCATCTACAGGGACCTGAAGCCGGAGAATCTGCTCATTGACCAGCAGGGCTAC
ATTCAGGTGACAGACTTCGGTTTCGCCAAGCGCGTGAAGGGCCGCACTTGGACCTTGTGC
GGCACCCCTGAGTACCTGGCCCCTGAGATTATCCTGAGCAAAGGCTACAACAAGGCCGTG
GACTGGTGGGCCCTGGGGGTTCTTATCTATGAAATGGCCGCTGGCTACCCGCCCTTCTTC
GCAGACCAGCCCATCCAGATCTATGAGAAGATCGTCTCTGGGAAGGTGCGCTTCCCTTCC
CACTTCAGCTCTGACTTGAAGGACCTGCTGCGGAACCTCCTGCAGGTAGATCTCACCAAG
CGCTTTGGGAACCTCAAGAATGGGGTCAACGATATCAAGAACCACAAGTGGTTTGCCACA
ACTGACTGGATTGCCATCTACCAGAGGAAGGTGGAAGCTCCCTTCATACCAAAGTTTAAA
GGCCCTGGGGATACGAGTAACTTTGACGACTATGAGGAAGAAGAAATCCGGGTCTCCATC
AATGAGAAGTGTGGCAAGGAGTTTTCTGAGTTTTAG
Enzyme 40 GenBank Gene ID X07767 Link Image
Enzyme 40 GeneCard ID PRKACA Link Image
Enzyme 40 GenAtlas ID PRKACA Link Image
Enzyme 40 HGNC ID HGNC:9380 Link Image
Enzyme 40 Chromosome Location 1
Enzyme 40 Locus 19p13.1
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Maldonado F, Hanks SK: A cDNA clone encoding human cAMP-dependent protein kinase catalytic subunit C alpha. Nucleic Acids Res. 1988 Aug 25;16(16):8189-90. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Agustin JT, Wilkerson CG, Witman GB: The unique catalytic subunit of sperm cAMP-dependent protein kinase is the product of an alternative Calpha mRNA expressed specifically in spermatogenic cells. Mol Biol Cell. 2000 Sep;11(9):3031-44. [PubMed Link Image]
  5. Desseyn JL, Burton KA, McKnight GS: Expression of a nonmyristylated variant of the catalytic subunit of protein kinase A during male germ-cell development. Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6433-8. [PubMed Link Image]
  6. Ficarro S, Chertihin O, Westbrook VA, White F, Jayes F, Kalab P, Marto JA, Shabanowitz J, Herr JC, Hunt DF, Visconti PE: Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation. J Biol Chem. 2003 Mar 28;278(13):11579-89. Epub 2002 Dec 30. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed Link Image]
  9. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  10. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  12. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 6695
Enzyme 41 Name Serine/threonine-protein kinase PRKY
Enzyme 41 Synonyms Not Available
Enzyme 41 Gene Name PRKY
Enzyme 41 Protein Sequence >Serine/threonine-protein kinase PRKY
MEAPGPAQAAAAESNSREVTEDAADWAPALCPSPEARSPEAPAYRLQDCDALVTMGTGTF
GRVHLVKEKTAKHFFALKVMSIPDVIRRKQEQHVHNEKSVLKEVSHPFLIRLFWTWHEER
FLYMLMEYVPGGELFSYLRNRGHFSSTTGLFYSAEIICAIEYLHSKEIVYRDLKPENILL
DRDGHIKLTDFGFAKKLVDRTWTLCGTPEYLAPEVIQSKGHGRAVDWWALGILIFEMLSG
FPPFFDDNPFGIYQKILAGKLYFPRHLDFHVKTGRMM
Enzyme 41 Number of Residues 277
Enzyme 41 Molecular Weight 31708.2
Enzyme 41 Theoretical pI 6.96
Enzyme 41 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
Enzyme 41 General Function Involved in protein kinase activity
Enzyme 41 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 2696012 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID O43930 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name PRKY_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >834 bp
ATGGAGGCGCCCGGGCCGGCCCAGGCGGCCGCGGCGGAGAGCAACTCCCGAGAGGTGACG
GAGGATGCCGCCGACTGGGCGCCCGCGCTCTGCCCCAGCCCCGAGGCGCGGTCGCCGGAG
GCVCCTGCCTACCGCCTGCAGGACTGCGACGCGCTGGTCACCATGGGCACTGGGACGTTC
GGGCGGGTGCACCTGGTGAAGGAGAAGACAGCCAAGCATTTCTTCGCCCTCAAGGTGATG
AGCATTCCCGACGTCATCCGCCGGAAGCAGGAGCAGCACGTGCACAATGAGAAGTCTGTC
CTGAAGGAAGTCAGCCACCCGTTCCTCATCAGGCTGTTCTGGACGTGGCATGAGGAGCGC
TTCCTCTACATGCTCATGGAGTATGTGCCGGGTGGCGAGCTCTTCAGCTACCTGCGCAAC
CGGGGGCACTTCTCCAGCACCACGGGGCTCTTCTACTCTGCGGAGATCATCTGTGCCATT
GAGTACCTGCACTCCAAGGAGATCGTCTACAGGGATTTGAAGCCGGAGAACATCCTGCTG
GATAGGGATGGTCACATCAAGCTCACGGACTTTGGGTTTGCCAAGAAGCTGGTAGACAGG
ACTTGGACCCTCTGTGGAACACCCGAGTACCTAGCCCCCGAAGTCATTCAGAGCAAGGGC
CACGGAAGGGCCGTGGACTGGTGGGCCCTCGGCATCCTGATATTCGAGATGCTTTCGGGG
TTTCCTCCATTTTTTGATGACAACCCGTTTGGCATTTATCAGAAAATTCTTGCAGGCAAA
CTATATTTCCCCAGACATTTGGATTTCCATGTAAAAACGGGGCGAATGATGTGA
Enzyme 41 GenBank Gene ID Y15801 Link Image
Enzyme 41 GeneCard ID PRKY Link Image
Enzyme 41 GenAtlas ID PRKY Link Image
Enzyme 41 HGNC ID HGNC:9444 Link Image
Enzyme 41 Chromosome Location Not Available
Enzyme 41 Locus Not Available
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Schiebel K, Winkelmann M, Mertz A, Xu X, Page DC, Weil D, Petit C, Rappold GA: Abnormal XY interchange between a novel isolated protein kinase gene, PRKY, and its homologue, PRKX, accounts for one third of all (Y+)XX males and (Y-)XY females. Hum Mol Genet. 1997 Oct;6(11):1985-9. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Schiebel K, Mertz A, Winkelmann M, Glaser B, Schempp W, Rappold G: FISH localization of the human Y-homolog of protein kinase PRKX (PRKY) to Yp11.2 and two pseudogenes to 15q26 and Xq12-->q13. Cytogenet Cell Genet. 1997;76(1-2):49-52. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 6711
Enzyme 42 Name cAMP-dependent protein kinase catalytic subunit beta
Enzyme 42 Synonyms
  1. PKA C-beta
Enzyme 42 Gene Name PRKACB
Enzyme 42 Protein Sequence >cAMP-dependent protein kinase catalytic subunit beta
MGNAATAKKGSEVESVKEFLAKAKEDFLKKWENPTQNNAGLEDFERKKTLGTGSFGRVML
VKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVRLEYAFKDNSNLYMV
MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY
IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF
ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFAT
TDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEDIRVSITEKCAKEFGEF
Enzyme 42 Number of Residues 351
Enzyme 42 Molecular Weight 40622.4
Enzyme 42 Theoretical pI 9.19
Enzyme 42 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
Enzyme 42 General Function Involved in protein serine/threonine kinase activity
Enzyme 42 Specific Function Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 189983 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID P22694 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name KAPCB_HUMAN Link Image
Enzyme 42 PDB ID 1CTP Link Image
Enzyme 42 PDB File Show
Enzyme 42 3D Structure
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >1056 bp
ATGGGGAACGCGGCGACCGCCAAGAAAGGCAGCGAGGTGGAGAGCGTGAAAGAGTTTCTA
GCCAAAGCCAAAGAAGACTTTTTGAAAAAATGGGAGAATCCAACTCAGAATAATGCCGGA
CTTGAAGATTTTGAAAGGAAAAAAACCCTTGGAACAGGTTCATTTGGAAGAGTCATGTTG
GTAAAACACAAAGCCACTGAACAGTATTATGCCATGAAGATCTTAGATAAGCAGAAGGTT
GTTAAACTGAAGCAAATAGAGCATACTTTGAATGAGAAAAGAATATTACAGGCAGTGAAT
TTTCCTTTCCTTGTTCGACTGGAGTATGCTTTTAAGGATAATTCTAATTTATACATGGTT
ATGGAATATGTCCCTGGGGGTGAAATGTTTTCACATCTAAGAAGAATTGGAAGGTTCAGT
GAGCCCCATGCACGGTTCTATGCAGCTCAGATAGTGCTAACATTCGAGTACCTCCATTCA
CTAGACCTCATCTACAGAGATCTAAAACCTGAAAATCTCTTAATTGACCATCAAGGCTAT
ATCCAGGTCACAGACTTTGGGTTTGCCAAAAGAGTTAAAGGCAGAACTTGGACATTATGT
GGAACTCCAGAGTATTTGGCTCCAGAAATAATTCTCAGCAAGGGCTACAATAAGGCAGTG
GATTGGTGGGCATTAGGAGTGCTAATCTATGAAATGGCAGCTGGCTATCCCCCATTCTTT
GCAGACCAACCAATTCAGATTTATGAAAAGATTGTTTCTGGAAAGGTCCGATTCCCATCC
CACTTCAGTTCAGATCTCAAGGACCTTCTACGGAACCTGCTGCAGGTGGATTTGACCAAG
AGATTTGGAAATCTAAAGAATGGTGTCAGTGATATAAAAACTCACAAGTGGTTTGCCACG
ACAGATTGGATTGCTATTTACCAGAGGAAGGTTGAAGCTCCATTCATACCAAAGTTTAGA
GGCTCTGGAGATACCAGCAACTTTGATGACTATGAAGAAGAAGATATCCGTGTCTCTATA
ACAGAAAAATGTGCAAAAGAATTTGGTGAATTTTAA
Enzyme 42 GenBank Gene ID M34181 Link Image
Enzyme 42 GeneCard ID PRKACB Link Image
Enzyme 42 GenAtlas ID PRKACB Link Image
Enzyme 42 HGNC ID HGNC:9381 Link Image
Enzyme 42 Chromosome Location 1
Enzyme 42 Locus 1p36.1
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Beebe SJ, Oyen O, Sandberg M, Froysa A, Hansson V, Jahnsen T: Molecular cloning of a tissue-specific protein kinase (C gamma) from human testis--representing a third isoform for the catalytic subunit of cAMP-dependent protein kinase. Mol Endocrinol. 1990 Mar;4(3):465-75. [PubMed Link Image]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Orstavik S, Reinton N, Frengen E, Langeland BT, Jahnsen T, Skalhegg BS: Identification of novel splice variants of the human catalytic subunit Cbeta of cAMP-dependent protein kinase. Eur J Biochem. 2001 Oct;268(19):5066-73. [PubMed Link Image]
  7. Wu KJ, Mattioli M, Morse HC 3rd, Dalla-Favera R: c-MYC activates protein kinase A (PKA) by direct transcriptional activation of the PKA catalytic subunit beta (PKA-Cbeta) gene. Oncogene. 2002 Nov 7;21(51):7872-82. [PubMed Link Image]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  9. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 6787
Enzyme 43 Name Ribosomal protein S6 kinase alpha-5
Enzyme 43 Synonyms
  1. S6K-alpha-5
  2. 90 kDa ribosomal protein S6 kinase 5
  3. Nuclear mitogen- and stress-activated protein kinase 1
  4. RSK-like protein kinase
  5. RSKL
Enzyme 43 Gene Name RPS6KA5
Enzyme 43 Protein Sequence >Ribosomal protein S6 kinase alpha-5
MEEEGGSSGGAAGTSADGGDGGEQLLTVKHELRTANLTGHAEKVGIENFELLKVLGTGAY
GKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYA
FQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKL
ENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWS
LGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRLLMKDPKK
RLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYS
PAALPQSSEKLFQGYSFVAPSILFKRNAAVIDPLQFHMGVERPGVTNVARSAMMKDSPFY
QHYDLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEGHPN
IVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGV
VHRDLKPENLLFTDENDNLEIKIIDFGFARLKPPDNQPLKTPCFTLHYAAPELLNQNGYD
ESCDLWSLGVILYTMLSGQVPFQSHDRSLTCTSAVEIMKKIKKGDFSFEGEAWKNVSQEA
KDLIQGLLTVDPNKRLKMSGLRYNEWLQDGSQLSSNPLMTPDILGSSGAAVHTCVKATFH
AFNKYKREGFCLQNVDKAPLAKRRKMKKTSTSTETRSSSSESSHSSSSHSHGKTTPTKTL
QPSNPADSNNPETLFQFSDSVA
Enzyme 43 Number of Residues 802
Enzyme 43 Molecular Weight 89864.7
Enzyme 43 Theoretical pI 7.10
Enzyme 43 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • magnesium ion binding
  • metal ion binding
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular protein kinase cascade
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signal transmission
  • signal transmission via phosphorylation event
  • signaling process
Component
Enzyme 43 General Function Involved in protein serine/threonine kinase activity
Enzyme 43 Specific Function Serine/threonine kinase required for the mitogen or stress-induced phosphorylation of the transcription factors CREB (cAMP response element-binding protein) and ATF1 (activating transcription factor-1). Essential role in the control of RELA transcriptional activity in response to TNF. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and epidemal growth-factor (EGF), which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 14 (HMG-14)
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein Not Available
Enzyme 43 UniProtKB/Swiss-Prot ID O75582 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name KS6A5_HUMAN Link Image
Enzyme 43 PDB ID 1VZO Link Image
Enzyme 43 PDB File Show
Enzyme 43 3D Structure
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >2409 bp
ATGGAGGAGGAGGGTGGCAGCAGCGGCGGCGCCGCGGGGACCAGCGCGGACGGCGGCGAC
GGAGGAGAGCAGCTCCTCACTGTCAAGCACGAGCTGCGGACTGCTAATTTGACAGGACAT
GCTGAGAAGGTGGGAATAGAAAATTTTGAGCTCCTGAAGGTCCTAGGAACTGGAGCTTAT
GGAAAAGTATTTCTAGTTCGTAAAATAAGTGGCCATGATACTGGAAAGCTGTATGCCATG
AAAGTTTTGAAAAAGGCAACAATCGTTCAAAAGGCCAAAACCACAGAGCATACAAGGACA
GAACGACAAGTCCTGGAACACATTAGGCAGTCGCCATTTTTGGTAACATTACATTATGCT
TTCCAGACAGAAACCAAACTTCATCTCATTTTAGATTATATAAATGGTGGTGAACTTTTT
ACTCATCTTTCTCAAAGAGAGCGTTTCACAGAGCATGAGGTGCAGATTTATGTTGGAGAG
ATTGTGCTTGCCCTCGAACATCTCCACAAGTTGGGGATTATATATCGTGATATTAAGCTT
GAGAATATTCTACTTGATTCTAATGGCCATGTGGTGCTGACAGATTTTGGTCTGAGTAAG
GAGTTTGTGGCTGATGAAACTGAAAGAGCATATTCCTTTTGTGGAACTATTGAATACATG
GCACCAGATATTGTCAGAGGGGGAGATTCAGGACATGACAAGGCAGTTGACTGGTGGAGT
TTGGGTGTTCTAATGTATGAATTACTAACTGGAGCATCTCCTTTCACTGTTGATGGAGAA
AAAAATTCCCAAGCTGAGATATCTAGGAGAATATTAAAAAGTGAGCCTCCATATCCCCAA
GAAATGAGTGCTTTAGCGAAAGACCTAATTCAGCGTCTTTTGATGAAAGATCCCAAGAAG
AGATTGGGATGTGGTCCACGTGATGCAGATGAAATCAAAGAACATCTCTTCTTTCAGAAA
ATAAATTGGGATGATTTAGCCGCCAAAAAAGTGCCTGCACCATTTAAGCCAGTCATTCGA
GATGAATTAGATGTGAGTAACTTTGCAGAAGAGTTCACAGAAATGGATCCCACTTATTCT
CCCGCAGCCCTGCCCCAGAGTTCTGAGAAGCTGTTTCAGGGCTATTCCTTTGTTGCTCCT
TCCATCCTATTCAAGCGTAATGCAGCTGTCATAGACCCTCTTCAGTTTCACATGGGAGTT
GAACGTCCTGGAGTGACAAATGTTGCCAGGAGTGCAATGATGAAGGACTCTCCATTCTAT
CAACACTATGACCTAGATTTGAAGGACAAACCCCTGGGAGAAGGTAGTTTTTCAATTTGT
CGAAAGTGTGTGCATAAAAAAAGTAACCAAGCTTTTGCAGTCAAAATAATCAGCAAAAGG
ATGGAAGCCAATACTCAAAAGGAAATAACAGCTCTGAAACTCTGTGAAGGACACCCCAAT
ATTGTGAAGTTGCATGAAGTTTTTCATGATCAGCTTCACACGTTTCTAGTGATGGAACTT
CTGAATGGAGGAGAACTGTTTGAGCGCATTAAGAAAAAGAAGCACTTCAGTGAGACGGAA
GCCAGCTACATCATGAGGAAGCTTGTTTCAGCTGTAAGCCACATGCATGATGTTGGAGTG
GTGCACAGGGATCTGAAACCTGAGAATTTATTGTTCACCGATGAAAATGACAATTTGGAA
ATTAAAATAATTGATTTTGGATTTGCACGGCTAAAGCCACCGGATAATCAGCCCCTGAAG
ACTCCATGCTTCACCCTTCATTATGCCGCCCCAGAGCTCTTGAATCAGAACGGCTACGAT
GAGTCCTGTGACCTGTGGAGCTTGGGCGTCATTTTGTACACAATGTTGTCAGGACAGGTT
CCCTTCCAATCTCATGACCGAAGTTTGACGTGTACCAGCGCGGTGGAAATCATGAAGAAA
ATTAAAAAGGGAGATTTCTCCTTTGAAGGAGAAGCCTGGAAGAATGTATCCCAAGAGGCT
AAAGATTTGATCCAAGGACTTCTCACAGTAGATCCAAACAAAAGGCTTAAAATGTCTGGC
TTGAGGTACAATGAATGGCTACAAGATGGAAGTCAGCTGTCCTCCAATCCTCTGATGACT
CCGGATATTCTAGGATCTTCCGGAGCTGCCGTGCATACCTGTGTGAAAGCAACCTTCCAC
GCCTTTAACAAATACAAGAGAGAGGGGTTTTGCCTTCAGAATGTTGATAAGGCCCCTTTG
GCTAAGAGAAGAAAAATGAAAAAGACTAGCACCAGTACCGAGACGCGCAGCAGTTCCAGT
GAGAGTTCCCATTCTTCTTCCTCTCATTCTCACGGTAAAACTACACCCACCAAGACACTG
CAGCCCAGCAATCCTGCCGACAGCAATAACCCGGAGACCCTCTTCCAGTTCTCGGACTCA
GTAGCTTAG
Enzyme 43 GenBank Gene ID AF074393 Link Image
Enzyme 43 GeneCard ID RPS6KA5 Link Image
Enzyme 43 GenAtlas ID RPS6KA5 Link Image
Enzyme 43 HGNC ID HGNC:10434 Link Image
Enzyme 43 Chromosome Location 1
Enzyme 43 Locus 14q31-q32.1
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Deak M, Clifton AD, Lucocq LM, Alessi DR: Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. EMBO J. 1998 Aug 3;17(15):4426-41. [PubMed Link Image]
  2. New L, Zhao M, Li Y, Bassett WW, Feng Y, Ludwig S, Padova FD, Gram H, Han J: Cloning and characterization of RLPK, a novel RSK-related protein kinase. J Biol Chem. 1999 Jan 8;274(2):1026-32. [PubMed Link Image]
  3. Jiang C, Yu L, Tu Q, Zhao Y, Zhang H, Zhao S: Assignment of a member of the ribosomal protein S6 kinase family, RPS6KA5, to human chromosome 14q31-->q32.1 by radiation hybrid mapping. Cytogenet Cell Genet. 1999;87(3-4):261-2. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Wiggin GR, Soloaga A, Foster JM, Murray-Tait V, Cohen P, Arthur JS: MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts. Mol Cell Biol. 2002 Apr;22(8):2871-81. [PubMed Link Image]
  6. Vermeulen L, De Wilde G, Van Damme P, Vanden Berghe W, Haegeman G: Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1). EMBO J. 2003 Mar 17;22(6):1313-24. [PubMed Link Image]
  7. Soloaga A, Thomson S, Wiggin GR, Rampersaud N, Dyson MH, Hazzalin CA, Mahadevan LC, Arthur JS: MSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation of histone H3 and HMG-14. EMBO J. 2003 Jun 2;22(11):2788-97. [PubMed Link Image]
  8. Zhang Y, Griffin K, Mondal N, Parvin JD: Phosphorylation of histone H2A inhibits transcription on chromatin templates. J Biol Chem. 2004 May 21;279(21):21866-72. Epub 2004 Mar 9. [PubMed Link Image]
  9. McCoy CE, Campbell DG, Deak M, Bloomberg GB, Arthur JS: MSK1 activity is controlled by multiple phosphorylation sites. Biochem J. 2005 Apr 15;387(Pt 2):507-17. [PubMed Link Image]
  10. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  11. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 6794
Enzyme 44 Name Serine/threonine-protein kinase PRKX
Enzyme 44 Synonyms
  1. Protein kinase PKX1
Enzyme 44 Gene Name PRKX
Enzyme 44 Protein Sequence >Serine/threonine-protein kinase PRKX
MEAPGLAQAAAAESDSRKVAEETPDGAPALCPSPEALSPEPPVYSLQDFDTLATVGTGTF
GRVHLVKEKTAKHFFALKVMSIPDVIRLKQEQHVHNEKSVLKEVSHPFLIRLFWTWHDER
FLYMLMEYVPGGELFSYLRNRGRFSSTTGLFYSAEIICAIEYLHSKEIVYRDLKPENILL
DRDGHIKLTDFGFAKKLVDRTWTLCGTPEYLAPEVIQSKGHGRAVDWWALGILIFEMLSG
FPPFFDDNPFGIYQKILAGKIDFPRHLDFHVKDLIKKLLVVDRTRRLGNMKNGANDVKHH
RWFRSVDWEAVPQRKLKPPIVPKIAGDGDTSNFETYPENDWDTAAPVPQKDLEIFKNF
Enzyme 44 Number of Residues 358
Enzyme 44 Molecular Weight 40895.5
Enzyme 44 Theoretical pI 6.85
Enzyme 44 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
Enzyme 44 General Function Involved in ATP binding
Enzyme 44 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 26996827 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID P51817 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name PRKX_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >1077 bp
ATGGAGGCGCCCGGGCTGGCCCAGGCGGCCGCGGCGGAGAGCGACTCCCGCAAGGTGGCG
GAGGAGACCCCCGACGGGGCGCCCGCGCTCTGCCCCAGCCCTGAGGCGCTGTCGCCGGAG
CCGCCTGTGTACAGCCTGCAGGACTTTGACACGCTGGCCACCGTGGGCACTGGGACGTTC
GGGCGGGTGCACCTGGTGAAGGAGAAGACAGCCAAGCATTTCTTCGCCCTCAAGGTGATG
AGCATTCCTGACGTCATCCGCCTAAAGCAGGAGCAACACGTACACAATGAGAAGTCTGTC
CTGAAGGAAGTCAGCCACCCGTTCCTCATCAGGCTGTTCTGGACGTGGCATGACGAGCGC
TTCCTCTACATGCTCATGGAGTACGTGCCGGGCGGCGAGCTCTTCAGCTACCTGCGCAAC
CGGGGGCGCTTCTCCAGCACCACGGGGCTCTTCTACTCTGCAGAGATCATCTGTGCCATC
GAGTACCTGCACTCCAAAGAGATCGTCTACAGGGACTTGAAGCCAGAGAACATCCTGCTG
GATAGGGATGGCCACATTAAGCTCACGGACTTTGGGTTCGCCAAGAAGCTGGTAGACAGG
ACTTGGACCCTCTGTGGAACACCCGAGTACCTAGCCCCCGAAGTCATTCAGAGCAAGGGC
CACGGAAGGGCCGTGGACTGGTGGGCCCTCGGCATCCTGATATTCGAGATGCTTTCGGGG
TTTCCTCCGTTTTTTGATGACAACCCGTTTGGCATTTATCAGAAAATTCTTGCAGGCAAA
ATAGATTTCCCCAGACATTTGGATTTCCATGTAAAAGACCTCATTAAGAAACTGCTCGTG
GTTGACAGAACAAGGCGATTAGGAAACATGAAGAACGGGGCGAATGATGTGAAGCATCAT
CGGTGGTTCCGCTCCGTGGACTGGGAAGCTGTTCCGCAGAGAAAACTGAAGCCTCCCATC
GTGCCCAAGATAGCTGGTGACGGCGACACTTCCAACTTCGAAACTTACCCTGAGAATGAC
TGGGACACAGCCGCGCCCGTGCCGCAGAAGGATTTAGAAATCTTCAAGAATTTCTGA
Enzyme 44 GenBank Gene ID BC041073 Link Image
Enzyme 44 GeneCard ID PRKX Link Image
Enzyme 44 GenAtlas ID Not Available
Enzyme 44 HGNC ID Not Available
Enzyme 44 Chromosome Location Not Available
Enzyme 44 Locus Not Available
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References
  1. Klink A, Schiebel K, Winkelmann M, Rao E, Horsthemke B, Ludecke HJ, Claussen U, Scherer G, Rappold G: The human protein kinase gene PKX1 on Xp22.3 displays Xp/Yp homology and is a site of chromosomal instability. Hum Mol Genet. 1995 May;4(5):869-78. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Schiebel K, Winkelmann M, Mertz A, Xu X, Page DC, Weil D, Petit C, Rappold GA: Abnormal XY interchange between a novel isolated protein kinase gene, PRKY, and its homologue, PRKX, accounts for one third of all (Y+)XX males and (Y-)XY females. Hum Mol Genet. 1997 Oct;6(11):1985-9. [PubMed Link Image]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 6826
Enzyme 45 Name Serine/threonine-protein kinase 11
Enzyme 45 Synonyms
  1. Renal carcinoma antigen NY-REN-19
  2. Serine/threonine-protein kinase LKB1
Enzyme 45 Gene Name STK11
Enzyme 45 Protein Sequence >Serine/threonine-protein kinase 11
MEVVDPQQLGMFTEGELMSVGMDTFIHRIDSTEVIYQPRRKRAKLIGKYLMGDLLGEGSY
GKVKEVLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRHKNVIQLVDVLYNE
EKQKMYMVMEYCVCGMQEMLDSVPEKRFPVCQAHGYFCQLIDGLEYLHSQGIVHKDIKPG
NLLLTTGGTLKISDLGVAEALHPFAADDTCRTSQGSPAFQPPEIANGLDTFSGFKVDIWS
AGVTLYNITTGLYPFEGDNIYKLFENIGKGSYAIPGDCGPPLSDLLKGMLEYEPAKRFSI
RQIRQHSWFRKKHPPAEAPVPIPPSPDTKDRWRSMTVVPYLEDLHGADEDEDLFDIEDDI
IYTQDFTVPGQVPEEEASHNGQRRGLPKAVCMNGTEAAQLSTKSRAEGRAPNPARKACSA
SSKIRRLSACKQQ
Enzyme 45 Number of Residues 433
Enzyme 45 Molecular Weight 48635.4
Enzyme 45 Theoretical pI 7.47
Enzyme 45 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 45 General Function Involved in protein kinase activity
Enzyme 45 Specific Function Essential role in G1 cell cycle arrest. Phosphorylates and activates members of the AMPK-related subfamily of protein kinases. Tumor suppressor
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 2754827 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID Q15831 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name STK11_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >1302 bp
ATGGAGGTGGTGGACCCGCAGCAGCTGGGCATGTTCACGGAGGGCGAGCTGATGTCGGTG
GGTATGGACACGTTCATCCACCGCATCGACTCCACCGAGGTCATCTACCAGCCGCGCCGC
AAGCGGGCCAAGCTCATCGGCAAGTACCTGATGGGGGACCTGCTGGGGGAAGGCTCTTAC
GGCAAGGTGAAGGAGGTGCTGGACTCGGAGACGCTGTGCAGGAGGGCCGTCAAGATCCTC
AAGAAGAAGAAGTTGCGAAGGATCCCCAACGGGGAGGCCAACGTGAAGAAGGAAATTCAA
CTACTGAGGAGGTTACGGCACAAAAATGTCATCCAGCTGGTGGATGTGTTATACAACGAA
GAGAAGCAGAAAATGTATATGGTGATGGAGTACTGCGTGTGTGGCATGCAGGAAATGCTG
GACAGCGTGCCGGAGAAGCGTTTCCCAGTGTGCCAGGCCCACGGGTACTTCTGTCAGCTG
ATTGACGGCCTGGAGTACCTGCATAGCCAGGGCATTGTGCACAAGGACATCAAGCCGGGG
AACCTGCTGCTCACCACCGGTGGCACCCTCAAAATCTCCGACCTGGGCGTGGCCGAGGCA
CTGCACCCGTTCGCGGCGGACGACACCTGCCGGACCAGCCAGGGCTCCCCGGCTTTCCAG
CCGCCCGAGATTGCCAACGGCCTGGACACCTTCTCCGGCTTCAAGGTGGACATCTGGTCG
GCTGGGGTCACCCTCTACAACATCACCACGGGTCTGTACCCCTTCGAAGGGGACAACATC
TACAAGTTGTTTGAGAACATCGGGAAGGGGAGCTACGCCATCCCGGGCGACTGTGGCCCC
CCGCTCTCTGACCTGCTGAAAGGGATGCTTGAGTACGAACCGGCCAAGAGGTTCTCCATC
CGGCAGATCCGGCAGCACAGCTGGTTCCGGAAGAAACATCCTCCGGCTGAAGCACCAGTG
CCCATCCCACCGAGCCCAGACACCAAGGACCGGTGGCGCAGCATGACTGTGGTGCCGTAC
TTGGAGGACCTGCACGGCGCGGACGAGGACGAGGACCTCTTCGACATCGAGGATGACATC
ATCTACACTCAGGACTTCACGGTGCCCGGACAGGTCCCAGAAGAGGAGGCCAGTCACAAT
GGACAGCGCCGGGGCCTCCCCAAGGCCGTGTGTATGAACGGCACAGAGGCGGCGCAGCTG
AGCACCAAATCCAGGGCGGAGGGCCGGGCCCCCAACCCTGCCCGCAAGGCCTGCTCCGCC
AGCAGCAAGATCCGCCGGCTGTCGGCCTGCAAGCAGCAGTGA
Enzyme 45 GenBank Gene ID AF035625 Link Image
Enzyme 45 GeneCard ID STK11 Link Image
Enzyme 45 GenAtlas ID STK11 Link Image
Enzyme 45 HGNC ID HGNC:11389 Link Image
Enzyme 45 Chromosome Location 1
Enzyme 45 Locus 19p13.3
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Jenne DE, Reimann H, Nezu J, Friedel W, Loff S, Jeschke R, Muller O, Back W, Zimmer M: Peutz-Jeghers syndrome is caused by mutations in a novel serine threonine kinase. Nat Genet. 1998 Jan;18(1):38-43. [PubMed Link Image]
  2. Bignell GR, Barfoot R, Seal S, Collins N, Warren W, Stratton MR: Low frequency of somatic mutations in the LKB1/Peutz-Jeghers syndrome gene in sporadic breast cancer. Cancer Res. 1998 Apr 1;58(7):1384-6. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed Link Image]
  6. Smith DP, Rayter SI, Niederlander C, Spicer J, Jones CM, Ashworth A: LIP1, a cytoplasmic protein functionally linked to the Peutz-Jeghers syndrome kinase LKB1. Hum Mol Genet. 2001 Dec 1;10(25):2869-77. [PubMed Link Image]
  7. Baas AF, Boudeau J, Sapkota GP, Smit L, Medema R, Morrice NA, Alessi DR, Clevers HC: Activation of the tumour suppressor kinase LKB1 by the STE20-like pseudokinase STRAD. EMBO J. 2003 Jun 16;22(12):3062-72. [PubMed Link Image]
  8. Boudeau J, Baas AF, Deak M, Morrice NA, Kieloch A, Schutkowski M, Prescott AR, Clevers HC, Alessi DR: MO25alpha/beta interact with STRADalpha/beta enhancing their ability to bind, activate and localize LKB1 in the cytoplasm. EMBO J. 2003 Oct 1;22(19):5102-14. [PubMed Link Image]
  9. Xie X, Wang Z, Chen Y: Association of LKB1 with a WD-repeat protein WDR6 is implicated in cell growth arrest and p27(Kip1) induction. Mol Cell Biochem. 2007 Jul;301(1-2):115-22. Epub 2007 Jan 10. [PubMed Link Image]
  10. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  12. Avizienyte E, Roth S, Loukola A, Hemminki A, Lothe RA, Stenwig AE, Fossa SD, Salovaara R, Aaltonen LA: Somatic mutations in LKB1 are rare in sporadic colorectal and testicular tumors. Cancer Res. 1998 May 15;58(10):2087-90. [PubMed Link Image]
  13. Nakagawa H, Koyama K, Miyoshi Y, Ando H, Baba S, Watatani M, Yasutomi M, Matsuura N, Monden M, Nakamura Y: Nine novel germline mutations of STK11 in ten families with Peutz-Jeghers syndrome. Hum Genet. 1998 Aug;103(2):168-72. [PubMed Link Image]
  14. Hemminki A, Markie D, Tomlinson I, Avizienyte E, Roth S, Loukola A, Bignell G, Warren W, Aminoff M, Hoglund P, Jarvinen H, Kristo P, Pelin K, Ridanpaa M, Salovaara R, Toro T, Bodmer W, Olschwang S, Olsen AS, Stratton MR, de la Chapelle A, Aaltonen LA: A serine/threonine kinase gene defective in Peutz-Jeghers syndrome. Nature. 1998 Jan 8;391(6663):184-7. [PubMed Link Image]
  15. Westerman AM, Entius MM, Boor PP, Koole R, de Baar E, Offerhaus GJ, Lubinski J, Lindhout D, Halley DJ, de Rooij FW, Wilson JH: Novel mutations in the LKB1/STK11 gene in Dutch Peutz-Jeghers families. Hum Mutat. 1999;13(6):476-81. [PubMed Link Image]
  16. Ylikorkala A, Avizienyte E, Tomlinson IP, Tiainen M, Roth S, Loukola A, Hemminki A, Johansson M, Sistonen P, Markie D, Neale K, Phillips R, Zauber P, Twama T, Sampson J, Jarvinen H, Makela TP, Aaltonen LA: Mutations and impaired function of LKB1 in familial and non-familial Peutz-Jeghers syndrome and a sporadic testicular cancer. Hum Mol Genet. 1999 Jan;8(1):45-51. [PubMed Link Image]
  17. Rowan A, Bataille V, MacKie R, Healy E, Bicknell D, Bodmer W, Tomlinson I: Somatic mutations in the Peutz-Jeghers (LKB1/STKII) gene in sporadic malignant melanomas. J Invest Dermatol. 1999 Apr;112(4):509-11. [PubMed Link Image]
  18. Guldberg P, thor Straten P, Ahrenkiel V, Seremet T, Kirkin AF, Zeuthen J: Somatic mutation of the Peutz-Jeghers syndrome gene, LKB1/STK11, in malignant melanoma. Oncogene. 1999 Mar 4;18(9):1777-80. [PubMed Link Image]
  19. Scott RJ, Crooks R, Meldrum CJ, Thomas L, Smith CJ, Mowat D, McPhillips M, Spigelman AD: Mutation analysis of the STK11/LKB1 gene and clinical characteristics of an Australian series of Peutz-Jeghers syndrome patients. Clin Genet. 2002 Oct;62(4):282-7. [PubMed Link Image]
  20. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 6941
Enzyme 46 Name ATP-binding cassette sub-family A member 1
Enzyme 46 Synonyms
  1. ATP-binding cassette transporter 1
  2. ABC-1
  3. ATP-binding cassette 1
  4. Cholesterol efflux regulatory protein
Enzyme 46 Gene Name ABCA1
Enzyme 46 Protein Sequence >ATP-binding cassette sub-family A member 1
MACWPQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKA
MPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVARLFSDARRLLLYSQKDT
SMKDMRKVLRTLQQIKKSSSNLKLQDFLVDNETFSGFLYHNLSLPKSTVDKMLRADVILH
KVFLQGYQLHLTSLCNGSKSEEMIQLGDQEVSELCGLPREKLAAAERVLRSNMDILKPIL
RTLNSTSPFPSKELAEATKTLLHSLGTLAQELFSMRSWSDMRQEVMFLTNVNSSSSSTQI
YQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDAETFYDNSTTPYCNDLMK
NLESSPLSRIIWKALKPLLVGKILYTPDTPATRQVMAEVNKTFQELAVFHDLEGMWEELS
PKIWTFMENSQEMDLVRMLLDSRDNDHFWEQQLDGLDWTAQDIVAFLAKHPEDVQSSNGS
VYTWREAFNETNQAIRTISRFMECVNLNKLEPIATEVWLINKSMELLDERKFWAGIVFTG
ITPGSIELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVV
EQAIIRVLTGTEKKTGVYMQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIV
YEKEARLKETMRIMGLDNSILWFSWFISSLIPLLVSAGLLVVILKLGNLLPYSDPSVVFV
FLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQDYVGFTLKIFAS
LLSPVAFGFGCEYFALFEEQGIGVQWDNLFESPVEEDGFNLTTSVSMMLFDTFLYGVMTW
YIEAVFPGQYGIPRPWYFPCTKSYWFGEESDEKSHPGSNQKRISEICMEEEPTHLKLGVS
IQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIL
GKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVG
LPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ
GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLS
SCRNSSSTVSYLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVSEARLVEDI
GHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAE
TSDGTLPARRNRRAFGDKQSCLRPFTEDDAADPNDSDIDPESRETDLLSGMDGKGSYQVK
GWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLELQ
PWMYNEQYTFVSNDAPEDTGTLELLNALTKDPGFGTRCMEGNPIPDTPCQAGEEEWTTAP
VPQTIMDLFQNGNWTMQNPSPACQCSSDKIKKMLPVCPPGAGGLPPPQRKQNTADILQDL
TGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGVSNTQALPPSQEVNDAIKQMKK
HLKLAKDSSADRFLNSLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQK
GENPSHYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQER
VSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLAL
LLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTDNKLNNIN
DILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEG
VVFFLITVLIQYRFFIRPRPVNAKLSPLNDEDEDVRRERQRILDGGGQNDILEIKELTKI
YRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSN
IHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEK
YAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLT
SHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKPVQDFFG
LAFPGSVLKEKHRNMLQYQLPSSLSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNF
AKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV
Enzyme 46 Number of Residues 2261
Enzyme 46 Molecular Weight 254299.9
Enzyme 46 Theoretical pI 6.84
Enzyme 46 GO Classification
Function
  • ATP binding
  • ATPase activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside binding
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleoside binding
  • pyrophosphatase activity
Process
Component
Enzyme 46 General Function Involved in ATP binding
Enzyme 46 Specific Function cAMP-dependent and sulfonylurea-sensitive anion transporter. Key gatekeeper influencing intracellular cholesterol transport
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • 22-42 640-660 683-703 716-736 745-765 777-797 827-847 1041-1057 1351-1371 1657-1677 1703-1723 1735-1755 1768-1788 1802-1822 1852-1872
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 9755159 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID O95477 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name ABCA1_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >6786 bp
ATGGCTTGTTGGCCTCAGCTGAGGTTGCTGCTGTGGAAGAACCTCACTTTCAGAAGAAGA
CAAACATGTCAGCTGTTACTGGAAGTGGCCTGGCCTCTATTTATCTTCCTGATCCTGATC
TCTGTTCGGCTGAGCTACCCACCCTATGAACAACATGAATGCCATTTTCCAAATAAAGCC
ATGCCCTCTGCAGGAACACTTCCTTGGGTTCAGGGGATTATCTGTAATGCCAACAACCCC
TGTTTCCGTTACCCGACTCCTGGGGAGGCTCCCGGAGTTGTTGGAAACTTTAACAAATCC
ATTGTGGCTCGCCTGTTCTCAGATGCTCGGAGGCTTCTTTTATACAGCCAGAAAGACACC
AGCATGAAGGACATGCGCAAAGTTCTGAGAACATTACAGCAGATCAAGAAATCCAGCTCA
AACTTGAAGCTTCAAGATTTCCTGGTGGACAATGAAACCTTCTCTGGGTTCCTATATCAC
AACCTCTCTCTCCCAAAGTCTACTGTGGACAAGATGCTGAGGGCTGATGTCATTCTCCAC
AAGGTATTTTTGCAAGGCTACCAGTTACATTTGACAAGTCTGTGCAATGGATCAAAATCA
GAAGAGATGATTCAACTTGGTGACCAAGAAGTTTCTGAGCTTTGTGGCCTACCAAAGGAG
AAACTGGCTGCAGCAGAGCGAGTACTTCGTTCCAACATGGACATCCTGAAGCCAATCCTG
AGAACACTAAACTCTACATCTCCCTTCCCGAGCAAGGAGCTGGCTGAAGCCACAAAAACA
TTGCTGCATAGTCTTGGGACTCTGGCCCAGGAGCTGTTCAGCATGAGAAGCTGGAGTGAC
ATGCGACAGGAGGTGATGTTTCTGACCAATGTGAACAGCTCCAGCTCCTCCACCCAAATC
TACCAGGCTGTGTCTCGTATTGTCTGCGGGCATCCCGAGGGAGGGGGGCTGAAGATCAAG
TCTCTCAACTGGTATGAGGACAACAACTACAAAGCCCTCTTTGGAGGCAATGGCACTGAG
GAAGATGCTGAAACCTTCTATGACAACTCTACAACTCCTTACTGCAATGATTTGATGAAG
AATTTGGAGTCTAGTCCTCTTTCCCGCATTATCTGGAAAGCTCTGAAGCCGCTGCTCGTT
GGGAAGATCCTGTATACACCTGACACTCCAGCCACAAGGCAGGTCATGGCTGAGGTGAAC
AAGACCTTCCAGGAACTGGCTGTGTTCCATGATCTGGAAGGCATGTGGGAGGAACTCAGC
CCCAAGATCTGGACCTTCATGGAGAACAGCCAAGAAATGGACCTTGTCCGGATGCTGTTG
GACAGCAGGGACAATGACCACTTTTGGGAACAGCAGTTGGATGGCTTAGATTGGACAGCC
CAAGACATCGTGGCGTTTTTGGCCAAGCACCCAGAGGATGTCCAGTCCAGTAATGGTTCT
GTGTACACCTGGAGAGAAGCTTTCAACGAGACTAACCAGGCAATCCGGACCATATCTCGC
TTCATGGAGTGTGTCAACCTGAACAAGCTAGAACCCATAGCAACAGAAGTCTGGCTCATC
AACAAGTCCATGGAGCTGCTGGATGAGAGGAAGTTCTGGGCTGGTATTGTGTTCACTGGA
ATTACTCCAGGCAGCATTGAGCTGCCCCATCATGTCAAGTACAAGATCCGAATGGACATT
GACAATGTGGAGAGGACAAATAAAATCAAGGATGGGTACTGGGACCCTGGTCCTCGAGCT
GACCCCTTTGAGGACATGCGGTACGTCTGGGGGGGCTTCGCCTACTTGCAGGATGTGGTG
GAGCAGGCAATCATCAGGGTGCTGACGGGCACCGAGAAGAAAACTGGTGTCTATATGCAA
CAGATGCCCTATCCCTGTTACGTTGATGACATCTTTCTGCGGGTGATGAGCCGGTCAATG
CCCCTCTTCATGACGCTGGCCTGGATTTACTCAGTGGCTGTGATCATCAAGGGCATCGTG
TATGAGAAGGAGGCACGGCTGAAAGAGACCATGCGGATCATGGGCCTGGACAACAGCATA
CTCTGGTTTAGCTGGTTCATTAGTAGCCTCATTCCTCTTCTTGTGAGCGCTGGCCTGCTA
GTGGTCATCCTGAAGTTAGGAAACCTGCTGCCCTACAGTGATCCCAGCGTGGTGTTTGTC
TTCCTGTCCGTGTTTGCTGTGGTGACAATCCTGCAGTGCTTCCTGATTAGCACACTCTTC
TCCAGAGCCAACCTGGCAGCAGCCTGTGGGGGCATCATCTACTTCACGCTGTACCTGCCC
TACGTCCTGTGTGTGGCATGGCAGGACTACGTGGGCTTCACACTCAAGATCTTCGCTAGC
CTGCTGTCTCCTGTGGCTTTTGGGTTTGGCTGTGAGTACTTTGCCCTTTTTGAGGAGCAG
GGCATTGGAGTGCAGTGGGACAACCTGTTTGAGAGTCCTGTGGAGGAAGATGGCTTCAAT
CTCACCACTTCGATCTCCATGATGCTGTTTGACACCTTCCTCTATGGGGTGATGACCTGG
TACATTGAGGCTGTCTTTCCAGGCCAGTACGGAATTCCCAGGCCCTGGTATTTTCCTTGC
ACCAAGTCCTACTGGTTTGGCGAGGAAAGTGATGAGAAGAGCCACCCTGGTTCCAACCAG
AAGAGAATGTCAGAAATCTGCATGGAGGAGGAACCCACCCACTTGAAGCTGGGCGTGTCC
ATTCAGAACCTGGTAAAAGTCTACCGAGATGGGATGAAGGTGGCTGTCGATGGCCTGGCA
CTGAATTTTTATGAGGGCCAGATCACCTCCTTCCTGGGCCACAATGGAGCGGGGAAGACG
ACCACCATGTCAATCCTGACCGGGTTGTTCCCCCCGACCTCGGGCACCGCCTACATCCTG
GGAAAAGACATTCGCTCTGAGATGAGCACCATCCGGCAGAACCTGGGGGTCTGTCCCCAG
CATAACGTGCTGTTTGACATGCTGACTGTCGAAGAACACATCTGGTTCTATGCCCGCTTG
AAAGGGCTCTCTGAGAAGCACGTGAAGGCGGAGATGGAGCAGATGGCCCTGGATGTTGGT
TTGCCATCAAGCAAGCTGAAAAGCAAAACAAGCCAGCTGTCAGGTGGAATGCAGAGAAAG
CTATCTGTGGCCTTGGCCTTTGTCGGGGGATCTAAGGTTGTCATTCTGGATGAACCCACA
GCTGGTGTGGACCCTTACTCCCGCAGGGGAATATGGGAGCTGCTGCTGAAATACCGACAA
GGCCGCACCATTATTCTCTCTACACACCACATGGATGAAGCGGACGTCCTGGGGGACAGG
ATTGCCATCATCTCCCATGGGAAGCTGTGCTGTGTGGGCTCCTCCCTGTTTCTGAAGAAC
CAGCTGGGAACAGGCTACTACCTGACCTTGGTCAAGAAAGATGTGGAATCCTCCCTCAGT
TCCTGCAGAAACAGTAGTAGCACTGTGTCATACCTGAAAAAGGAGGACAGTGTTTCTCAG
AGCAGTTCTGATGCTGGCCTGGGCAGCGACCATGAGAGTGACACGCTGACCATCGATGTC
TCTGCTATCTCCAACCTCATCAGGAAGCATGTGTCTGAAGCCCGGCTGGTGGAAGACATA
GGGCATGAGCTGACCTATGTGCTGCCATATGAAGCTGCTAAGGAGGGAGCCTTTGTGGAA
CTCTTTCATGAGATTGATGACCGGCTCTCAGACCTGGGCATTTCTAGTTATGGCATCTCA
GAGACGACCCTGGAAGAAATATTCCTCAAGGTGGCCGAAGAGAGTGGGGTGGATGCTGAG
ACCTCAGATGGTACCTTGCCAGCAAGACGAAACAGGCGGGCCTTCGGGGACAAGCAGAGC
TGTCTTCGCCCGTTCACTGAAGATGATGCTGCTGATCCAAATGATTCTGACATAGACCCA
GAATCCAGAGAGACAGACTTGCTCAGTGGGATGGATGGCAAAGGGTCCTACCAGGTGAAA
GGCTGGAAACTTACACAGCAACAGTTTGTGGCCCTTTTGTGGAAGAGACTGCTAATTGCC
AGACGGAGTCGGAAAGGATTTTTTGCTCAGATTGTCTTGCCAGCTGTGTTTGTCTGCATT
GCCCTTGTGTTCAGCCTGATCGTGCCACCCTTTGGCAAGTACCCCAGCCTGGAACTTCAG
CCCTGGATGTACAACGAACAGTACACATTTGTCAGCAATGATGCTCCTGAGGACACGGGA
ACCCTGGAACTCTTAAACGCCCTCACCAAAGACCCTGGCTTCGGGACCCGCTGTATGGAA
GGAAACCCAATCCCAGACACGCCCTGCCAGGCAGGGGAGGAAGAGTGGACCACTGCCCCA
GTTCCCCAGACCATCATGGACCTCTTCCAGAATGGGAACTGGACAATGCAGAACCCTTCA
CCTGCATGCCAGTGTAGCAGCGACAAAATCAAGAAGATGCTGCCTGTGTGTCCCCCAGGG
GCAGGGGGGCTGCCTCCTCCACAAAGAAAACAAAACACTGCAGATATCCTTCAGGACCTG
ACAGGAAGAAACATTTCGGATTATCTGGTGAAGACGTATGTGCAGATCATAGCCAAAAGC
TTAAAGAACAAGATCTGGGTGAATGAGTTTAGGTATGGCGGCTTTTCCCTGGGTGTCAGT
AATACTCAAGCACTTCCTCCGAGTCAAGAAGTTAATGATGCCATCAAACAAATGAAGAAA
CACCTAAAGCTGGCCAAGGACAGTTCTGCAGATCGATTTCTCAACAGCTTGGGAAGATTT
ATGACAGGACTGGACACCAGAAATAATGTCAAGGTGTGGTTCAATAACAAGGGCTGGCAT
GCAATCAGCTCTTTCCTGAATGTCATCAACAATGCCATTCTCCGGGCCAACCTGCAAAAG
GGAGAGAACCCTAGCCATTATGGAATTACTGCTTTCAATCATCCCCTGAATCTCACCAAG
CAGCAGCTCTCAGAGGTGGCTCTGATGACCACATCAGTGGATGTCCTTGTGTCCATCTGT
GTCATCTTTGCAATGTCCTTCGTCCCAGCCAGCTTTGTCGTATTCCTGATCCAGGAGCGG
GTCAGCAAAGCAAAACACCTGCAGTTCATCAGTGGAGTGAAGCCTGTCATCTACTGGCTC
TCTAATTTTGTCTGGGATATGTGCAATTACGTTGTCCCTGCCACACTGGTCATTATCATC
TTCATCTGCTTCCAGCAGAAGTCCTATGTGTCCTCCACCAATCTGCCTGTGCTAGCCCTT
CTACTTTTGCTGTATGGGTGGTCAATCACACCTCTCATGTACCCAGCCTCCTTTGTGTTC
AAGATCCCCAGCACAGCCTATGTGGTGCTCACCAGCGTGAACCTCTTCATTGGCATTAAT
GGCAGCGTGGCCACCTTTGTGCTGGAGCTGTTCACCGACAATAAGCTGAATAATATCAAT
GATATCCTGAAGTCCGTGTTCTTGATCTTCCCACATTTTTGCCTGGGACGAGGGCTCATC
GACATGGTGAAAAACCAGGCAATGGCTGATGCCCTGGAAAGGTTTGGGGAGAATCGCTTT
GTGTCACCATTATCTTGGGACTTGGTGGGACGAAACCTCTTCGCCATGGCCGTGGAAGGG
GTGGTGTTCTTCCTCATTACTGTTCTGATCCAGTACAGATTCTTCATCAGGCCCAGACCT
GTAAATGCAAAGCTATCTCCTCTGAATGATGAAGATGAAGATGTGAGGCGGGAAAGACAG
AGAATTCTTGATGGTGGAGGCCAGAATGACATCTTAGAAATCAAGGAGTTGACGAAGATA
TATAGAAGGAAGCGGAAGCCTGCTGTTGACAGGATTTGCGTGGGCATTCCTCCTGGTGAG
TGCTTTGGGCTCCTGGGAGTTAATGGGGCTGGAAAATCATCAACTTTCAAGATGTTAACA
GGAGATACCACTGTTACCAGAGGAGATGCTTTCCTTAACAAAAATAGTATCTTATCAAAC
ATCCATGAAGTACATCAGAACATGGGCTACTGCCCTCAGTTTGATGCCATCACAGAGCTG
TTGACTGGGAGAGAACACGTGGAGTTCTTTGCCCTTTTGAGAGGAGTCCCAGAGAAAGAA
GTTGGCAAGGTTGGTGAGTGGGCGATTCGGAAACTGGGCCTCGTGAAGTATGGAGAAAAA
TATGCTGGTAACTATAGTGGAGGCAACAAACGCAAGCTCTCTACAGCCATGGCTTTGATC
GGCGGGCCTCCTGTGGTGTTTCTGGATGAACCCACCACAGGCATGGATCCCAAAGCCCGG
CGGTTCTTGTGGAATTGTGCCCTAAGTGTTGTCAAGGAGGGGAGATCAGTAGTGCTTACA
TCTCATAGTATGGAAGAATGTGAAGCTCTTTGCACTAGGATGGCAATCATGGTCAATGGA
AGGTTCAGGTGCCTTGGCAGTGTCCAGCATCTAAAAAATAGGTTTGGAGATGGTTATACA
ATAGTTGTACGAATAGCAGGGTCCAACCCGGACCTGAAGCCTGTCCAGGATTTCTTTGGA
CTTGCATTTCCTGGAAGTGTTCTAAAAGAGAAACACCGGAACATGCTACAATACCAGCTT
CCATCTTCATTATCTTCTCTGGCCAGGATATTCAGCATCCTCTCCCAGAGCAAAAAGCGA
CTCCACATAGAAGACTACTCTGTTTCTCAGACAACACTTGACCAAGTATTTGTGAACTTT
GCCAAGGACCAAAGTGATGATGACCACTTAAAAGACCTCTCATTACACAAAAACCAGACA
GTAGTGGACGTTGCAGTTCTCACATCTTTTCTACAGGATGAGAAAGTGAAAGAAAGCTAT
GTATGA
Enzyme 46 GenBank Gene ID AF285167 Link Image
Enzyme 46 GeneCard ID ABCA1 Link Image
Enzyme 46 GenAtlas ID ABCA1 Link Image
Enzyme 46 HGNC ID HGNC:29 Link Image
Enzyme 46 Chromosome Location 9
Enzyme 46 Locus 9q31.1
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Santamarina-Fojo S, Peterson K, Knapper C, Qiu Y, Freeman L, Cheng JF, Osorio J, Remaley A, Yang XP, Haudenschild C, Prades C, Chimini G, Blackmon E, Francois T, Duverger N, Rubin EM, Rosier M, Denefle P, Fredrickson DS, Brewer HB Jr: Complete genomic sequence of the human ABCA1 gene: analysis of the human and mouse ATP-binding cassette A promoter. Proc Natl Acad Sci U S A. 2000 Jul 5;97(14):7987-92. [PubMed Link Image]
  2. Qiu Y, Cavelier L, Chiu S, Yang X, Rubin E, Cheng JF: Human and mouse ABCA1 comparative sequencing and transgenesis studies revealing novel regulatory sequences. Genomics. 2001 Apr 1;73(1):66-76. [PubMed Link Image]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  4. Langmann T, Klucken J, Reil M, Liebisch G, Luciani MF, Chimini G, Kaminski WE, Schmitz G: Molecular cloning of the human ATP-binding cassette transporter 1 (hABC1): evidence for sterol-dependent regulation in macrophages. Biochem Biophys Res Commun. 1999 Apr 2;257(1):29-33. [PubMed Link Image]
  5. Rust S, Rosier M, Funke H, Real J, Amoura Z, Piette JC, Deleuze JF, Brewer HB, Duverger N, Denefle P, Assmann G: Tangier disease is caused by mutations in the gene encoding ATP-binding cassette transporter 1. Nat Genet. 1999 Aug;22(4):352-5. [PubMed Link Image]
  6. See RH, Caday-Malcolm RA, Singaraja RR, Zhou S, Silverston A, Huber MT, Moran J, James ER, Janoo R, Savill JM, Rigot V, Zhang LH, Wang M, Chimini G, Wellington CL, Tafuri SR, Hayden MR: Protein kinase A site-specific phosphorylation regulates ATP-binding cassette A1 (ABCA1)-mediated phospholipid efflux. J Biol Chem. 2002 Nov 1;277(44):41835-42. Epub 2002 Aug 23. [PubMed Link Image]
  7. Porsch-Ozcurumez M, Langmann T, Heimerl S, Borsukova H, Kaminski WE, Drobnik W, Honer C, Schumacher C, Schmitz G: The zinc finger protein 202 (ZNF202) is a transcriptional repressor of ATP binding cassette transporter A1 (ABCA1) and ABCG1 gene expression and a modulator of cellular lipid efflux. J Biol Chem. 2001 Apr 13;276(15):12427-33. Epub 2001 Jan 22. [PubMed Link Image]
  8. Kaplan R, Gan X, Menke JG, Wright SD, Cai TQ: Bacterial lipopolysaccharide induces expression of ABCA1 but not ABCG1 via an LXR-independent pathway. J Lipid Res. 2002 Jun;43(6):952-9. [PubMed Link Image]
  9. Hamon Y, Trompier D, Ma Z, Venegas V, Pophillat M, Mignotte V, Zhou Z, Chimini G: Cooperation between engulfment receptors: the case of ABCA1 and MEGF10. PLoS One. 2006 Dec 27;1:e120. [PubMed Link Image]
  10. Singaraja RR, Brunham LR, Visscher H, Kastelein JJ, Hayden MR: Efflux and atherosclerosis: the clinical and biochemical impact of variations in the ABCA1 gene. Arterioscler Thromb Vasc Biol. 2003 Aug 1;23(8):1322-32. Epub 2003 May 22. [PubMed Link Image]
  11. Singaraja RR, Kang MH, Vaid K, Sanders SS, Vilas GL, Arstikaitis P, Coutinho J, Drisdel RC, El-Husseini Ael D, Green WN, Berthiaume L, Hayden MR: Palmitoylation of ATP-binding cassette transporter A1 is essential for its trafficking and function. Circ Res. 2009 Jul 17;105(2):138-47. Epub 2009 Jun 25. [PubMed Link Image]
  12. Hozoji M, Kimura Y, Kioka N, Ueda K: Formation of two intramolecular disulfide bonds is necessary for ApoA-I-dependent cholesterol efflux mediated by ABCA1. J Biol Chem. 2009 Apr 24;284(17):11293-300. Epub 2009 Mar 3. [PubMed Link Image]
  13. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  14. Marcil M, Brooks-Wilson A, Clee SM, Roomp K, Zhang LH, Yu L, Collins JA, van Dam M, Molhuizen HO, Loubster O, Ouellette BF, Sensen CW, Fichter K, Mott S, Denis M, Boucher B, Pimstone S, Genest J Jr, Kastelein JJ, Hayden MR: Mutations in the ABC1 gene in familial HDL deficiency with defective cholesterol efflux. Lancet. 1999 Oct 16;354(9187):1341-6. [PubMed Link Image]
  15. Brooks-Wilson A, Marcil M, Clee SM, Zhang LH, Roomp K, van Dam M, Yu L, Brewer C, Collins JA, Molhuizen HO, Loubser O, Ouelette BF, Fichter K, Ashbourne-Excoffon KJ, Sensen CW, Scherer S, Mott S, Denis M, Martindale D, Frohlich J, Morgan K, Koop B, Pimstone S, Kastelein JJ, Genest J Jr, Hayden MR: Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency. Nat Genet. 1999 Aug;22(4):336-45. [PubMed Link Image]
  16. Bodzioch M, Orso E, Klucken J, Langmann T, Bottcher A, Diederich W, Drobnik W, Barlage S, Buchler C, Porsch-Ozcurumez M, Kaminski WE, Hahmann HW, Oette K, Rothe G, Aslanidis C, Lackner KJ, Schmitz G: The gene encoding ATP-binding cassette transporter 1 is mutated in Tangier disease. Nat Genet. 1999 Aug;22(4):347-51. [PubMed Link Image]
  17. Clee SM, Kastelein JJ, van Dam M, Marcil M, Roomp K, Zwarts KY, Collins JA, Roelants R, Tamasawa N, Stulc T, Suda T, Ceska R, Boucher B, Rondeau C, DeSouich C, Brooks-Wilson A, Molhuizen HO, Frohlich J, Genest J Jr, Hayden MR: Age and residual cholesterol efflux affect HDL cholesterol levels and coronary artery disease in ABCA1 heterozygotes. J Clin Invest. 2000 Nov;106(10):1263-70. [PubMed Link Image]
  18. Brousseau ME, Schaefer EJ, Dupuis J, Eustace B, Van Eerdewegh P, Goldkamp AL, Thurston LM, FitzGerald MG, Yasek-McKenna D, O'Neill G, Eberhart GP, Weiffenbach B, Ordovas JM, Freeman MW, Brown RH Jr, Gu JZ: Novel mutations in the gene encoding ATP-binding cassette 1 in four tangier disease kindreds. J Lipid Res. 2000 Mar;41(3):433-41. [PubMed Link Image]
  19. Wang J, Burnett JR, Near S, Young K, Zinman B, Hanley AJ, Connelly PW, Harris SB, Hegele RA: Common and rare ABCA1 variants affecting plasma HDL cholesterol. Arterioscler Thromb Vasc Biol. 2000 Aug;20(8):1983-9. [PubMed Link Image]
  20. Bertolini S, Pisciotta L, Seri M, Cusano R, Cantafora A, Calabresi L, Franceschini G, Ravazzolo R, Calandra S: A point mutation in ABC1 gene in a patient with severe premature coronary heart disease and mild clinical phenotype of Tangier disease. Atherosclerosis. 2001 Feb 15;154(3):599-605. [PubMed Link Image]
  21. Brousseau ME, Bodzioch M, Schaefer EJ, Goldkamp AL, Kielar D, Probst M, Ordovas JM, Aslanidis C, Lackner KJ, Bloomfield Rubins H, Collins D, Robins SJ, Wilson PW, Schmitz G: Common variants in the gene encoding ATP-binding cassette transporter 1 in men with low HDL cholesterol levels and coronary heart disease. Atherosclerosis. 2001 Feb 15;154(3):607-11. [PubMed Link Image]
  22. Lapicka-Bodzioch K, Bodzioch M, Krull M, Kielar D, Probst M, Kiec B, Andrikovics H, Bottcher A, Hubacek J, Aslanidis C, Suttorp N, Schmitz G: Homogeneous assay based on 52 primer sets to scan for mutations of the ABCA1 gene and its application in genetic analysis of a new patient with familial high-density lipoprotein deficiency syndrome. Biochim Biophys Acta. 2001 Jul 27;1537(1):42-8. [PubMed Link Image]
  23. Huang W, Moriyama K, Koga T, Hua H, Ageta M, Kawabata S, Mawatari K, Imamura T, Eto T, Kawamura M, Teramoto T, Sasaki J: Novel mutations in ABCA1 gene in Japanese patients with Tangier disease and familial high density lipoprotein deficiency with coronary heart disease. Biochim Biophys Acta. 2001 Jul 27;1537(1):71-8. [PubMed Link Image]
  24. Clee SM, Zwinderman AH, Engert JC, Zwarts KY, Molhuizen HO, Roomp K, Jukema JW, van Wijland M, van Dam M, Hudson TJ, Brooks-Wilson A, Genest J Jr, Kastelein JJ, Hayden MR: Common genetic variation in ABCA1 is associated with altered lipoprotein levels and a modified risk for coronary artery disease. Circulation. 2001 Mar 6;103(9):1198-205. [PubMed Link Image]
  25. Hong SH, Rhyne J, Zeller K, Miller M: ABCA1(Alabama): a novel variant associated with HDL deficiency and premature coronary artery disease. Atherosclerosis. 2002 Oct;164(2):245-50. [PubMed Link Image]
  26. Ho Hong S, Rhyne J, Zeller K, Miller M: Novel ABCA1 compound variant associated with HDL cholesterol deficiency. Biochim Biophys Acta. 2002 May 21;1587(1):60-4. [PubMed Link Image]
  27. Nishida Y, Hirano K, Tsukamoto K, Nagano M, Ikegami C, Roomp K, Ishihara M, Sakane N, Zhang Z, Tsujii Ki K, Matsuyama A, Ohama T, Matsuura F, Ishigami M, Sakai N, Hiraoka H, Hattori H, Wellington C, Yoshida Y, Misugi S, Hayden MR, Egashira T, Yamashita S, Matsuzawa Y: Expression and functional analyses of novel mutations of ATP-binding cassette transporter-1 in Japanese patients with high-density lipoprotein deficiency. Biochem Biophys Res Commun. 2002 Jan 18;290(2):713-21. [PubMed Link Image]
  28. Hong SH, Riley W, Rhyne J, Friel G, Miller M: Lack of association between increased carotid intima-media thickening and decreased HDL-cholesterol in a family with a novel ABCA1 variant, G2265T. Clin Chem. 2002 Nov;48(11):2066-70. [PubMed Link Image]
  29. Guo Z, Inazu A, Yu W, Suzumura T, Okamoto M, Nohara A, Higashikata T, Sano R, Wakasugi K, Hayakawa T, Yoshida K, Suehiro T, Schmitz G, Mabuchi H: Double deletions and missense mutations in the first nucleotide-binding fold of the ATP-binding cassette transporter A1 ( ABCA1) gene in Japanese patients with Tangier disease. J Hum Genet. 2002;47(6):325-9. [PubMed Link Image]
  30. Ishii J, Nagano M, Kujiraoka T, Ishihara M, Egashira T, Takada D, Tsuji M, Hattori H, Emi M: Clinical variant of Tangier disease in Japan: mutation of the ABCA1 gene in hypoalphalipoproteinemia with corneal lipidosis. J Hum Genet. 2002;47(7):366-9. [PubMed Link Image]
  31. Hong SH, Rhyne J, Miller M: Novel polypyrimidine variation (IVS46: del T -39...-46) in ABCA1 causes exon skipping and contributes to HDL cholesterol deficiency in a family with premature coronary disease. Circ Res. 2003 Nov 14;93(10):1006-12. Epub 2003 Oct 23. [PubMed Link Image]
  32. Tan JH, Low PS, Tan YS, Tong MC, Saha N, Yang H, Heng CK: ABCA1 gene polymorphisms and their associations with coronary artery disease and plasma lipids in males from three ethnic populations in Singapore. Hum Genet. 2003 Jul;113(2):106-17. Epub 2003 Apr 23. [PubMed Link Image]
  33. Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed Link Image]
  34. Cenarro A, Artieda M, Castillo S, Mozas P, Reyes G, Tejedor D, Alonso R, Mata P, Pocovi M, Civeira F: A common variant in the ABCA1 gene is associated with a lower risk for premature coronary heart disease in familial hypercholesterolaemia. J Med Genet. 2003 Mar;40(3):163-8. [PubMed Link Image]
  35. Probst MC, Thumann H, Aslanidis C, Langmann T, Buechler C, Patsch W, Baralle FE, Dallinga-Thie GM, Geisel J, Keller C, Menys VC, Schmitz G: Screening for functional sequence variations and mutations in ABCA1. Atherosclerosis. 2004 Aug;175(2):269-79. [PubMed Link Image]
  36. Pisciotta L, Hamilton-Craig I, Tarugi P, Bellocchio A, Fasano T, Alessandrini P, Bon GB, Siepi D, Mannarino E, Cattin L, Averna M, Cefalu AB, Cantafora A, Calandra S, Bertolini S: Familial HDL deficiency due to ABCA1 gene mutations with or without other genetic lipoprotein disorders. Atherosclerosis. 2004 Feb;172(2):309-20. [PubMed Link Image]
  37. Albrecht C, Baynes K, Sardini A, Schepelmann S, Eden ER, Davies SW, Higgins CF, Feher MD, Owen JS, Soutar AK: Two novel missense mutations in ABCA1 result in altered trafficking and cause severe autosomal recessive HDL deficiency. Biochim Biophys Acta. 2004 May 24;1689(1):47-57. [PubMed Link Image]
  38. Frikke-Schmidt R, Nordestgaard BG, Jensen GB, Tybjaerg-Hansen A: Genetic variation in ABC transporter A1 contributes to HDL cholesterol in the general population. J Clin Invest. 2004 Nov;114(9):1343-53. [PubMed Link Image]
  39. Cohen JC, Kiss RS, Pertsemlidis A, Marcel YL, McPherson R, Hobbs HH: Multiple rare alleles contribute to low plasma levels of HDL cholesterol. Science. 2004 Aug 6;305(5685):869-72. [PubMed Link Image]
  40. Albrecht C, McVey JH, Elliott JI, Sardini A, Kasza I, Mumford AD, Naoumova RP, Tuddenham EG, Szabo K, Higgins CF: A novel missense mutation in ABCA1 results in altered protein trafficking and reduced phosphatidylserine translocation in a patient with Scott syndrome. Blood. 2005 Jul 15;106(2):542-9. Epub 2005 Mar 24. [PubMed Link Image]
  41. Frikke-Schmidt R, Nordestgaard BG, Schnohr P, Steffensen R, Tybjaerg-Hansen A: Mutation in ABCA1 predicted risk of ischemic heart disease in the Copenhagen City Heart Study Population. J Am Coll Cardiol. 2005 Oct 18;46(8):1516-20. Epub 2005 Sep 23. [PubMed Link Image]
  42. Fasano T, Bocchi L, Pisciotta L, Bertolini S, Calandra S: Denaturing high-performance liquid chromatography in the detection of ABCA1 gene mutations in familial HDL deficiency. J Lipid Res. 2005 Apr;46(4):817-22. Epub 2005 Feb 1. [PubMed Link Image]
  43. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 7150
Enzyme 47 Name Na(+)/H(+) exchange regulatory cofactor NHE-RF1
Enzyme 47 Synonyms
  1. NHERF-1
  2. Ezrin-radixin-moesin-binding phosphoprotein 50
  3. EBP50
  4. Regulatory cofactor of Na(+)/H(+) exchanger
  5. Sodium-hydrogen exchanger regulatory factor 1
  6. Solute carrier family 9 isoform A3 regulatory factor 1
Enzyme 47 Gene Name SLC9A3R1
Enzyme 47 Protein Sequence >Na(+)/H(+) exchange regulatory cofactor NHE-RF1
MSADAAAGAPLPRLCCLEKGPNGYGFHLHGEKGKLGQYIRLVEPGSPAEKAGLLAGDRLV
EVNGENVEKETHQQVVSRIRAALNAVRLLVVDPETDEQLQKLGVQVREELLRAQEAPGQA
EPPAAAEVQGAGNENEPREADKSHPEQRELRPRLCTMKKGPSGYGFNLHSDKSKPGQFIR
SVDPDSPAEASGLRAQDRIVEVNGVCMEGKQHGDVVSAIRAGGDETKLLVVDRETDEFFK
KCRVIPSQEHLNGPLPVPFTNGEIQKENSREALAEAALESPRPALVRSASSDTSEELNSQ
DSPPKQDSTAPSSTSSSDPILDFNISLAMAKERAHQKRSSKRAPQMDWSKKNELFSNL
Enzyme 47 Number of Residues 358
Enzyme 47 Molecular Weight 38868.1
Enzyme 47 Theoretical pI 5.52
Enzyme 47 GO Classification
Function
  • binding
  • protein binding
Process
Component
Enzyme 47 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 47 Specific Function Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for recycling of internalized ADRB2. Was first known to play a role in the regulation of the activity and subcellular location of SLC9A3. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May enhance Wnt signaling. May participate in HTR4 targeting to microvilli. Interacts with MCC
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions Not Available
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 3220019 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID O14745 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name NHRF1_HUMAN Link Image
Enzyme 47 PDB ID 1G9O Link Image
Enzyme 47 PDB File Show
Enzyme 47 3D Structure
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >1077 bp
ATGAGCGCGGACGCAGCGGCCGGGGCGCCCCTGCCCCGGCTCTGCTGCCTGGAGAAGGGT
CCGAACGGCTACGGCTTCCACCTGCACGGGGAGAAGGGCAAGTTGGGCCAGTACATCCGG
CTGGTGGAGCCCGGCTCGCCGGCCGAGAAGGCGGGGCTGCTGGCGGGGGACCGGCTGGTG
GAGGTGAACGGCGAAAACGTGGAGAAGGAGACCCACCAGCAGGTGGTGAGCCGCATCCGC
GCCGCACTCAACGCCGTGCGCCTGCTGGTGGTCGACCCCGAGACGGACGAGCAGCTGCAG
AAGCTCGGCGTCCAGGTCCGAGAGGAGCTGCTGCGCGCCCAGGAAGCGCCGGGGCAGGCC
GAGCCGCCGGCCGCCGCCGAGGTGCAGGGGGCTGGCAACGAAAATGAGCCTCGCGAGGCC
GACAAGAGCCACCCGGAGCAGCGCGAGCTTCGGCCTCGGCTCTGTACCATGAAGAAGGGC
CCCAGTGGCTATGGCTTCAACCTGCACAGCGACAAGTCCAAGCCAGGCCAGTTCATCCGG
TCAGTGGACCCAGACTCCCCGGCTGAGGCTTCAGGGCTCCGGGCCCAGGATCGCATTGTG
GAGGTGAACGGGGTCTGCATGGAGGGGAAGCAGCATGGGGACGTGGTGTCCGCCATCAGG
GCTGGCGGGGACGAGACCAAGCTGCTGGTGGTGGACAGGGAAACTGACGAGTTCTTCAAG
AAATGCAGAGTGATCCCATCTCAGGAGCACCTGAATGGTCCCCTGCCTGTGCCCTTCACC
AATGGGGAGATACAGAAGGAGAACAGTCGTGAAGCCCTGGCAGAGGCAGCCTTGGAGAGC
CCCAGGCCAGCCCTGGTGAGATCCGCCTCCAGTGACACCAGCGAGGAGCTGAATTCCCAA
GACAGCCCCCCAAAACAGGACTCCACAGCGCCCTCGTCTACCTCCTCCTCCGACCCCATC
CTAGACTTCAACATCTCCCTGGCCATGGCCAAAGAGAGGGCCCACCAGAAACGCAGCAGC
AAACGGGCCCCGCAGATGGACTGGAGCAAGAAAAACGAACTCTTCAGCAACCTCTGA
Enzyme 47 GenBank Gene ID AF015926 Link Image
Enzyme 47 GeneCard ID SLC9A3R1 Link Image
Enzyme 47 GenAtlas ID Not Available
Enzyme 47 HGNC ID Not Available
Enzyme 47 Chromosome Location 1
Enzyme 47 Locus 17q25.1
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Reczek D, Berryman M, Bretscher A: Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family. J Cell Biol. 1997 Oct 6;139(1):169-79. [PubMed Link Image]
  2. Murthy A, Gonzalez-Agosti C, Cordero E, Pinney D, Candia C, Solomon F, Gusella J, Ramesh V: NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins. J Biol Chem. 1998 Jan 16;273(3):1273-6. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  5. Yun CH, Oh S, Zizak M, Steplock D, Tsao S, Tse CM, Weinman EJ, Donowitz M: cAMP-mediated inhibition of the epithelial brush border Na+/H+ exchanger, NHE3, requires an associated regulatory protein. Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):3010-5. [PubMed Link Image]
  6. Cao TT, Deacon HW, Reczek D, Bretscher A, von Zastrow M: A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor. Nature. 1999 Sep 16;401(6750):286-90. [PubMed Link Image]
  7. Brdickova N, Brdicka T, Andera L, Spicka J, Angelisova P, Milgram SL, Horejsi V: Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton. FEBS Lett. 2001 Oct 26;507(2):133-6. [PubMed Link Image]
  8. Reczek D, Bretscher A: Identification of EPI64, a TBC/rabGAP domain-containing microvillar protein that binds to the first PDZ domain of EBP50 and E3KARP. J Cell Biol. 2001 Apr 2;153(1):191-206. [PubMed Link Image]
  9. Liedtke CM, Yun CH, Kyle N, Wang D: Protein kinase C epsilon-dependent regulation of cystic fibrosis transmembrane regulator involves binding to a receptor for activated C kinase (RACK1) and RACK1 binding to Na+/H+ exchange regulatory factor. J Biol Chem. 2002 Jun 21;277(25):22925-33. Epub 2002 Apr 15. [PubMed Link Image]
  10. Li JG, Chen C, Liu-Chen LY: Ezrin-radixin-moesin-binding phosphoprotein-50/Na+/H+ exchanger regulatory factor (EBP50/NHERF) blocks U50,488H-induced down-regulation of the human kappa opioid receptor by enhancing its recycling rate. J Biol Chem. 2002 Jul 26;277(30):27545-52. Epub 2002 May 9. [PubMed Link Image]
  11. Glynne PA, Darling KE, Picot J, Evans TJ: Epithelial inducible nitric-oxide synthase is an apical EBP50-binding protein that directs vectorial nitric oxide output. J Biol Chem. 2002 Sep 6;277(36):33132-8. Epub 2002 Jun 21. [PubMed Link Image]
  12. Rochdi MD, Watier V, La Madeleine C, Nakata H, Kozasa T, Parent JL: Regulation of GTP-binding protein alpha q (Galpha q) signaling by the ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50). J Biol Chem. 2002 Oct 25;277(43):40751-9. Epub 2002 Aug 21. [PubMed Link Image]
  13. Park M, Ko SB, Choi JY, Muallem G, Thomas PJ, Pushkin A, Lee MS, Kim JY, Lee MG, Muallem S, Kurtz I: The cystic fibrosis transmembrane conductance regulator interacts with and regulates the activity of the HCO3- salvage transporter human Na+-HCO3- cotransport isoform 3. J Biol Chem. 2002 Dec 27;277(52):50503-9. Epub 2002 Oct 25. [PubMed Link Image]
  14. Mery L, Strauss B, Dufour JF, Krause KH, Hoth M: The PDZ-interacting domain of TRPC4 controls its localization and surface expression in HEK293 cells. J Cell Sci. 2002 Sep 1;115(Pt 17):3497-508. [PubMed Link Image]
  15. Ediger TR, Park SE, Katzenellenbogen BS: Estrogen receptor inducibility of the human Na+/H+ exchanger regulatory factor/ezrin-radixin-moesin binding protein 50 (NHE-RF/EBP50) gene involving multiple half-estrogen response elements. Mol Endocrinol. 2002 Aug;16(8):1828-39. [PubMed Link Image]
  16. Pushkin A, Abuladze N, Newman D, Muronets V, Sassani P, Tatishchev S, Kurtz I: The COOH termini of NBC3 and the 56-kDa H+-ATPase subunit are PDZ motifs involved in their interaction. Am J Physiol Cell Physiol. 2003 Mar;284(3):C667-73. Epub 2002 Nov 20. [PubMed Link Image]
  17. Shibata T, Chuma M, Kokubu A, Sakamoto M, Hirohashi S: EBP50, a beta-catenin-associating protein, enhances Wnt signaling and is over-expressed in hepatocellular carcinoma. Hepatology. 2003 Jul;38(1):178-86. [PubMed Link Image]
  18. Gentzsch M, Cui L, Mengos A, Chang XB, Chen JH, Riordan JR: The PDZ-binding chloride channel ClC-3B localizes to the Golgi and associates with cystic fibrosis transmembrane conductance regulator-interacting PDZ proteins. J Biol Chem. 2003 Feb 21;278(8):6440-9. Epub 2002 Dec 5. [PubMed Link Image]
  19. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  20. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  21. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  22. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  23. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  24. Arnaud C, Sebbagh M, Nola S, Audebert S, Bidaut G, Hermant A, Gayet O, Dusetti NJ, Ollendorff V, Santoni MJ, Borg JP, Lecine P: MCC, a new interacting protein for Scrib, is required for cell migration in epithelial cells. FEBS Lett. 2009 Jul 21;583(14):2326-32. Epub 2009 Jun 24. [PubMed Link Image]
  25. Karthikeyan S, Leung T, Ladias JA: Structural basis of the Na+/H+ exchanger regulatory factor PDZ1 interaction with the carboxyl-terminal region of the cystic fibrosis transmembrane conductance regulator. J Biol Chem. 2001 Jun 8;276(23):19683-6. Epub 2001 Apr 13. [PubMed Link Image]
  26. Karthikeyan S, Leung T, Birrane G, Webster G, Ladias JA: Crystal structure of the PDZ1 domain of human Na(+)/H(+) exchanger regulatory factor provides insights into the mechanism of carboxyl-terminal leucine recognition by class I PDZ domains. J Mol Biol. 2001 May 18;308(5):963-73. [PubMed Link Image]
  27. Karthikeyan S, Leung T, Ladias JA: Structural determinants of the Na+/H+ exchanger regulatory factor interaction with the beta 2 adrenergic and platelet-derived growth factor receptors. J Biol Chem. 2002 May 24;277(21):18973-8. Epub 2002 Mar 6. [PubMed Link Image]
  28. Finnerty CM, Chambers D, Ingraffea J, Faber HR, Karplus PA, Bretscher A: The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain. J Cell Sci. 2004 Mar 15;117(Pt 8):1547-52. [PubMed Link Image]
  29. Terawaki S, Maesaki R, Hakoshima T: Structural basis for NHERF recognition by ERM proteins. Structure. 2006 Apr;14(4):777-89. [PubMed Link Image]
  30. Karim Z, Gerard B, Bakouh N, Alili R, Leroy C, Beck L, Silve C, Planelles G, Urena-Torres P, Grandchamp B, Friedlander G, Prie D: NHERF1 mutations and responsiveness of renal parathyroid hormone. N Engl J Med. 2008 Sep 11;359(11):1128-35. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 7255
Enzyme 48 Name Aryl hydrocarbon receptor
Enzyme 48 Synonyms
  1. Ah receptor
  2. AhR
  3. Class E basic helix-loop-helix protein 76
  4. bHLHe76
Enzyme 48 Gene Name AHR
Enzyme 48 Protein Sequence >Aryl hydrocarbon receptor
MNSSSANITYASRKRRKPVQKTVKPIPAEGIKSNPSKRHRDRLNTELDRLASLLPFPQDV
INKLDKLSVLRLSVSYLRAKSFFDVALKSSPTERNGGQDNCRAANFREGLNLQEGEFLLQ
ALNGFVLVVTTDALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALNP
SQCTESGQGIEEATGLPQTVVCYNPDQIPPENSPLMERCFICRLRCLLDNSSGFLAMNFQ
GKLKYLHGQKKKGKDGSILPPQLALFAIATPLQPPSILEIRTKNFIFRTKHKLDFTPIGC
DAKGRIVLGYTEAELCTRGSGYQFIHAADMLYCAESHIRMIKTGESGMIVFRLLTKNNRW
TWVQSNARLLYKNGRPDYIIVTQRPLTDEEGTEHLRKRNTKLPFMFTTGEAVLYEATNPF
PAIMDPLPLRTKNGTSGKDSATTSTLSKDSLNPSSLLAAMMQQDESIYLYPASSTSSTAP
FENNFFNESMNECRNWQDNTAPMGNDTILKHEQIDQPQDVNSFAGGHPGLFQDSKNSDLY
SIMKNLGIDFEDIRHMQNEKFFRNDFSGEVDFRDIDLTDEILTYVQDSLSKSPFIPSDYQ
QQQSLALNSSCMVQEHLHLEQQQQHHQKQVVVEPQQQLCQKMKHMQVNGMFENWNSNQFV
PFNCPQQDPQQYNVFTDLHGISQEFPYKSEMDSMPYTQNFISCNQPVLPQHSKCTELDYP
MGSFEPSPYPTTSSLEDFVTCLQLPENQKHGLNPQSAIITPQTCYAGAVSMYQCQPEPQH
THVGQMQYNPVLPGQQAFLNKFQNGVLNETYPAELNNINNTQTTTHLQPLHHPSEARPFP
DLTSSGFL
Enzyme 48 Number of Residues 848
Enzyme 48 Molecular Weight 96146.7
Enzyme 48 Theoretical pI 6.34
Enzyme 48 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
  • transcription regulator activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • signal transduction
Component
Enzyme 48 General Function Involved in transcription regulator activity
Enzyme 48 Specific Function Ligand-activated transcriptional activator. Binds to the XRE promoter region of genes it activates. Activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons. Involved in cell-cycle regulation. Likely to play an important role in the development and maturation of many tissues
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions Not Available
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 4502003 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID P35869 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name AHR_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >2547 bp
ATGAACAGCAGCAGCGCCAACATCACCTACGCCAGTCGCAAGCGGCGGAAGCCGGTGCAG
AAAACAGTAAAGCCAATCCCAGCTGAAGGAATCAAGTCAAATCCTTCCAAGCGGCATAGA
GACCGACTTAATACAGAGTTGGACCGTTTGGCTAGCCTGCTGCCTTTCCCACAAGATGTT
ATTAATAAGTTGGACAAACTTTCAGTTCTTAGGCTCAGCGTCAGTTACCTGAGAGCCAAG
AGCTTCTTTGATGTTGCATTAAAATCCTCCCCTACTGAAAGAAACGGAGGCCAGGATAAC
TGTAGAGCAGCAAATTTCAGAGAAGGCCTGAACTTACAAGAAGGAGAATTCTTATTACAG
GCTCTGAATGGCTTTGTATTAGTTGTCACTACAGATGCTTTGGTCTTTTATGCTTCTTCT
ACTATACAAGATTATCTAGGGTTTCAGCAGTCTGATGTCATACATCAGAGTGTATATGAA
CTTATCCATACCGAAGACCGAGCTGAATTTCAGCGTCAGCTACACTGGGCATTAAATCCT
TCTCAGTGTACAGAGTCTGGACAAGGAATTGAAGAAGCCACTGGTCTCCCCCAGACAGTA
GTCTGTTATAACCCAGACCAGATTCCTCCAGAAAACTCTCCTTTAATGGAGAGGTGCTTC
ATATGTCGTCTAAGGTGTCTGCTGGATAATTCATCTGGTTTTCTGGCAATGAATTTCCAA
GGGAAGTTAAAGTATCTTCATGGACAGAAAAAGAAAGGGAAAGATGGATCAATACTTCCA
CCTCAGTTGGCTTTGTTTGCGATAGCTACTCCACTTCAGCCACCATCCATACTTGAAATC
CGGACCAAAAATTTTATCTTTAGAACCAAACACAAACTAGACTTCACACCTATTGGTTGT
GATGCCAAAGGAAGAATTGTTTTAGGATATACTGAAGCAGAGCTGTGCACGAGAGGCTCA
GGTTATCAGTTTATTCATGCAGCTGATATGCTTTATTGTGCCGAGTCCCATATCCGAATG
ATTAAGACTGGAGAAAGTGGCATGATAGTTTTCCGGCTTCTTACAAAAAACAACCGATGG
ACTTGGGTCCAGTCTAATGCACGCCTGCTTTATAAAAATGGAAGACCAGATTATATCATT
GTAACTCAGAGACCACTAACAGATGAGGAAGGAACAGAGCATTTACGAAAACGAAATACG
AAGTTGCCTTTTATGTTTACCACTGGAGAAGCTGTGTTGTATGAGGCAACCAACCCTTTT
CCTGCCATAATGGATCCCTTACCACTAAGGACTAAAAATGGCACTAGTGGAAAAGACTCT
GCTACCACATCCACTCTAAGCAAGGACTCTCTCAATCCTAGTTCCCTCCTGGCTGCCATG
ATGCAACAAGATGAGTCTATTTATCTCTATCCTGCTTCAAGTACTTCAAGTACTGCACCT
TTTGAAAACAACTTTTTCAACGAATCTATGAATGAATGCAGAAATTGGCAAGATAATACT
GCACCGATGGGAAATGATACTATCCTGAAACATGAGCAAATTGACCAGCCTCAGGATGTG
AACTCATTTGCTGGAGGTCACCCAGGGCTCTTTCAAGATAGTAAAAACAGTGACTTGTAC
AGCATAATGAAAAACCTAGGCATTGATTTTGAAGACATCAGACACATGCAGAATGAAAAA
TTTTTCAGAAATGATTTTTCTGGTGAGGTTGACTTCAGAGACATTGACTTAACGGATGAA
ATCCTGACGTATGTCCAAGATTCTTTAAGTAAGTCTCCCTTCATACCTTCAGATTATCAA
CAGCAACAGTCCTTGGCTCTGAACTCAAGCTGTATGGTACAGGAACACCTACATCTAGAA
CAGCAACAGCAACATCACCAAAAGCAAGTAGTAGTGGAGCCACAGCAACAGCTGTGTCAG
AAGATGAAGCACATGCAAGTTAATGGCATGTTTGAAAATTGGAACTCTAACCAATTCGTG
CCTTTCAATTGTCCACAGCAAGACCCACAACAATATAATGTCTTTACAGACTTACATGGG
ATCAGTCAAGAGTTCCCCTACAAATCTGAAATGGATTCTATGCCTTATACACAGAACTTT
ATTTCCTGTAATCAGCCTGTATTACCACAACATTCCAAATGTACAGAGCTGGACTACCCT
ATGGGGAGTTTTGAACCATCCCCATACCCCACTACTTCTAGTTTAGAAGATTTTGTCACT
TGTTTACAACTTCCTGAAAACCAAAAGCATGGATTAAATCCACAGTCAGCCATAATAACT
CCTCAGACATGTTATGCTGGGGCCGTGTCGATGTATCAGTGCCAGCCAGAACCTCAGCAC
ACCCACGTGGGTCAGATGCAGTACAATCCAGTACTGCCAGGCCAACAGGCATTTTTAAAC
AAGTTTCAGAATGGAGTTTTAAATGAAACATATCCAGCTGAATTAAATAACATAAATAAC
ACTCAGACTACCACACATCTTCAGCCACTTCATCATCCGTCAGAAGCCAGACCTTTTCCT
GATTTGACATCCAGTGGATTCCTGTAA
Enzyme 48 GenBank Gene ID NM_001621.4 Link Image
Enzyme 48 GeneCard ID AHR Link Image
Enzyme 48 GenAtlas ID AHR Link Image
Enzyme 48 HGNC ID HGNC:348 Link Image
Enzyme 48 Chromosome Location 7
Enzyme 48 Locus 7p15
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Itoh S, Kamataki T: Human Ah receptor cDNA: analysis for highly conserved sequences. Nucleic Acids Res. 1993 Jul 25;21(15):3578. [PubMed Link Image]
  2. Dolwick KM, Schmidt JV, Carver LA, Swanson HI, Bradfield CA: Cloning and expression of a human Ah receptor cDNA. Mol Pharmacol. 1993 Nov;44(5):911-7. [PubMed Link Image]
  3. Ema M, Matsushita N, Sogawa K, Ariyama T, Inazawa J, Nemoto T, Ota M, Oshimura M, Fujii-Kuriyama Y: Human arylhydrocarbon receptor: functional expression and chromosomal assignment to 7p21. J Biochem. 1994 Oct;116(4):845-51. [PubMed Link Image]
  4. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  5. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Bennett P, Ramsden DB, Williams AC: Complete structural characterisation of the human aryl hydrocarbon receptor gene. Clin Mol Pathol. 1996 Feb;49(1):M12-6. [PubMed Link Image]
  8. Hayashi S, Watanabe J, Nakachi K, Eguchi H, Gotoh O, Kawajiri K: Interindividual difference in expression of human Ah receptor and related P450 genes. Carcinogenesis. 1994 May;15(5):801-6. [PubMed Link Image]
  9. Ema M, Ohe N, Suzuki M, Mimura J, Sogawa K, Ikawa S, Fujii-Kuriyama Y: Dioxin binding activities of polymorphic forms of mouse and human arylhydrocarbon receptors. J Biol Chem. 1994 Nov 4;269(44):27337-43. [PubMed Link Image]
  10. Nguyen TA, Hoivik D, Lee JE, Safe S: Interactions of nuclear receptor coactivator/corepressor proteins with the aryl hydrocarbon receptor complex. Arch Biochem Biophys. 1999 Jul 15;367(2):250-7. [PubMed Link Image]
  11. Wolff S, Harper PA, Wong JM, Mostert V, Wang Y, Abel J: Cell-specific regulation of human aryl hydrocarbon receptor expression by transforming growth factor-beta(1). Mol Pharmacol. 2001 Apr;59(4):716-24. [PubMed Link Image]
  12. Puga A, Xia Y, Elferink C: Role of the aryl hydrocarbon receptor in cell cycle regulation. Chem Biol Interact. 2002 Sep 20;141(1-2):117-30. [PubMed Link Image]
  13. Antenos M, Casper RF, Brown TJ: Interaction with Nedd8, a ubiquitin-like protein, enhances the transcriptional activity of the aryl hydrocarbon receptor. J Biol Chem. 2002 Nov 15;277(46):44028-34. Epub 2002 Sep 4. [PubMed Link Image]
  14. Dunham EE, Stevens EA, Glover E, Bradfield CA: The aryl hydrocarbon receptor signaling pathway is modified through interactions with a Kelch protein. Mol Pharmacol. 2006 Jul;70(1):8-15. Epub 2006 Mar 31. [PubMed Link Image]
  15. Harper PA, Wong JY, Lam MS, Okey AB: Polymorphisms in the human AH receptor. Chem Biol Interact. 2002 Sep 20;141(1-2):161-87. [PubMed Link Image]
  16. Kawajiri K, Watanabe J, Eguchi H, Nakachi K, Kiyohara C, Hayashi S: Polymorphisms of human Ah receptor gene are not involved in lung cancer. Pharmacogenetics. 1995 Jun;5(3):151-8. [PubMed Link Image]
  17. Smart J, Daly AK: Variation in induced CYP1A1 levels: relationship to CYP1A1, Ah receptor and GSTM1 polymorphisms. Pharmacogenetics. 2000 Feb;10(1):11-24. [PubMed Link Image]
  18. Cauchi S, Stucker I, Solas C, Laurent-Puig P, Cenee S, Hemon D, Jacquet M, Kremers P, Beaune P, Massaad-Massade L: Polymorphisms of human aryl hydrocarbon receptor (AhR) gene in a French population: relationship with CYP1A1 inducibility and lung cancer. Carcinogenesis. 2001 Nov;22(11):1819-24. [PubMed Link Image]
  19. Wong JM, Okey AB, Harper PA: Human aryl hydrocarbon receptor polymorphisms that result in loss of CYP1A1 induction. Biochem Biophys Res Commun. 2001 Nov 9;288(4):990-6. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 7259
Enzyme 49 Name Cyclic AMP-responsive element-binding protein 5
Enzyme 49 Synonyms
  1. CREB-5
  2. cAMP-responsive element-binding protein 5
  3. CRE-BPa
Enzyme 49 Gene Name CREB5
Enzyme 49 Protein Sequence >Cyclic AMP-responsive element-binding protein 5
MIYEESKMNLEQERPSVCSAPGCSQRFPTEDHLMIHRHKHEMTLKFPSIKTDNMLSDQTP
TPTRFLKNCEEVGLFSELDCSLEHEFRKAQEEESSKRNISMHNAVGGAMTGPGTHQLSSA
RLPNHDTNVVIQQAMPSPQSSSVITQAPSTNRQIGPVPGSLSSLLHLHNRQRQPMPASMP
GTLPNPTMPGSSAVLMPMERQMSVNSSIMGMQGPNLSNPCASPQVQPMHSEAKMRLKAAL
THHPAAMSNGNMNTMGHMMEMMGSRQDQTPHHHMHSHPHQHQTLPPHHPYPHQHQHPAHH
PHPQPHHQQNHPHHHSHSHLHAHPAHHQTSPHPPLHTGNQAQVSPATQQMQPTQTIQPPQ
PTGGRRRRVVDEDPDERRRKFLERNRAAATRCRQKRKVWVMSLEKKAEELTQTNMQLQNE
VSMLKNEVAQLKQLLLTHKDCPITAMQKESQGYLSPESSPPASPVPACSQQQVIQHNTIT
TSSSVSEVVGSSTLSQLTTHRTDLNPIL
Enzyme 49 Number of Residues 508
Enzyme 49 Molecular Weight 56858.0
Enzyme 49 Theoretical pI 8.63
Enzyme 49 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • nucleic acid binding
  • protein binding
  • protein dimerization activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • cell part
  • intracellular
Enzyme 49 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 49 Specific Function Binds to the cAMP response element and activates transcription
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions Not Available
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • None
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 59938770 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q02930 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name CREB5_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >1527 bp
ATGATTTATGAGGAATCCAAGATGAATTTGGAGCAGGAGAGGCCGTTTGTCTGCAGTGCC
CCAGGCTGCTCCCAGCGCTTCCCAACAGAGGACCATCTGATGATTCATAGGCACAAACAT
GAAATGACTTTGAAGTTTCCTTCAATAAAAACAGACAATATGTTATCAGATCAAACTCCG
ACCCCAACGAGATTCCTGAAGAACTGCGAGGAGGTGGGCCTCTTCAGCGAGCTGGACTGC
TCCCTGGAGCACGAGTTCAGGAAGGCTCAGGAAGAGGAGAGCAGCAAGCGGAATATCTCG
ATGCATAATGCAGTTGGTGGGGCCATGACGGGGCCCGGAACTCACCAGCTTAGCAGCGCT
CGGCTGCCCAACCATGACACCAACGTTGTGATTCAGCAAGCCATGCCGTCGCCTCAGTCC
AGCTCTGTCATCACTCAGGCACCTTCCACCAACCGCCAGATCGGGCCTGTCCCAGGCTCT
CTATCTTCTCTGCTACATCTCCACAACAGACAGAGACAGCCCATGCCAGCCTCCATGCCT
GGGACCCTGCCCAACCCTACAATGCCAGGATCTTCCGCCGTCTTGATGCCAATGGAGCGA
CAAATGTCAGTGAACTCCAGCATCATGGGGATGCAAGGTCCAAATCTCAGCAACCCCTGT
GCTTCTCCCCAGGTCCAGCCAATGCATTCAGAAGCCAAAATGAGGTTGAAGGCTGCATTG
ACTCACCACCCTGCTGCCATGTCAAATGGGAACATGAACACCATGGGACACATGATGGAG
ATGATGGGCTCCCGGCAGGACCAGACGCCACACCATCACATGCACTCGCACCCGCATCAG
CACCAGACACTGCCACCCCATCACCCTTACCCACACCAGCACCAGCACCCAGCACACCAT
CCTCACCCTCAACCCCATCACCAGCAGAACCATCCACATCACCACTCCCATTCCCACCTT
CATGCACACCCAGCACATCACCAGACCTCGCCACATCCGCCCCTGCACACCGGCAACCAA
GCACAGGTTTCACCAGCAACACAACAGATGCAGCCAACCCAGACAATACAGCCACCCCAG
CCCACAGGGGGGCGCCGGCGAAGGGTGGTAGACGAGGATCCGGACGAGAGGCGGCGGAAA
TTTCTGGAACGGAACCGGGCAGCTGCCACCCGCTGCAGACAGAAGAGGAAGGTCTGGGTG
ATGTCATTGGAAAAGAAAGCAGAAGAACTCACCCAGACAAACATGCAGCTTCAGAATGAA
GTGTCTATGTTGAAAAATGAGGTGGCCCAGCTGAAACAGTTGTTGTTAACACATAAAGAC
TGCCCAATAACAGCCATGCAGAAAGAATCACAAGGATATCTAAGTCCAGAGAGTAGCCCT
CCTGCTAGTCCTGTCCCAGCTTGCTCCCAGCAACAAGTCATCCAGCATAATACCATCACT
ACTTCCTCATCGGTCAGCGAGGTGGTAGGAAGCTCCACCCTCAGCCAGCTCACCACTCAC
AGAACAGACCTGAATCCGATTCTTTAA
Enzyme 49 GenBank Gene ID NM_182898.2 Link Image
Enzyme 49 GeneCard ID CREB5 Link Image
Enzyme 49 GenAtlas ID CREB5 Link Image
Enzyme 49 HGNC ID HGNC:16844 Link Image
Enzyme 49 Chromosome Location 7
Enzyme 49 Locus 7p15.1
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Nomura N, Zu YL, Maekawa T, Tabata S, Akiyama T, Ishii S: Isolation and characterization of a novel member of the gene family encoding the cAMP response element-binding protein CRE-BP1. J Biol Chem. 1993 Feb 25;268(6):4259-66. [PubMed Link Image]
  2. Zu YL, Maekawa T, Nomura N, Nakata T, Ishii S: Regulation of trans-activating capacity of CRE-BPa by phorbol ester tumor promoter TPA. Oncogene. 1993 Oct;8(10):2749-58. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 7333
Enzyme 50 Name Class E basic helix-loop-helix protein 40
Enzyme 50 Synonyms
  1. bHLHe40
  2. Class B basic helix-loop-helix protein 2
  3. bHLHb2
  4. Differentially expressed in chondrocytes protein 1
  5. DEC1
  6. Enhancer-of-split and hairy-related protein 2
  7. SHARP-2
  8. Stimulated by retinoic acid gene 13 protein
Enzyme 50 Gene Name BHLHE40
Enzyme 50 Protein Sequence >Class E basic helix-loop-helix protein 40
MERIPSAQPPPACLPKAPGLEHGDLPGMYPAHMYQVYKSRRGIKRSEDSKETYKLPHRLI
EKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIIA
LQSGLQAGELSGRNVETGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVS
ELLQGGTSRKPSDPAPKVMDFKEKPSSPAKGSEGPGKNCVPVIQRTFAHSSGEQSGSDTD
TDSGYGGESEKGDLRSEQPCFKSDHGRRFTMGERIGAIKQESEEPPTKKNRMQLSDDEGH
FTSSDLISSPFLGPHPHQPPFCLPFYLIPPSATAYLPMLEKCWYPTSVPVLYPGLNASAA
ALSSFMNPDKISAPLLMPQRLPSPLPAHPSVDSSVLLQALKPIPPLNLETKD
Enzyme 50 Number of Residues 412
Enzyme 50 Molecular Weight 45509.6
Enzyme 50 Theoretical pI 8.22
Enzyme 50 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
  • transcription regulator activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 50 General Function Involved in transcription regulator activity
Enzyme 50 Specific Function May function as a transcriptional factor to modulate chondrogenesis in response to the cAMP pathway
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 2308997 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID O14503 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name BHE40_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >1239 bp
ATGGAGCGGATCCCCAGCGCGCAACCACCCCCCGCCTGCCTGCCCAAAGCACCGGGACTG
GAGCACGGAGACCTACCAGGGATGTACCCTGCCCACATGTACCAAGTGTACAAGTCAAGA
CGGGGAATAAAGCGGAGCGAGGACAGCAAGGAGACCTACAAATTGCCGCACCGGCTCATC
GAGAAAAAGAGACGTGACCGGATTAACGAGTGCATCGCCCAGCTGAAGGATCTCCTACCC
GAACATCTCAAACTTACAACTTTGGGTCACTTGGAAAAAGCAGTGGTTCTTGAACTTACC
TTGAAGCATGTGAAAGCACTAACAAACCTAATTGATCAGCAGCAGCAGAAAATCATTGCC
CTGCAGAGTGGTTTACAAGCTGGTGAGCTGTCAGGGAGAAATGTCGAAACAGGTCAAGAG
ATGTTCTGCTCAGGTTTCCAGACATGTGCCCGGGAGGTGCTTCAGTATCTGGCCAAGCAC
GAGAACACTCGGGACCTGAAGTCTTCGCAGCTTGTCACCCACCTCCACCGGGTGGTCTCG
GAGCTGCTGCAGGGTGGTACCTCCAGGAAGCCATCAGACCCAGCTCCCAAAGTGATGGAC
TTCAAGGAAAAACCCAGCTCTCCGGCCAAAGGTTCGGAAGGTCCTGGGAAAAACTGCGTG
CCAGTCATCCAGCGGACTTTCGCTCACTCGAGTGGGGAGCAGAGCGGCAGCGACACGGAC
ACAGACAGTGGCTATGGAGGAGAATCGGAGAAGGGCGACTTGCGCAGTGAGCAGCCGTGC
TTCAAAAGTGACCACGGACGCAGGTTCACGATGGGAGAAAGGATCGGCGCAATTAAGCAA
GAGTCCGAAGAACCCCCCACAAAAAAGAACCGGATGCAGCTTTCGGATGATGAAGGCCAT
TTCACTAGCAGTGACCTGATCAGCTCCCCGTTCCTGGGCCCACACCCACACCAGCCTCCT
TTCTGCCTGCCCTTCTACCTGATCCCACCTTCAGCGACTGCCTACCTGCCCATGCTGGAG
AAGTGCTGGTATCCCACCTCAGTGCCAGTGCTATACCCAGGCCTCAACGCCTCTGCCGCA
GCCCTCTCTAGCTTCATGAACCCAGACAAGATCTCGGCTCCCTTGCTCATGCCCCAGAGA
CTCCCTTCTCCCTTGCCAGCTCATCCGTCCGTCGACTCTTCTGTCTTGCTCCAAGCTCTG
AAGCCAATCCCCCCTTTAAACTTAGAAACCAAAGACTAA
Enzyme 50 GenBank Gene ID AB004066 Link Image
Enzyme 50 GeneCard ID BHLHE40 Link Image
Enzyme 50 GenAtlas ID BHLHE40 Link Image
Enzyme 50 HGNC ID HGNC:1046 Link Image
Enzyme 50 Chromosome Location 3
Enzyme 50 Locus 3p26
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Shen M, Kawamoto T, Yan W, Nakamasu K, Tamagami M, Koyano Y, Noshiro M, Kato Y: Molecular characterization of the novel basic helix-loop-helix protein DEC1 expressed in differentiated human embryo chondrocytes. Biochem Biophys Res Commun. 1997 Jul 18;236(2):294-8. [PubMed Link Image]
  2. Teramoto M, Nakamasu K, Noshiro M, Matsuda Y, Gotoh O, Shen M, Tsutsumi S, Kawamoto T, Iwamoto Y, Kato Y: Gene structure and chromosomal location of a human bHLH transcriptional factor DEC1 x Stra13 x SHARP-2/BHLHB2. J Biochem (Tokyo). 2001 Mar;129(3):391-6. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ivanova AV, Ivanov SV, Danilkovitch-Miagkova A, Lerman MI: Regulation of STRA13 by the von Hippel-Lindau tumor suppressor protein, hypoxia, and the UBC9/ubiquitin proteasome degradation pathway. J Biol Chem. 2001 May 4;276(18):15306-15. Epub 2001 Feb 6. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 7368
Enzyme 51 Name Splicing factor, proline- and glutamine-rich
Enzyme 51 Synonyms
  1. 100 kDa DNA-pairing protein
  2. hPOMp100
  3. DNA-binding p52/p100 complex, 100 kDa subunit
  4. Polypyrimidine tract-binding protein-associated-splicing factor
  5. PSF
  6. PTB-associated-splicing factor
Enzyme 51 Gene Name SFPQ
Enzyme 51 Protein Sequence >Splicing factor, proline- and glutamine-rich
MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPI
PPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPG
VGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQ
AGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGE
PRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLF
VGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGR
QLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFAS
KPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRF
AQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLM
RRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRM
GYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGS
DMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF
Enzyme 51 Number of Residues 707
Enzyme 51 Molecular Weight 76149.1
Enzyme 51 Theoretical pI 9.95
Enzyme 51 GO Classification
Function
  • binding
  • nucleic acid binding
  • nucleotide binding
Process
Component
Enzyme 51 General Function Involved in nucleotide binding
Enzyme 51 Specific Function DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as an heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer may be involved in DNA nonhomologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Transcriptional repression is probably mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO/SF-1 complex binds to the CYP17 promoter and regulates basal and cAMP- dependent transcriptional avtivity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions Not Available
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • None
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 55960496 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID P23246 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name SFPQ_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >2124 bp
ATGTCTCGGGATCGGTTCCGGAGTCGTGGCGGTGGCGGTGGTGGCTTCCACAGGCGTGGA
GGAGGCGGCGGCCGCGGCGGCCTCCACGACTTCCGTTCTCCGCCGCCCGGCATGGGCCTC
AATCAGAATCGCGGCCCCATGGGTCCTGGCCCGGGCCAGAGCGGCCCTAAGCCTCCGATC
CCGCCACCGCCTCCACACCAACAGCAGCAACAGCCACCACCGCAGCAGCCACCGCCGCAG
CAGCCGCCACCGCATCAGCCGCCGCCGCATCCACAGCCGCATCAGCAGCAGCAGCCGCCG
CCACCGCCGCAGGACTCTTCCAAGCCCGTCGTTGCTCAGGGACCCGGCCCCGCTCCCGGA
GTAGGCAGCGCACCACCAGCCTCCAGCTCGGCCCCGCCCGCCACTCCACCAACCTCGGGG
GCCCCGCCAGGGTCCGGGCCAGGCCCGACTCCGACCCCGCCGCCTGCAGTCACCTCGGCC
CCTCCCGGGGCGCCGCCACCCACCCCGCCAAGCAGCGGGGTCCCTACCACACCTCCTCAG
GCCGGAGGCCCGCCGCCTCCGCCCGCGGCAGTCCCGGGCCCGGGTCCAGGGCCTAAGCAG
GGCCCAGGTCCGGGTGGTCCCAAAGGCGGCAAAATGCCTGGCGGGCCGAAGCCAGGTGGC
GGCCCGGGCCTAAGTACGCCTGGCGGCCACCCCAAGCCGCCGCATCGAGGCGGCGGGGAG
CCCCGCGGGGGCCGCCAGCACCACCCGCCCTACCACCAGCAGCATCACCAGGGGCCCCCG
CCCGGCGGGCCCGGCGGCCGCAGCGAGGAGAAGATCTCGGACTCGGAGGGGTTTAAAGCC
AATTTGTCTCTCTTGAGGAGGCCTGGAGAGAAAACTTACACACAGCGATGTCGGTTGTTT
GTTGGGAATCTACCTGCTGATATCACGGAGGATGAATTCAAAAGACTATTTGCTAAATAT
GGAGAACCAGGAGAAGTTTTTATCAACAAAGGCAAAGGATTCGGATTTATTAAGCTTGAA
TCTAGAGCTTTGGCTGAAATTGCCAAAGCCGAACTGGATGATACACCCATGAGAGGTAGA
CAGCTTCGAGTTCGCTTTGCCACACATGCTGCTGCCCTTTCTGTTCGTAATCTTTCACCT
TATGTTTCCAATGAACTGTTGGAAGAAGCCTTTAGCCAATTTGGTCCTATTGAAAGGGCT
GTTGTAATAGTGGATGATCGTGGAAGATCTACAGGGAAAGGCATTGTTGAATTTGCTTCT
AAGCCAGCAGCAAGAAAGGCATTTGAACGATGCAGTGAAGGTGTTTTCTTACTGACGACA
ACTCCTCGTCCAGTCATTGTGGAACCACTTGAACAACTAGATGATGAAGATGGTCTTCCT
GAAAAACTTGCCCAGAAGAATCCAATGTATCAAAAGGAGAGAGAAACCCCTCCTCGTTTT
GCCCAGCATGGCACGTTTGAGTACGAATATTCTCAGCGATGGAAGTCTTTGGATGAAATG
GAAAAACAGCAAAGGGAACAAGTTGAAAAAAACATGAAAGATGCAAAAGACAAATTGGAA
AGTGAAATGGAAGATGCCTATCATGAACATCAGGCAAATCTTTTGCGCCAAGATCTGATG
AGACGACAGGAAGAATTAAGACGCATGGAAGAACTTCACAATCAAGAAATGCAGAAACGT
AAAGAAATGCAATTGAGGCAAGAGGAGGAACGACGTAGAAGAGAGGAAGAGATGATGATT
CGTCAACGTGAGATGGAAGAACAAATGAGGCGCCAAAGAGAGGAAAGTTACAGCCGAATG
GGCTACATGGATCCACGGGAAAGAGACATGCGAATGGGTGGCGGAGGAGCAATGAACATG
GGAGATCCCTATGGTTCAGGAGGCCAGAAATTTCCACCTCTAGGAGGTGGTGGTGGCATA
GGTTATGAAGCTAATCCTGGCGTTCCACCAGCAACCATGAGTGGTTCCATGATGGGAAGT
GACATGCGTACTGAGCGCTTTGGGCAGGGAGGTGCGGGGCCTGTGGGTGGACAGGGTCCT
AGAGGAATGGGGCCTGGAACTCCAGCAGGATATGGTAGAGGGAGAGAAGAGTACGAAGGC
CCAAACAAAAAACCCCGATTTTAG
Enzyme 51 GenBank Gene ID AL590434 Link Image
Enzyme 51 GeneCard ID SFPQ Link Image
Enzyme 51 GenAtlas ID SFPQ Link Image
Enzyme 51 HGNC ID HGNC:10774 Link Image
Enzyme 51 Chromosome Location 1
Enzyme 51 Locus 1p34.3
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References
  1. Patton JG, Porro EB, Galceran J, Tempst P, Nadal-Ginard B: Cloning and characterization of PSF, a novel pre-mRNA splicing factor. Genes Dev. 1993 Mar;7(3):393-406. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Zhang WW, Zhang LX, Busch RK, Farres J, Busch H: Purification and characterization of a DNA-binding heterodimer of 52 and 100 kDa from HeLa cells. Biochem J. 1993 Feb 15;290 ( Pt 1):267-72. [PubMed Link Image]
  4. Teigelkamp S, Mundt C, Achsel T, Will CL, Luhrmann R: The human U5 snRNP-specific 100-kD protein is an RS domain-containing, putative RNA helicase with significant homology to the yeast splicing factor Prp28p. RNA. 1997 Nov;3(11):1313-26. [PubMed Link Image]
  5. Gower HJ, Moore SE, Dickson G, Elsom VL, Nayak R, Walsh FS: Cloning and characterization of a myoblast cell surface antigen defined by 24.1D5 monoclonal antibody. Development. 1989 Apr;105(4):723-31. [PubMed Link Image]
  6. Lutz CS, Cooke C, O'Connor JP, Kobayashi R, Alwine JC: The snRNP-free U1A (SF-A) complex(es): identification of the largest subunit as PSF, the polypyrimidine-tract binding protein-associated splicing factor. RNA. 1998 Dec;4(12):1493-9. [PubMed Link Image]
  7. Meissner M, Dechat T, Gerner C, Grimm R, Foisner R, Sauermann G: Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB. J Cell Biochem. 2000 Jan;76(4):559-66. [PubMed Link Image]
  8. Gozani O, Patton JG, Reed R: A novel set of spliceosome-associated proteins and the essential splicing factor PSF bind stably to pre-mRNA prior to catalytic step II of the splicing reaction. EMBO J. 1994 Jul 15;13(14):3356-67. [PubMed Link Image]
  9. Clark J, Lu YJ, Sidhar SK, Parker C, Gill S, Smedley D, Hamoudi R, Linehan WM, Shipley J, Cooper CS: Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3 gene in papillary renal cell carcinoma. Oncogene. 1997 Oct;15(18):2233-9. [PubMed Link Image]
  10. Straub T, Grue P, Uhse A, Lisby M, Knudsen BR, Tange TO, Westergaard O, Boege F: The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I activity by a direct interaction. J Biol Chem. 1998 Oct 9;273(41):26261-4. [PubMed Link Image]
  11. Straub T, Knudsen BR, Boege F: PSF/p54(nrb) stimulates "jumping" of DNA topoisomerase I between separate DNA helices. Biochemistry. 2000 Jun 27;39(25):7552-8. [PubMed Link Image]
  12. Urban RJ, Bodenburg Y, Kurosky A, Wood TG, Gasic S: Polypyrimidine tract-binding protein-associated splicing factor is a negative regulator of transcriptional activity of the porcine p450scc insulin-like growth factor response element. Mol Endocrinol. 2000 Jun;14(6):774-82. [PubMed Link Image]
  13. Akhmedov AT, Lopez BS: Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion. Nucleic Acids Res. 2000 Aug 15;28(16):3022-30. [PubMed Link Image]
  14. Zhang Z, Carmichael GG: The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs. Cell. 2001 Aug 24;106(4):465-75. [PubMed Link Image]
  15. Shav-Tal Y, Cohen M, Lapter S, Dye B, Patton JG, Vandekerckhove J, Zipori D: Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions. Mol Biol Cell. 2001 Aug;12(8):2328-40. [PubMed Link Image]
  16. Mathur M, Tucker PW, Samuels HH: PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors. Mol Cell Biol. 2001 Apr;21(7):2298-311. [PubMed Link Image]
  17. Sewer MB, Nguyen VQ, Huang CJ, Tucker PW, Kagawa N, Waterman MR: Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, and SF-1, a complex that also participates in repression of transcription. Endocrinology. 2002 Apr;143(4):1280-90. [PubMed Link Image]
  18. Peng R, Dye BT, Perez I, Barnard DC, Thompson AB, Patton JG: PSF and p54nrb bind a conserved stem in U5 snRNA. RNA. 2002 Oct;8(10):1334-47. [PubMed Link Image]
  19. Ong SE, Mittler G, Mann M: Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nat Methods. 2004 Nov;1(2):119-26. Epub 2004 Oct 21. [PubMed Link Image]
  20. Bladen CL, Udayakumar D, Takeda Y, Dynan WS: Identification of the polypyrimidine tract binding protein-associated splicing factor.p54(nrb) complex as a candidate DNA double-strand break rejoining factor. J Biol Chem. 2005 Feb 18;280(7):5205-10. Epub 2004 Dec 7. [PubMed Link Image]
  21. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  22. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  23. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  24. Miyamoto K, Sakurai H, Sugiura T: Proteomic identification of a PSF/p54nrb heterodimer as RNF43 oncoprotein-interacting proteins. Proteomics. 2008 Jul;8(14):2907-10. [PubMed Link Image]
  25. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  26. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  27. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 7390
Enzyme 52 Name Ras-related protein Rap-1A
Enzyme 52 Synonyms
  1. C21KG
  2. G-22K
  3. GTP-binding protein smg p21A
  4. Ras-related protein Krev-1
Enzyme 52 Gene Name RAP1A
Enzyme 52 Protein Sequence >Ras-related protein Rap-1A
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAG
TEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDL
EDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINRKTPVEKKKPKKKS
CLLL
Enzyme 52 Number of Residues 184
Enzyme 52 Molecular Weight 20987.1
Enzyme 52 Theoretical pI 6.55
Enzyme 52 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
  • membrane
Enzyme 52 General Function Involved in GTP binding
Enzyme 52 Specific Function Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions Not Available
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 20147717 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID P62834 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name RAP1A_HUMAN Link Image
Enzyme 52 PDB ID 1C1Y Link Image
Enzyme 52 PDB File Show
Enzyme 52 3D Structure
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >555 bp
ATGCGTGAGTACAAGCTAGTGGTCCTTGGTTCAGGAGGCGTTGGGAAGTCTGCTCTGACA
GTTCAGTTTGTTCAGGGAATTTTTGTTGAAAAATATGACCCAACGATAGAAGATTCCTAC
AGAAAGCAAGTTGAAGTCGATTGCCAACAGTGTATGCTCGAAATCCTGGATACTGCAGGG
ACAGAGCAATTTACAGCAATGAGGGATTTGTATATGAAGAACGGCCAAGGTTTTGCACTA
GTATATTCTATTACAGCTCAGTCCACGTTTAACGACTTACAGGACCTGAGGGAACAGATT
TTACGGGTTAAGGACACGGAAGATGTTCCAATGATTTTGGTTGGCAATAAATGTGACCTG
GAAGATGAGCGAGTAGTTGGCAAAGAGCAGGGCCAGAATTTAGCAAGACAGTGGTGTAAC
TGTGCCTTTTTAGAATCTTCTGCAAAGTCAAAGATCAATGTTAATGAGATATTTTATGAC
CTGGTCAGACAGATAAATAGGAAAACACCAGTGGAAAAGAAGAAGCCTAAAAAGAAATCA
TGTCTGCTGCTCTAG
Enzyme 52 GenBank Gene ID AF493912 Link Image
Enzyme 52 GeneCard ID RAP1A Link Image
Enzyme 52 GenAtlas ID RAP1A Link Image
Enzyme 52 HGNC ID HGNC:9855 Link Image
Enzyme 52 Chromosome Location 1
Enzyme 52 Locus 1p13.3
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References
  1. Pizon V, Chardin P, Lerosey I, Olofsson B, Tavitian A: Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region. Oncogene. 1988 Aug;3(2):201-4. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Nagata K, Itoh H, Katada T, Takenaka K, Ui M, Kaziro Y, Nozawa Y: Purification, identification, and characterization of two GTP-binding proteins with molecular weights of 25,000 and 21,000 in human platelet cytosol. One is the rap1/smg21/Krev-1 protein and the other is a novel GTP-binding protein. J Biol Chem. 1989 Oct 15;264(29):17000-5. [PubMed Link Image]
  5. Bokoch GM, Parkos CA, Mumby SM: Purification and characterization of the 22,000-dalton GTP-binding protein substrate for ADP-ribosylation by botulinum toxin, G22K. J Biol Chem. 1988 Nov 15;263(32):16744-9. [PubMed Link Image]
  6. Ohmori T, Kikuchi A, Yamamoto K, Kawata M, Kondo J, Takai Y: Identification of a platelet Mr 22,000 GTP-binding protein as the novel smg-21 gene product having the same putative effector domain as the ras gene products. Biochem Biophys Res Commun. 1988 Dec 15;157(2):670-6. [PubMed Link Image]
  7. Buss JE, Quilliam LA, Kato K, Casey PJ, Solski PA, Wong G, Clark R, McCormick F, Bokoch GM, Der CJ: The COOH-terminal domain of the Rap1A (Krev-1) protein is isoprenylated and supports transformation by an H-Ras:Rap1A chimeric protein. Mol Cell Biol. 1991 Mar;11(3):1523-30. [PubMed Link Image]
  8. Song C, Hu CD, Masago M, Kariyai K, Yamawaki-Kataoka Y, Shibatohge M, Wu D, Satoh T, Kataoka T: Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras. J Biol Chem. 2001 Jan 26;276(4):2752-7. Epub 2000 Oct 5. [PubMed Link Image]
  9. Song C, Satoh T, Edamatsu H, Wu D, Tadano M, Gao X, Kataoka T: Differential roles of Ras and Rap1 in growth factor-dependent activation of phospholipase C epsilon. Oncogene. 2002 Nov 21;21(53):8105-13. [PubMed Link Image]
  10. Smolen GA, Schott BJ, Stewart RA, Diederichs S, Muir B, Provencher HL, Look AT, Sgroi DC, Peterson RT, Haber DA: A Rap GTPase interactor, RADIL, mediates migration of neural crest precursors. Genes Dev. 2007 Sep 1;21(17):2131-6. Epub 2007 Aug 17. [PubMed Link Image]
  11. Yang H, Sasaki T, Minoshima S, Shimizu N: Identification of three novel proteins (SGSM1, 2, 3) which modulate small G protein (RAP and RAB)-mediated signaling pathway. Genomics. 2007 Aug;90(2):249-60. Epub 2007 May 23. [PubMed Link Image]
  12. Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A: The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature. 1995 Jun 15;375(6532):554-60. [PubMed Link Image]
  13. Nassar N, Horn G, Herrmann C, Block C, Janknecht R, Wittinghofer A: Ras/Rap effector specificity determined by charge reversal. Nat Struct Biol. 1996 Aug;3(8):723-9. [PubMed Link Image]
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 7577
Enzyme 53 Name Calcitonin gene-related peptide 1
Enzyme 53 Synonyms
  1. Alpha-type CGRP
  2. Calcitonin gene-related peptide I
  3. CGRP-I
Enzyme 53 Gene Name CALCA
Enzyme 53 Protein Sequence >Calcitonin gene-related peptide 1
MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQNYVQ
MKASELEQEQEREGSRIIAQKRACDTATCVTHRLAGLLSRSGGVVKNNFVPTNVGSKAFG
RRRRDLQA
Enzyme 53 Number of Residues 128
Enzyme 53 Molecular Weight 13897.8
Enzyme 53 Theoretical pI 9.97
Enzyme 53 GO Classification
Function
  • binding
  • hormone activity
  • protein binding
  • receptor binding
Process
  • circulatory system process
  • multicellular organismal process
  • regulation of blood vessel size
  • system process
  • vascular process in circulatory system
  • vasodilation
Component
  • extracellular region
Enzyme 53 General Function Involved in hormone activity
Enzyme 53 Specific Function CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role. It also elevates platelet cAMP
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions Not Available
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • 1-25
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein 76880478 Link Image
Enzyme 53 UniProtKB/Swiss-Prot ID P06881 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name CALCA_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >387 bp
ATGGGCTTCCAAAAGTTCTCCCCCTTCCTGGCTCTCAGCATCTTGGTCCTGTTGCAGGCA
GGCAGCCTCCATGCAGCACCATTCAGGTCTGCCCTGGAGAGCAGCCCAGCAGACCCGGCC
ACGCTCAGTGAGGACGAAGCGCGCCTCCTGCTGGCTGCACTGGTGCAGGACTATGTGCAG
ATGAAGGCCAGTGAGCTGGAGCAGGAGCAAGAGAGAGAGGGCTCCAGAATCATTGCCCAG
AAGAGAGCCTGTGACACTGCCACCTGTGTGACTCATCGGCTGGCAGGCTTGCTGAGCAGA
TCAGGGGGTGTGGTGAAGAACAACTTTGTGCCCACCAATGTGGGTTCCAAAGCCTTTGGC
AGGCGCCGCAGGGACCTTCAAGCCTGA
Enzyme 53 GenBank Gene ID NM_001033953.2 Link Image
Enzyme 53 GeneCard ID CALCA Link Image
Enzyme 53 GenAtlas ID CALCA Link Image
Enzyme 53 HGNC ID HGNC:1437 Link Image
Enzyme 53 Chromosome Location Not Available
Enzyme 53 Locus Not Available
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 General References
  1. Jonas V, Lin CR, Kawashima E, Semon D, Swanson LW, Mermod JJ, Evans RM, Rosenfeld MG: Alternative RNA processing events in human calcitonin/calcitonin gene-related peptide gene expression. Proc Natl Acad Sci U S A. 1985 Apr;82(7):1994-8. [PubMed Link Image]
  2. Broad PM, Symes AJ, Thakker RV, Craig RK: Structure and methylation of the human calcitonin/alpha-CGRP gene. Nucleic Acids Res. 1989 Sep 12;17(17):6999-7011. [PubMed Link Image]
  3. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
  4. Nelkin BD, Rosenfeld KI, de Bustros A, Leong SS, Roos BA, Baylin SB: Structure and expression of a gene encoding human calcitonin and calcitonin gene related peptide. Biochem Biophys Res Commun. 1984 Sep 17;123(2):648-55. [PubMed Link Image]
  5. Edbrooke MR, Parker D, McVey JH, Riley JH, Sorenson GD, Pettengill OS, Craig RK: Expression of the human calcitonin/CGRP gene in lung and thyroid carcinoma. EMBO J. 1985 Mar;4(3):715-24. [PubMed Link Image]
  6. Steenbergh PH, Hoppener JW, Zandberg J, Van de Ven WJ, Jansz HS, Lips CJ: Calcitonin gene related peptide coding sequence is conserved in the human genome and is expressed in medullary thyroid carcinoma. J Clin Endocrinol Metab. 1984 Aug;59(2):358-60. [PubMed Link Image]
  7. Craig RK, Riley JH, Edbrooke MR, Broad PM, Foord SM, Al-Kazwini SJ, Holman JJ, Marshall I: Expression and function of the human calcitonin/alpha-CGRP gene in health and disease. Biochem Soc Symp. 1986;52:91-105. [PubMed Link Image]
  8. Morris HR, Panico M, Etienne T, Tippins J, Girgis SI, MacIntyre I: Isolation and characterization of human calcitonin gene-related peptide. Nature. 1984 Apr 19-25;308(5961):746-8. [PubMed Link Image]
  9. Petermann JB, Born W, Chang JY, Fischer JA: Identification in the human central nervous system, pituitary, and thyroid of a novel calcitonin gene-related peptide, and partial amino acid sequence in the spinal cord. J Biol Chem. 1987 Jan 15;262(2):542-5. [PubMed Link Image]
  10. Kitamura K, Kangawa K, Kawamoto M, Ichiki Y, Matsuo H, Eto T: Isolation and characterization of peptides which act on rat platelets, from a pheochromocytoma. Biochem Biophys Res Commun. 1992 May 29;185(1):134-41. [PubMed Link Image]
  11. Breeze AL, Harvey TS, Bazzo R, Campbell ID: Solution structure of human calcitonin gene-related peptide by 1H NMR and distance geometry with restrained molecular dynamics. Biochemistry. 1991 Jan 15;30(2):575-82. [PubMed Link Image]
  12. Hubbard JA, Martin SR, Chaplin LC, Bose C, Kelly SM, Price NC: Solution structures of calcitonin-gene-related-peptide analogues of calcitonin-gene-related peptide and amylin. Biochem J. 1991 May 1;275 ( Pt 3):785-8. [PubMed Link Image]
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 7615
Enzyme 54 Name Cyclic AMP-responsive element-binding protein 1
Enzyme 54 Synonyms
  1. CREB-1
  2. cAMP-responsive element-binding protein 1
Enzyme 54 Gene Name CREB1
Enzyme 54 Protein Sequence >Cyclic AMP-responsive element-binding protein 1
MTMESGAENQQSGDAAVTEAENQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPN
GQTVQVHGVIQAAQPSVIQSPQVQTVQSSCKDLKRLFSGTQISTIAESEDSQESVDSVTD
SQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSG
QYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQV
VVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAAREC
RRKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKSD
Enzyme 54 Number of Residues 341
Enzyme 54 Molecular Weight 36687.9
Enzyme 54 Theoretical pI 5.24
Enzyme 54 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
  • protein binding
  • protein dimerization activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 54 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 54 Specific Function This protein binds the cAMP response element (CRE), a sequence present in many viral and cellular promoters. CREB stimulates transcription on binding to the CRE. Transcription activation is enhanced by the TORC coactivators which act independently of Ser-133 phosphorylation. Implicated in synchronization of circadian rhythmicity
Enzyme 54 Pathways Not Available
Enzyme 54 Reactions Not Available
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein 287638 Link Image
Enzyme 54 UniProtKB/Swiss-Prot ID P16220 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name CREB1_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >1026 bp
ATGACCATGGAATCTGGAGCCGAGAACCAGCAGAGTGGAGATGCAGCTGTAACAGAAGCT
GAAAACCAACAAATGACAGTTCAAGCCCAGCCACAGATTGCCACATTAGCCCAGGTATCT
ATGCCAGCAGCTCATGCAACATCATCTGCTCCCACCGTAACTCTAGTACAGCTGCCCAAT
GGGCAGACAGTTCAAGTCCATGGAGTCATTCAGGCGGCCCAGCCATCAGTTATTCAGTCT
CCACAAGTCCAAACAGTTCAGTCTTCCTGTAAGGACTTAAAAAGACTTTTCTCCGGAACA
CAGATTTCAACTATTGCAGAAAGTGAAGATTCACAGGAGTCAGTGGATAGTGTAACTGAT
TCCCAAAAGCGAAGGGAAATTCTTTCAAGGAGGCCTTCCTACAGGAAAATTTTGAATGAC
TTATCTTCTGATGCACCAGGAGTGCCAAGGATTGAAGAAGAGAAGTCTGAAGAGGAGACT
TCAGCACCTGCCATCACCACTGTAACGGTGCCAACTCCAATTTACCAAACTAGCAGTGGA
CAGTATATTGCCATTACCCAGGGAGGAGCAATACAGCTGGCTAACAATGGTACCGATGGG
GTACAGGGCCTGCAAACATTAACCATGACCAATGCAGCAGCCACTCAGCCGGGTACTACC
ATTCTACAGTATGCACAGACCACTGATGGACAGCAGATCTTAGTGCCCAGCAACCAAGTT
GTTGTTCAAGCTGCCTCTGGAGACGTACAAACATACCAGATTCGCACAGCACCCACTAGC
ACTATTGCCCCTGGAGTTGTTATGGCATCCTCCCCAGCACTTCCTACACAGCCTGCTGAA
GAAGCAGCACGAAAGAGAGAGGTCCGTCTAATGAAGAACAGGGAAGCAGCTCGAGAGTGT
CGTAGAAAGAAGAAAGAATATGTGAAATGTTTAGAAAACAGAGTGGCAGTGCTTGAAAAT
CAAAACAAGACATTGATTGAGGAGCTAAAAGCACTTAAGGACCTTTACTGCCACAAATCA
GATTAA
Enzyme 54 GenBank Gene ID X55545 Link Image
Enzyme 54 GeneCard ID CREB1 Link Image
Enzyme 54 GenAtlas ID CREB1 Link Image
Enzyme 54 HGNC ID HGNC:2345 Link Image
Enzyme 54 Chromosome Location 2
Enzyme 54 Locus 2q34
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References
  1. Berkowitz LA, Gilman MZ: Two distinct forms of active transcription factor CREB (cAMP response element binding protein). Proc Natl Acad Sci U S A. 1990 Jul;87(14):5258-62. [PubMed Link Image]
  2. Yoshimura T, Fujisawa J, Yoshida M: Multiple cDNA clones encoding nuclear proteins that bind to the tax-dependent enhancer of HTLV-1: all contain a leucine zipper structure and basic amino acid domain. EMBO J. 1990 Aug;9(8):2537-42. [PubMed Link Image]
  3. Waeber G, Meyer TE, Hoeffler JP, Habener JF: Diversification of cyclic AMP-responsive enhancer binding proteins-generated by alternative exon splicing. Trans Assoc Am Physicians. 1990;103:28-37. [PubMed Link Image]
  4. Hoeffler JP, Meyer TE, Yun Y, Jameson JL, Habener JF: Cyclic AMP-responsive DNA-binding protein: structure based on a cloned placental cDNA. Science. 1988 Dec 9;242(4884):1430-3. [PubMed Link Image]
  5. Short ML, Manohar CF, Furtado MR, Ghadge GD, Wolinsky SM, Thimmapaya B, Jungmann RA: Nucleotide and derived amino-acid sequences of the CRE-binding proteins from rat C6 glioma and HeLa cells. Nucleic Acids Res. 1991 Aug 11;19(15):4290. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
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  9. Zhao LJ, Giam CZ: Human T-cell lymphotropic virus type I (HTLV-I) transcriptional activator, Tax, enhances CREB binding to HTLV-I 21-base-pair repeats by protein-protein interaction. Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):7070-4. [PubMed Link Image]
  10. Lee HJ, Mignacca RC, Sakamoto KM: Transcriptional activation of egr-1 by granulocyte-macrophage colony-stimulating factor but not interleukin 3 requires phosphorylation of cAMP response element-binding protein (CREB) on serine 133. J Biol Chem. 1995 Jul 7;270(27):15979-83. [PubMed Link Image]
  11. Conkright MD, Canettieri G, Screaton R, Guzman E, Miraglia L, Hogenesch JB, Montminy M: TORCs: transducers of regulated CREB activity. Mol Cell. 2003 Aug;12(2):413-23. [PubMed Link Image]
  12. Iourgenko V, Zhang W, Mickanin C, Daly I, Jiang C, Hexham JM, Orth AP, Miraglia L, Meltzer J, Garza D, Chirn GW, McWhinnie E, Cohen D, Skelton J, Terry R, Yu Y, Bodian D, Buxton FP, Zhu J, Song C, Labow MA: Identification of a family of cAMP response element-binding protein coactivators by genome-scale functional analysis in mammalian cells. Proc Natl Acad Sci U S A. 2003 Oct 14;100(21):12147-52. Epub 2003 Sep 23. [PubMed Link Image]
  13. Screaton RA, Conkright MD, Katoh Y, Best JL, Canettieri G, Jeffries S, Guzman E, Niessen S, Yates JR 3rd, Takemori H, Okamoto M, Montminy M: The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector. Cell. 2004 Oct 1;119(1):61-74. [PubMed Link Image]
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Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 7617
Enzyme 55 Name Thyrotropin receptor
Enzyme 55 Synonyms
  1. Thyroid-stimulating hormone receptor
  2. TSH-R
Enzyme 55 Gene Name TSHR
Enzyme 55 Protein Sequence >Thyrotropin receptor
MRPADLLQLVLLLDLPRDLGGMGCSSPPCECHQEEDFRVTCKDIQRIPSLPPSTQTLKLI
ETHLRTIPSHAFSNLPNISRIYVSIDVTLQQLESHSFYNLSKVTHIEIRNTRNLTYIDPD
ALKELPLLKFLGIFNTGLKMFPDLTKVYSTDIFFILEITDNPYMTSIPVNAFQGLCNETL
TLKLYNNGFTSVQGYAFNGTKLDAVYLNKNKYLTVIDKDAFGGVYSGPSLLDVSQTSVTA
LPSKGLEHLKELIARNTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILESLM
CNESSMQSLRQRKSVNALNSPLHQEYEENLGDSIVGYKEKSKFQDTHNNAHYYVFFEEQE
DEIIGFGQELKNPQEETLQAFDSHYDYTICGDSEDMVCTPKSDEFNPCEDIMGYKFLRIV
VWFVSLLALLGNVFVLLILLTSHYKLNVPRFLMCNLAFADFCMGMYLLLIASVDLYTHSE
YYNHAIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKIRLRHACA
IMVGGWVCCFLLALLPLVGISSYAKVSICLPMDTETPLALAYIVFVLTLNIVAFVIVCCC
YVKIYITVRNPQYNPGDKDTKIAKRMAVLIFTDFICMAPISFYALSAILNKPLITVSNSK
ILLVLFYPLNSCANPFLYAIFTKAFQRDVFILLSKFGICKRQAQAYRGQRVPPKNSTDIQ
VQKVTHDMRQGLHNMEDVYELIENSHLTPKKQGQISEEYMQTVL
Enzyme 55 Number of Residues 764
Enzyme 55 Molecular Weight 86829.0
Enzyme 55 Theoretical pI 6.98
Enzyme 55 GO Classification
Function
  • G-protein coupled receptor activity
  • molecular transducer activity
  • protein-hormone receptor activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 55 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 55 Specific Function Receptor for thyrothropin. Plays a central role in controlling thyroid cell metabolism. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Also acts as a receptor for thyrostimulin (GPA2+GPB5)
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions Not Available
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • 1-20
Enzyme 55 Transmembrane Regions
  • 414-441 451-473 495-517 538-560 581-602 626-649 661-682
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 64085121 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID P16473 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name TSHR_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >2295 bp
ATGAGGCCGGCGGACTTGCTGCAGCTGGTGCTGCTGCTCGACCTGCCCAGGGACCTGGGC
GGAATGGGGTGTTCGTCTCCACCCTGCGAGTGCCATCAGGAGGAGGACTTCAGAGTCACC
TGCAAGGATATTCAACGCATCCCCAGCTTACCGCCCAGTACGCAGACTCTGAAGCTTATT
GAGACTCACCTGAGAACTATTCCAAGTCATGCATTTTCTAATCTGCCCAATATTTCCAGA
ATCTACGTATCTATAGATGTGACTCTGCAGCAGCTGGAATCACACTCCTTCTACAATTTG
AGTAAAGTGACTCACATAGAAATTCGGAATACCAGGAACTTAACTTACATAGACCCTGAT
GCCCTCAAAGAGCTCCCCCTCCTAAAGTTCCTTGGCATTTTCAACACTGGACTTAAAATG
TTCCCTGACCTGACCAAAGTTTATTCCACTGATATATTCTTTATACTTGAAATTACAGAC
AACCCTTACATGACGTCAATCCCTGTGAATGCTTTTCAGGGACTATGCAATGAAACCTTG
ACACTGAAGCTGTACAACAATGGCTTTACTTCAGTCCAAGGATATGCTTTCAATGGGACA
AAGCTGGATGCTGTTTACCTAAACAAGAATAAATACCTGACAGTTATTGACAAAGATGCA
TTTGGAGGAGTATACAGTGGACCAAGCTTGCTGGACGTGTCTCAAACCAGTGTCACTGCC
CTTCCATCCAAAGGCCTGGAGCACCTGAAGGAACTGATAGCAAGAAACACCTGGACTCTT
AAGAAACTTCCACTTTCCTTGAGTTTCCTTCACCTCACACGGGCTGACCTTTCTTACCCA
AGCCACTGCTGTGCTTTTAAGAATCAGAAGAAAATCAGAGGAATCCTTGAGTCCTTGATG
TGTAATGAGAGCAGTATGCAGAGCTTGCGCCAGAGAAAATCTGTGAATGCCTTGAATAGC
CCCCTCCACCAGGAATATGAAGAGAATCTGGGTGACAGCATTGTTGGGTACAAGGAAAAG
TCCAAGTTCCAGGATACTCATAACAACGCTCATTATTACGTCTTCTTTGAAGAACAAGAG
GATGAGATCATTGGTTTTGGCCAGGAGCTCAAAAACCCCCAGGAAGAGACTCTACAAGCT
TTTGACAGCCATTATGACTACACCATATGTGGGGACAGTGAAGACATGGTGTGTACCCCC
AAGTCCGATGAGTTCAACCCGTGTGAAGACATAATGGGCTACAAGTTCCTGAGAATTGTG
GTGTGGTTCGTTAGTCTGCTGGCTCTCCTGGGCAATGTCTTTGTCCTGCTTATTCTCCTC
ACCAGCCACTACAAACTGAACGTCCCCCGCTTTCTCATGTGCAACCTGGCCTTTGCGGAT
TTCTGCATGGGGATGTACCTGCTCCTCATCGCCTCTGTAGACCTCTACACTCACTCTGAG
TACTACAACCATGCCATCGACTGGCAGACAGGCCCTGGGTGCAACACGGCTGGTTTCTTC
ACTGTCTTTGCAAGCGAGTTATCGGTGTATACGCTGACGGTCATCACCCTGGAGCGCTGG
TATGCCATCACCTTCGCCATGCGCCTGGACCGGAAGATCCGCCTCAGGCACGCATGTGCC
ATCATGGTTGGGGGCTGGGTTTGCTGCTTCCTTCTCGCCCTGCTTCCTTTGGTGGGAATA
AGTAGCTATGCCAAAGTCAGTATCTGCCTGCCCATGGACACCGAGACCCCTCTTGCTCTG
GCATATATTGTTTTTGTTCTGACGCTCAACATAGTTGCCTTCGTCATCGTCTGCTGCTGT
TATGTGAAGATCTACATCACAGTCCGAAATCCGCAGTACAACCCAGGGGACAAAGATACC
AAAATTGCCAAGAGGATGGCTGTGTTGATCTTCACCGACTTCATATGCATGGCCCCAATC
TCATTCTATGCTCTGTCAGCAATTCTGAACAAGCCTCTCATCACTGTTAGCAACTCCAAA
ATCTTGCTGGTACTCTTCTATCCACTTAACTCCTGTGCCAATCCATTCCTCTATGCTATT
TTCACCAAGGCCTTCCAGAGGGATGTGTTCATCCTACTCAGCAAGTTTGGCATCTGTAAA
CGCCAGGCTCAGGCATACCGGGGGCAGAGGGTTCCTCCAAAGAACAGCACTGATATTCAG
GTTCAAAAGGTTACCCACGAGATGAGGCAGGGTCTCCACAACATGGAAGATGTCTATGAA
CTGATTGAAAACTCCCATCTAACCCCAAAGAAGCAAGGCCAAATCTCAGAAGAGTATATG
CAAACGGTTTTGTAA
Enzyme 55 GenBank Gene ID NM_000369.2 Link Image
Enzyme 55 GeneCard ID TSHR Link Image
Enzyme 55 GenAtlas ID TSHR Link Image
Enzyme 55 HGNC ID HGNC:12373 Link Image
Enzyme 55 Chromosome Location 1
Enzyme 55 Locus 14q31
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
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  2. Libert F, Lefort A, Gerard C, Parmentier M, Perret J, Ludgate M, Dumont JE, Vassart G: Cloning, sequencing and expression of the human thyrotropin (TSH) receptor: evidence for binding of autoantibodies. Biochem Biophys Res Commun. 1989 Dec 29;165(3):1250-5. [PubMed Link Image]
  3. Misrahi M, Loosfelt H, Atger M, Sar S, Guiochon-Mantel A, Milgrom E: Cloning, sequencing and expression of human TSH receptor. Biochem Biophys Res Commun. 1990 Jan 15;166(1):394-403. [PubMed Link Image]
  4. Frazier AL, Robbins LS, Stork PJ, Sprengel R, Segaloff DL, Cone RD: Isolation of TSH and LH/CG receptor cDNAs from human thyroid: regulation by tissue specific splicing. Mol Endocrinol. 1990 Aug;4(8):1264-76. [PubMed Link Image]
  5. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  6. Graves PN, Tomer Y, Davies TF: Cloning and sequencing of a 1.3 KB variant of human thyrotropin receptor mRNA lacking the transmembrane domain. Biochem Biophys Res Commun. 1992 Sep 16;187(2):1135-43. [PubMed Link Image]
  7. Cornelis S, Uttenweiler-Joseph S, Panneels V, Vassart G, Costagliola S: Purification and characterization of a soluble bioactive amino-terminal extracellular domain of the human thyrotropin receptor. Biochemistry. 2001 Aug 21;40(33):9860-9. [PubMed Link Image]
  8. Nakabayashi K, Matsumi H, Bhalla A, Bae J, Mosselman S, Hsu SY, Hsueh AJ: Thyrostimulin, a heterodimer of two new human glycoprotein hormone subunits, activates the thyroid-stimulating hormone receptor. J Clin Invest. 2002 Jun;109(11):1445-52. [PubMed Link Image]
  9. Lahuna O, Quellari M, Achard C, Nola S, Meduri G, Navarro C, Vitale N, Borg JP, Misrahi M: Thyrotropin receptor trafficking relies on the hScrib-betaPIX-GIT1-ARF6 pathway. EMBO J. 2005 Apr 6;24(7):1364-74. Epub 2005 Mar 17. [PubMed Link Image]
  10. Jiang X, Dreano M, Buckler DR, Cheng S, Ythier A, Wu H, Hendrickson WA, el Tayar N: Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions. Structure. 1995 Dec 15;3(12):1341-53. [PubMed Link Image]
  11. Chistiakov DA, Savost'anov KV, Turakulov RI, Petunina N, Balabolkin MI, Nosikov VV: Further studies of genetic susceptibility to Graves' disease in a Russian population. Med Sci Monit. 2002 Mar;8(3):CR180-4. [PubMed Link Image]
  12. Ban Y, Greenberg DA, Concepcion ES, Tomer Y: A germline single nucleotide polymorphism at the intracellular domain of the human thyrotropin receptor does not have a major effect on the development of Graves' disease. Thyroid. 2002 Dec;12(12):1079-83. [PubMed Link Image]
  13. Ho SC, Goh SS, Khoo DH: Association of Graves' disease with intragenic polymorphism of the thyrotropin receptor gene in a cohort of Singapore patients of multi-ethnic origins. Thyroid. 2003 Jun;13(6):523-8. [PubMed Link Image]
  14. Farid NR, Kascur V, Balazs C: The human thyrotropin receptor is highly mutable: a review of gain-of-function mutations. Eur J Endocrinol. 2000 Jul;143(1):25-30. [PubMed Link Image]
  15. Heldin NE, Gustavsson B, Westermark K, Westermark B: A somatic point mutation in a putative ligand binding domain of the TSH receptor in a patient with autoimmune hyperthyroidism. J Clin Endocrinol Metab. 1991 Dec;73(6):1374-6. [PubMed Link Image]
  16. Parma J, Duprez L, Van Sande J, Cochaux P, Gervy C, Mockel J, Dumont J, Vassart G: Somatic mutations in the thyrotropin receptor gene cause hyperfunctioning thyroid adenomas. Nature. 1993 Oct 14;365(6447):649-51. [PubMed Link Image]
  17. Bahn RS, Dutton CM, Heufelder AE, Sarkar G: A genomic point mutation in the extracellular domain of the thyrotropin receptor in patients with Graves' ophthalmopathy. J Clin Endocrinol Metab. 1994 Feb;78(2):256-60. [PubMed Link Image]
  18. Porcellini A, Ciullo I, Laviola L, Amabile G, Fenzi G, Avvedimento VE: Novel mutations of thyrotropin receptor gene in thyroid hyperfunctioning adenomas. Rapid identification by fine needle aspiration biopsy. J Clin Endocrinol Metab. 1994 Aug;79(2):657-61. [PubMed Link Image]
  19. Paschke R, Tonacchera M, Van Sande J, Parma J, Vassart G: Identification and functional characterization of two new somatic mutations causing constitutive activation of the thyrotropin receptor in hyperfunctioning autonomous adenomas of the thyroid. J Clin Endocrinol Metab. 1994 Dec;79(6):1785-9. [PubMed Link Image]
  20. Duprez L, Parma J, Van Sande J, Allgeier A, Leclere J, Schvartz C, Delisle MJ, Decoulx M, Orgiazzi J, Dumont J, et al.: Germline mutations in the thyrotropin receptor gene cause non-autoimmune autosomal dominant hyperthyroidism. Nat Genet. 1994 Jul;7(3):396-401. [PubMed Link Image]
  21. Gustavsson B, Eklof C, Westermark K, Westermark B, Heldin NE: Functional analysis of a variant of the thyrotropin receptor gene in a family with Graves' disease. Mol Cell Endocrinol. 1995 Jun;111(2):167-73. [PubMed Link Image]
  22. Kopp P, van Sande J, Parma J, Duprez L, Gerber H, Joss E, Jameson JL, Dumont JE, Vassart G: Brief report: congenital hyperthyroidism caused by a mutation in the thyrotropin-receptor gene. N Engl J Med. 1995 Jan 19;332(3):150-4. [PubMed Link Image]
  23. Sunthornthepvarakui T, Gottschalk ME, Hayashi Y, Refetoff S: Brief report: resistance to thyrotropin caused by mutations in the thyrotropin-receptor gene. N Engl J Med. 1995 Jan 19;332(3):155-60. [PubMed Link Image]
  24. Ohno M, Endo T, Ohta K, Gunji K, Onaya T: Point mutations in the thyrotropin receptor in human thyroid tumors. Thyroid. 1995 Apr;5(2):97-100. [PubMed Link Image]
  25. Cuddihy RM, Bryant WP, Bahn RS: Normal function in vivo of a homozygotic polymorphism in the human thyrotropin receptor. Thyroid. 1995 Aug;5(4):255-7. [PubMed Link Image]
  26. Tonacchera M, Van Sande J, Cetani F, Swillens S, Schvartz C, Winiszewski P, Portmann L, Dumont JE, Vassart G, Parma J: Functional characteristics of three new germline mutations of the thyrotropin receptor gene causing autosomal dominant toxic thyroid hyperplasia. J Clin Endocrinol Metab. 1996 Feb;81(2):547-54. [PubMed Link Image]
  27. de Roux N, Polak M, Couet J, Leger J, Czernichow P, Milgrom E, Misrahi M: A neomutation of the thyroid-stimulating hormone receptor in a severe neonatal hyperthyroidism. J Clin Endocrinol Metab. 1996 Jun;81(6):2023-6. [PubMed Link Image]
  28. de Roux N, Misrahi M, Brauner R, Houang M, Carel JC, Granier M, Le Bouc Y, Ghinea N, Boumedienne A, Toublanc JE, Milgrom E: Four families with loss of function mutations of the thyrotropin receptor. J Clin Endocrinol Metab. 1996 Dec;81(12):4229-35. [PubMed Link Image]
  29. Russo D, Tumino S, Arturi F, Vigneri P, Grasso G, Pontecorvi A, Filetti S, Belfiore A: Detection of an activating mutation of the thyrotropin receptor in a case of an autonomously hyperfunctioning thyroid insular carcinoma. J Clin Endocrinol Metab. 1997 Mar;82(3):735-8. [PubMed Link Image]
  30. Clifton-Bligh RJ, Gregory JW, Ludgate M, John R, Persani L, Asteria C, Beck-Peccoz P, Chatterjee VK: Two novel mutations in the thyrotropin (TSH) receptor gene in a child with resistance to TSH. J Clin Endocrinol Metab. 1997 Apr;82(4):1094-100. [PubMed Link Image]
  31. Parma J, Duprez L, Van Sande J, Hermans J, Rocmans P, Van Vliet G, Costagliola S, Rodien P, Dumont JE, Vassart G: Diversity and prevalence of somatic mutations in the thyrotropin receptor and Gs alpha genes as a cause of toxic thyroid adenomas. J Clin Endocrinol Metab. 1997 Aug;82(8):2695-701. [PubMed Link Image]
  32. Biebermann H, Schoneberg T, Krude H, Schultz G, Gudermann T, Gruters A: Mutations of the human thyrotropin receptor gene causing thyroid hypoplasia and persistent congenital hypothyroidism. J Clin Endocrinol Metab. 1997 Oct;82(10):3471-80. [PubMed Link Image]
  33. Holzapfel HP, Wonerow P, von Petrykowski W, Henschen M, Scherbaum WA, Paschke R: Sporadic congenital hyperthyroidism due to a spontaneous germline mutation in the thyrotropin receptor gene. J Clin Endocrinol Metab. 1997 Nov;82(11):3879-84. [PubMed Link Image]
  34. Fuhrer D, Wonerow P, Willgerodt H, Paschke R: Identification of a new thyrotropin receptor germline mutation (Leu629Phe) in a family with neonatal onset of autosomal dominant nonautoimmune hyperthyroidism. J Clin Endocrinol Metab. 1997 Dec;82(12):4234-8. [PubMed Link Image]
  35. Abramowicz MJ, Duprez L, Parma J, Vassart G, Heinrichs C: Familial congenital hypothyroidism due to inactivating mutation of the thyrotropin receptor causing profound hypoplasia of the thyroid gland. J Clin Invest. 1997 Jun 15;99(12):3018-24. [PubMed Link Image]
  36. Kopp P, Muirhead S, Jourdain N, Gu WX, Jameson JL, Rodd C: Congenital hyperthyroidism caused by a solitary toxic adenoma harboring a novel somatic mutation (serine281-->isoleucine) in the extracellular domain of the thyrotropin receptor. J Clin Invest. 1997 Sep 15;100(6):1634-9. [PubMed Link Image]
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  39. Rodien P, Bremont C, Sanson ML, Parma J, Van Sande J, Costagliola S, Luton JP, Vassart G, Duprez L: Familial gestational hyperthyroidism caused by a mutant thyrotropin receptor hypersensitive to human chorionic gonadotropin. N Engl J Med. 1998 Dec 17;339(25):1823-6. [PubMed Link Image]
  40. Khoo DH, Parma J, Rajasoorya C, Ho SC, Vassart G: A germline mutation of the thyrotropin receptor gene associated with thyrotoxicosis and mitral valve prolapse in a Chinese family. J Clin Endocrinol Metab. 1999 Apr;84(4):1459-62. [PubMed Link Image]
  41. Gabriel EM, Bergert ER, Grant CS, van Heerden JA, Thompson GB, Morris JC: Germline polymorphism of codon 727 of human thyroid-stimulating hormone receptor is associated with toxic multinodular goiter. J Clin Endocrinol Metab. 1999 Sep;84(9):3328-35. [PubMed Link Image]
  42. Russo D, Wong MG, Costante G, Chiefari E, Treseler PA, Arturi F, Filetti S, Clark OH: A Val 677 activating mutation of the thyrotropin receptor in a Hurthle cell thyroid carcinoma associated with thyrotoxicosis. Thyroid. 1999 Jan;9(1):13-7. [PubMed Link Image]
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  44. Kosugi S, Hai N, Okamoto H, Sugawa H, Mori T: A novel activating mutation in the thyrotropin receptor gene in an autonomously functioning thyroid nodule developed by a Japanese patient. Eur J Endocrinol. 2000 Oct;143(4):471-7. [PubMed Link Image]
  45. Kaczur V, Takacs M, Szalai C, Falus A, Nagy Z, Berencsi G, Balazs C: Analysis of the genetic variability of the 1st (CCC/ACC, P52T) and the 10th exons (bp 1012-1704) of the TSH receptor gene in Graves' disease. Eur J Immunogenet. 2000 Feb;27(1):17-23. [PubMed Link Image]
  46. Tonacchera M, Agretti P, Pinchera A, Rosellini V, Perri A, Collecchi P, Vitti P, Chiovato L: Congenital hypothyroidism with impaired thyroid response to thyrotropin (TSH) and absent circulating thyroglobulin: evidence for a new inactivating mutation of the TSH receptor gene. J Clin Endocrinol Metab. 2000 Mar;85(3):1001-8. [PubMed Link Image]
  47. Tonacchera M, Agretti P, Chiovato L, Rosellini V, Ceccarini G, Perri A, Viacava P, Naccarato AG, Miccoli P, Pinchera A, Vitti P: Activating thyrotropin receptor mutations are present in nonadenomatous hyperfunctioning nodules of toxic or autonomous multinodular goiter. J Clin Endocrinol Metab. 2000 Jun;85(6):2270-4. [PubMed Link Image]
  48. Muhlberg T, Herrmann K, Joba W, Kirchberger M, Heberling HJ, Heufelder AE: Lack of association of nonautoimmune hyperfunctioning thyroid disorders and a germline polymorphism of codon 727 of the human thyrotropin receptor in a European Caucasian population. J Clin Endocrinol Metab. 2000 Aug;85(8):2640-3. [PubMed Link Image]
  49. Russo D, Betterle C, Arturi F, Chiefari E, Girelli ME, Filetti S: A novel mutation in the thyrotropin (TSH) receptor gene causing loss of TSH binding but constitutive receptor activation in a family with resistance to TSH. J Clin Endocrinol Metab. 2000 Nov;85(11):4238-42. [PubMed Link Image]
  50. Biebermann H, Schoneberg T, Krude H, Gudermann T, Gruters A: Constitutively activating TSH-receptor mutations as a molecular cause of non-autoimmune hyperthyroidism in childhood. Langenbecks Arch Surg. 2000 Oct;385(6):390-2. [PubMed Link Image]
  51. Tonacchera M, Agretti P, Rosellini V, Ceccarini G, Perri A, Zampolli M, Longhi R, Larizza D, Pinchera A, Vitti P, Chiovato L: Sporadic nonautoimmune congenital hyperthyroidism due to a strong activating mutation of the thyrotropin receptor gene. Thyroid. 2000 Oct;10(10):859-63. [PubMed Link Image]
  52. Camacho P, Gordon D, Chiefari E, Yong S, DeJong S, Pitale S, Russo D, Filetti S: A Phe 486 thyrotropin receptor mutation in an autonomously functioning follicular carcinoma that was causing hyperthyroidism. Thyroid. 2000 Nov;10(11):1009-12. [PubMed Link Image]
  53. Fuhrer D, Warner J, Sequeira M, Paschke R, Gregory J, Ludgate M: Novel TSHR germline mutation (Met463Val) masquerading as Graves' disease in a large Welsh kindred with hyperthyroidism. Thyroid. 2000 Dec;10(12):1035-41. [PubMed Link Image]
  54. Alberti L, Proverbio MC, Costagliola S, Weber G, Beck-Peccoz P, Chiumello G, Persani L: A novel germline mutation in the TSH receptor gene causes non-autoimmune autosomal dominant hyperthyroidism. Eur J Endocrinol. 2001 Sep;145(3):249-54. [PubMed Link Image]
  55. Biebermann H, Schoneberg T, Hess C, Germak J, Gudermann T, Gruters A: The first activating TSH receptor mutation in transmembrane domain 1 identified in a family with nonautoimmune hyperthyroidism. J Clin Endocrinol Metab. 2001 Sep;86(9):4429-33. [PubMed Link Image]
  56. Trulzsch B, Krohn K, Wonerow P, Chey S, Holzapfel HP, Ackermann F, Fuhrer D, Paschke R: Detection of thyroid-stimulating hormone receptor and Gsalpha mutations: in 75 toxic thyroid nodules by denaturing gradient gel electrophoresis. J Mol Med. 2001;78(12):684-91. [PubMed Link Image]
  57. Nagashima T, Murakami M, Onigata K, Morimura T, Nagashima K, Mori M, Morikawa A: Novel inactivating missense mutations in the thyrotropin receptor gene in Japanese children with resistance to thyrotropin. Thyroid. 2001 Jun;11(6):551-9. [PubMed Link Image]
  58. Vanvooren V, Uchino S, Duprez L, Costa MJ, Vandekerckhove J, Parma J, Vassart G, Dumont JE, Van Sande J, Noguchi S: Oncogenic mutations in the thyrotropin receptor of autonomously functioning thyroid nodules in the Japanese population. Eur J Endocrinol. 2002 Sep;147(3):287-91. [PubMed Link Image]
  59. Alberti L, Proverbio MC, Costagliola S, Romoli R, Boldrighini B, Vigone MC, Weber G, Chiumello G, Beck-Peccoz P, Persani L: Germline mutations of TSH receptor gene as cause of nonautoimmune subclinical hypothyroidism. J Clin Endocrinol Metab. 2002 Jun;87(6):2549-55. [PubMed Link Image]
  60. Sykiotis GP, Neumann S, Georgopoulos NA, Sgourou A, Papachatzopoulou A, Markou KB, Kyriazopoulou V, Paschke R, Vagenakis AG, Papavassiliou AG: Functional significance of the thyrotropin receptor germline polymorphism D727E. Biochem Biophys Res Commun. 2003 Feb 21;301(4):1051-6. [PubMed Link Image]
  61. Peeters RP, van Toor H, Klootwijk W, de Rijke YB, Kuiper GG, Uitterlinden AG, Visser TJ: Polymorphisms in thyroid hormone pathway genes are associated with plasma TSH and iodothyronine levels in healthy subjects. J Clin Endocrinol Metab. 2003 Jun;88(6):2880-8. [PubMed Link Image]
  62. Tonacchera M, Perri A, De Marco G, Agretti P, Montanelli L, Banco ME, Corrias A, Bellone J, Tosi MT, Vitti P, Martino E, Pinchera A, Chiovato L: TSH receptor and Gs(alpha) genetic analysis in children with Down's syndrome and subclinical hypothyroidism. J Endocrinol Invest. 2003 Oct;26(10):997-1000. [PubMed Link Image]
  63. Park SM, Clifton-Bligh RJ, Betts P, Chatterjee VK: Congenital hypothyroidism and apparent athyreosis with compound heterozygosity or compensated hypothyroidism with probable hemizygosity for inactivating mutations of the TSH receptor. Clin Endocrinol (Oxf). 2004 Feb;60(2):220-7. [PubMed Link Image]
  64. Vaidya B, Campbell V, Tripp JH, Spyer G, Hattersley AT, Ellard S: Premature birth and low birth weight associated with nonautoimmune hyperthyroidism due to an activating thyrotropin receptor gene mutation. Clin Endocrinol (Oxf). 2004 Jun;60(6):711-8. [PubMed Link Image]
  65. Tonacchera M, Perri A, De Marco G, Agretti P, Banco ME, Di Cosmo C, Grasso L, Vitti P, Chiovato L, Pinchera A: Low prevalence of thyrotropin receptor mutations in a large series of subjects with sporadic and familial nonautoimmune subclinical hypothyroidism. J Clin Endocrinol Metab. 2004 Nov;89(11):5787-93. [PubMed Link Image]
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 7660
Enzyme 56 Name Glial cell line-derived neurotrophic factor
Enzyme 56 Synonyms
  1. hGDNF
  2. Astrocyte-derived trophic factor
  3. ATF
Enzyme 56 Gene Name GDNF
Enzyme 56 Protein Sequence >Glial cell line-derived neurotrophic factor
MKLWDVVAVCLVLLHTASAFPLPAGKRPPEAPAEDRSLGRRRAPFALSSDSNMPEDYPDQ
FDDVMDFIQATIKRLKRSPDKQMAVLPRRERNRQAAAANPENSRGKGRRGQRGKNRGCVL
TAIHLNVTDLGLGYETKEELIFRYCSGSCDAAETTYDKILKNLSRNRRLVSDKVGQACCR
PIAFDDDLSFLDDNLVYHILRKHSAKRCGCI
Enzyme 56 Number of Residues 211
Enzyme 56 Molecular Weight 23719.8
Enzyme 56 Theoretical pI 9.34
Enzyme 56 GO Classification
Function
  • binding
  • growth factor activity
  • protein binding
  • receptor binding
Process
Component
Enzyme 56 General Function Involved in growth factor activity
Enzyme 56 Specific Function Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake
Enzyme 56 Pathways Not Available
Enzyme 56 Reactions Not Available
Enzyme 56 Pfam Domain Function
Enzyme 56 Signals
  • 1-19
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein 4503975 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID P39905 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name GDNF_HUMAN Link Image
Enzyme 56 PDB ID 1AGQ Link Image
Enzyme 56 PDB File Show
Enzyme 56 3D Structure
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence >636 bp
ATGAAGTTATGGGATGTCGTGGCTGTCTGCCTGGTGCTGCTCCACACCGCGTCCGCCTTC
CCGCTGCCCGCCGGTAAGAGGCCTCCCGAGGCGCCCGCCGAAGACCGCTCCCTCGGCCGC
CGCCGCGCGCCCTTCGCGCTGAGCAGTGACTCAAATATGCCAGAGGATTATCCTGATCAG
TTCGATGATGTCATGGATTTTATTCAAGCCACCATTAAAAGACTGAAAAGGTCACCAGAT
AAACAAATGGCAGTGCTTCCTAGAAGAGAGCGGAATCGGCAGGCTGCAGCTGCCAACCCA
GAGAATTCCAGAGGAAAAGGTCGGAGAGGCCAGAGGGGCAAAAACCGGGGTTGTGTCTTA
ACTGCAATACATTTAAATGTCACTGACTTGGGTCTGGGCTATGAAACCAAGGAGGAACTG
ATTTTTAGGTACTGCAGCGGCTCTTGCGATGCAGCTGAGACAACGTACGACAAAATATTG
AAAAACTTATCCAGAAATAGAAGGCTGGTGAGTGACAAAGTAGGGCAGGCATGTTGCAGA
CCCATCGCCTTTGATGATGACCTGTCGTTTTTAGATGATAACCTGGTTTACCATATTCTA
AGAAAGCATTCCGCTAAAAGGTGTGGATGTATCTGA
Enzyme 56 GenBank Gene ID NM_000514.3 Link Image
Enzyme 56 GeneCard ID GDNF Link Image
Enzyme 56 GenAtlas ID GDNF Link Image
Enzyme 56 HGNC ID HGNC:4232 Link Image
Enzyme 56 Chromosome Location 5
Enzyme 56 Locus 5p13.1-p12
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 General References
  1. Lin LF, Doherty DH, Lile JD, Bektesh S, Collins F: GDNF: a glial cell line-derived neurotrophic factor for midbrain dopaminergic neurons. Science. 1993 May 21;260(5111):1130-2. [PubMed Link Image]
  2. Schaar DG, Sieber BA, Sherwood AC, Dean D, Mendoza G, Ramakrishnan L, Dreyfus CF, Black IB: Multiple astrocyte transcripts encode nigral trophic factors in rat and human. Exp Neurol. 1994 Dec;130(2):387-93. [PubMed Link Image]
  3. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Baecker PA, Lee WH, Verity AN, Eglen RM, Johnson RM: Characterization of a promoter for the human glial cell line-derived neurotrophic factor gene. Brain Res Mol Brain Res. 1999 Jun 8;69(2):209-22. [PubMed Link Image]
  6. Grimm L, Holinski-Feder E, Teodoridis J, Scheffer B, Schindelhauer D, Meitinger T, Ueffing M: Analysis of the human GDNF gene reveals an inducible promoter, three exons, a triplet repeat within the 3'-UTR and alternative splice products. Hum Mol Genet. 1998 Nov;7(12):1873-86. [PubMed Link Image]
  7. Haniu M, Hui J, Young Y, Le J, Katta V, Lee R, Shimamoto G, Rohde MF: Glial cell line-derived neurotrophic factor: selective reduction of the intermolecular disulfide linkage and characterization of its disulfide structure. Biochemistry. 1996 Dec 24;35(51):16799-805. [PubMed Link Image]
  8. Hofstra RM, Osinga J, Buys CH: Mutations in Hirschsprung disease: when does a mutation contribute to the phenotype. Eur J Hum Genet. 1997 Jul-Aug;5(4):180-5. [PubMed Link Image]
  9. Ivanchuk SM, Myers SM, Eng C, Mulligan LM: De novo mutation of GDNF, ligand for the RET/GDNFR-alpha receptor complex, in Hirschsprung disease. Hum Mol Genet. 1996 Dec;5(12):2023-6. [PubMed Link Image]
  10. Angrist M, Bolk S, Halushka M, Lapchak PA, Chakravarti A: Germline mutations in glial cell line-derived neurotrophic factor (GDNF) and RET in a Hirschsprung disease patient. Nat Genet. 1996 Nov;14(3):341-4. [PubMed Link Image]
  11. Salomon R, Attie T, Pelet A, Bidaud C, Eng C, Amiel J, Sarnacki S, Goulet O, Ricour C, Nihoul-Fekete C, Munnich A, Lyonnet S: Germline mutations of the RET ligand GDNF are not sufficient to cause Hirschsprung disease. Nat Genet. 1996 Nov;14(3):345-7. [PubMed Link Image]
  12. Amiel J, Salomon R, Attie T, Pelet A, Trang H, Mokhtari M, Gaultier C, Munnich A, Lyonnet S: Mutations of the RET-GDNF signaling pathway in Ondine's curse. Am J Hum Genet. 1998 Mar;62(3):715-7. [PubMed Link Image]
  13. Martucciello G, Ceccherini I, Lerone M, Jasonni V: Pathogenesis of Hirschsprung's disease. J Pediatr Surg. 2000 Jul;35(7):1017-25. [PubMed Link Image]
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 7697
Enzyme 57 Name Potassium voltage-gated channel subfamily H member 2
Enzyme 57 Synonyms
  1. Eag homolog
  2. Ether-a-go-go-related gene potassium channel 1
  3. ERG-1
  4. Eag-related protein 1
  5. Ether-a-go-go-related protein 1
  6. H-ERG
  7. hERG-1
  8. hERG1
  9. Voltage-gated potassium channel subunit Kv11.1
Enzyme 57 Gene Name KCNH2
Enzyme 57 Protein Sequence >Potassium voltage-gated channel subfamily H member 2
MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRAEVM
QRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDG
AVIMFILNFEVVMEKDMVGSPAHDTNHRGPPTSWLAPGRAKTFRLKLPALLALTARESSV
RSGGAGGAGAPGAVVVDVDLTPAAPSSESLALDEVTAMDNHVAGLGPAEERRALVGPGSP
PRSAPGQLPSPRAHSLNPDASGSSCSLARTRSRESCASVRRASSADDIEAMRAGVLPPPP
RHASTGAMHPLRSGLLNSTSDSDLVRYRTISKIPQITLNFVDLKGDPFLASPTSDREIIA
PKIKERTHNVTEKVTQVLSLGADVLPEYKLQAPRIHRWTILHYSPFKAVWDWLILLLVIY
TAVFTPYSAAFLLKETEEGPPATECGYACQPLAVVDLIVDIMFIVDILINFRTTYVNANE
EVVSHPGRIAVHYFKGWFLIDMVAAIPFDLLIFGSGSEELIGLLKTARLLRLVRVARKLD
RYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNMEQPHMDSRIGWLHNLGDQIGKPYNSS
GLGGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVS
AIIQRLYSGTARYHTQMLRVREFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGF
PECLQADICLHLNRSLLQHCKPFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALY
FISRGSIEILRGDVVVAILGKNDIFGEPLNLYARPGKSNGDVRALTYCDLHKIHRDDLLE
VLDMYPEFSDHFWSSLEITFNLRDTNMIPGSPGSTELEGGFSRQRKRKLSFRRRTDKDTE
QPGEVSALGPGRAGAGPSSRGRPGGPWGESPSSGPSSPESSEDEGPGRSSSPLRLVPFSS
PRPPGEPPGGEPLMEDCEKSSDTCNPLSGAFSGVSNIFSFWGDSRGRQYQELPRCPAPTP
SLLNIPLSSPGRRPRGDVESRLDALQRQLNRLETRLSADMATVLQLLQRQMTLVPPAYSA
VTTPGPGPTSTSPLLPVSPLPTLTLDSLSQVSQFMACEELPPGAPELPQEGPTRRLSLPG
QLGALTSQPLHRHGSDPGS
Enzyme 57 Number of Residues 1159
Enzyme 57 Molecular Weight 126653.5
Enzyme 57 Theoretical pI 7.97
Enzyme 57 GO Classification
Function
  • catalytic activity
  • cation channel activity
  • ion channel activity
  • ion transmembrane transporter activity
  • kinase activity
  • molecular transducer activity
  • potassium channel activity
  • protein histidine kinase activity
  • protein kinase activity
  • signal transducer activity
  • substrate-specific transmembrane transporter activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transmembrane transporter activity
  • transporter activity
  • two-component sensor activity
  • voltage-gated potassium channel activity
Process
  • biological regulation
  • cation transport
  • establishment of localization
  • ion transport
  • monovalent inorganic cation transport
  • potassium ion transport
  • regulation of biological process
  • regulation of cellular process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • signal transduction
  • signal transmission
  • signaling process
  • transmembrane transport
  • transport
  • two-component signal transduction system (phosphorelay)
Component
  • cell part
  • membrane
Enzyme 57 General Function Involved in ion channel activity
Enzyme 57 Specific Function Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr). Isoform 3 has no channel activity by itself, but modulates channel characteristics when associated with isoform 1
Enzyme 57 Pathways Not Available
Enzyme 57 Reactions Not Available
Enzyme 57 Pfam Domain Function
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • 404-424 451-471 496-516 521-541 548-568 639-659
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein Not Available
Enzyme 57 UniProtKB/Swiss-Prot ID Q12809 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name KCNH2_HUMAN Link Image
Enzyme 57 PDB ID 1BYW Link Image
Enzyme 57 PDB File Show
Enzyme 57 3D Structure
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence >3480 bp
ATGCCGGTGCGGAGGGGCCACGTCGCGCCGCAGAACACCTTCCTGGACACCATCATCCGC
AAGTTTGAGGGCCAGAGCCGTAAGTTCATCATCGCCAACGCTCGGGTGGAGAACTGCGCC
GTCATCTACTGCAACGACGGCTTCTGCGAGCTGTGCGGCTACTCGCGGGCCGAGGTGATG
CAGCGACCCTGCACCTGCGACTTCCTGCACGGGCCGCGCACGCAGCGCCGCGCTGCCGCG
CAGATCGCGCAGGCACTGCTGGGCGCCGAGGAGCGCAAAGTGGAAATCGCCTTCTACCGG
AAAGATGGGAGCTGCTTCCTATGTCTGGTGGATGTGGTGCCCGTGAAGAACGAGGATGGG
GCTGTCATCATGTTCATCCTCAATTTCGAGGTGGTGATGGAGAAGGACATGGTGGGGTCC
CCGGCTCATGACACCAACCACCGGGGCCCCCCCACCAGCTGGCTGGCCCCAGGCCGCGCC
AAGACCTTCCGCCTGAAGCTGCCCGCGCTGCTGGCGCTGACGGCCCGGGAGTCGTCGGTG
CGGTCGGGCGGCGCGGGCGGCGCGGGCGCCCCGGGGGCCGTGGTGGTGGACGTGGACCTG
ACGCCCGCGGCACCCAGCAGCGAGTCGCTGGCCCTGGACGAAGTGACAGCCATGGACAAC
CACGTGGCAGGGCTCGGGCCCGCGGAGGAGCGGCGTGCGCTGGTGGGTCCCGGCTCTCCG
CCCCGCAGCGCGCCCGGCCAGCTCCCATCGCCCCGGGCGCACAGCCTCAACCCCGACGCC
TCGGGCTCCAGCTGCAGCCTGGCCCGGACGCGCTCCCGAGAAAGCTGCGCCAGCGTGCGC
CGCGCCTCGTCGGCCGACGACATCGAGGCCATGCGCGCCGGGGTGCTGCCCCCGCCACCG
CGCCACGCCAGCACCGGGGCCATGCACCCACTGCGCAGCGGCTTGCTCAACTCCACCTCG
GACTCCGACCTCGTGCGCTACCGCACCATTAGCAAGATTCCCCAAATCACCCTCAACTTT
GTGGACCTCAAGGGCGACCCCTTCTTGGCTTCGCCCACCAGTGACCGTGAGATCATAGCA
CCTAAGATAAAGGAGCGAACCCACAATGTCACTGAGAAGGTCACCCAGGTCCTGTCCCTG
GGCGCCGACGTGCTGCCTGAGTACAAGCTGCAGGCACCGCGCATCCACCGCTGGACCATC
CTGCATTACAGCCCCTTCAAGGCCGTGTGGGACTGGCTCATCCTGCTGCTGGTCATCTAC
ACGGCTGTCTTCACACCCTACTCGGCTGCCTTCCTGCTGAAGGAGACGGAAGAAGGCCCG
CCTGCTACCGAGTGTGGCTACGCCTGCCAGCCGCTGGCTGTGGTGGACCTCATCGTGGAC
ATCATGTTCATTGTGGACATCCTCATCAACTTCCGCACCACCTACGTCAATGCCAACGAG
GAGGTGGTCAGCCACCCCGGCCGCATCGCCGTCCACTACTTCAAGGGCTGGTTCCTCATC
GACATGGTGGCCGCCATCCCCTTCGACCTGCTCATCTTCGGCTCTGGCTCTGAGGAGCTG
ATCGGGCTGCTGAAGACTGCGCGGCTGCTGCGGCTGGTGCGCGTGGCGCGGAAGCTGGAT
CGCTACTCAGAGTACGGCGCGGCCGTGCTGTTCTTGCTCATGTGCACCTTTGCGCTCATC
GCGCACTGGCTAGCCTGCATCTGGTACGCCATCGGCAACATGGAGCAGCCACACATGGAC
TCACGCATCGGCTGGCTGCACAACCTGGGCGACCAGATAGGCAAACCCTACAACAGCAGC
GGCCTGGGCGGCCCCTCCATCAAGGACAAGTATGTGACGGCGCTCTACTTCACCTTCAGC
AGCCTCACCAGTGTGGGCTTCGGCAACGTCTCTCCCAACACCAACTCAGAGAAGATCTTC
TCCATCTGCGTCATGCTCATTGGCTCCCTCATGTATGCTAGCATCTTCGGCAACGTGTCG
GCCATCATCCAGCGGCTGTACTCGGGCACAGCCCGCTACCACACACAGATGCTGCGGGTG
CGGGAGTTCATCCGCTTCCACCAGATCCCCAATCCCCTGCGCCAGCGCCTCGAGGAGTAC
TTCCAGCACGCCTGGTCCTACACCAACGGCATCGACATGAACGCGGTGCTGAAGGGCTTC
CCTGAGTGCCTGCAGGCTGACATCTGCCTGCACCTGAACCGCTCACTGCTGCAGCACTGC
AAACCCTTCCGAGGGGCCACCAAGGGCTGCCTTCGGGCCCTGGCCATGAAGTTCAAGACC
ACACATGCACCGCCAGGGGACACACTGGTGCATGCTGGGGACCTGCTCACCGCCCTGTAC
TTCATCTCCCGGGGCTCCATCGAGATCCTGCGGGGCGACGTCGTCGTGGCCATCCTGGGG
AAGAATGACATCTTTGGGGAGCCTCTGAACCTGTATGCAAGGCCTGGCAAGTCGAACGGG
GATGTGCGGGCCCTCACCTACTGTGACCTACACAAGATCCATCGGGACGACCTGCTGGAG
GTGCTGGACATGTACCCTGAGTTCTCCGACCACTTCTGGTCCAGCCTGGAGATCACCTTC
AACCTGCGAGATACCAACATGATCCCGGGCTCCCCCGGCAGTACGGAGTTAGAGGGTGGC
TTCAGTCGGCAACGCAAGCGCAAGTTGTCCTTCCGCAGGCGCACGGACAAGGACACGGAG
CAGCCAGGGGAGGTGTCGGCCTTGGGGCCGGGCCGGGCGGGGGCAGGGCCGAGTAGCCGG
GGCCGGCCGGGGGGGCCGTGGGGGGAGAGCCCGTCCAGTGGCCCCTCCAGCCCTGAGAGC
AGTGAGGATGAGGGCCCAGGCCGCAGCTCCAGCCCCCTCCGCCTGGTGCCCTTCTCCAGC
CCCAGGCCCCCCGGAGAGCCGCCGGGTGGGGAGCCCCTGATGGAGGACTGCGAGAAGAGC
AGCGACACTTGCAACCCCCTGTCAGGCGCCTTCTCAGGAGTGTCCAACATTTTCAGCTTC
TGGGGGGACAGTCGGGGCCGCCAGTACCAGGAGCTCCCTCGATGCCCCGCCCCCACCCCC
AGCCTCCTCAACATCCCCCTCTCCAGCCCGGGTCGGCGGCCCCGGGGCGACGTGGAGAGC
AGGCTGGATGCCCTCCAGCGCCAGCTCAACAGGCTGGAGACCCGGCTGAGTGCAGACATG
GCCACTGTCCTGCAGCTGCTACAGAGGCAGATGACGCTGGTCCCGCCCGCCTACAGTGCT
GTGACCACCCCGGGGCCTGGCCCCACTTCCACATCCCCGCTGTTGCCCGTCAGCCCCCTC
CCCACCCTCACCTTGGACTCGCTTTCTCAGGTTTCCCAGTTCATGGCGTGTGAGGAGCTG
CCCCCGGGGGCCCCAGAGCTTCCCCAAGAAGGCCCCACACGACGCCTCTCCCTACCGGGC
CAGCTGGGGGCCCTCACCTCCCAGCCCCTGCACAGACACGGCTCGGACCCGGGCAGTTAG
Enzyme 57 GenBank Gene ID U04270 Link Image
Enzyme 57 GeneCard ID KCNH2 Link Image
Enzyme 57 GenAtlas ID KCNH2 Link Image
Enzyme 57 HGNC ID HGNC:6251 Link Image
Enzyme 57 Chromosome Location 7
Enzyme 57 Locus 7q36.1
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 General References
  1. Warmke JW, Ganetzky B: A family of potassium channel genes related to eag in Drosophila and mammals. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):3438-42. [PubMed Link Image]
  2. Itoh T, Tanaka T, Nagai R, Kamiya T, Sawayama T, Nakayama T, Tomoike H, Sakurada H, Yazaki Y, Nakamura Y: Genomic organization and mutational analysis of HERG, a gene responsible for familial long QT syndrome. Hum Genet. 1998 Apr;102(4):435-9. [PubMed Link Image]
  3. Crociani O, Guasti L, Balzi M, Becchetti A, Wanke E, Olivotto M, Wymore RS, Arcangeli A: Cell cycle-dependent expression of HERG1 and HERG1B isoforms in tumor cells. J Biol Chem. 2003 Jan 31;278(5):2947-55. Epub 2002 Nov 12. [PubMed Link Image]
  4. Soejima H, Kawamoto S, Akai J, Miyoshi O, Arai Y, Morohka T, Matsuo S, Niikawa N, Kimura A, Okubo K, Mukai T: Isolation of novel heart-specific genes using the BodyMap database. Genomics. 2001 May 15;74(1):115-20. [PubMed Link Image]
  5. London B, Trudeau MC, Newton KP, Beyer AK, Copeland NG, Gilbert DJ, Jenkins NA, Satler CA, Robertson GA: Two isoforms of the mouse ether-a-go-go-related gene coassemble to form channels with properties similar to the rapidly activating component of the cardiac delayed rectifier K+ current. Circ Res. 1997 Nov;81(5):870-8. [PubMed Link Image]
  6. Lees-Miller JP, Kondo C, Wang L, Duff HJ: Electrophysiological characterization of an alternatively processed ERG K+ channel in mouse and human hearts. Circ Res. 1997 Nov;81(5):719-26. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Kupershmidt S, Snyders DJ, Raes A, Roden DM: A K+ channel splice variant common in human heart lacks a C-terminal domain required for expression of rapidly activating delayed rectifier current. J Biol Chem. 1998 Oct 16;273(42):27231-5. [PubMed Link Image]
  9. Gong Q, Anderson CL, January CT, Zhou Z: Role of glycosylation in cell surface expression and stability of HERG potassium channels. Am J Physiol Heart Circ Physiol. 2002 Jul;283(1):H77-84. [PubMed Link Image]
  10. Cui J, Melman Y, Palma E, Fishman GI, McDonald TV: Cyclic AMP regulates the HERG K(+) channel by dual pathways. Curr Biol. 2000 Jun 1;10(11):671-4. [PubMed Link Image]
  11. McDonald TV, Yu Z, Ming Z, Palma E, Meyers MB, Wang KW, Goldstein SA, Fishman GI: A minK-HERG complex regulates the cardiac potassium current I(Kr). Nature. 1997 Jul 17;388(6639):289-92. [PubMed Link Image]
  12. Abbott GW, Sesti F, Splawski I, Buck ME, Lehmann MH, Timothy KW, Keating MT, Goldstein SA: MiRP1 forms IKr potassium channels with HERG and is associated with cardiac arrhythmia. Cell. 1999 Apr 16;97(2):175-87. [PubMed Link Image]
  13. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  14. Morais Cabral JH, Lee A, Cohen SL, Chait BT, Li M, Mackinnon R: Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain. Cell. 1998 Nov 25;95(5):649-55. [PubMed Link Image]
  15. Curran ME, Splawski I, Timothy KW, Vincent GM, Green ED, Keating MT: A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome. Cell. 1995 Mar 10;80(5):795-803. [PubMed Link Image]
  16. Satler CA, Walsh EP, Vesely MR, Plummer MH, Ginsburg GS, Jacob HJ: Novel missense mutation in the cyclic nucleotide-binding domain of HERG causes long QT syndrome. Am J Med Genet. 1996 Oct 2;65(1):27-35. [PubMed Link Image]
  17. Benson DW, MacRae CA, Vesely MR, Walsh EP, Seidman JG, Seidman CE, Satler CA: Missense mutation in the pore region of HERG causes familial long QT syndrome. Circulation. 1996 May 15;93(10):1791-5. [PubMed Link Image]
  18. Dausse E, Berthet M, Denjoy I, Andre-Fouet X, Cruaud C, Bennaceur M, Faure S, Coumel P, Schwartz K, Guicheney P: A mutation in HERG associated with notched T waves in long QT syndrome. J Mol Cell Cardiol. 1996 Aug;28(8):1609-15. [PubMed Link Image]
  19. Tanaka T, Nagai R, Tomoike H, Takata S, Yano K, Yabuta K, Haneda N, Nakano O, Shibata A, Sawayama T, Kasai H, Yazaki Y, Nakamura Y: Four novel KVLQT1 and four novel HERG mutations in familial long-QT syndrome. Circulation. 1997 Feb 4;95(3):565-7. [PubMed Link Image]
  20. Splawski I, Shen J, Timothy KW, Vincent GM, Lehmann MH, Keating MT: Genomic structure of three long QT syndrome genes: KVLQT1, HERG, and KCNE1. Genomics. 1998 Jul 1;51(1):86-97. [PubMed Link Image]
  21. Satler CA, Vesely MR, Duggal P, Ginsburg GS, Beggs AH: Multiple different missense mutations in the pore region of HERG in patients with long QT syndrome. Hum Genet. 1998 Mar;102(3):265-72. [PubMed Link Image]
  22. Akimoto K, Furutani M, Imamura S, Furutani Y, Kasanuki H, Takao A, Momma K, Matsuoka R: Novel missense mutation (G601S) of HERG in a Japanese long QT syndrome family. Hum Mutat. 1998;Suppl 1:S184-6. [PubMed Link Image]
  23. Berthet M, Denjoy I, Donger C, Demay L, Hammoude H, Klug D, Schulze-Bahr E, Richard P, Funke H, Schwartz K, Coumel P, Hainque B, Guicheney P: C-terminal HERG mutations: the role of hypokalemia and a KCNQ1-associated mutation in cardiac event occurrence. Circulation. 1999 Mar 23;99(11):1464-70. [PubMed Link Image]
  24. Jongbloed RJ, Wilde AA, Geelen JL, Doevendans P, Schaap C, Van Langen I, van Tintelen JP, Cobben JM, Beaufort-Krol GC, Geraedts JP, Smeets HJ: Novel KCNQ1 and HERG missense mutations in Dutch long-QT families. Hum Mutat. 1999;13(4):301-10. [PubMed Link Image]
  25. Chen J, Zou A, Splawski I, Keating MT, Sanguinetti MC: Long QT syndrome-associated mutations in the Per-Arnt-Sim (PAS) domain of HERG potassium channels accelerate channel deactivation. J Biol Chem. 1999 Apr 9;274(15):10113-8. [PubMed Link Image]
  26. Yoshida H, Horie M, Otani H, Takano M, Tsuji K, Kubota T, Fukunami M, Sasayama S: Characterization of a novel missense mutation in the pore of HERG in a patient with long QT syndrome. J Cardiovasc Electrophysiol. 1999 Sep;10(9):1262-70. [PubMed Link Image]
  27. Larsen LA, Svendsen IH, Jensen AM, Kanters JK, Andersen PS, Moller M, Sorensen SA, Sandoe E, Jacobsen JR, Vuust J, Christiansen M: Long QT syndrome with a high mortality rate caused by a novel G572R missense mutation in KCNH2. Clin Genet. 2000 Feb;57(2):125-30. [PubMed Link Image]
  28. Splawski I, Shen J, Timothy KW, Lehmann MH, Priori S, Robinson JL, Moss AJ, Schwartz PJ, Towbin JA, Vincent GM, Keating MT: Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A, KCNE1, and KCNE2. Circulation. 2000 Sep 5;102(10):1178-85. [PubMed Link Image]
  29. Paulussen A, Yang P, Pangalos M, Verhasselt P, Marrannes R, Verfaille C, Vandenberk I, Crabbe R, Konings F, Luyten W, Armstrong M: Analysis of the human KCNH2(HERG) gene: identification and characterization of a novel mutation Y667X associated with long QT syndrome and a non-pathological 9 bp insertion. Hum Mutat. 2000 May;15(5):483. [PubMed Link Image]
  30. Laitinen P, Fodstad H, Piippo K, Swan H, Toivonen L, Viitasalo M, Kaprio J, Kontula K: Survey of the coding region of the HERG gene in long QT syndrome reveals six novel mutations and an amino acid polymorphism with possible phenotypic effects. Hum Mutat. 2000 Jun;15(6):580-1. [PubMed Link Image]
  31. Yoshida H, Horie M, Otani H, Kawashima T, Onishi Y, Sasayama S: Bradycardia-induced long QT syndrome caused by a de novo missense mutation in the S2-S3 inner loop of HERG. Am J Med Genet. 2001 Feb 1;98(4):348-52. [PubMed Link Image]
  32. Hayashi K, Shimizu M, Ino H, Yamaguchi M, Mabuchi H, Hoshi N, Higashida H: Characterization of a novel missense mutation E637K in the pore-S6 loop of HERG in a patient with long QT syndrome. Cardiovasc Res. 2002 Apr;54(1):67-76. [PubMed Link Image]
  33. Yang P, Kanki H, Drolet B, Yang T, Wei J, Viswanathan PC, Hohnloser SH, Shimizu W, Schwartz PJ, Stanton M, Murray KT, Norris K, George AL Jr, Roden DM: Allelic variants in long-QT disease genes in patients with drug-associated torsades de pointes. Circulation. 2002 Apr 23;105(16):1943-8. [PubMed Link Image]
  34. Paulussen A, Raes A, Matthijs G, Snyders DJ, Cohen N, Aerssens J: A novel mutation (T65P) in the PAS domain of the human potassium channel HERG results in the long QT syndrome by trafficking deficiency. J Biol Chem. 2002 Dec 13;277(50):48610-6. Epub 2002 Sep 26. [PubMed Link Image]
  35. Johnson WH Jr, Yang P, Yang T, Lau YR, Mostella BA, Wolff DJ, Roden DM, Benson DW: Clinical, genetic, and biophysical characterization of a homozygous HERG mutation causing severe neonatal long QT syndrome. Pediatr Res. 2003 May;53(5):744-8. Epub 2003 Mar 5. [PubMed Link Image]
  36. Brugada R, Hong K, Dumaine R, Cordeiro J, Gaita F, Borggrefe M, Menendez TM, Brugada J, Pollevick GD, Wolpert C, Burashnikov E, Matsuo K, Wu YS, Guerchicoff A, Bianchi F, Giustetto C, Schimpf R, Brugada P, Antzelevitch C: Sudden death associated with short-QT syndrome linked to mutations in HERG. Circulation. 2004 Jan 6;109(1):30-5. Epub 2003 Dec 15. [PubMed Link Image]
  37. Westenskow P, Splawski I, Timothy KW, Keating MT, Sanguinetti MC: Compound mutations: a common cause of severe long-QT syndrome. Circulation. 2004 Apr 20;109(15):1834-41. Epub 2004 Mar 29. [PubMed Link Image]
  38. Hong K, Bjerregaard P, Gussak I, Brugada R: Short QT syndrome and atrial fibrillation caused by mutation in KCNH2. J Cardiovasc Electrophysiol. 2005 Apr;16(4):394-6. [PubMed Link Image]
  39. Millat G, Chevalier P, Restier-Miron L, Da Costa A, Bouvagnet P, Kugener B, Fayol L, Gonzalez Armengod C, Oddou B, Chanavat V, Froidefond E, Perraudin R, Rousson R, Rodriguez-Lafrasse C: Spectrum of pathogenic mutations and associated polymorphisms in a cohort of 44 unrelated patients with long QT syndrome. Clin Genet. 2006 Sep;70(3):214-27. [PubMed Link Image]
Enzyme 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 7730
Enzyme 58 Name Potassium voltage-gated channel subfamily H member 6
Enzyme 58 Synonyms
  1. Ether-a-go-go-related gene potassium channel 2
  2. ERG-2
  3. Eag-related protein 2
  4. Ether-a-go-go-related protein 2
  5. hERG-2
  6. hERG2
  7. Voltage-gated potassium channel subunit Kv11.2
Enzyme 58 Gene Name KCNH6
Enzyme 58 Protein Sequence >Potassium voltage-gated channel subfamily H member 6
MPVRRGHVAPQNTYLDTIIRKFEGQSRKFLIANAQMENCAIIYCNDGFCELFGYSRVEVM
QQPCTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDG
AVIMFILNFEDLAQLLAKCSSRSLSQRLLSQSFLGSEGSHGRPGGPGPGTGRGKYRTISQ
IPQFTLNFVEFNLEKHRSSSTTEIEIIAPHKVVERTQNVTEKVTQVLSLGADVLPEYKLQ
APRIHRWTILHYSPFKAVWDWLILLLVIYTAVFTPYSAAFLLSDQDESRRGACSYTCSPL
TVVDLIVDIMFVVDIVINFRTTYVNTNDEVVSHPRRIAVHYFKGWFLIDMVAAIPFDLLI
FRTGSDETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVLFLLMCTFALIAHWLACIWY
AIGNVERPYLEHKIGWLDSLGVQLGKRYNGSDPASGPSVQDKYVTALYFTFSSLTSVGFG
NVSPNTNSEKVFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQ
IPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGFPECLQADICLHLHRALLQHCPAFSGAGK
GCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRDDVVVAILGKNDIFGEP
VSLHAQPGKSSADVRALTYCDLHKIQRADLLEVLDMYPAFAESFWSKLEVTFNLRDAAGG
LHSSPRQAPGSQDHQGFFLSDNQSGSPHELGPQFPSKGYSLLGPGSQNSMGAGPCAPGHP
DAAPPLSISDASGLWPELLQEMPPRHSPQSPQEDPDCWPLKLGSRLEQLQAQMNRLESRV
SSDLSRILQLLQKPMPQGHASYILEAPASNDLALVPIASETTSPGPRLPQGFLPPAQTPS
YGDLDDCSPKHRNSSPRMPHLAVATDKTLAPSSEQEQPEGLWPPLASPLHPLEVQGLICG
PCFSSLPEHLGSVPKQLDFQRHGSDPGFAGSWGH
Enzyme 58 Number of Residues 994
Enzyme 58 Molecular Weight 109923.7
Enzyme 58 Theoretical pI 7.00
Enzyme 58 GO Classification
Function
  • cation channel activity
  • ion channel activity
  • ion transmembrane transporter activity
  • potassium channel activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
  • voltage-gated potassium channel activity
Process
  • biological regulation
  • cation transport
  • establishment of localization
  • ion transport
  • monovalent inorganic cation transport
  • potassium ion transport
  • regulation of biological process
  • regulation of cellular process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • signal transduction
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 58 General Function Involved in ion channel activity
Enzyme 58 Specific Function Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a slowly activating, rectifying current. Channel properties may be modulated by cAMP and subunit assembly
Enzyme 58 Pathways Not Available
Enzyme 58 Reactions Not Available
Enzyme 58 Pfam Domain Function
Enzyme 58 Signals
  • None
Enzyme 58 Transmembrane Regions
  • 262-282 299-319 341-361 371-391 399-419 491-511
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein Not Available
Enzyme 58 UniProtKB/Swiss-Prot ID Q9H252 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name KCNH6_HUMAN Link Image
Enzyme 58 PDB ID Not Available
Enzyme 58 Cellular Location Not Available
Enzyme 58 Gene Sequence >2985 bp
ATGCCGGTCCGCAGGGGCCACGTCGCTCCCCAAAACACTTACCTGGACACCATCATCCGC
AAGTTCGAGGGCCAAAGTCGGAAGTTCCTGATTGCCAATGCTCAGATGGAGAACTGCGCC
ATCATTTACTGCAACGACGGCTTCTGCGAACTCTTCGGCTACTCCCGAGTGGAGGTGATG
CAGCAACCCTGCACCTGCGACTTCCTCACAGGCCCCAACACACCAAGCAGCGCCGTGTCC
CGCCTAGCGCAGGCCCTGCTGGGGGCTGAGGAGTGCAAGGTGGACATCCTCTACTACCGC
AAGGATGCCTCCAGCTTCCGCTGCCTGGTAGATGTGGTGCCCGTGAAGAACGAGGACGGG
GCTGTCATCATGTTCATTCTCAACTTCGAGGACCTGGCCCAGCTCCTGGCCAAGTGCAGC
AGCCGCAGCTTGTCCCAGCGCCTGTTGTCCCAGAGCTTCCTGGGCTCCGAGGGCTCTCAC
GGCAGGCCAGGCGGACCAGGGCCAGGCACAGGCAGGGGCAAGTACAGGACCATCAGCCAG
ATCCCACAGTTCACGCTCAACTTCGTGGAGTTCAACTTGGAGAAGCACCGCTCCAGCTCC
ACCACGGAGATTGAGATCATCGCGCCCCATAAGGTGGTGGAGCGGACACAGAACGTCACT
GAGAAGGTCACCCAGGTCCTGTCCCTGGGCGCGGATGTGCTGCCGGAGTACAAGCTGCAG
GCGCCGCGCATCCACCGCTGGACCATCCTGCACTACAGCCCCTTCAAGGCCGTGTGGGAC
TGGCTCATCCTGCTGCTGGTCATCTACACGGCTGTCTTCACGCCCTACTCAGCCGCCTTC
CTGCTCAGCGACCAGGACGAATCACGGCGTGGGGCCTGCAGCTATACCTGCAGTCCCCTC
ACTGTGGTGGATCTCATCGTGGACATCATGTTCGTCGTGGACATCGTCATCAACTTCCGC
ACCACCTATGTCAACACCAATGATGAGGTGGTCAGCCACCCCCGCCGCATCGCCGTCCAC
TACTTCAAGGGCTGGTTCCTCATTGACATGGTGGCCGCCATCCCTTTCGACCTCCTGATC
TTCCGCACTGGCTCCGATGAGACCACAACCCTGATTGGGCTATTGAAGACAGCGCGGCTG
CTGCGGCTGGTGCGCGTAGCACGGAAGCTGGACCGCTACTCTGAGTATGGGGCGGCTGTG
CTCTTCTTGCTCATGTGCACCTTCGCGCTCATAGCGCACTGGCTGGCCTGCATCTGGTAC
GCCATCGGCAATGTGGAGCGGCCCTACCTAGAACACAAGATCGGCTGGCTGGACAGCCTG
GGTGTGCAGCTTGGCAAGCGCTACAACGGCAGCGACCCAGCCTCGGGCCCCTCGGTGCAG
GACAAGTATGTCACAGCCCTCTACTTCACCTTCAGCAGCCTCACCAGCGTGGGCTTCGGC
AATGTCTCGCCCAACACCAACTCCGAGAAGGTCTTCTCCATCTGCGTCATGCTCATCGGC
TCCCTGATGTACGCCAGCATCTTCGGGAACGTGTCCGCGATCATCCAGCGCCTGTACTCG
GGCACCGCGCGCTACCACACGCAGATGCTGCGTGTCAAGGAGTTCATCCGCTTCCACCAG
ATCCCCAACCCACTGCGCCAGCGCCTGGAGGAGTATTTCCAGCACGCCTGGTCCTACACC
AATGGCATTGACATGAACGCGGTGCTGAAGGGCTTCCCCGAGTGCCTGCAGGCTGACATC
TGCCTGCACCTGCACCGCGCACTGCTGCAGCACTGCCCAGCTTTCAGCGGCGCCGGCAAG
GGCTGCCTGCGCGCGCTAGCCGTCAAGTTCAAGACCACCCACGCGCCGCCTGGGGACACG
CTGGTGCACCTCGGCGACGTGCTCTCCACCCTCTACTTCATCTCCCGAGGCTCCATCGAG
ATCCTGCGCGACGACGTGGTCGTGGCCATCCTAGGAAAGAATGACATCTTTGGGGAACCC
GTCAGCCTCCATGCCCAGCCAGGCAAGTCCAGTGCAGACGTGCGGGCTCTGACCTACTGC
GACCTGCACAAGATCCAGCGGGCAGATCTGCTGGAGGTGCTGGACATGTACCCGGCCTTT
GCGGAGAGCTTCTGGAGTAAGCTGGAGGTCACCTTCAACCTGCGGGACGCAGCCGGGGGT
CTCCACTCATCCCCCCGACAGGCTCCTGGCAGCCAAGACCACCAAGGTTTCTTTCTCAGT
GACAACCAGTCAGGGTCTCCCCATGAGCTGGGGCCCCAGTTCCCCTCTAAGGGCTACAGC
CTCCTGGGTCCTGGGAGCCAGAACTCCATGGGGGCAGGACCTTGTGCTCCAGGGCACCCA
GATGCAGCCCCTCCCCTGAGCATCTCAGATGCATCTGGCCTCTGGCCTGAGCTACTGCAG
GAAATGCCCCCAAGGCACAGCCCCCAAAGCCCTCAGGAAGACCCAGATTGCTGGCCTCTG
AAGCTGGGCTCCAGGCTAGAGCAGCTCCAGGCCCAGATGAACAGGCTGGAGTCCCGCGTG
TCCTCAGACCTCAGCCGCATCTTGCAGCTCCTCCAGAAGCCCATGCCCCAGGGCCACGCC
AGCTACATTCTGGAAGCCCCTGCCTCCAATGACCTGGCCTTGGTTCCTATAGCCTCGGAG
ACGACGAGTCCAGGGCCCAGGCTGCCCCAGGGCTTTCTGCCTCCTGCACAGACCCCAAGC
TATGGAGACTTGGATGACTGTAGTCCAAAGCACAGGAACTCCTCCCCCAGGATGCCTCAC
CTGGCTGTGGCAACGGACAAAACTCTGGCACCATCCTCAGAACAGGAACAGCCTGAGGGG
CTCTGGCCACCCCTAGCCTCACCTCTACATCCCCTGGAAGTACAAGGACTCATCTGTGGT
CCCTGCTTCTCCTCCCTCCCTGAACACCTTGGCTCTGTTCCCAAGCAGCTGGACTTCCAG
AGACATGGCTCAGATCCTGGATTTGCAGGGAGTTGGGGCCACTGA
Enzyme 58 GenBank Gene ID AF311913 Link Image
Enzyme 58 GeneCard ID KCNH6 Link Image
Enzyme 58 GenAtlas ID KCNH6 Link Image
Enzyme 58 HGNC ID HGNC:18862 Link Image
Enzyme 58 Chromosome Location 1
Enzyme 58 Locus 17q23.3
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Bauer CK, Wulfsen I, Schafer R, Glassmeier G, Wimmers S, Flitsch J, Ludecke DK, Schwarz JR: HERG K(+) currents in human prolactin-secreting adenoma cells. Pflugers Arch. 2003 Feb;445(5):589-600. Epub 2002 Dec 6. [PubMed Link Image]
Enzyme 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 7735
Enzyme 59 Name Methyl-CpG-binding domain protein 2
Enzyme 59 Synonyms
  1. Demethylase
  2. DMTase
  3. Methyl-CpG-binding protein MBD2
Enzyme 59 Gene Name MBD2
Enzyme 59 Protein Sequence >Methyl-CpG-binding domain protein 2
MRAHPGGGRCCPEQEEGESAAGGSGAGGDSAIEQGGQGSALAPSPVSGVRREGARGGGRG
RGRWKQAGRGGGVCGRGRGRGRGRGRGRGRGRGRGRPPSGGSGLGGDGGGCGGGGSGGGG
APRREPVPFPSGSAGPGPRGPRATESGKRMDCPALPPGWKKEEVIRKSGLSAGKSDVYYF
SPSGKKFRSKPQLARYLGNTVDLSSFDFRTGKMMPSKLQKNKQRLRNDPLNQNKGKPDLN
TTLPIRQTASIFKQPVTKVTNHPSNKVKSDPQRMNEQPRQLFWEKRLQGLSASDVTEQII
KTMELPKGLQGVGPGSNDETLLSAVASALHTSSAPITGQVSAAVEKNPAVWLNTSQPLCK
AFIVTDEDIRKQEERVQQVRKKLEEALMADILSRAADTEEMDIEMDSGDEA
Enzyme 59 Number of Residues 411
Enzyme 59 Molecular Weight 43254.3
Enzyme 59 Theoretical pI 10.76
Enzyme 59 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
Process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 59 General Function Involved in DNA binding
Enzyme 59 Specific Function Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binds hemi-methylated DNA as well. Recruits histone deacetylases and DNA methyltransferases. Acts as transcriptional repressor and plays a role in gene silencing. Isoform 1 may enhance the activation of some unmethylated cAMP-responsive promoters. Reports about DNA demethylase activity of isoform 2 are contradictory
Enzyme 59 Pathways Not Available
Enzyme 59 Reactions Not Available
Enzyme 59 Pfam Domain Function
Enzyme 59 Signals
  • None
Enzyme 59 Transmembrane Regions
  • None
Enzyme 59 Essentiality Not Available
Enzyme 59 GenBank ID Protein 3800793 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID Q9UBB5 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name MBD2_HUMAN Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence >1236 bp
ATGCGCGCGCACCCGGGGGGAGGCCGCTGCTGCCCGGAGCAGGAGGAGGGGGAGAGTGCG
GCGGGCGGCAGCGGCGCTGGCGGCGACTCCGCCATAGAGCAGGGGGGCCAGGGCAGCGCG
CTCGCCCCGTCCCCGGTGAGCGGCGTGCGCAGGGAAGGCGCTCGGGGCGGCGGCCGTGGC
CGGGGGCGGTGGAAGCAGGCGGGCCGGGGCGGCGGCGTCTGTGGCCGTGGCCGGGGCCGG
GGCCGTGGCCGGGGACGGGGACGGGGCCGGGGCCGGGGCCGCGGCCGTCCCCCGAGTGGC
GGCAGCGGCCTTGGCGGCGACGGCGGCGGCTGCGGCGGCGGCGGCAGCGGTGGCGGCGGC
GCCCCCCGGCGGGAGCCGGTCCCTTTCCCGTCGGGGAGCGCGGGGCCGGGGCCCAGGGGA
CCCCGGGCCACGGAGAGCGGGAAGAGGATGGATTGCCCGGCCCTCCCCCCCGGATGGAAG
AAGGAGGAAGTGATCCGAAAATCTGGGCTAAGTGCTGGCAAGAGCGATGTCTACTACTTC
AGTCCAAGTGGTAAGAAGTTCAGAAGCAAGCCTCAGTTGGCAAGGTACCTGGGAAATACT
GTTGATCTCAGCAGTTTTGACTTCAGAACTGGAAAGATGATGCCTAGTAAATTACAGAAG
AACAAACAGAGACTGCGAAACGATCCTCTCAATCAAAATAAGGGTAAACCAGACTTGAAT
ACAACATTGCCAATTAGACAAACAGCATCAATTTTCAAACAACCGGTAACCAAAGTCACA
AATCATCCTAGTAATAAAGTGAAATCAGACCCACAACGAATGAATGAACAGCCACGTCAG
CTTTTCTGGGAGAAGAGGCTACAAGGACTTAGTGCATCAGATGTAACAGAACAAATTATA
AAAACCATGGAACTACCCAAAGGTCTTCAAGGAGTTGGTCCAGGTAGCAATGATGAGACC
CTTTTATCTGCTGTTGCCAGTGCTTTGCACACAAGCTCTGCGCCAATCACAGGGCAAGTC
TCCGCTGCTGTGGAAAAGAACCCTGCTGTTTGGCTTAACACATCTCAACCCCTCTGCAAA
GCTTTTATTGTCACAGATGAAGACATCAGGAAACAGGAAGAGCGAGTACAGCAAGTACGC
AAGAAATTGGAAGAAGCACTGATGGCAGACATCTTGTCGCGAGCTGCTGATACAGAAGAG
ATGGATATTGAAATGGACAGTGGAGATGAAGCCTAA
Enzyme 59 GenBank Gene ID AF072242 Link Image
Enzyme 59 GeneCard ID MBD2 Link Image
Enzyme 59 GenAtlas ID MBD2 Link Image
Enzyme 59 HGNC ID HGNC:6917 Link Image
Enzyme 59 Chromosome Location 1
Enzyme 59 Locus 18q21
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 General References
  1. Hendrich B, Bird A: Identification and characterization of a family of mammalian methyl-CpG binding proteins. Mol Cell Biol. 1998 Nov;18(11):6538-47. [PubMed Link Image]
  2. Hendrich B, Abbott C, McQueen H, Chambers D, Cross S, Bird A: Genomic structure and chromosomal mapping of the murine and human Mbd1, Mbd2, Mbd3, and Mbd4 genes. Mamm Genome. 1999 Sep;10(9):906-12. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Bhattacharya SK, Ramchandani S, Cervoni N, Szyf M: A mammalian protein with specific demethylase activity for mCpG DNA. Nature. 1999 Feb 18;397(6720):579-83. [PubMed Link Image]
  5. Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A: MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex. Nat Genet. 1999 Sep;23(1):58-61. [PubMed Link Image]
  6. Tatematsu KI, Yamazaki T, Ishikawa F: MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase. Genes Cells. 2000 Aug;5(8):677-88. [PubMed Link Image]
  7. Boeke J, Ammerpohl O, Kegel S, Moehren U, Renkawitz R: The minimal repression domain of MBD2b overlaps with the methyl-CpG-binding domain and binds directly to Sin3A. J Biol Chem. 2000 Nov 10;275(45):34963-7. [PubMed Link Image]
  8. Humphrey GW, Wang Y, Russanova VR, Hirai T, Qin J, Nakatani Y, Howard BH: Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1. J Biol Chem. 2001 Mar 2;276(9):6817-24. Epub 2000 Dec 1. [PubMed Link Image]
  9. Sekimata M, Takahashi A, Murakami-Sekimata A, Homma Y: Involvement of a novel zinc finger protein, MIZF, in transcriptional repression by interacting with a methyl-CpG-binding protein, MBD2. J Biol Chem. 2001 Nov 16;276(46):42632-8. Epub 2001 Sep 11. [PubMed Link Image]
  10. Brackertz M, Boeke J, Zhang R, Renkawitz R: Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3. J Biol Chem. 2002 Oct 25;277(43):40958-66. Epub 2002 Aug 14. [PubMed Link Image]
  11. Lembo F, Pero R, Angrisano T, Vitiello C, Iuliano R, Bruni CB, Chiariotti L: MBDin, a novel MBD2-interacting protein, relieves MBD2 repression potential and reactivates transcription from methylated promoters. Mol Cell Biol. 2003 Mar;23(5):1656-65. [PubMed Link Image]
  12. Fujita H, Fujii R, Aratani S, Amano T, Fukamizu A, Nakajima T: Antithetic effects of MBD2a on gene regulation. Mol Cell Biol. 2003 Apr;23(8):2645-57. [PubMed Link Image]
  13. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  14. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  15. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  16. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 7894
Enzyme 60 Name Relaxin receptor 1
Enzyme 60 Synonyms
  1. Leucine-rich repeat-containing G-protein coupled receptor 7
  2. Relaxin family peptide receptor 1
Enzyme 60 Gene Name RXFP1
Enzyme 60 Protein Sequence >Relaxin receptor 1
MTSGSVFFYILIFGKYFSHGGGQDVKCSLGYFPCGNITKCLPQLLHCNGVDDCGNQADED
NCGDNNGWSLQFDKYFASYYKMTSQYPFEAETPECLVGSVPVQCLCQGLELDCDETNLRA
VPSVSSNVTAMSLQWNLIRKLPPDCFKNYHDLQKLYLQNNKITSISIYAFRGLNSLTKLY
LSHNRITFLKPGVFEDLHRLEWLIIEDNHLSRISPPTFYGLNSLILLVLMNNVLTRLPDK
PLCQHMPRLHWLDLEGNHIHNLRNLTFISCSNLTVLVMRKNKINHLNENTFAPLQKLDEL
DLGSNKIENLPPLIFKDLKELSQLNLSYNPIQKIQANQFDYLVKLKSLSLEGIEISNIQQ
RMFRPLMNLSHIYFKKFQYCGYAPHVRSCKPNTDGISSLENLLASIIQRVFVWVVSAVTC
FGNIFVICMRPYIRSENKLYAMSIISLCCADCLMGIYLFVIGGFDLKFRGEYNKHAQLWM
ESTHCQLVGSLAILSTEVSVLLLTFLTLEKYICIVYPFRCVRPGKCRTITVLILIWITGF
IVAFIPLSNKEFFKNYYGTNGVCFPLHSEDTESIGAQIYSVAIFLGINLAAFIIIVFSYG
SMFYSVHQSAITATEIRNQVKKEMILAKRFFFIVFTDALCWIPIFVVKFLSLLQVEIPGT
ITSWVVIFILPINSALNPILYTLTTRPFKEMIHRFWYNYRQRKSMDSKGQKTYAPSFIWV
EMWPLQEMPPELMKPDLFTYPCEMSLISQSTRLNSYS
Enzyme 60 Number of Residues 757
Enzyme 60 Molecular Weight 86973.8
Enzyme 60 Theoretical pI 8.11
Enzyme 60 GO Classification
Function
  • G-protein coupled receptor activity
  • binding
  • molecular transducer activity
  • protein binding
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • biological regulation
  • cell surface receptor linked signaling pathway
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 60 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 60 Specific Function Receptor for relaxins. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. Binding of the ligand may also activate a tyrosine kinase pathway that inhibits the activity of a phosphodiesterase that degrades cAMP
Enzyme 60 Pathways Not Available
Enzyme 60 Reactions Not Available
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • None
Enzyme 60 Transmembrane Regions
  • 410-430 444-464 487-507 528-548 578-598 630-650 652-672
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein 10441730 Link Image
Enzyme 60 UniProtKB/Swiss-Prot ID Q9HBX9 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name RXFP1_HUMAN Link Image
Enzyme 60 PDB ID Not Available
Enzyme 60 Cellular Location Not Available
Enzyme 60 Gene Sequence >2274 bp
ATGACATCTGGTTCTGTCTTCTTCTACATCTTAATTTTTGGAAAATATTTTTCTCATGGG
GGTGGACAGGATGTCAAGTGCTCCCTTGGCTATTTCCCCTGTGGGAACATCACAAAGTGC
TTGCCTCAGCTCCTGCACTGTAACGGTGTGGACGACTGCGGGAATCAGGCCGATGAGGAC
AACTGTGGAGACAACAATGGATGGTCCATGCAATTTGACAAATATTTTGCCAGTTACTAC
AAAATGACTTCCCAATATCCTTTTGAGGCAGAAACACCTGAATGTTTGGTCGGTTCTGTG
CCAGTGCAATGTCTTTGCCAAGGTCTGGAGCTTGACTGTGATGAAACCAATTTACGAGCT
GTTCCATCGGTTTCTTCAAATGTGACTGCAATGTCACTTCAGTGGAACTTAATAAGAAAG
CTTCCTCCTGATTGCTTCAAGAATTATCATGATCTTCAGAAGCTGTACCTGCAAAACAAT
AAGATTACATCCATCTCCATCTATGCTTTCAGAGGACTGAATAGCCTTACTAAACTGTAT
CTCAGTCATAACAGAATAACCTTCCTGAAGCCGGGTGTTTTTGAAGATCTTCACAGACTA
GAATGGCTGATAATTGAAGATAATCACCTCAGTCGAATTTCCCCACCAACATTTTATGGA
CTAAATTCTCTTATTCTCTTAGTCCTGATGAATAACGTCCTCACCCGTTTACCTGATAAA
CCTCTCTGTCAACACATGCCAAGACTACATTGGCTGGACCTTGAAGGCAACCATATCCAT
AATTTAAGAAATTTGACTTTTATTTCCTGCAGTAATTTAACTGTTTTAGTGATGAGGAAA
AACAAAATTAATCACTTAAATGAAAATACTTTTGCACCTCTCCAGAAACTGGATGAATTG
GATTTAGGAAGTAATAAGATTGAAAATCTTCCACCGCTTATATTCAAGGACCTGAAGGAG
CTGTCACAATTGAATCTTTCCTATAATCCAATCCAGAAAATTCAAGCAAACCAATTTGAT
TATCTTGTCAAACTCAAGTCTCTCAGCCTAGAAGGGATTGAAATTTCAAATATCCAACAA
AGGATGTTTAGACCTCTTATGAATCTCTCTCACATATATTTTAAGAAATTCCAGTACTGT
GGGTATGCACCACATGTTCGCAGCTGTAAACCAAACACTGATGGAATTTCATCTCTAGAG
AATCTCTTGGCAAGCATTATTCAGAGAGTATTTGTCTGGGTTGTATCTGCAGTTACCTGC
TTTGGAAACATTTTTGTCATTTGCATGCGACCTTATATCAGGTCTGAGAACAAGCTGTAT
GCCATGTCAATCATTTCTCTCTGCTGTGCCGACTGCTTAATGGGAATATATTTATTCGTG
ATCGGAGGCTTTGACCTAAAGTTTCGTGGAGAATACAATAAGCATGCGCAGCTGTGGATG
GAGAGTACTCATTGTCAGCTTGTAGGATCTTTGGCCATTCTGTCCACAGAAGTATCAGTT
TTACTGTTAACATTTCTGACATTGGAAAAATACATCTGCATTGTCTATCCTTTTAGATGT
GTGAGACCTGGAAAATGCAGAACAATTACAGTTCTGATTCTCATTTGGATTACTGGTTTT
ATAGTGGCTTTCATTCCATTGAGCAATAAGGAATTTTTCAAAAACTACTATGGCACCAAT
GGAGTATGCTTCCCTCTTCATTCAGAAGATACAGAAAGTATTGGAGCCCAGATTTATTCA
GTGGCAATTTTTCTTGGTATTAATTTGGCCGCATTTATCATCATAGTTTTTTCCTATGGA
AGCATGTTTTATAGTGTTCATCAAAGTGCCATAACAGCAACTGAAATACGGAATCAAGTT
AAAAAAGAGATGATCCTTGCCAAACGTTTTTTCTTTATAGTATTTACTGATGCATTATGC
TGGATACCCATTTTTGTAGTGAAATTTCTTTCACTGCTTCAGGTAGAAATACCAGGTACC
ATAACCTCTTGGGTAGTGATTTTTATTCTGCCCATTAACAGTGCTTTGAACCCAATTCTC
TATACTCTGACCACAAGACCATTTAAAGAAATGATTCATCGGTTTTGGTATAACTACAGA
CAAAGAAAATCTATGGACAGCAAAGGTCAGAAAACATATGCTCCATCATTCATCTGGGTG
GAAATGTGGCCACTGCAGGAGATGCCACCTGAGTTAATGAAGCCGGACCTTTTCACATAC
CCCTGTGAAATGTCACTGATTTCTCAATCAACGAGACTCAATTCCTATTCATGA
Enzyme 60 GenBank Gene ID AF190500 Link Image
Enzyme 60 GeneCard ID RXFP1 Link Image
Enzyme 60 GenAtlas ID RXFP1 Link Image
Enzyme 60 HGNC ID HGNC:19718 Link Image
Enzyme 60 Chromosome Location 4
Enzyme 60 Locus 4q32.1
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 General References
  1. Hsu SY, Kudo M, Chen T, Nakabayashi K, Bhalla A, van der Spek PJ, van Duin M, Hsueh AJ: The three subfamilies of leucine-rich repeat-containing G protein-coupled receptors (LGR): identification of LGR6 and LGR7 and the signaling mechanism for LGR7. Mol Endocrinol. 2000 Aug;14(8):1257-71. [PubMed Link Image]
  2. Muda M, He C, Martini PG, Ferraro T, Layfield S, Taylor D, Chevrier C, Schweickhardt R, Kelton C, Ryan PL, Bathgate RA: Splice variants of the relaxin and INSL3 receptors reveal unanticipated molecular complexity. Mol Hum Reprod. 2005 Aug;11(8):591-600. Epub 2005 Jul 28. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Bartsch O, Bartlick B, Ivell R: Relaxin signalling links tyrosine phosphorylation to phosphodiesterase and adenylyl cyclase activity. Mol Hum Reprod. 2001 Sep;7(9):799-809. [PubMed Link Image]
  6. Sudo S, Kumagai J, Nishi S, Layfield S, Ferraro T, Bathgate RA, Hsueh AJ: H3 relaxin is a specific ligand for LGR7 and activates the receptor by interacting with both the ectodomain and the exoloop 2. J Biol Chem. 2003 Mar 7;278(10):7855-62. Epub 2002 Dec 27. [PubMed Link Image]
  7. Hopkins EJ, Layfield S, Ferraro T, Bathgate RA, Gooley PR: The NMR solution structure of the relaxin (RXFP1) receptor lipoprotein receptor class A module and identification of key residues in the N-terminal region of the module that mediate receptor activation. J Biol Chem. 2007 Feb 9;282(6):4172-84. Epub 2006 Dec 4. [PubMed Link Image]
Enzyme 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 7915
Enzyme 61 Name cAMP-responsive element modulator
Enzyme 61 Synonyms
  1. Inducible cAMP early repressor
  2. ICER
Enzyme 61 Gene Name CREM
Enzyme 61 Protein Sequence >cAMP-responsive element modulator
MSKCARKKYIKTNPRQMTMETVESQHDGSITASLTESKSAHVQTQTGQNSIPALAQVSVA
GSGTRRGSPAVTLVQLPSGQTIHVQGVIQTPQPWVIQSSEIHTVQVAAIAETDESAESEG
VIDSHKRREILSRRPSYRKILNELSSDVPGVPKIEEERSEEEGTPPSIATMAVPTSIYQT
STGQYIAIAQGGTIQISNPGSDGVQGLQALTMTNSGAPPPGATIVQYAAQSADGTQQFFV
PGSQVVVQDEETELAPSHMAAATGDMPTYQIRAPTAALPQGVVMAASPGSLHSPQQLAEE
ATRKRELRLMKNREAAKECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKDICSPKTD
Y
Enzyme 61 Number of Residues 361
Enzyme 61 Molecular Weight 38939.6
Enzyme 61 Theoretical pI 6.63
Enzyme 61 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
  • protein binding
  • protein dimerization activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 61 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 61 Specific Function Transcriptional regulator that binds the cAMP response element (CRE), a sequence present in many viral and cellular promoters. Isoforms are either transcriptional activators or repressors. Plays a role in spermatogenesis and is involved in spermatid maturation
Enzyme 61 Pathways Not Available
Enzyme 61 Reactions Not Available
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • None
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein 114630088 Link Image
Enzyme 61 UniProtKB/Swiss-Prot ID Q03060 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name CREM_HUMAN Link Image
Enzyme 61 PDB ID Not Available
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence >1050 bp
ATGAGCAAATGTGCAAGGAAAAAATATATTAAGACAAATCCAAGACAAATGACCATGGAA
ACAGTTGAATCCCAGCATGATGGAAGTATAACAGCTTCTTTGACAGAGAGCAAGTCTGCT
CATGTGCAGACTCAGACTGGCCAAAATTCAATCCCTGCTTTAGCTCAGGTTTCTGTGGCT
GGATCAGGCACCGGAAGAGGCTCCCCAGCTGTAACTCTAGTGCAGTTACCTTCGGGCCAA
ACTATACATGTCCAGGGAGTAATTCAGACACCACAGCCATCGGTTATTCAGTCATCACAA
ATACACACCGTTCAGGTAGCAGCAATTGCAGAGACAGATGAATCTGCAGAATCAGAAGGT
GTAATTGATTCTCATAAACGTAGAGAAATCCTTTCACGAAGACCCTCTTATAGGAAAATA
CTGAATGAACTGTCCTCTGATGTGCCTGGTGTTCCCAAGATTGAAGAAGAGAGATCAGAG
GAAGAAGGAACACCACCTAGTATTGCTACCATGGCAGTACCAACTAGCATATATCAGACT
AGCACGGGGCAATACATTGCTATAGCCCAAGGTGGAACAATCCAGATTTCTAACCCAGGA
TCTGATGGTGTTCAGGGACTGCAGGCATTAACAATGACAAATTCAGGAGCTCCTCCACCA
GGTGCTACAATTGTACAGTATGCAGCACAATCAGCTGATGGCACACAGCAGTTCTTTGTC
CCAGGCAGCCAGGTTGTTGTTCCAGCTGCCACTGGTGACATGCCAACTTACCAGATCCGA
GCTCCTACTGCTGCTTTGCCACAGGGAGTGGTGATGGCTGCATCGCCCGGAAGTTTGCAC
AGTCCCCAGCAGCTGGCAGAAGAAGCAACACGCAAACGAGAGCTAAGGCTAATGAAAAAC
AGGGAAGCTGCCAAAGAATGTCGACGTCGAAAGAAAGAATATGTAAAATGTCTGGAGAGC
CGAGTTGCAGTGCTGGAAGTCCAGAACAAGAAGCTTATAGAGGAACTTGAAACCTTGAAA
GACATTTGTTCTCCCAAAACAGATTACTAG
Enzyme 61 GenBank Gene ID XM_001148291 Link Image
Enzyme 61 GeneCard ID CREM Link Image
Enzyme 61 GenAtlas ID CREM Link Image
Enzyme 61 HGNC ID HGNC:2352 Link Image
Enzyme 61 Chromosome Location 1
Enzyme 61 Locus 10p11.21
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 General References
  1. Fujimoto T, Fujisawa J, Yoshida M: Novel isoforms of human cyclic AMP-responsive element modulator (hCREM) mRNA. J Biochem. 1994 Feb;115(2):298-303. [PubMed Link Image]
  2. Bodor J, Spetz AL, Strominger JL, Habener JF: cAMP inducibility of transcriptional repressor ICER in developing and mature human T lymphocytes. Proc Natl Acad Sci U S A. 1996 Apr 16;93(8):3536-41. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gellersen B, Kempf R, Sandhowe R, Weinbauer GF, Behr R: Novel leader exons of the cyclic adenosine 3',5'-monophosphate response element modulator (CREM) gene, transcribed from promoters P3 and P4, are highly testis-specific in primates. Mol Hum Reprod. 2002 Nov;8(11):965-76. [PubMed Link Image]
  7. Masquilier D, Foulkes NS, Mattei MG, Sassone-Corsi P: Human CREM gene: evolutionary conservation, chromosomal localization, and inducibility of the transcript. Cell Growth Differ. 1993 Nov;4(11):931-7. [PubMed Link Image]
  8. Meyer TE, Habener JF: Cyclic AMP response element binding protein CREB and modulator protein CREM are products of distinct genes. Nucleic Acids Res. 1992 Nov 25;20(22):6106. [PubMed Link Image]
  9. Vouk K, Hudler P, Strmsnik L, Fink M, Majdic G, Zorn B, Lalli E, Sassone-Corsi P, Debeljak N, Komel R, Rozman D: Combinations of genetic changes in the human cAMP-responsive element modulator gene: a clue towards understanding some forms of male infertility? Mol Hum Reprod. 2005 Aug;11(8):567-74. Epub 2005 Sep 2. [PubMed Link Image]
  10. Pati D, Meistrich ML, Plon SE: Human Cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors of cyclic AMP-induced transcription for proteolysis. Mol Cell Biol. 1999 Jul;19(7):5001-13. [PubMed Link Image]
  11. Behr R, Weinbauer GF: CREM activator and repressor isoforms in human testis: sequence variations and inaccurate splicing during impaired spermatogenesis. Mol Hum Reprod. 2000 Nov;6(11):967-72. [PubMed Link Image]
  12. Blocher S, Behr R, Weinbauer GF, Bergmann M, Steger K: Different CREM-isoform gene expression between equine and human normal and impaired spermatogenesis. Theriogenology. 2003 Oct 15;60(7):1357-69. [PubMed Link Image]
  13. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  14. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 8008
Enzyme 62 Name Adiponectin
Enzyme 62 Synonyms
  1. 30 kDa adipocyte complement-related protein
  2. Adipocyte complement-related 30 kDa protein
  3. ACRP30
  4. Adipocyte, C1q and collagen domain-containing protein
  5. Adipose most abundant gene transcript 1 protein
  6. apM-1
  7. Gelatin-binding protein
Enzyme 62 Gene Name ADIPOQ
Enzyme 62 Protein Sequence >Adiponectin
MLLLGAVLLLLALPGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDG
TPGEKGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSVGLE
TYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKDVKVSLFKKDK
AMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGERNGLYADNDNDSTFTGFLLY
HDTN
Enzyme 62 Number of Residues 244
Enzyme 62 Molecular Weight 26413.6
Enzyme 62 Theoretical pI 5.53
Enzyme 62 GO Classification Not Available
Enzyme 62 General Function Involved in cytokine activity
Enzyme 62 Specific Function Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW
Enzyme 62 Pathways Not Available
Enzyme 62 Reactions Not Available
Enzyme 62 Pfam Domain Function
Enzyme 62 Signals
  • 1-18
Enzyme 62 Transmembrane Regions
  • None
Enzyme 62 Essentiality Not Available
Enzyme 62 GenBank ID Protein 6362247 Link Image
Enzyme 62 UniProtKB/Swiss-Prot ID Q15848 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name ADIPO_HUMAN Link Image
Enzyme 62 PDB ID 1C3H Link Image
Enzyme 62 PDB File Show
Enzyme 62 3D Structure
Enzyme 62 Cellular Location Not Available
Enzyme 62 Gene Sequence >735 bp
ATGCTGTTGCTGGGAGCTGTTCTACTGCTATTAGCTCTGCCCGGTCATGACCAGGAAACC
ACGACTCAAGGGCCCGGAGTCCTGCTTCCCCTGCCCAAGGGGGCCTGCACAGGTTGGATG
GCGGGCATCCCAGGGCATCCGGGCCATAATGGGGCCCCAGGCCGTGATGGCAGAGATGGC
ACCCCTGGTGAGAAGGGTGAGAAAGGAGATCCAGGTCTTATTGGTCCTAAGGGAGACATC
GGTGAAACCGGAGTACCCGGGGCTGAAGGTCCCCGAGGCTTTCCGGGAATCCAAGGCAGG
AAAGGAGAACCTGGAGAAGGTGCCTATGTATACCGCTCAGCATTCAGTGTGGGATTGGAG
ACTTACGTTACTATCCCCAACATGCCCATTCGCTTTACCAAGATCTTCTACAATCAGCAA
AACCACTATGATGGCTCCACTGGTAAATTCCACTGCAACATTCCTGGGCTGTACTACTTT
GCCTACCACATCACAGTCTATATGAAGGATGTGAAGGTCAGCCTCTTCAAGAAGGACAAG
GCTATGCTCTTCACCTATGATCAGTACCAGGAAAATAATGTGGACCAGGCCTCCGGCTCT
GTGCTCCTGCATCTGGAGGTGGGCGACCAAGTCTGGCTCCAGGTGTATGGGGAAGGAGAG
CGTAATGGACTCTATGCTGATAATGACAATGACTCCACCTTCACAGGCTTTCTTCTCTAC
CATGACACCAACTGA
Enzyme 62 GenBank Gene ID AB012165 Link Image
Enzyme 62 GeneCard ID ADIPOQ Link Image
Enzyme 62 GenAtlas ID ADIPOQ Link Image
Enzyme 62 HGNC ID HGNC:13633 Link Image
Enzyme 62 Chromosome Location 3
Enzyme 62 Locus 3q27
Enzyme 62 SNPs SNPJam Report Link Image
Enzyme 62 General References
  1. Maeda K, Okubo K, Shimomura I, Funahashi T, Matsuzawa Y, Matsubara K: cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1). Biochem Biophys Res Commun. 1996 Apr 16;221(2):286-9. [PubMed Link Image]
  2. Saito K, Tobe T, Minoshima S, Asakawa S, Sumiya J, Yoda M, Nakano Y, Shimizu N, Tomita M: Organization of the gene for gelatin-binding protein (GBP28). Gene. 1999 Mar 18;229(1-2):67-73. [PubMed Link Image]
  3. Schaffler A, Orso E, Palitzsch KD, Buchler C, Drobnik W, Furst A, Scholmerich J, Schmitz G: The human apM-1, an adipocyte-specific gene linked to the family of TNF's and to genes expressed in activated T cells, is mapped to chromosome 1q21.3-q23, a susceptibility locus identified for familial combined hyperlipidaemia (FCH). Biochem Biophys Res Commun. 1999 Jul 5;260(2):416-25. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [PubMed Link Image]
  6. Nakano Y, Tobe T, Choi-Miura NH, Mazda T, Tomita M: Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma. J Biochem. 1996 Oct;120(4):803-12. [PubMed Link Image]
  7. Yokota T, Oritani K, Takahashi I, Ishikawa J, Matsuyama A, Ouchi N, Kihara S, Funahashi T, Tenner AJ, Tomiyama Y, Matsuzawa Y: Adiponectin, a new member of the family of soluble defense collagens, negatively regulates the growth of myelomonocytic progenitors and the functions of macrophages. Blood. 2000 Sep 1;96(5):1723-32. [PubMed Link Image]
  8. Ouchi N, Kihara S, Arita Y, Okamoto Y, Maeda K, Kuriyama H, Hotta K, Nishida M, Takahashi M, Muraguchi M, Ohmoto Y, Nakamura T, Yamashita S, Funahashi T, Matsuzawa Y: Adiponectin, an adipocyte-derived plasma protein, inhibits endothelial NF-kappaB signaling through a cAMP-dependent pathway. Circulation. 2000 Sep 12;102(11):1296-301. [PubMed Link Image]
  9. Yamauchi T, Kamon J, Waki H, Terauchi Y, Kubota N, Hara K, Mori Y, Ide T, Murakami K, Tsuboyama-Kasaoka N, Ezaki O, Akanuma Y, Gavrilova O, Vinson C, Reitman ML, Kagechika H, Shudo K, Yoda M, Nakano Y, Tobe K, Nagai R, Kimura S, Tomita M, Froguel P, Kadowaki T: The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity. Nat Med. 2001 Aug;7(8):941-6. [PubMed Link Image]
  10. Waki H, Yamauchi T, Kamon J, Ito Y, Uchida S, Kita S, Hara K, Hada Y, Vasseur F, Froguel P, Kimura S, Nagai R, Kadowaki T: Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin. J Biol Chem. 2003 Oct 10;278(41):40352-63. Epub 2003 Jul 23. [PubMed Link Image]
  11. Richards AA, Stephens T, Charlton HK, Jones A, Macdonald GA, Prins JB, Whitehead JP: Adiponectin multimerization is dependent on conserved lysines in the collagenous domain: evidence for regulation of multimerization by alterations in posttranslational modifications. Mol Endocrinol. 2006 Jul;20(7):1673-87. Epub 2006 Feb 23. [PubMed Link Image]
  12. Takahashi M, Arita Y, Yamagata K, Matsukawa Y, Okutomi K, Horie M, Shimomura I, Hotta K, Kuriyama H, Kihara S, Nakamura T, Yamashita S, Funahashi T, Matsuzawa Y: Genomic structure and mutations in adipose-specific gene, adiponectin. Int J Obes Relat Metab Disord. 2000 Jul;24(7):861-8. [PubMed Link Image]
  13. Hara K, Boutin P, Mori Y, Tobe K, Dina C, Yasuda K, Yamauchi T, Otabe S, Okada T, Eto K, Kadowaki H, Hagura R, Akanuma Y, Yazaki Y, Nagai R, Taniyama M, Matsubara K, Yoda M, Nakano Y, Tomita M, Kimura S, Ito C, Froguel P, Kadowaki T: Genetic variation in the gene encoding adiponectin is associated with an increased risk of type 2 diabetes in the Japanese population. Diabetes. 2002 Feb;51(2):536-40. [PubMed Link Image]
  14. Kondo H, Shimomura I, Matsukawa Y, Kumada M, Takahashi M, Matsuda M, Ouchi N, Kihara S, Kawamoto T, Sumitsuji S, Funahashi T, Matsuzawa Y: Association of adiponectin mutation with type 2 diabetes: a candidate gene for the insulin resistance syndrome. Diabetes. 2002 Jul;51(7):2325-8. [PubMed Link Image]
  15. Vasseur F, Helbecque N, Dina C, Lobbens S, Delannoy V, Gaget S, Boutin P, Vaxillaire M, Lepretre F, Dupont S, Hara K, Clement K, Bihain B, Kadowaki T, Froguel P: Single-nucleotide polymorphism haplotypes in the both proximal promoter and exon 3 of the APM1 gene modulate adipocyte-secreted adiponectin hormone levels and contribute to the genetic risk for type 2 diabetes in French Caucasians. Hum Mol Genet. 2002 Oct 1;11(21):2607-14. [PubMed Link Image]
Enzyme 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 8059
Enzyme 63 Name cAMP-dependent protein kinase type I-alpha regulatory subunit
Enzyme 63 Synonyms
  1. Tissue-specific extinguisher 1
  2. TSE1
Enzyme 63 Gene Name PRKAR1A
Enzyme 63 Protein Sequence >cAMP-dependent protein kinase type I-alpha regulatory subunit
MESGSTAASEEARSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFERLEKE
EAKQIQNLQKAGTRTDSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPK
DYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFSVSFIAGETVIQQGDEGDNFYVIDQG
ETDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTL
RKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSA
AVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLG
PCSDILKRNIQQYNSFVSLSV
Enzyme 63 Number of Residues 381
Enzyme 63 Molecular Weight 42981.3
Enzyme 63 Theoretical pI 5.00
Enzyme 63 GO Classification
Function
  • cAMP-dependent protein kinase regulator activity
  • enzyme regulator activity
  • kinase regulator activity
  • protein kinase regulator activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular metabolic process
  • regulation of cellular process
  • regulation of cellular protein metabolic process
  • regulation of metabolic process
  • regulation of protein amino acid phosphorylation
  • regulation of protein modification process
  • signal transduction
Component
  • cAMP-dependent protein kinase complex
  • macromolecular complex
  • protein complex
Enzyme 63 General Function Involved in cAMP-dependent protein kinase regulator activity
Enzyme 63 Specific Function Not Available
Enzyme 63 Pathways Not Available
Enzyme 63 Reactions Not Available
Enzyme 63 Pfam Domain Function
Enzyme 63 Signals
  • None
Enzyme 63 Transmembrane Regions
  • None
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein 179922 Link Image
Enzyme 63 UniProtKB/Swiss-Prot ID P10644 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name KAP0_HUMAN Link Image
Enzyme 63 PDB ID 1RL3 Link Image
Enzyme 63 PDB File Show
Enzyme 63 3D Structure
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence >1146 bp
ATGGAGTCTGGCAGTACCGCCGCCAGTGAGGAGGCACGCAGCCTTCGAGAATGTGAGCTC
TACGTCCAGAAGCATAACATTCAAGCGCTGCTCAAAGATTCTATTGTGCAGTTGTGCACT
GCTCGACCTGAGAGACCCATGGCATTCCTCAGGGAATACTTTGAGAGGTTGGAGAAGGAG
GAGGCAAAACAGATTCAGAATCTGCAGAAAGCAGGCACTCGTACAGACTCAAGGGAGGAT
GAGATTTCTCCTCCTCCACCCAACCCAGTGGTTAAAGGTAGGAGGCGACGAGGTGCTATC
AGCGCTGAGGTCTACACGGAGGAAGATGCGGCATCCTATGTTAGAAAGGTTATACCAAAA
GATTACAAGACAATGGCCGCTTTAGCCAAAGCCATTGAAAAGAATGTGCTGTTTTCACAT
CTTGATGATAATGAGAGAAGTGATATTTTTGATGCCATGTTTTCGGTCTCCTTTATCGCA
GGAGAGACTGTGATTCAGCAAGGTGATGAAGGGGATAACTTCTATGTGATTGATCAAGGA
GAGACGGATGTCTATGTTAACAATGAATGGGCAACCAGTGTTGGGGAAGGAGGGAGCTTT
GGAGAACTTGCTTTGATTTATGGAACACCGAGAGCAGCCACTGTCAAAGCAAAGACAAAT
GTGAAATTGTGGGGCATCGACCGAGACAGCTATAGAAGAATCCTCATGGGAAGCACACTG
AGAAAGCGGAAGATGTATGAGGAATTCCTTAGTAAAGTCTCTATTTTAGAGTCTCTGGAC
AAGTGGGAACGTCTTACGGTAGCTGATGCATTGGAACCAGTGCAGTTTGAAGATGGGCAG
AAGATTGTGGTGCAGGGAGAACCAGGGGATGAGTTCTTCATTATTTTAGAGGGGTCAGCT
GCTGTGCTACAACGTCGGTCAGAAAATGAAGAGTTTGTTGAAGTGGGAAGATTGGGGCCT
TCTGATTATTTTGGTGAAATTGCACTACTGATGAATCGTCCTCGTGCTGCCACAGTTGTT
GCTCGTGGCCCCTTGAAGTGCGTTAAGCTGGACCGACCTAGATTTGAACGTGTTCTTGGC
CCATGCTCAGACATCCTCAAACGAAACATCCAGCAGTACAACAGTTTTGTGTCACTGTCT
GTCTGA
Enzyme 63 GenBank Gene ID M18468 Link Image
Enzyme 63 GeneCard ID PRKAR1A Link Image
Enzyme 63 GenAtlas ID PRKAR1A Link Image
Enzyme 63 HGNC ID HGNC:9388 Link Image
Enzyme 63 Chromosome Location 1
Enzyme 63 Locus 17q23-q24
Enzyme 63 SNPs SNPJam Report Link Image
Enzyme 63 General References
  1. Sandberg M, Tasken K, Oyen O, Hansson V, Jahnsen T: Molecular cloning, cDNA structure and deduced amino acid sequence for a type I regulatory subunit of cAMP-dependent protein kinase from human testis. Biochem Biophys Res Commun. 1987 Dec 31;149(3):939-45. [PubMed Link Image]
  2. Sandberg M, Skalhegg B, Jahnsen T: The two mRNA forms for the type I alpha regulatory subunit of cAMP-dependent protein kinase from human testis are due to the use of different polyadenylation site signals. Biochem Biophys Res Commun. 1990 Feb 28;167(1):323-30. [PubMed Link Image]
  3. Jones KW, Shapero MH, Chevrette M, Fournier RE: Subtractive hybridization cloning of a tissue-specific extinguisher: TSE1 encodes a regulatory subunit of protein kinase A. Cell. 1991 Sep 6;66(5):861-72. [PubMed Link Image]
  4. Solberg R, Sandberg M, Natarajan V, Torjesen PA, Hansson V, Jahnsen T, Tasken K: The human gene for the regulatory subunit RI alpha of cyclic adenosine 3', 5'-monophosphate-dependent protein kinase: two distinct promoters provide differential regulation of alternately spliced messenger ribonucleic acids. Endocrinology. 1997 Jan;138(1):169-81. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  7. Groussin L, Jullian E, Perlemoine K, Louvel A, Leheup B, Luton JP, Bertagna X, Bertherat J: Mutations of the PRKAR1A gene in Cushing's syndrome due to sporadic primary pigmented nodular adrenocortical disease. J Clin Endocrinol Metab. 2002 Sep;87(9):4324-9. [PubMed Link Image]
  8. Gupte RS, Weng Y, Liu L, Lee MY: The second subunit of the replication factor C complex (RFC40) and the regulatory subunit (RIalpha) of protein kinase A form a protein complex promoting cell survival. Cell Cycle. 2005 Feb;4(2):323-9. Epub 2005 Feb 13. [PubMed Link Image]
  9. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  10. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  11. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  12. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  13. Carrascal M, Ovelleiro D, Casas V, Gay M, Abian J: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. J Proteome Res. 2008 Dec;7(12):5167-76. [PubMed Link Image]
  14. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  15. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  16. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
  17. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  18. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  19. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  20. Veugelers M, Wilkes D, Burton K, McDermott DA, Song Y, Goldstein MM, La Perle K, Vaughan CJ, O'Hagan A, Bennett KR, Meyer BJ, Legius E, Karttunen M, Norio R, Kaariainen H, Lavyne M, Neau JP, Richter G, Kirali K, Farnsworth A, Stapleton K, Morelli P, Takanashi Y, Bamforth JS, Eitelberger F, Noszian I, Manfroi W, Powers J, Mochizuki Y, Imai T, Ko GT, Driscoll DA, Goldmuntz E, Edelberg JM, Collins A, Eccles D, Irvine AD, McKnight GS, Basson CT: Comparative PRKAR1A genotype-phenotype analyses in humans with Carney complex and prkar1a haploinsufficient mice. Proc Natl Acad Sci U S A. 2004 Sep 28;101(39):14222-7. Epub 2004 Sep 15. [PubMed Link Image]
  21. Greene EL, Horvath AD, Nesterova M, Giatzakis C, Bossis I, Stratakis CA: In vitro functional studies of naturally occurring pathogenic PRKAR1A mutations that are not subject to nonsense mRNA decay. Hum Mutat. 2008 May;29(5):633-9. [PubMed Link Image]
Enzyme 63 Metabolite References Not Available
Enzyme 64 [top]
Enzyme 64 ID 8117
Enzyme 64 Name Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
Enzyme 64 Synonyms
  1. Brain cyclic nucleotide-gated channel 2
  2. BCNG-2
Enzyme 64 Gene Name HCN2
Enzyme 64 Protein Sequence >Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
MDARGGGGRPGESPGATPAPGPPPPPPPAPPQQQPPPPPPPAPPPGPGPAPPQHPPRAEA
LPPEAADEGGPRGRLRSRDSSCGRPGTPGAASTAKGSPNGECGRGEPQCSPAGPEGPARG
PKVSFSCRGAASGPAPGPGPAEEAGSEEAGPAGEPRGSQASFMQRQFGALLQPGVNKFSL
RMFGSQKAVEREQERVKSAGAWIIHPYSDFRFYWDFTMLLFMVGNLIIIPVGITFFKDET
TAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIP
VDYIFLIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDL
ASAVMRICNLISMMLLLCHWDGCLQFLVPMLQDFPRNCWVSINGMVNHSWSELYSFALFK
AMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKY
KQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVA
SMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKEMK
LSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRL
DRIGKKNSILLHKVQHDLNSGVFNNQENAIIQEIVKYDREMVQQAELGQRVGLFPPPPPP
PQVTSAIATLQQAAAMSFCPQVARPLVGPLALGSPRLVRRPPPGPAPAAASPGPPPPASP
PGAPASPRAPRTSPYGGLPAAPLAGPALPARRLSRASRPLSASQPSLPHGAPGPAASTRP
ASSSTPRLGPTPAARAAAPSPDRRDSASPGAAGGLDPQDSARSRLSSNL
Enzyme 64 Number of Residues 889
Enzyme 64 Molecular Weight 96949.4
Enzyme 64 Theoretical pI 9.21
Enzyme 64 GO Classification
Function
  • cation channel activity
  • ion channel activity
  • ion transmembrane transporter activity
  • potassium channel activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
  • voltage-gated potassium channel activity
Process
  • cation transport
  • establishment of localization
  • ion transport
  • monovalent inorganic cation transport
  • potassium ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 64 General Function Involved in ion channel activity
Enzyme 64 Specific Function Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Produces a large instantaneous current. Activated by cAMP. Modulated by intracellular chloride ions and pH; acidic pH shifts the activation to more negative voltages
Enzyme 64 Pathways Not Available
Enzyme 64 Reactions Not Available
Enzyme 64 Pfam Domain Function
Enzyme 64 Signals
  • None
Enzyme 64 Transmembrane Regions
  • 216-236 241-261 289-309 318-338 370-390 441-461
Enzyme 64 Essentiality Not Available
Enzyme 64 GenBank ID Protein 4996894 Link Image
Enzyme 64 UniProtKB/Swiss-Prot ID Q9UL51 Link Image
Enzyme 64 UniProtKB/Swiss-Prot Entry Name HCN2_HUMAN Link Image
Enzyme 64 PDB ID 1Q3E Link Image
Enzyme 64 PDB File Show
Enzyme 64 3D Structure
Enzyme 64 Cellular Location Not Available
Enzyme 64 Gene Sequence >2670 bp
ATGGACGCGCGCGGGGGCGGCGGGCGGCCCGGGGAGAGCCCGGGCGCGAGCCCCACGACC
GGGCCGCCGCCGCCGCCGCCCCCGCGCCCCCCCAAACAGCAGCCGCCGCCGCCGCCGCCG
CCCGCGCCCCCCCCGGGCCCCGGGCCCGCGCCCCCCCAGCACCCGCCCCGGGCCGAGGCG
TTGCCCCCGGAGGCGGCGGATGAGGGCGGCCCGCGGGGCCGGCTCCGCAGCCGCGACAGC
TCGTGCGGCCGCCCCGGCACCCCGGGCGCGGCGAGCACGGCCAAGGGCAGCCCGAACGGC
GAGTGCGGGCGCGGCGAGCCGCAGTGCAGCCCCGCGGGGCCCGAGGGCCCGGCGCGGGGG
CCCAAGGTGTCGTTCTCGTGCCGCGGGGCGGCCTCGGGGCCCGCGCCGGGGCCGGGGCCG
GCGGAGGAGGCGGGCAGCGAGGAGGCGGGCCCGGCGGGGGAGCCGCGCGGCAGCCAGGCC
AGCTTCATGCAGCGCCAGTTCGGCGCGCTCCTGCAGCCGGGCGTCAACAAGTTCTCGCTG
CGGATGTTCGGCAGCCAGAAGGCCGTGGAGCGCGAGCAGGAGCGCGTCAAGTCGGCGGGG
GCCTGGATCATCCACCCGTACAGCGACTTCAGGTTCTACTGGGACTTCACCATGCTGCTG
TTCATGGTGGGAAACCTCATCATCATCCCAGTGGGCATCACCTTCTTCAAGGATGAGACC
ACTGCCCCGTGGATCGTGTTCAACGTGGTCTCGGACACCTTCTTCCTCATGGACCTGGTG
TTGAACTTCCGCACCGGCATTGTGATCGAGGACAACACGGAGATCATCCTGGACCCCGAG
AAGATCAAGAAGAAGTATCTGCGCACGTGGTTCGTGGTGGACTTCGTGTCCTCCATCCCC
GTGGACTACATCTTCCTTATCGTGGAGAAGGGCATTGACTCCGAGGTCTACAAGACGGCA
CGCGCCCTGCGCATCGTGCGCTTCACCAAGATCCTCAGCCTCCTGCGGCTGCTGCGCCTC
TCACGCCTGATCCGCTACATCCATCAGTGGGAGGAGATCTTCCACATGACCTATGACCTG
GCCAGCGCGGTGATGAGGATCTGCAATCTCATCAGCATGATGCTGCTGCTCTGCCACTGG
GACGGCTGCCTGCAGTTCCTGGTGCCTATGCTGCAGGACTTCCCGCGCAACTGCTGGGTG
TCCATCAATGGCATGGTGAACCACTCGTGGAGTGAACTGTACTCCTTCGCACTCTTCAAG
GCCATGAGCCACATGCTGTGCATCGGGTACGGCCGGCAGGCGCCCGAGAGCATGACGGAC
ATCTGGCTGACCATGCTCAGCATGATTGTGGGTGCCACCTGCTACGCCATGTTCATCGGC
CACGCCACTGCCCTCATCCAGTCGCTGGACTCCTCGCGGCGCCAGTACCAGGAGAAGTAC
AAGCAGGTGGAGCAGTACATGTCCTTCCACAAGCTGCCAGCTGACTTCCGCCAGAAGATC
CACGACTACTATGAGCACCGTTACCAGGGCAAGATGTTTGACGAGGACAGCATCCTGGGC
GAGCTCAACGGGCCCCTGCGGGAGGAGATCGTCAACTTCAACTGCCGGAAGCTGGTGGCC
TCCATGCCGCTGTTCGCCAACGCCGACCCCAACTTCGTCACGGCCATGCTGACCAAGCTC
AAGTTCGAGGTCTTCCAGCCGGGTGACTACATCATCCGCGAAGGCACCATCGGGAAGAAG
ATGTACTTCATCCAGCACGGCGTGGTCAGCGTGCTCACTAAGGGCAACAAGGAGATGAAG
CTGTCCGATGGCTCCTACTTCGGGGAGATCTGCCTGCTCACCCGGGGCCGCCGCACGGCG
AGCGTGCGGGCTGACACCTACTGCCGCCTCTATTCGCTGAGCGTGGACAACTTCAACGAG
GTGCTGGAGGAGTACCCCATGATGCGGCGCGCCTTCGAGACGGTGGCCATCGACCGCCTG
GACCGCATCGGCAAGAAGAATTCCATCCTCCTGCACAAGGTGCAGCATGACCTCAACTCG
GGCGTATTCAACAACCAGGAGAACGCCATCATCCAGGAGATCGTCAAGTACGACCGCGAG
ATGGTGCAGCAGGCCGAGCTGGGTCAGCGCGTGGGCCTCTTCCCGCCGCCGCCGCCGCCG
CCGCAGGTCACCTCGGCCATCGCCACGCTGCAGCAGGCGGCGGCCATGAGCTTCTGCCCG
CAGGTGGCGCGGCCGCTCGTGGGGCCGCTGGCGCTCGGCTCGCCGCGCCTCGTGCGCCGC
CCGCCCCCGGGGCCCGCACCTGCCGCCGCCTCACCCGGGCCCCCGCCCCCCGCCAGCCCC
CCGGGCGCGCCCGCCAGCCCCCGGGCACCGCGGACCTCGCCCTACGGCGGCCTGCCCGCC
GCCCCCCTTGCTGGGCCCGCCCTGCCCGCGCGCCGCCTGAGCCGCGCGTCGCGCCCACTG
TCCGCCTCGCAGCCCTCGCTGCCTCACGGCGCCCCCGGCCCCGCGGCCTCCACACGCCCG
GCCAGCAGCTCCACACCGCGCTTGGGGCCCACGCCCGCTGCCCGGGCCGCCGCGCCCAGC
CCGGACCGCAGGGACTCGGCCTCACCCGGCGCCGCCGGCGGCCTGGACCCCCAGGACTCC
GCGCGCTCGCGCCTCTCGTCCAACTTGTGA
Enzyme 64 GenBank Gene ID AF065164 Link Image
Enzyme 64 GeneCard ID HCN2 Link Image
Enzyme 64 GenAtlas ID HCN2 Link Image
Enzyme 64 HGNC ID HGNC:4846 Link Image
Enzyme 64 Chromosome Location 1
Enzyme 64 Locus 19p13.3
Enzyme 64 SNPs SNPJam Report Link Image
Enzyme 64 General References
  1. Vaccari T, Moroni A, Rocchi M, Gorza L, Bianchi ME, Beltrame M, DiFrancesco D: The human gene coding for HCN2, a pacemaker channel of the heart. Biochim Biophys Acta. 1999 Sep 3;1446(3):419-25. [PubMed Link Image]
  2. Ludwig A, Zong X, Stieber J, Hullin R, Hofmann F, Biel M: Two pacemaker channels from human heart with profoundly different activation kinetics. EMBO J. 1999 May 4;18(9):2323-9. [PubMed Link Image]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Santoro B, Liu DT, Yao H, Bartsch D, Kandel ER, Siegelbaum SA, Tibbs GR: Identification of a gene encoding a hyperpolarization-activated pacemaker channel of brain. Cell. 1998 May 29;93(5):717-29. [PubMed Link Image]
Enzyme 64 Metabolite References Not Available
Enzyme 65 [top]
Enzyme 65 ID 8122
Enzyme 65 Name Cortistatin
Enzyme 65 Synonyms
  1. Cortistatin-29
  2. Cortistatin-17
Enzyme 65 Gene Name CORT
Enzyme 65 Protein Sequence >Cortistatin
MPLSPGLLLLLLSGATATAALPLEGGPTGRDSEHMQEAAGIRKSSLLTFLAWWFEWTSQA
SAGPLIGEEAREVARRQEGAPPQQSARRDRMPCRNFFWKTFSSCK
Enzyme 65 Number of Residues 105
Enzyme 65 Molecular Weight 11532.0
Enzyme 65 Theoretical pI 8.82
Enzyme 65 GO Classification
Function
  • binding
  • hormone activity
  • protein binding
  • receptor binding
Process
Component
  • extracellular region
Enzyme 65 General Function Involved in hormone activity
Enzyme 65 Specific Function Binds to all human somatostatin receptor (SSTR) subtypes. It also inhibits cAMP production induced by forskolin through SSTRs
Enzyme 65 Pathways Not Available
Enzyme 65 Reactions Not Available
Enzyme 65 Pfam Domain Function
Enzyme 65 Signals
  • 1-18
Enzyme 65 Transmembrane Regions
  • None
Enzyme 65 Essentiality Not Available
Enzyme 65 GenBank ID Protein 2055232 Link Image
Enzyme 65 UniProtKB/Swiss-Prot ID O00230 Link Image
Enzyme 65 UniProtKB/Swiss-Prot Entry Name CORT_HUMAN Link Image
Enzyme 65 PDB ID Not Available
Enzyme 65 Cellular Location Not Available
Enzyme 65 Gene Sequence >318 bp
ATGCCATTGTCCCCCGGCCTCCTGCTGCTGCTGCTCTCCGGGGCCACGGCCACCGCTGCC
CTGCCCCTGGAGGGTGGCCCCACCGGCCGAGACAGCGAGCATATGCAGGAAGCGGCAGGA
ATAAGGAAAAGCAGCCTCCTGACTTTCCTCGCTTGGTGGTTTGAGTGGACCTCCCAGGCC
AGTGCCGGGCCCCTCATAGGAGAGGAAGCTCGGGAGGTGGCCAGGCGGCAGGAAGGCGCA
CCCCCCCAGCAATCCGCGCGCCGGGACAGAATGCCCTGCAGGAACTTCTTCTGGAAGACC
TTCTCCTCCTGCAAATAA
Enzyme 65 GenBank Gene ID AB000263 Link Image
Enzyme 65 GeneCard ID CORT Link Image
Enzyme 65 GenAtlas ID CORT Link Image
Enzyme 65 HGNC ID HGNC:2257 Link Image
Enzyme 65 Chromosome Location 1
Enzyme 65 Locus 1p36|1p36.22
Enzyme 65 SNPs SNPJam Report Link Image
Enzyme 65 General References
  1. Fukusumi S, Kitada C, Takekawa S, Kizawa H, Sakamoto J, Miyamoto M, Hinuma S, Kitano K, Fujino M: Identification and characterization of a novel human cortistatin-like peptide. Biochem Biophys Res Commun. 1997 Mar 6;232(1):157-63. [PubMed Link Image]
  2. de Lecea L, Ruiz-Lozano P, Danielson PE, Peelle-Kirley J, Foye PE, Frankel WN, Sutcliffe JG: Cloning, mRNA expression, and chromosomal mapping of mouse and human preprocortistatin. Genomics. 1997 Jun 15;42(3):499-506. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 65 Metabolite References Not Available
Enzyme 66 [top]
Enzyme 66 ID 8165
Enzyme 66 Name Perilipin-1
Enzyme 66 Synonyms
  1. Lipid droplet-associated protein
Enzyme 66 Gene Name PLIN1
Enzyme 66 Protein Sequence >Perilipin-1
MAVNKGLTLLDGDLPEQENVLQRVLQLPVVSGTCECFQKTYTSTKEAHPLVASVCNAYEK
GVQSASSLAAWSMEPVVRRLSTQFTAANELACRGLDHLEEKIPALQYPPEKIASELKDTI
STRLRSARNSISVPIASTSDKVLGAALAGCELAWGVARDTAEFAANTRAGRLASGGADLA
LGSIEKVVEYLLPPDKEESAPAPGHQQAQKSPKAKPSLLSRVGALTNTLSRYTVQTMARA
LEQGHTVAMWIPGVVPLSSLAQWGASVAMQAVSRRRSEVRVPWLHSLAAAQEEDHEDQTD
TEGEDTEEEEELETEENKFSEVAALPGPRGLLGGVAHTLQKTLQTTISAVTWAPAAVLGM
AGRVLHLTPAPAVSSTKGRAMSLSDALKGVTDNVVDTVVHYVPLPRLSLMEPESEFRDID
NPPAEVERREAERRASGAPSAGPEPAPRLAQPRRSLRSAQSPGAPPGPGLEDEVATPAAP
RPGFPAVPREKPKRRVSDSFFRPSVMEPILGRTHYSQLRKKS
Enzyme 66 Number of Residues 522
Enzyme 66 Molecular Weight 55989.8
Enzyme 66 Theoretical pI 6.37
Enzyme 66 GO Classification Not Available
Enzyme 66 General Function Involved in lipid binding
Enzyme 66 Specific Function Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone- sensitive lipase (HSL). Its absence may result in leanness
Enzyme 66 Pathways Not Available
Enzyme 66 Reactions Not Available
Enzyme 66 Pfam Domain Function
Enzyme 66 Signals
  • None
Enzyme 66 Transmembrane Regions
  • None
Enzyme 66 Essentiality Not Available
Enzyme 66 GenBank ID Protein 3041771 Link Image
Enzyme 66 UniProtKB/Swiss-Prot ID O60240 Link Image
Enzyme 66 UniProtKB/Swiss-Prot Entry Name PLIN1_HUMAN Link Image
Enzyme 66 PDB ID Not Available
Enzyme 66 Cellular Location Not Available
Enzyme 66 Gene Sequence >1569 bp
ATGGCAGTCAACAAAGGCCTCACCTTGCTGGATGGAGACCTCCCTGAGCAGGAGAATGTG
CTGCAGCGGGTCCTGCAGCTGCCGGTGGTGAGTGGCACCTGCGAATGCTTCCAGAAGACC
TACACCAGCACTAAGGAAGCCCACCCCCTGGTGGCCTCTGTGTGCAATGCCTATGAGAAG
GGCGTGCAGAGCGCCAGTAGCTTGGCTGCCTGGAGCATGGAGCCGGTGGTCCGCAGGCTG
TCCACCCAGTTCACAGCTGCCAATGAGCTGGCCTGCCGAGGCTTGGACCACCTGGAGGAA
AAGATCCCCGCCCTCCAGTACCCCCCTGAAAAGATTGCTTCTGAGCTGAAGGACACCATC
TCCACCCGCCTCCGCAGTGCCAGAAACAGCATCAGCGTTCCCATCGCGAGCACTTCAGAC
AAGGTCCTGGGGGCCGCTTTGGCCGGGTGCGAGCTTGCCTGGGGGGTGGCCAGAGACACT
GCGGAATTTGCTGCCAACACTCGAGCTGGCCGACTGGCTTCTGGAGGGGCCGACTTGGCC
TTGGGCAGCATTGAGAAGGTGGTGGAGTACCTCCTCCCTGCAGACAAGGAAGAGTCAGCC
CCTGCTCCTGGACACCAGCAAGCCCAGAAGTCTCCCAAGGCCAAGCCAAGCCTCTTGAGC
AGGGTTGGGGCTCTGACCAACACCCTCTCTCGATACACCGTGCAGACCATGGCCCGGGCC
CTGGAGCAGGGCCACACCGTGGCCATGTGGATCCCAGGCGTGGTGCCCCTGAGCAGCCTG
GCCCAGTGGGGTGCCTCAGTGGCCATGCAGGCGGTGTCCCGGCGGAGGAGCGAAGTGCGG
GTACCCTGGCTGCACAGCCTCGCAGCCGCCCAGGAGGAGGATCATGAGGACCAGACAGAC
ACGGAGGGAGAGGACACGGAGGAGGAGGAAGAATTGGAGACTGAGGAGAACAAGTTCAGT
GAGGTAGCAGCCCTGCCAGGCCCTCGAGGCCTCCTGGGTGGTGTGGCACATACCCTGCAG
AAGACCCTCCAGACCACCATCTCGGCTGTGACATGGGCACCTGCAGCTGTGCTGGGCATG
GCAGGGAGGGTGCTGCACCTCACACCAGCCCCCGCTGTCTCCTCAACCAAGGGGAGGGCC
ATGTCCCTATCAGATGCCCTGAAGGGCGTTACTGACAACGTGGTGGACACAGTGGTGCAT
TACGTGCCGCTCCCCAGGCTGTCGCTGATGGAGCCCGAGAGCGAATTCCGGGACATCGAC
AACCCACCAGCCGAGGTCGAGCGCCGGGAGGCGGAGCGCAGAGCGTCTGGGGCGCCGTCC
GCCGGCCCGGAGCCCGCCCCGCGTCTCGCACAGCCCCGCCGCAGCCTGCGCAGCGCGCAG
AGCCCCGGCGCGCCCCCCGGCCCGGGCCTGGAGGACGAAGTCGCCACGCCCGCAGCGCCG
CGCCCGGGCTTCCCGGCCGTGCCCCGCGAGAAGCCAAAGCGCAGGGTCAGCGACAGCTTC
TTCCGGCCCAGCGTCATGGAGCCCATCGTGGGCCGCACGCATTACAGCCAGCTGCGCAAG
AAGAGCTGA
Enzyme 66 GenBank Gene ID AB005293 Link Image
Enzyme 66 GeneCard ID PLIN1 Link Image
Enzyme 66 GenAtlas ID PLIN1 Link Image
Enzyme 66 HGNC ID HGNC:9076 Link Image
Enzyme 66 Chromosome Location 1
Enzyme 66 Locus 15q26
Enzyme 66 SNPs SNPJam Report Link Image
Enzyme 66 General References
  1. Nishiu J, Tanaka T, Nakamura Y: Isolation and chromosomal mapping of the human homolog of perilipin (PLIN), a rat adipose tissue-specific gene, by differential display method. Genomics. 1998 Mar 1;48(2):254-7. [PubMed Link Image]
  2. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 66 Metabolite References Not Available
Enzyme 67 [top]
Enzyme 67 ID 8264
Enzyme 67 Name Prostaglandin D2 receptor
Enzyme 67 Synonyms
  1. PGD receptor
  2. PGD2 receptor
  3. Prostanoid DP receptor
Enzyme 67 Gene Name PTGDR
Enzyme 67 Protein Sequence >Prostaglandin D2 receptor
MKSPFYRCQNTTSVEKGNSAVMGGVLFSTGLLGNLLALGLLARSGLGWCSRRPLRPLPSV
FYMLVCGLTVTDLLGKCLLSPVVLAAYAQNRSLRVLAPALDNSLCQAFAFFMSFFGLSST
LQLLAMALECWLSLGHPFFYRRHITLRLGALVAPVVSAFSLAFCALPFMGFGKFVQYCPG
TWCFIQMVHEEGSLSVLGYSVLYSSLMALLVLATVLCNLGAMRNLYAMHRRLQRHPRSCT
RDCAEPRADGREASPQPLEELDHLLLLALMTVLFTMCSLPVIYRAYYGAFKDVKEKNRTS
EEAEDLRALRFLSVISIVDPWIFIIFRSPVFRIFFHKIFIRPLRYRSRCSNSTNMESSL
Enzyme 67 Number of Residues 359
Enzyme 67 Molecular Weight 40270.1
Enzyme 67 Theoretical pI 9.32
Enzyme 67 GO Classification
Function
  • G-protein coupled receptor activity
  • icosanoid receptor activity
  • molecular transducer activity
  • prostaglandin D receptor activity
  • prostaglandin receptor activity
  • prostanoid receptor activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 67 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 67 Specific Function Receptor for prostaglandin D2 (PGD2). The activity of this receptor is mainly mediated by G(s) proteins that stimulate adenylate cyclase, resulting in an elevation of intracellular cAMP. A mobilization of calcium is also observed, but without formation of inositol 1,4,5-trisphosphate
Enzyme 67 Pathways Not Available
Enzyme 67 Reactions Not Available
Enzyme 67 Pfam Domain Function
Enzyme 67 Signals
  • None
Enzyme 67 Transmembrane Regions
  • 22-42 60-80 108-128 151-171 196-216 263-283 311-331
Enzyme 67 Essentiality Not Available
Enzyme 67 GenBank ID Protein 28466969 Link Image
Enzyme 67 UniProtKB/Swiss-Prot ID Q13258 Link Image
Enzyme 67 UniProtKB/Swiss-Prot Entry Name PD2R_HUMAN Link Image
Enzyme 67 PDB ID Not Available
Enzyme 67 Cellular Location Not Available
Enzyme 67 Gene Sequence >1080 bp
ATGAAGTCGCCGTTCTACCGCTGCCAGAACACCACCTCTGTGGAAAAAGGCAACTCGGCG
GTGATGGGCGGGGTGCTCTTCAGCACCGGCCTCCTGGGCAACCTGCTGGCCCTGGGGCTG
CTGGCGCGCTCGGGGCTGGGGTGGTGCTCGCGGCGTCCACTGCGCCCGCTGCCCTCGGTC
TTCTACATGCTGGTGTGTGGCCTGACGGTCACCGACTTGCTGGGCAAGTGCCTCCTAAGC
CCGGTGGTGCTGGCTGCCTACGCTCAGAACCGGAGTCTGCGGGTGCTTGCGCCCGCATTG
GACAACTCGTTGTGCCAAGCCTTCGCCTTCTTCATGTCCTTCTTTGGGCTCTCCTCGACA
CTGCAACTCCTGGCCATGGCACTGGAGTGCTGGCTCTCCCTAGGGCACCCTTTCTTCTAC
CGACGGCACATCACCCTGCGCCTGGGCGCACTGGTGGCCCCGGTGGTGAGCGCCTTCTCC
CTGGCTTTCTGCGCGCTACCTTTCATGGGCTTCGGGAAGTTCGTGCAGTACTGCCCCGGC
ACCTGGTGCTTTATCCAGATGGTCCACGAGGAGGGCTCGCTGTCGGTGCTGGGGTACTCT
GTGCTCTACTCCAGCCTCATGGCGCTGCTGGTCCTCGCCACCGTGCTGTGCAACCTCGGC
GCCATGCGCAACCTCTATGCGATGCACCGGCGGCTGCAGCGGCACCCGCGCTCCTGCACC
AGGGACTGTGCCGAGCCGCGCGCGGACGGGAGGGAAGCGTCCCCTCAGCCCCTGGAGGAG
CTGGATCACCTCCTGCTGCTGGCGCTGATGACCGTGCTCTTCACTATGTGTTCTCTGCCC
GTAATTTATCGCGCTTACTATGGAGCATTTAAGGATGTCAAGGAGAAAAACAGGACCTCT
GAAGAAGCAGAAGACCTCCGAGCCTTGCGATTTCTATCTGTGATTTCAATTGTGGACCCT
TGGATTTTTATCATTTTCAGATCTCCAGTATTTCGGATATTTTTTCACAAGATTTTCATT
AGACCTCTTAGGTACAGGAGCCGGTGCAGCAATTCCACTAACATGGAATCCAGTCTGTGA
Enzyme 67 GenBank Gene ID NM_000953.2 Link Image
Enzyme 67 GeneCard ID PTGDR Link Image
Enzyme 67 GenAtlas ID PTGDR Link Image
Enzyme 67 HGNC ID HGNC:9591 Link Image
Enzyme 67 Chromosome Location 1
Enzyme 67 Locus 14q22.1
Enzyme 67 SNPs SNPJam Report Link Image
Enzyme 67 General References
  1. Boie Y, Sawyer N, Slipetz DM, Metters KM, Abramovitz M: Molecular cloning and characterization of the human prostanoid DP receptor. J Biol Chem. 1995 Aug 11;270(32):18910-6. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Town MH, Casals-Stenzel J, Schillinger E: Pharmacological and cardiovascular properties of a hydantoin derivative, BW 245 C, with high affinity and selectivity for PGD2 receptors. Prostaglandins. 1983 Jan;25(1):13-28. [PubMed Link Image]
  4. Sharif NA, Williams GW, Davis TL: Pharmacology and autoradiography of human DP prostanoid receptors using [(3)H]-BWA868C, a DP receptor-selective antagonist radioligand. Br J Pharmacol. 2000 Nov;131(6):1025-38. [PubMed Link Image]
  5. Oguma T, Palmer LJ, Birben E, Sonna LA, Asano K, Lilly CM: Role of prostanoid DP receptor variants in susceptibility to asthma. N Engl J Med. 2004 Oct 21;351(17):1752-63. [PubMed Link Image]
Enzyme 67 Metabolite References Not Available
Enzyme 68 [top]
Enzyme 68 ID 8268
Enzyme 68 Name Rap guanine nucleotide exchange factor 3
Enzyme 68 Synonyms
  1. Exchange factor directly activated by cAMP 1
  2. Exchange protein directly activated by cAMP 1
  3. EPAC 1
  4. Rap1 guanine-nucleotide-exchange factor directly activated by cAMP
  5. cAMP-regulated guanine nucleotide exchange factor I
  6. cAMP-GEFI
Enzyme 68 Gene Name RAPGEF3
Enzyme 68 Protein Sequence >Rap guanine nucleotide exchange factor 3
MKVGWPGESCWQVGLAVEDSPALGAPRVGALPDVVPEGTLLNMVLRRMHRPRSCSYQLLL
EHQRPSCIQGLRWTPLTNSEESLDFSESLEQASTERVLRAGRQLHRHLLATCPNLIRDRK
YHLRLYRQCCSGRELVDGILALGLGVHSRSQVVGICQVLLDEGALCHVKHDWAFQDRDAQ
FYRFPGPEPEPVGTHEMEEELAEAVALLSQRGPDALLTVALRKPPGQRTDEELDLIFEEL
LHIKAVAHLSNSVKRELAAVLLFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKGL
VTTLHEGDDFGQLALVNDAPRAATIILREDNCHFLRVDKQDFNRIIKDVEAKTMRLEEHG
KVVLVLERASQGAGPSRPPTPGRNRYTVMSGTPEKILELLLEAMGPDSSAHDPTETFLSD
FLLTHRVFMPSAQLCAALLHHFHVEPAGGSEQERSTYVCNKRQQILRLVSQWVALYGSML
HTDPVATSFLQKLSDLVGRDTRLSNLLREQWPERRRCHRLENGCGNASPQMKARNLPVWL
PNQDEPLPGSSCAIQVGDKVPYDICRPDHSVLTLQLPVTASVREVMAALAQEDGWTKGQV
LVKVNSAGDAIGLQPDARGVATSLGLNERLFVVNPQEVHELIPHPDQLGPTVGSAEGLDL
VSAKDLAGQLTDHDWSLFNSIHQVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVAT
ELCLCPVPGPRAQLLRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKV
RKLYSALERLLDPSWNHRVYRLALAKLSPPVIPFMPLLLKDMTFIHEGNHTLVENLINFE
KMRMMARAARMLHHCRSHNPVPLSPLRSRVSHLHEDSQVARISTCSEQSLSTRSPASTWA
YVQQLKVIDNQRELSRLSRELEP
Enzyme 68 Number of Residues 923
Enzyme 68 Molecular Weight 103651.0
Enzyme 68 Theoretical pI 7.49
Enzyme 68 GO Classification
Function
  • GTPase regulator activity
  • cAMP-dependent protein kinase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • kinase regulator activity
  • nucleoside-triphosphatase regulator activity
  • protein kinase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular metabolic process
  • regulation of cellular process
  • regulation of cellular protein metabolic process
  • regulation of metabolic process
  • regulation of protein amino acid phosphorylation
  • regulation of protein modification process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • signaling
  • signaling pathway
  • small GTPase mediated signal transduction
Component
  • cAMP-dependent protein kinase complex
  • cell part
  • intracellular
  • macromolecular complex
  • protein complex
Enzyme 68 General Function Involved in cAMP-dependent protein kinase regulator activity
Enzyme 68 Specific Function Guanine nucleotide exchange factor (GEF) for RAP1A and RAP2A small GTPases that is activated by binding cAMP
Enzyme 68 Pathways Not Available
Enzyme 68 Reactions Not Available
Enzyme 68 Pfam Domain Function
Enzyme 68 Signals
  • None
Enzyme 68 Transmembrane Regions
  • None
Enzyme 68 Essentiality Not Available
Enzyme 68 GenBank ID Protein 148747859 Link Image
Enzyme 68 UniProtKB/Swiss-Prot ID O95398 Link Image
Enzyme 68 UniProtKB/Swiss-Prot Entry Name RPGF3_HUMAN Link Image
Enzyme 68 PDB ID Not Available
Enzyme 68 Cellular Location Not Available
Enzyme 68 Gene Sequence >2772 bp
ATGAAGGTGGGCTGGCCAGGTGAGAGCTGCTGGCAGGTGGGCCTGGCTGTGGAGGATAGC
CCAGCTCTGGGAGCACCGCGGGTGGGAGCCCTCCCTGACGTGGTGCCGGAGGGGACACTA
CTCAACATGGTGTTGAGAAGGATGCACCGGCCCCGAAGCTGCTCCTACCAGCTGCTGCTG
GAGCACCAGCGTCCGAGCTGCATCCAGGGGCTGCGCTGGACACCACTCACCAACAGCGAG
GAGTCCCTGGATTTCAGCGAGAGCCTGGAGCAGGCCTCCACAGAGCGGGTGCTCAGGGCT
GGGAGGCAGCTGCATCGGCATCTGCTGGCCACCTGCCCAAACCTCATCCGAGACCGGAAG
TACCACCTTAGGCTCTATCGGCAGTGCTGCTCTGGCCGGGAGCTGGTGGATGGGATCTTG
GCCCTGGGACTTGGGGTCCATTCCCGGAGCCAAGTTGTGGGAATCTGCCAGGTGCTGCTG
GATGAAGGTGCCCTCTGCCATGTGAAACACGACTGGGCCTTCCAGGACCGAGATGCCCAA
TTCTACCGGTTCCCCGGGCCCGAGCCCGAGCCCGTGGGAACTCATGAGATGGAGGAGGAG
TTGGCCGAAGCTGTGGCCCTGCTCTCCCAGCGGGGGCCTGACGCCCTGCTCACTGTGGCA
CTTCGAAAGCCCCCAGGTCAGCGCACGGATGAAGAGCTGGACCTCATCTTTGAGGAGCTG
CTGCACATCAAGGCTGTGGCCCACCTCTCCAACTCGGTGAAGCGAGAATTAGCGGCTGTT
CTGCTCTTTGAACCACACAGCAAGGCAGGGACCGTGTTGTTCAGCCAGGGGGACAAGGGC
ACTTCGTGGTACATTATCTGGAAGGGATCTGTCAACGTGGTGACCCATGGCAAGGGGCTG
GTGACCACCCTGCATGAGGGAGATGATTTTGGACAGCTGGCTCTGGTGAATGATGCACCC
CGGGCAGCCACCATCATCCTGCGAGAAGACAACTGTCATTTCCTGCGTGTGGACAAGCAG
GACTTCAACCGTATCATCAAGGATGTGGAGGCAAAGACCATGCGGCTGGAAGAACATGGC
AAAGTGGTGCTGGTGCTGGAGAGAGCCTCTCAGGGCGCCGGCCCTTCCCGACCCCCAACC
CCAGGCAGGAACCGGTATACAGTGATGTCTGGCACCCCAGAGAAGATCCTAGAGCTTCTG
TTGGAGGCCATGGGACCAGATTCCAGTGCTCATGACCCAACAGAGACATTCCTCAGCGAC
TTCCTCCTGACCCACAGGGTCTTCATGCCCAGCGCCCAACTCTGCGCTGCCCTTCTGCAC
CACTTCCATGTGGAGCCTGCGGGTGGCAGCGAGCAGGAGCGCAGCACCTACGTCTGCAAC
AAGAGGCAGCAGATCTTGCGGCTGGTCAGCCAGTGGGTGGCCCTGTATGGCTCCATGCTC
CACACTGACCCTGTGGCCACCAGCTTCCTCCAGAAACTCTCAGACCTGGTGGGCAGGGAC
ACCCGACTCAGCAACCTGCTGAGGGAGCAGTGGCCAGAGAGGCGGCGATGCCACAGGTTG
GAGAATGGCTGTGGGAATGCATCTCCTCAGATGAAGGCCCGGAACTTGCCTGTTTGGCTC
CCCAACCAGGACGAGCCCCTTCCTGGCAGCAGCTGTGCCATCCAAGTTGGGGATAAAGTC
CCCTATGACATCTGCCGGCCAGACCACTCAGTGTTGACCCTGCAGCTGCCTGTGACAGCC
TCCGTGAGAGAGGTGATGGCAGCGTTGGCCCAGGAGGATGGCTGGACCAAGGGGCAGGTG
CTGGTGAAGGTCAATTCTGCAGGTGATGCCATTGGCCTGCAGCCAGATGCCCGTGGTGTG
GCCACATCTCTGGGGCTCAATGAGCGTCTCTTTGTTGTCAACCCACAGGAAGTGCATGAG
CTGATCCCACACCCTGACCAGCTGGGGCCCACTGTGGGCTCTGCTGAGGGGCTGGACCTG
GTGAGTGCCAAGGACCTGGCAGGCCAGCTGACGGACCACGACTGGAGCCTCTTCAACAGT
ATCCACCAGGTGGAGCTGATCCACTATGTGCTGGGCCCCCAGCATCTGCGGGATGTCACC
ACCGCCAACCTGGAGCGCTTCATGCGCCGCTTCAATGAGCTGCAGTACTGGGTGGCCACC
GAGCTGTGTCTCTGCCCCGTGCCCGGCCCCCGGGCCCAGCTGCTCAGGAAGTTCATTAAG
CTGGCGGCCCACCTCAAGGAGCAGAAGAATCTCAATTCCTTCTTTGCCGTCATGTTTGGC
CTCAGCAACTCGGCCATCAGCCGCCTAGCCCACACCTGGGAGCGGCTGCCTCACAAAGTC
CGGAAGCTGTACTCCGCCCTCGAGAGGCTGCTGGATCCCTCATGGAACCACCGGGTATAC
CGACTGGCCCTCGCCAAGCTCTCCCCTCCTGTCATCCCCTTCATGCCCCTTCTTCTCAAA
GACATGACCTTCATTCATGAGGGAAACCACACACTAGTGGAGAATCTCATCAACTTTGAG
AAGATGAGAATGATGGCCAGAGCCGCGCGGATGCTGCACCACTGCCGAAGCCACAACCCT
GTGCCTCTCTCACCACTCAGAAGCCGAGTTTCCCACCTCCACGAGGACAGCCAGGTGGCG
AGGATTTCCACATGCTCGGAGCAGTCCCTGAGCACCCGGAGTCCAGCCAGCACCTGGGCT
TATGTCCAGCAGCTGAAGGTCATTGACAACCAGCGGGAACTCTCCCGCCTCTCCCGAGAG
CTGGAGCCATGA
Enzyme 68 GenBank Gene ID NM_001098531.2 Link Image
Enzyme 68 GeneCard ID RAPGEF3 Link Image
Enzyme 68 GenAtlas ID RAPGEF3 Link Image
Enzyme 68 HGNC ID HGNC:16629 Link Image
Enzyme 68 Chromosome Location 1
Enzyme 68 Locus 12q13.1
Enzyme 68 SNPs SNPJam Report Link Image
Enzyme 68 General References
  1. Kawasaki H, Springett GM, Mochizuki N, Toki S, Nakaya M, Matsuda M, Housman DE, Graybiel AM: A family of cAMP-binding proteins that directly activate Rap1. Science. 1998 Dec 18;282(5397):2275-9. [PubMed Link Image]
  2. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. de Rooij J, Zwartkruis FJ, Verheijen MH, Cool RH, Nijman SM, Wittinghofer A, Bos JL: Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP. Nature. 1998 Dec 3;396(6710):474-7. [PubMed Link Image]
  5. de Rooij J, Rehmann H, van Triest M, Cool RH, Wittinghofer A, Bos JL: Mechanism of regulation of the Epac family of cAMP-dependent RapGEFs. J Biol Chem. 2000 Jul 7;275(27):20829-36. [PubMed Link Image]
  6. Rehmann H, Prakash B, Wolf E, Rueppel A, de Rooij J, Bos JL, Wittinghofer A: Structure and regulation of the cAMP-binding domains of Epac2. Nat Struct Biol. 2003 Jan;10(1):26-32. [PubMed Link Image]
Enzyme 68 Metabolite References Not Available
Enzyme 69 [top]
Enzyme 69 ID 8274
Enzyme 69 Name Platelet basic protein
Enzyme 69 Synonyms
  1. PBP
  2. C-X-C motif chemokine 7
  3. Leukocyte-derived growth factor
  4. LDGF
  5. Macrophage-derived growth factor
  6. MDGF
  7. Small-inducible cytokine B7
  8. Connective tissue-activating peptide III
  9. CTAP-III
  10. LA-PF4
  11. Low-affinity platelet factor IV
  12. TC-2
  13. Connective tissue-activating peptide III(1-81)
  14. CTAP-III(1-81)
  15. Beta-thromboglobulin
  16. Beta-TG
  17. Neutrophil-activating peptide 2(74)
  18. NAP-2(74)
  19. Neutrophil-activating peptide 2(73)
  20. NAP-2(73)
  21. Neutrophil-activating peptide 2
  22. NAP-2
  23. TC-1
  24. Neutrophil-activating peptide 2(1-66)
  25. NAP-2(1-66)
  26. Neutrophil-activating peptide 2(1-63)
  27. NAP-2(1-63)
Enzyme 69 Gene Name PPBP
Enzyme 69 Protein Sequence >Platelet basic protein
MSLRLDTTPSCNSARPLHALQVLLLLSLLLTALASSTKGQTKRNLAKGKEESLDSDLYAE
LRCMCIKTTSGIHPKNIQSLEVIGKGTHCNQVEVIATLKDGRKICLDPDAPRIKKIVQKK
LAGDESAD
Enzyme 69 Number of Residues 128
Enzyme 69 Molecular Weight 13894.0
Enzyme 69 Theoretical pI 9.07
Enzyme 69 GO Classification
Function
  • binding
  • chemokine activity
  • cytokine activity
  • protein binding
  • receptor binding
Process
  • immune response
  • immune system process
Component
  • extracellular region
Enzyme 69 General Function Involved in cytokine activity
Enzyme 69 Specific Function LA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by human synovial cells. NAP-2 is a ligand for CXCR1 and CXCR2, and NAP-2, NAP-2(73), NAP-2(74), NAP-2(1-66), and most potent NAP-2(1-63) are chemoattractants and activators for neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro released from activated platelet alpha-granules. CTAP-III(1-81) is more potent than CTAP-III desensitize chemokine-induced neutrophil activation
Enzyme 69 Pathways Not Available
Enzyme 69 Reactions Not Available
Enzyme 69 Pfam Domain Function
Enzyme 69 Signals
  • 1-34
Enzyme 69 Transmembrane Regions
  • None
Enzyme 69 Essentiality Not Available
Enzyme 69 GenBank ID Protein 181176 Link Image
Enzyme 69 UniProtKB/Swiss-Prot ID P02775 Link Image
Enzyme 69 UniProtKB/Swiss-Prot Entry Name CXCL7_HUMAN Link Image
Enzyme 69 PDB ID 1F9P Link Image
Enzyme 69 PDB File Show
Enzyme 69 3D Structure
Enzyme 69 Cellular Location Not Available
Enzyme 69 Gene Sequence >387 bp
ATGAGCCTCAGACTTGATACCACCCCTTCCTGTAACAGTGCGAGACCACTTCATGCCTTG
CAGGTGCTGCTGCTTCTGTCATTGCTGCTGACTGCTCTGGCTTCCTCCACCAAAGGACAA
ACTAAGAGAAACTTGGCGAAAGGCAAAGAGGAAAGTCTAGACAGTGACTTGTATGCTGAA
CTCCGCTGCATGTGTATAAAGACAACCTCTGGAATTCATCCCAAAAACATCCAAAGTTTG
GAAGTGATCGGGAAAGGAACCCATTGCAACCAAGTCGAAGTGATAGCCACACTGAAGGAT
GGGAGGAAAATCTGCCTGGACCCAGATGCTCCCAGAATCAAGAAAATTGTACAGAAAAAA
TTGGCAGGTGATGAATCTGCTGATTAA
Enzyme 69 GenBank Gene ID M54995 Link Image
Enzyme 69 GeneCard ID PPBP Link Image
Enzyme 69 GenAtlas ID PPBP Link Image
Enzyme 69 HGNC ID HGNC:9240 Link Image
Enzyme 69 Chromosome Location 4
Enzyme 69 Locus 4q12-q13
Enzyme 69 SNPs SNPJam Report Link Image
Enzyme 69 General References
  1. Wenger RH, Wicki AN, Walz A, Kieffer N, Clemetson KJ: Cloning of cDNA coding for connective tissue activating peptide III from a human platelet-derived lambda gt11 expression library. Blood. 1989 May 1;73(6):1498-503. [PubMed Link Image]
  2. Majumdar S, Gonder D, Koutsis B, Poncz M: Characterization of the human beta-thromboglobulin gene. Comparison with the gene for platelet factor 4. J Biol Chem. 1991 Mar 25;266(9):5785-9. [PubMed Link Image]
  3. Zhang C, Thornton MA, Kowalska MA, Sachis BS, Feldman M, Poncz M, McKenzie SE, Reilly MP: Localization of distal regulatory domains in the megakaryocyte-specific platelet basic protein/platelet factor 4 gene locus. Blood. 2001 Aug 1;98(3):610-7. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Holt JC, Harris ME, Holt AM, Lange E, Henschen A, Niewiarowski S: Characterization of human platelet basic protein, a precursor form of low-affinity platelet factor 4 and beta-thromboglobulin. Biochemistry. 1986 Apr 22;25(8):1988-96. [PubMed Link Image]
  8. Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [PubMed Link Image]
  9. Krijgsveld J, Zaat SA, Meeldijk J, van Veelen PA, Fang G, Poolman B, Brandt E, Ehlert JE, Kuijpers AJ, Engbers GH, Feijen J, Dankert J: Thrombocidins, microbicidal proteins from human blood platelets, are C-terminal deletion products of CXC chemokines. J Biol Chem. 2000 Jul 7;275(27):20374-81. [PubMed Link Image]
  10. Castor CW, Miller JW, Walz DA: Structural and biological characteristics of connective tissue activating peptide (CTAP-III), a major human platelet-derived growth factor. Proc Natl Acad Sci U S A. 1983 Feb;80(3):765-9. [PubMed Link Image]
  11. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  12. Begg GS, Pepper DS, Chesterman CN, Morgan FJ: Complete covalent structure of human beta-thromboglobulin. Biochemistry. 1978 May 2;17(9):1739-44. [PubMed Link Image]
  13. Piccardoni P, Evangelista V, Piccoli A, de Gaetano G, Walz A, Cerletti C: Thrombin-activated human platelets release two NAP-2 variants that stimulate polymorphonuclear leukocytes. Thromb Haemost. 1996 Nov;76(5):780-5. [PubMed Link Image]
  14. Castor CW, Walz DA, Ragsdale CG, Hossler PA, Smith EM, Bignall MC, Aaron BP, Mountjoy K: Connective tissue activation. XXXIII. Biologically active cleavage products of CTAP-III from human platelets. Biochem Biophys Res Commun. 1989 Sep 15;163(2):1071-8. [PubMed Link Image]
  15. Walz A, Baggiolini M: A novel cleavage product of beta-thromboglobulin formed in cultures of stimulated mononuclear cells activates human neutrophils. Biochem Biophys Res Commun. 1989 Mar 31;159(3):969-75. [PubMed Link Image]
  16. Ehlert JE, Petersen F, Kubbutat MH, Gerdes J, Flad HD, Brandt E: Limited and defined truncation at the C terminus enhances receptor binding and degranulation activity of the neutrophil-activating peptide 2 (NAP-2). Comparison of native and recombinant NAP-2 variants. J Biol Chem. 1995 Mar 17;270(11):6338-44. [PubMed Link Image]
  17. Walz A, Baggiolini M: Generation of the neutrophil-activating peptide NAP-2 from platelet basic protein or connective tissue-activating peptide III through monocyte proteases. J Exp Med. 1990 Feb 1;171(2):449-54. [PubMed Link Image]
  18. Clark-Lewis I, Moser B, Walz A, Baggiolini M, Scott GJ, Aebersold R: Chemical synthesis, purification, and characterization of two inflammatory proteins, neutrophil activating peptide 1 (interleukin-8) and neutrophil activating peptide. Biochemistry. 1991 Mar 26;30(12):3128-35. [PubMed Link Image]
  19. Ehlert JE, Gerdes J, Flad HD, Brandt E: Novel C-terminally truncated isoforms of the CXC chemokine beta-thromboglobulin and their impact on neutrophil functions. J Immunol. 1998 Nov 1;161(9):4975-82. [PubMed Link Image]
  20. Kungl AJ, Machius M, Huber R, Schwer C, Lam C, Aschauer H, Ehn G, Lindley IJ, Auer M: Purification, crystallization and preliminary X-ray diffraction analysis of recombinant human neutrophil-activating peptide 2 (rhNAP-2). FEBS Lett. 1994 Jun 27;347(2-3):300-3. [PubMed Link Image]
  21. Malkowski MG, Wu JY, Lazar JB, Johnson PH, Edwards BF: The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-A resolution. J Biol Chem. 1995 Mar 31;270(13):7077-87. [PubMed Link Image]
Enzyme 69 Metabolite References Not Available
Enzyme 70 [top]
Enzyme 70 ID 8330
Enzyme 70 Name Vasodilator-stimulated phosphoprotein
Enzyme 70 Synonyms
  1. VASP
Enzyme 70 Gene Name VASP
Enzyme 70 Protein Sequence >Vasodilator-stimulated phosphoprotein
MSETVICSSRATVMLYDDGNKRWLPAGTGPQAFSRVQIYHNPTANSFRVVGRKMQPDQQV
VINCAIVRGVKYNQATPNFHQWRDARQVWGLNFGSKEDAAQFAAGMASALEALEGGGPPP
PPALPTWSVPNGPSPEEVEQQKRQQPGPSEHIERRVSNAGGPPAPPAGGPPPPPGPPPPP
GPPPPPGLPPSGVPAAAHGAGGGPPPAPPLPAAQGPGGGGAGAPGLAAAIAGAKLRKVSK
QEEASGGPTAPKAESGRSGGGGLMEEMNAMLARRRKATQVGEKTPKDESANQEEPEARVP
AQSESVRRPWEKNSTTLPRMKSSSSVTTSETQPCTPSSSDYSDLQRVKQELLEEVKKELQ
KVKEEIIEAFVQELRKRGSP
Enzyme 70 Number of Residues 380
Enzyme 70 Molecular Weight 39829.5
Enzyme 70 Theoretical pI 9.41
Enzyme 70 GO Classification Not Available
Enzyme 70 General Function Cell cycle control, cell division, chromosome partitioning
Enzyme 70 Specific Function Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin- bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation
Enzyme 70 Pathways Not Available
Enzyme 70 Reactions Not Available
Enzyme 70 Pfam Domain Function
Enzyme 70 Signals
  • None
Enzyme 70 Transmembrane Regions
  • None
Enzyme 70 Essentiality Not Available
Enzyme 70 GenBank ID Protein 189054561 Link Image
Enzyme 70 UniProtKB/Swiss-Prot ID P50552 Link Image
Enzyme 70 UniProtKB/Swiss-Prot Entry Name VASP_HUMAN Link Image
Enzyme 70 PDB ID 1EGX Link Image
Enzyme 70 PDB File Show
Enzyme 70 3D Structure
Enzyme 70 Cellular Location Not Available
Enzyme 70 Gene Sequence >1143 bp
ATGAGCGAGACGGTCATCTGTTCCAGCCGGGCCACTGTGATGCTTTATGATGATGGCAAC
AAGCGATGGCTCCCTGCTGGCACGGGTCCCCAGGCCTTCAGCCGCGTCCAGATCTACCAC
AACCCCACGGCCAATTCCTTTCGCGTCGTGGGCCGGAAGATGCAGCCCGACCAGCAGGTG
GTCATCAACTGTGCCATCGTCCGGGGTGTCAAGTATAACCAGGCCACCCCCAACTTCCAT
CAGTGGCGCGACGCTCGCCAGGTCTGGGGCCTCAACTTCGGCAGCAAGGAGGATGCGGCC
CAGTTTGCCGCCGGCATGGCCAGTGCCCTAGAGGCGTTGGAAGGAGGTGGGCCCCCTCCA
CCCCCAGCACTTCCCACCTGGTCGGTCCCGAACGGCCCCTCCCCGGAGGAGGTGGAGCAG
CAGAAAAGGCAGCAGCCCGGCCCGTCGGAGCACATAGAGCGCCGGGTCTCCAATGCAGGA
GGCCCACCTGCTCCCCCCGCTGGGGGTCCACCCCCACCACCAGGACCTCCCCCTCCTCCA
GGTCCCCCCCCACCCCCAGGTTTGCCCCCTTCGGGGGTCCCAGCTGCAGCGCACGGAGCA
GGGGGAGGACCACCCCCTGCACCCCCTCTCCCGGCAGCACAGGGCCCTGGTGGTGGGGGA
GCTGGGGCCCCAGGCCTGGCCGCAGCTATTGCTGGAGCCAAACTCAGGAAAGTCAGCAAG
CAGGAGGAGGCCTCAGGGGGGCCCACAGCCCCCAAAGCTGAGAGTGGTCGAAGCGGAGGT
GGGGGACTCATGGAAGAGATGAACGCCATGCTGGCCCGGAGAAGGAAAGCCACGCAAGTT
GGGGAGAAAACCCCCAAGGATGAATCTGCCAATCAGGAGGAGCCAGAGGCCAGAGTCCCG
GCCCAGAGTGAATCTGTGCGGAGACCCTGGGAGAAGAACAGCACAACCTTGCCAAGGATG
AAGTCGTCTTCTTCGGTGACCACTTCCGAGACCCAACCCTGCACGCCCAGCTCCAGTGAT
TACTCGGACCTACAGAGGGTGAAACAGGAGCTTCTGGAAGAGGTGAAGAAGGAATTGCAG
AAAGTGAAAGAGGAAATCATTGAAGCCTTCGTCCAGGAGCTGAGGAAGCGGGGTTCTCCC
TGA
Enzyme 70 GenBank Gene ID AK314812 Link Image
Enzyme 70 GeneCard ID VASP Link Image
Enzyme 70 GenAtlas ID VASP Link Image
Enzyme 70 HGNC ID HGNC:12652 Link Image
Enzyme 70 Chromosome Location 1
Enzyme 70 Locus 19q13.2-q13.3
Enzyme 70 SNPs SNPJam Report Link Image
Enzyme 70 General References
  1. Haffner C, Jarchau T, Reinhard M, Hoppe J, Lohmann SM, Walter U: Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP. EMBO J. 1995 Jan 3;14(1):19-27. [PubMed Link Image]
  2. Laurent V, Loisel TP, Harbeck B, Wehman A, Grobe L, Jockusch BM, Wehland J, Gertler FB, Carlier MF: Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes. J Cell Biol. 1999 Mar 22;144(6):1245-58. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  6. Zimmer M, Fink T, Fischer L, Hauser W, Scherer K, Lichter P, Walter U: Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in human and mouse: structure, sequence, and chromosomal localization. Genomics. 1996 Sep 1;36(2):227-33. [PubMed Link Image]
  7. Butt E, Abel K, Krieger M, Palm D, Hoppe V, Hoppe J, Walter U: cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets. J Biol Chem. 1994 May 20;269(20):14509-17. [PubMed Link Image]
  8. Horstrup K, Jablonka B, Honig-Liedl P, Just M, Kochsiek K, Walter U: Phosphorylation of focal adhesion vasodilator-stimulated phosphoprotein at Ser157 in intact human platelets correlates with fibrinogen receptor inhibition. Eur J Biochem. 1994 Oct 1;225(1):21-7. [PubMed Link Image]
  9. Reinhard M, Giehl K, Abel K, Haffner C, Jarchau T, Hoppe V, Jockusch BM, Walter U: The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins. EMBO J. 1995 Apr 18;14(8):1583-9. [PubMed Link Image]
  10. Bachmann C, Fischer L, Walter U, Reinhard M: The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation. J Biol Chem. 1999 Aug 13;274(33):23549-57. [PubMed Link Image]
  11. Drees B, Friederich E, Fradelizi J, Louvard D, Beckerle MC, Golsteyn RM: Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins. J Biol Chem. 2000 Jul 21;275(29):22503-11. [PubMed Link Image]
  12. Petit MM, Fradelizi J, Golsteyn RM, Ayoubi TA, Menichi B, Louvard D, Van de Ven WJ, Friederich E: LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity. Mol Biol Cell. 2000 Jan;11(1):117-29. [PubMed Link Image]
  13. Krause M, Leslie JD, Stewart M, Lafuente EM, Valderrama F, Jagannathan R, Strasser GA, Rubinson DA, Liu H, Way M, Yaffe MB, Boussiotis VA, Gertler FB: Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of lamellipodial dynamics. Dev Cell. 2004 Oct;7(4):571-83. [PubMed Link Image]
  14. Chitaley K, Chen L, Galler A, Walter U, Daum G, Clowes AW: Vasodilator-stimulated phosphoprotein is a substrate for protein kinase C. FEBS Lett. 2004 Jan 2;556(1-3):211-5. [PubMed Link Image]
  15. Barzik M, Kotova TI, Higgs HN, Hazelwood L, Hanein D, Gertler FB, Schafer DA: Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins. J Biol Chem. 2005 Aug 5;280(31):28653-62. Epub 2005 Jun 6. [PubMed Link Image]
  16. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  17. Wentworth JK, Pula G, Poole AW: Vasodilator-stimulated phosphoprotein (VASP) is phosphorylated on Ser157 by protein kinase C-dependent and -independent mechanisms in thrombin-stimulated human platelets. Biochem J. 2006 Jan 15;393(Pt 2):555-64. [PubMed Link Image]
  18. van der Ven PF, Ehler E, Vakeel P, Eulitz S, Schenk JA, Milting H, Micheel B, Furst DO: Unusual splicing events result in distinct Xin isoforms that associate differentially with filamin c and Mena/VASP. Exp Cell Res. 2006 Jul 1;312(11):2154-67. Epub 2006 Apr 24. [PubMed Link Image]
  19. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  20. Blume C, Benz PM, Walter U, Ha J, Kemp BE, Renne T: AMP-activated protein kinase impairs endothelial actin cytoskeleton assembly by phosphorylating vasodilator-stimulated phosphoprotein. J Biol Chem. 2007 Feb 16;282(7):4601-12. Epub 2006 Nov 2. [PubMed Link Image]
  21. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  22. Li Calzi S, Purich DL, Chang KH, Afzal A, Nakagawa T, Busik JV, Agarwal A, Segal MS, Grant MB: Carbon monoxide and nitric oxide mediate cytoskeletal reorganization in microvascular cells via vasodilator-stimulated phosphoprotein phosphorylation: evidence for blunted responsiveness in diabetes. Diabetes. 2008 Sep;57(9):2488-94. Epub 2008 Jun 16. [PubMed Link Image]
  23. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  24. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  25. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  26. Ball LJ, Kuhne R, Hoffmann B, Hafner A, Schmieder P, Volkmer-Engert R, Hof M, Wahl M, Schneider-Mergener J, Walter U, Oschkinat H, Jarchau T: Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity. EMBO J. 2000 Sep 15;19(18):4903-14. [PubMed Link Image]
  27. Kuhnel K, Jarchau T, Wolf E, Schlichting I, Walter U, Wittinghofer A, Strelkov SV: The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat. Proc Natl Acad Sci U S A. 2004 Dec 7;101(49):17027-32. Epub 2004 Nov 29. [PubMed Link Image]
  28. Ferron F, Rebowski G, Lee SH, Dominguez R: Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP. EMBO J. 2007 Oct 31;26(21):4597-606. Epub 2007 Oct 4. [PubMed Link Image]
  29. Baek K, Liu X, Ferron F, Shu S, Korn ED, Dominguez R: Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding. Proc Natl Acad Sci U S A. 2008 Aug 19;105(33):11748-53. Epub 2008 Aug 8. [PubMed Link Image]
Enzyme 70 Metabolite References Not Available
Enzyme 71 [top]
Enzyme 71 ID 8356
Enzyme 71 Name Inositol 1,4,5-trisphosphate receptor type 1
Enzyme 71 Synonyms
  1. IP3 receptor isoform 1
  2. IP3R 1
  3. InsP3R1
  4. Type 1 inositol 1,4,5-trisphosphate receptor
  5. Type 1 InsP3 receptor
Enzyme 71 Gene Name ITPR1
Enzyme 71 Protein Sequence >Inositol 1,4,5-trisphosphate receptor type 1
MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPETGDLNNPPKKFRDCLFKL
CPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNV
IQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGD
KVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVV
RLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWN
SLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPE
GNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGT
SPVKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDL
VYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEE
LGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLH
NNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPT
NADILIETKLVLSRFEFEGVSSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDA
KEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRA
SFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEF
VEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVH
VTTIFPISKMAKGEENKGNNDVEKLKSSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAA
PEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQTSE
TSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMH
DYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSE
LWVYKGQGPDETMDGASGENEHKKTEEGNNKPQKHESTSSYNYRVVKEILIRLSKLCVQE
SASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQ
NQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIK
FLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSP
LMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCY
VDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFF
SSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAI
PVDLDSQVNNLFLKSHSIVQKTAMNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSAL
EDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKL
CIKVLQTLREMMTKDRGYGEKLISIDELDNAELPPAPDSENSTEELEPSPPLRQLEDHKR
GEALRQVLVNRYYGNVRPSGRRESLTSFGNGPLSAGGPGKPGGGGGGSGSSSMSRGEMSL
AEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKK
SEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEV
RDQLLEASAATRKAFTTFRREADPDDHYQPGEGTQATADKAKDDLEMSAVITIMQPILRF
LQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVAL
INQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNA
SKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNV
GHNIYILAHQLARHNKELQSMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPV
PSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARN
MSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHG
IRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEF
LYHLLYLVICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILV
YLFSIVGYLFFKDDFILEVDRLPNETAVPETGESLASEFLFSDVCRVESGENCSSPAPRE
ELVPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLL
FFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHI
KEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIKERNLDWFPRMRAMSLVSSDSEGEQ
NELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA
Enzyme 71 Number of Residues 2758
Enzyme 71 Molecular Weight 313942.4
Enzyme 71 Theoretical pI 5.91
Enzyme 71 GO Classification
Function
  • calcium channel activity
  • cation channel activity
  • inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity
  • intracellular ligand-gated ion channel activity
  • ion channel activity
  • ion transmembrane transporter activity
  • ligand-gated ion channel activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • calcium ion transport
  • cation transport
  • di-, tri-valent inorganic cation transport
  • divalent metal ion transport
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • endoplasmic reticulum
  • intracellular membrane-bounded organelle
  • membrane
  • membrane-bounded organelle
  • organelle
Enzyme 71 General Function Involved in calcium channel activity
Enzyme 71 Specific Function Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5- trisphosphate
Enzyme 71 Pathways Not Available
Enzyme 71 Reactions Not Available
Enzyme 71 Pfam Domain Function
Enzyme 71 Signals
  • None
Enzyme 71 Transmembrane Regions
  • 2283-2303 2315-2335 2362-2382 2406-2426 2449-2469 2578-2598
Enzyme 71 Essentiality Not Available
Enzyme 71 GenBank ID Protein 269954692 Link Image
Enzyme 71 UniProtKB/Swiss-Prot ID Q14643 Link Image
Enzyme 71 UniProtKB/Swiss-Prot Entry Name ITPR1_HUMAN Link Image
Enzyme 71 PDB ID 1N4K Link Image
Enzyme 71 PDB File Show
Enzyme 71 3D Structure
Enzyme 71 Cellular Location Not Available
Enzyme 71 Gene Sequence >8088 bp
ATGTCTGACAAAATGTCTAGCTTCCTACATATTGGAGACATTTGTTCTCTGTACGCGGAG
GGATCGACAAATGGATTTATTAGCACCTTGGGCCTGGTTGATGATCGTTGTGTTGTACAG
CCAGAAACCGGGGACCTTAACAATCCACCTAAGAAATTCAGAGACTGCCTCTTTAAGCTA
TGTCCCATGAACCGCTACTCTGCCCAAAAGCAGTTCTGGAAAGCCGCTAAGCCTGGGGCC
AACAGCACCACAGACGCAGTGCTACTCAACAAACTGCACCACGCTGCAGACTTGGAAAAG
AAGCAGAATGAGACAGAAAACAGGAAATTGCTGGGGACCGTAATCCAGTATGGCAATGTG
ATCCAGCTCCTGCATTTGAAAAGTAATAAATACCTAACAGTGAATAAGAGGCTTCCTGCT
CTGTTGGAGAAGAATGCCATGAGAGTCACATTGGACGAGGCTGGAAATGAAGGGTCCTGG
TTTTATATTCAGCCATTCTACAAGCTGCGATCCATTGGAGACAGCGTGGTCATAGGTGAC
AAGGTGGTTCTGAACCCCGTCAATGCTGGTCAGCCCCTACATGCTAGCAGCCATCAACTG
GTAGATAACCCAGGCTGCAATGAGGTCAATTCCGTCAACTGCAATACAAGCTGGAAAATA
GTCCTTTTCATGAAATGGAGTGATAACAAAGACGACATATTAAAGGGGGGTGACGTGGTG
AGGCTGTTTCATGCTGAGCAGGAGAAGTTTCTCACCTGTGACGAACACAGGAAGAAGCAG
CACGTCTTCCTGAGAACCACGGGCCGGCAGTCGGCCACATCTGCCACCAGTTCAAAAGCC
CTGTGGGAGGTGGAGGTGGTCCAGCATGACCCATGTCGGGGCGGAGCAGGGTATTGGAAC
AGCCTTTTCCGTTTCAAGCATCTGGCCACGGGGCATTACTTGGCAGCAGAGGTGGACCCT
GATCAGGACGCCTCTCGAAGTAGGTTGCGGAATGCCCAAGAAAAGATGGTATACTCCCTG
GTCTCTGTGCCTGAAGGCAATGACATCTCCTCCATTTTCGAGCTAGATCCCACCACTCTG
CGTGGAGGTGACAGCCTTGTCCCAAGGAACTCTTATGTTCGGCTCAGACACCTATGTACT
AATACCTGGGTTCACAGCACAAATATTCCTATTGACAAGGAAGAAGAAAAGCCCGTGATG
CTGAAAATTGGCACCTCTCCTGTGAAGGAGGATAAGGAAGCATTTGCCATAGTTCCGGTT
TCTCCTGCTGAAGTTCGGGACCTGGACTTTGCCAATGATGCCAGCAAGGTGCTGGGCTCC
ATTGCTGGGAAGCTAGAGAAGGGCACCATCACCCAGAATGAAAGGAGGTCTGTAACCAAG
CTGCTAGAAGATTTGGTTTACTTCGTCACTGGTGGAACTAATTCTGGTCAAGATGTTCTC
GAAGTTGTCTTCTCCAAGCCCAACAGAGAACGGCAGAAACTGATGAGAGAACAGAATATT
CTCAAGCAGATCTTCAAGTTGTTACAAGCCCCATTCACAGACTGCGGTGATGGCCCAATG
CTTCGGCTGGAAGAGCTCGGGGACCAGCGGCACGCTCCTTTCAGACACATCTGCCGGCTC
TGCTACAGGGTGCTGAGACACTCGCAGCAAGACTACAGGAAGAACCAGGAGTATATAGCC
AAGCAGTTTGGCTTCATGCAGAAGCAGATTGGCTATGATGTGTTGGCTGAAGACACTATC
ACTGCCCTGCTCCACAATAATCGGAAACTCCTGGAAAAACACATTACCGCGGCAGAGATT
GACACATTTGTCAGCCTGGTGCGAAAGAACAGGGAGCCCAGATTCTTAGATTACCTCTCC
GACCTCTGTGTCTCCATGAACAAATCAATTCCAGTGACCCAGGAACTGATATGTAAAGCT
GTGCTGAACCCCACCAACGCTGACATCCTGATTGAGACCAAGTTGGTTCTTTCTCGTTTT
GAATTTGAAGGTGTCTCTTCCACTGGAGAGAATGCTCTGGAGGCAGGAGAAGACGAGGAA
GAGGTGTGGCTGTTTTGGAGGGACAGCAACAAAGAGATTCGCAGCAAGAGTGTGAGGGAA
TTGGCTCAGGATGCTAAAGAAGGGCAGAAGGAGGACCGAGACGTTCTCAGCTACTACAGA
TATCAGCTGAACCTCTTTGCGAGGATGTGTCTGGACCGCCAATACCTGGCCATCAACGAA
ATCTCAGGCCAGCTGGATGTCGATCTCATTCTCCGCTGCATGTCTGACGAGAACCTGCCC
TATGACCTCAGGGCGTCCTTCTGCCGCCTCATGCTTCACATGCATGTGGACCGAGATCCC
CAGGAACAAGTCACCCCCGTGAAATATGCCCGCCTCTGGTCGGAGATTCCCTCGGAGATC
GCCATTGACGACTATGATAGTAGTGGAGCTTCCAAAGATGAAATTAAGGAGAGATTTGCT
CAGACCATGGAGTTTGTGGAGGAGTATTTAAGAGATGTGGTTTGTCAGAGGTTCCCTTTC
TCTGATAAAGAGAAGAATAAGCTTACGTTTGAGGTTGTAAATTTAGCTAGGAATCTCATA
TACTTTGGTTTCTACAACTTCTCTGACCTTCTACGATTAACTAAGATCCTTCTGGCCATA
TTGGACTGTGTACATGTGACAACAATCTTCCCCATTAGCAAGATGGCGAAAGGAGAAGAG
AATAAAGGCAGTAACGTGATGAGATCTATTCATGGCGTGGGAGAGCTGATGACCCAGGTG
GTGCTCCGGGGAGGAGGCTTTTTGCCCATGACTCCCATGGCTGCTGCCCCTGAAGGCAAT
GTGAAGCAGGCAGAGCCTGAGAAGGAGGACATCATGGTCATGGACACCAAGCTGAAGATC
ATTGAGATACTCCAGTTTATTTTGAATGTGAGGTTGGATTATAGGATCTCCTGCCTCCTG
TGTATATTTAAGCGAGAGTTTGATGAAAGCAATTCCCAGACTTCAGAAACATCCTCCGGA
AACAGCAGCCAAGAAGGGCCAAGTAATGTACCAGGTGCTCTTGACTTTGAACACATTGAA
GAACAAGCAGAAGGCATCTTTGGAGGAAGTGAGGAGAACACCCCACTGGACTTGGATGAC
CACGGCGGCAGAACCTTTCTCCGTGTCCTGCTCCACTTGACGATGCATGACTACCCACCC
CTGGTGTCAGGGGCCCTGCAGCTCCTCTTCCGGCACTTCAGCCAGAGGCAGGAGGTGCTC
CAGGCCTTCAAACAGGTTCAACTGCTGGTTACCAGCCAAGATGTGGACAACTACAAACAG
ATCAAACAAGACTTGGATCAACTGAGGTCCATCGTGGAAAAGTCAGAGCTTTGGGTGTAC
AAAGGGCAGGGCCCCGATGAGACTATGGATGGTGCATCTGGAGAAAATGAACATAAGAAA
ACGGAGGAGGGAAATAACAAGCCACAAAAGCATGAAAGCACCAGCAGCTACAACTACAGA
GTGGTCAAAGAGATTTTGATTCGGCTTAGCAAACTCTGTGTTCAAGAGAGTGCCTCAGTG
AGAAAGAGCAGGAAGCAGCAACAGCGTCTGCTCCGGAACATGGGCGCGCACGCCGTGGTG
CTGGAGCTGCTGCAGATTCCCTATGAGAAGGCCGAAGATACCAAGATGCAAGAGATAATG
AGGTTGGCTCATGAATTTTTGCAGAATTTCTGCGCAGGCAACCAGCAGAATCAAGCTTTG
CTACATAAACACATAAACCTGTTTCTCAACCCAGGGATCCTGGAGGCAGTAACCATGCAG
CACATCTTCATGAACAATTTCCAGCTTTGCAGTGAGATCAACGAGAGAGTTGTTCAGCAC
TTCGTTCACTGCATAGAGACTCACGGTCGGAATGTCCAGTATATAAAGTTCTTACAGACA
ATTGTCAAGGCAGAAGGGAAATTTATTAAAAAATGCCAAGACATGGTTATGGCCGAGCTG
GTCAATTCGGGAGAGGATGTCCTCGTGTTCTACAACGACAGAGCCTCTTTCCAGACTCTG
ATCCAGATGATGCGGTCAGAACGGGATCGGATGGATGAGAACAGCCCTCTCATGTACCAC
ATCCACTTGGTCGAGCTCCTGGCTGTGTGCACGGAGGGTAAGAATGTCTACACAGAGATC
AAGTGCAACTCCCTGCTCCCGCTGGATGACATCGTTCGCGTGGTGACCCACGAGGACTGC
ATCCCTGAGGTTAAAATTGCATACATTAACTTCCTGAATCACTGCTATGTGGATACAGAG
GTGGAAATGAAGGAGATTTATACCAGCAATCACATGTGGAAATTGTTTGAGAATTTCCTT
GTAGACATCTGCAGGGCCTGTAACAACACTAGTGACAGGAAACATGCAGACTCGATTTTG
GAGAAGTATGTCACCGAAATCGTCATGAGTATTGTTACTACTTTCTTCAGCTCTCCCTTC
TCAGACCAGAGTACGACTTTGCAGACTCGCCAGCCTGTCTTTGTGCAACTGCTGCAAGGC
GTGTTCAGGGTTTACCACTGCAACTGGTTAATGCCAAGCCAAAAAGCCTCCGTGGAGAGC
TGTATTCGGGTGCTGTCTGATGTAGCCAAGAGCCGGGCCATTGCCATTCCCGTGGACCTG
GACAGCCAAGTCAACAACCTCTTTCTCAAGTCCCACAGCATTGTGCAGAAAACAGCCATG
AACTGGCGGCTCTCAGCCCGCAATGCCGCACGCAGGGACTCTGTTCTGGCAGCTTCCAGA
GACTACCGGAATATCATTGAGAGATTGCAGGACATCGTCTCCGCGCTGGAGGACCGTCTC
AGGCCCCTGGTGCAGGCAGAGTTATCTGTGCTCGTGGATGTTCTCCACAGACCCGAGCTG
CTTTTCCCAGAGAACACAGACGCCAGAAGGAAATGTGAAAGTGGCGGTTTCATTTGCAAG
TTAATAAAGCATACAAAACAGCTGCTAGAAGAAAATGAAGAGAAGCTCTGCATTAAGGTC
CTACAGACCCTGAGGGAAATGATGACCAAAGATAGAGGCTATGGAGAAAAGGGTGAGGCG
CTCAGGCAAGTTCTGGTCAACCGTTACTATGGAAACGTCAGACCTTCGGGACGAAGAGAG
AGCCTTACCAGCTTTGGCAATGGCCCACTGTCAGCAGGAGGACCCGGCAAGCCCGGGGGA
GGAGGGGGAGGTTCCGGATCCAGCTCTATGAGCAGGGGTGAGATGAGTCTGGCCGAGGTT
CAGTGTCACCTTGACAAGGAGGGGGCTTCCAATCTAGTTATCGACCTCATCATGAACGCA
TCCAGTGACCGAGTGTTCCATGAAAGCATTCTCCTGGCCATTGCCCTTCTGGAAGGAGGC
AACACCACCATCCAGCACTCCTTTTTCTGTCGCTTGACAGAAGATAAGAAGTCAGAGAAA
TTCTTTAAGGTGTTTTATGACCGGATGAAGGTGGCCCAGCAAGAAATCAAAGCAACAGTG
ACAGTGAACACCAGTGACTTGGGAAATAAAAAGAAAGACGATGAGGTAGACAGGGATGCC
CCATCACGGAAAAAAGCTAAAGAGCCCACAACACAGATAACAGAAGAGGTCCGGGATCAG
CTCCTGGAGGCCTCCGCTGCCACCAGGAAAGCCTTCACCACTTTCAGGAGGGAGGCTGAT
CCCGACGACCACTACCAGCCTGGAGAGGGCACCCAGGCCACTGCCGACAAGGCCAAGGAC
GACCTGGAGATGAGCGCGGTCATCACCATCATGCAGCCCATCCTCCGCTTCCTTCAGCTC
CTGTGTGAAAACCACAACCGAGACCTGCAGAACTTCCTCCGTTGCCAAAATAACAAGACC
AACTACAATTTGGTATGTGAGACCCTGCAGTTTCTGGACTGTATTTGTGGAAGCACAACT
GGAGGCCTTGGTCTTCTGGGCTTGTATATAAATGAAAAGAACGTAGCGCTTATCAACCAA
ACCCTGGAAAGTCTGACCGAATACTGTCAAGGACCTTGCCATGAGAACCAGAACTGCATA
GCCACCCATGAATCCAATGGCATTGACATCATCACAGCCCTGATCCTCAATGATATCAAT
CCTTTGGGAAAGAAGAGGATGGACCTTGTGTTAGAACTGAAGAACAATGCCTCGAAGTTG
CTCCTGGCCATCATGGAAAGCAGGCACGACAGTGAAAACGCAGAGAGGATACTTTATAAC
ATGAGGCCCAAGGAACTGGTGGAAGTGATCAAGAAAGCCTACATGCAAGGTGAAGTGGAA
TTTGAGGATGGAGAAAACGGTGAGGATGGGGCGGCGTCCCCCAGGAACGTGGGGCACAAC
ATCTACATATTAGCCCATCAGTTGGCTCGGCATAACAAAGAACTTCAGAGCATGCTGAAA
CCTGGTGGCCAAGTGGACGGAGATGAAGCCCTGGAGTTTTATGCCAAGCACACGGCGCAG
ATAGAGATTGTCAGATTAGACCGAACAATGGAACAGATAGTCTTTCCCGTGCCCAGCATA
TGTGAATTCCTAACCAAGGAGTCAAAACTACGAATTTACTATACTACAGAGAGAGACGAA
CAAGGCAGCAAAATCAATGATTTCTTTCTGCGGTCTGAAGACCTCTTCAATGAAATGAAT
TGGCAGAAGAAACTGAGAGCCCAGCCCGTGTTGTACTGGTGTGCCCGCAACATGTCTTTC
TGGAGCAGCATTTCGTTTAACCTGGCCGTCCTGATGAACCTGCTGGTGGCGTTTTTCTAC
CCGTTTAAGGGAGTCCGAGGAGGAACCCTGGAGCCCCACTGGTCGGGACTCCTGTGGACA
GCCATGCTCATCTCTCTGGCCATCGTCATTGCCCTCCCCAAGCCCCATGGCATCCGGGCC
TTAATTGCCTCCACAATTCTACGACTGATATTTTCAGTCGGGTTACAACCCACGTTGTTT
CTTCTGGGCGCTTTCAATGTATGCAATAAAATCATCTTTCTAATGAGCTTTGTGGGCAAC
TGTGGGACATTCACAAGAGGCTACCGAGCCATGGTTCTGGATGTTGAGTTCCTCTATCAT
TTGTTGTATCTGGTGATCTGTGCCATGGGGCTCTTTGTCCATGAATTCTTCTACAGTCTG
CTGCTTTTTGATTTAGTGTACAGAGAAGAGACTTTGCTTAATGTCATTAAAAGTGTCACT
CGCAATGGACGGTCCATCATCCTGACAGCAGTTCTGGCTCTGATCCTCGTTTACCTGTTC
TCAATAGTGGGCTATCTTTTCTTCAAGGATGACTTTATCTTGGAAGTAGATAGGCTGCCC
AATGAAACAGCTGTTCCAGAAACCGGCGAGAGTTTGGCAAGCGAGTTCCTGTTCTCCGAT
GTGTGTAGGGTGGAGAGTGGGGAGAACTGCTCCTCTCCTGCACCCAGAGAAGAGCTGGTC
CCTGCAGAAGAGACGGAACAGGATAAAGAGCACACATGTGAGACGCTGCTGATGTGCATT
GTCACTGTGCTGAGTCACGGGCTGCGGAGCGGGGGTGGAGTAGGAGATGTACTCAGGAAG
CCGTCCAAAGAGGAACCCCTGTTTGCTGCTAGAGTTATTTATGACCTCTTGTTCTTCTTC
ATGGTCATCATCATTGTTCTTAACCTGATTTTTGGGGTTATCATTGACACTTTTGCTGAC
CTGAGGAGTGAGAAGCAGAAGAAGGAAGAGATCTTGAAGACCACGTGCTTTATCTGTGGC
TTGGAAAGAGACAAGTTTGACAACAAGACTGTCACCTTTGAAGAGCACATCAAGGAAGAA
CACAACATGTGGCACTATCTGTGCTTCATCGTCCTGGTGAAAGTAAAGGACTCCACCGAA
TATACTGGGCCTGAGAGTTACGTGGCAGAAATGATCAAGGAAAGAAACCTTGACTGGTTC
CCCAGGATGAGAGCCATGTCATTGGTCAGCAGTGATTCTGAAGGAGAACAGAATGAGCTG
AGAAACCTGCAGGAGAAGCTGGAGTCCACCATGAAACTTGTCACGAACCTTTCTGGCCAG
CTGTCGGAATTAAAGGATCAGATGACAGAACAAAGGAAGCAGAAACAAAGAATTGGTCTT
CTAGGACATCCTCCTCACATGAATGTCAACCCACAACAACCAGCATAA
Enzyme 71 GenBank Gene ID Not Available
Enzyme 71 GeneCard ID ITPR1 Link Image
Enzyme 71 GenAtlas ID ITPR1 Link Image
Enzyme 71 HGNC ID HGNC:6180 Link Image
Enzyme 71 Chromosome Location 3
Enzyme 71 Locus 3p26.1
Enzyme 71 SNPs SNPJam Report Link Image
Enzyme 71 General References
  1. Yamada N, Makino Y, Clark RA, Pearson DW, Mattei MG, Guenet JL, Ohama E, Fujino I, Miyawaki A, Furuichi T, et al.: Human inositol 1,4,5-trisphosphate type-1 receptor, InsP3R1: structure, function, regulation of expression and chromosomal localization. Biochem J. 1994 Sep 15;302 ( Pt 3):781-90. [PubMed Link Image]
  2. Harnick DJ, Jayaraman T, Ma Y, Mulieri P, Go LO, Marks AR: The human type 1 inositol 1,4,5-trisphosphate receptor from T lymphocytes. Structure, localization, and tyrosine phosphorylation. J Biol Chem. 1995 Feb 10;270(6):2833-40. [PubMed Link Image]
  3. Nucifora FC Jr, Li SH, Danoff S, Ullrich A, Ross CA: Molecular cloning of a cDNA for the human inositol 1,4,5-trisphosphate receptor type 1, and the identification of a third alternatively spliced variant. Brain Res Mol Brain Res. 1995 Sep;32(2):291-6. [PubMed Link Image]
  4. Yan J, Khanna KK, Lavin MF: Induction of inositol 1,4,5 trisphosphate receptor genes by ionizing radiation. Int J Radiat Biol. 1996 May;69(5):539-46. [PubMed Link Image]
  5. Yang J, McBride S, Mak DO, Vardi N, Palczewski K, Haeseleer F, Foskett JK: Identification of a family of calcium sensors as protein ligands of inositol trisphosphate receptor Ca(2+) release channels. Proc Natl Acad Sci U S A. 2002 May 28;99(11):7711-6. [PubMed Link Image]
  6. Kasri NN, Holmes AM, Bultynck G, Parys JB, Bootman MD, Rietdorf K, Missiaen L, McDonald F, De Smedt H, Conway SJ, Holmes AB, Berridge MJ, Roderick HL: Regulation of InsP3 receptor activity by neuronal Ca2+-binding proteins. EMBO J. 2004 Jan 28;23(2):312-21. Epub 2003 Dec 18. [PubMed Link Image]
  7. Higo T, Hattori M, Nakamura T, Natsume T, Michikawa T, Mikoshiba K: Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44. Cell. 2005 Jan 14;120(1):85-98. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Antl M, von Bruhl ML, Eiglsperger C, Werner M, Konrad I, Kocher T, Wilm M, Hofmann F, Massberg S, Schlossmann J: IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation. Blood. 2007 Jan 15;109(2):552-9. Epub 2006 Sep 21. [PubMed Link Image]
  10. van de Leemput J, Chandran J, Knight MA, Holtzclaw LA, Scholz S, Cookson MR, Houlden H, Gwinn-Hardy K, Fung HC, Lin X, Hernandez D, Simon-Sanchez J, Wood NW, Giunti P, Rafferty I, Hardy J, Storey E, Gardner RJ, Forrest SM, Fisher EM, Russell JT, Cai H, Singleton AB: Deletion at ITPR1 underlies ataxia in mice and spinocerebellar ataxia 15 in humans. PLoS Genet. 2007 Jun;3(6):e108. Epub 2007 May 16. [PubMed Link Image]
  11. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  12. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  14. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  15. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 71 Metabolite References Not Available
Enzyme 72 [top]
Enzyme 72 ID 8453
Enzyme 72 Name Rap guanine nucleotide exchange factor 4
Enzyme 72 Synonyms
  1. Exchange factor directly activated by cAMP 2
  2. Exchange protein directly activated by cAMP 2
  3. EPAC 2
  4. cAMP-regulated guanine nucleotide exchange factor II
  5. cAMP-GEFII
Enzyme 72 Gene Name RAPGEF4
Enzyme 72 Protein Sequence >Rap guanine nucleotide exchange factor 4
MVAAHAAHSSSSAEWIACLDKRPLERSSEDVDIIFTRLKEVKAFEKFHPNLLHQICLCGY
YENLEKGITLFRQGDIGTNWYAVLAGSLDVKVSETSSHQDAVTICTLGIGTAFGESILDN
TPRHATIVTRESSELLRIEQKDFKALWEKYRQYMAGLLAPPYGVMETGSNNDRIPDKENT
PLIEPHVPLRPANTITKVPSEKILRAGKILRNAILSRAPHMIRDRKYHLKTYRQCCVGTE
LVDWMMQQTPCVHSRTQAVGMWQVLLEDGVLNHVDQEHHFQDKYLFYRFLDDEHEDAPLP
TEEEKKECDEELQDTMLLLSQMGPDAHMRMILRKPPGQRTVDDLEIIYEELLHIKALSHL
STTVKRELAGVLIFESHAKGGTVLFNQGEEGTSWYIILKGSVNVVIYGKGVVCTLHEGDD
FGKLALVNDAPRAASIVLREDNCHFLRVDKEDFNRILRDVEANTVRLKEHDQDVLVLEKV
PAGNRASNQGNSQPQQKYTVMSGTPEKILEHFLETIRLEATLNEATDSVLNDFIMMHCVF
MPNTQLCPALVAHYHAQPSQGTEQEKMDYALNNKRRVIRLVLQWAAMYGDLLQEDDVSMA
FLEEFYVSVSDDARMIAALKEQLPELEKIVKQISEDAKAPQKKHKVLLQQFNTGDERAQK
RQPIRGSDEVLFKVYCMDHTYTTIRVPVATSVKEVISAVADKLGSGEGLIIVKMSSGGEK
VVLKPNDVSVFTTLTINGRLFACPREQFDSLTPLPEQEGPTVGTVGTFELMSSKDLAYQM
TIYDWELFNCVHELELIYHTFGRHNFKKTTANLDLFLRRFNEIQFWVVTEICLCSQLSKR
VQLLKKFIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLM
DPSRNHRAYRLTVAKLEPPLIPFMPLLIKDMTFTHEGNKTFIDNLVNFEKMRMIANTART
VRYYRSQPFNPDAAQANKNHQDVRSYVRQLNVIDNQRTLSQMSHRLEPRRP
Enzyme 72 Number of Residues 1011
Enzyme 72 Molecular Weight 115520.7
Enzyme 72 Theoretical pI 6.83
Enzyme 72 GO Classification
Function
  • GTPase regulator activity
  • cAMP-dependent protein kinase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • kinase regulator activity
  • nucleoside-triphosphatase regulator activity
  • protein kinase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular metabolic process
  • regulation of cellular process
  • regulation of cellular protein metabolic process
  • regulation of metabolic process
  • regulation of protein amino acid phosphorylation
  • regulation of protein modification process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • signaling
  • signaling pathway
  • small GTPase mediated signal transduction
Component
  • cAMP-dependent protein kinase complex
  • cell part
  • intracellular
  • macromolecular complex
  • protein complex
Enzyme 72 General Function Involved in cAMP-dependent protein kinase regulator activity
Enzyme 72 Specific Function Guanine nucleotide exchange factor (GEF) for RAP1A, RAP1B and RAP2A small GTPases that is activated by binding cAMP. Seems not to activate RAB3A. Involved in cAMP-dependent, PKA- independent exocytosis through interaction with RIMS2
Enzyme 72 Pathways Not Available
Enzyme 72 Reactions Not Available
Enzyme 72 Pfam Domain Function
Enzyme 72 Signals
  • None
Enzyme 72 Transmembrane Regions
  • None
Enzyme 72 Essentiality Not Available
Enzyme 72 GenBank ID Protein 17061825 Link Image
Enzyme 72 UniProtKB/Swiss-Prot ID Q8WZA2 Link Image
Enzyme 72 UniProtKB/Swiss-Prot Entry Name RPGF4_HUMAN Link Image
Enzyme 72 PDB ID Not Available
Enzyme 72 Cellular Location Not Available
Enzyme 72 Gene Sequence >3036 bp
ATGGTCGCTGCGCACGCTGCCCATTCTTCCTCCTCTGCCGAGTGGATCGCCTGCCTGGAT
AAAAGACCACTGGAGCGATCCAGCGAAGATGTGGATATAATCTTCACTCGACTGAAAGAA
GTTAAAGCTTTTGAGAAATTTCACCCAAATCTCCTTCATCAGATTTGCTTATGTGGTTAT
TATGAGAATCTGGAAAAGGGAATAACATTATTTCGCCAGGGTGATATTGGAACAAACTGG
TATGCTGTCCTGGCAGGGTCTTTGGATGTTAAAGTATCTGAGACCAGCAGTCACCAGGAT
GCTGTGACCATCTGTACCCTGGGAATTGGGACGGCCTTTGGAGAGTCCATTCTGGACAAC
ACACCCCGCCATGCAACCATCGTTACCAGGGAGAGCAGTGAATTGCTCCGCATCGAGCAG
AAGGACTTCAAGGCACTATGGGAGAAATATCGACAGTATATGGCAGGACTTCTGGCTCCT
CCTTATGGTGTTATGGAAACGGGCTCTAACAATGACAGGATTCCTGACAAGGAGAACACA
CCTCTCATTGAACCTCACGTTCCTCTTCGTCCTGCTAACACCATTACCAAGGTCCCTTCA
GAGAAGATCCTCAGAGCTGGAAAAATTTTACGAAATGCCATTCTCTCTCGAGCACCTCAC
ATGATAAGAGATAGAAAATACCACCTAAAGACATACAGACAATGCTGTGTGGGAACTGAA
CTGGTGGACTGGATGATGCAGCAGACACCATGTGTTCACTCCCGGACTCAAGCTGTTGGC
ATGTGGCAAGTCCTGTTAGAAGATGGTGTTCTCAACCACGTGGACCAGGAGCACCATTTC
CAAGACAAATATTTATTCTATCGATTTCTGGATGATGAGCACGAGGATGCCCCTTTGCCT
ACTGAGGAGGAGAAGAAGGAGTGTGATGAGGAGCTCCAGGACACCATGCTGCTGCTGTCA
CAGATGGGCCCCGACGCCCACATGAGGATGATCCTTCGCAAACCACCTGGCCAGAGGACT
GTGGATGACCTAGAGATTATCTATGAGGAGCTTCTTCATATTAAAGCCTTATCCCATCTT
TCTACCACAGTGAAACGAGAGTTAGCAGGTGTTCTCATTTTTGAGTCTCACGCCAAAGGA
GGGACTGTGTTGTTTAACCAGGGGGAAGAAGGTACCTCCTGGTACATTATTCTAAAAGGA
TCAGTGAATGTAGTCATTTACGGCAAGGGTGTGGTCTGCACCCTGCATGAAGGAGATGAC
TTCGGCAAGTTAGCACTAGTGAATGATGCCCCACGAGCTGCCTCTATCGTCTTACGAGAA
GATAACTGCCATTTCTTAAGAGTAGACAAGGAGGATTTCAACCGGATCCTAAGGGACGTG
GAGGCGAATACAGTCAGACTTAAAGAACATGACCAAGATGTCTTGGTGCTGGAGAAGGTC
CCAGCAGGGAACAGAGCTTCTAATCAAGGAAACTCACAGCCTCAGCAAAAGTATACTGTG
ATGTCAGGAACACCTGAAAAAATTTTAGAGCATTTTCTAGAAACAATACGCCTTGAGGCA
ACTTTAAATGAAGCAACAGATTCTGTTTTAAATGACTTTATTATGATGCACTGTGTTTTT
ATGCCAAATACCCAGCTTTGCCCGGCACTGGTGGCCCACTACCACGCACAGCCTTCACAA
GGTACAGAACAGGAGAAAATGGATTATGCCCTCAACAATAAGAGGCGAGTCATCCGCCTG
GTTCTACAGTGGGCTGCCATGTATGGAGACCTCCTGCAAGAGGATGACGTGTCTATGGCC
TTCCTGGAGGAGTTTTATGTATCTGTATCAGATGATGCCCGGATGATTGCTGCCCTCAAG
GAGCAACTGCCAGAGTTGGAGAAGATTGTCAAGCAAATCTCAGAAGATGCAAAGGCACCA
CAAAAGAAGCACAAGGTTCTTTTGCAACAGTTCAATACGGGCGATGAGAGAGCCCAGAAG
CGCCAGCCTATCCGCGGCTCTGATGAAGTTCTGTTTAAGGTCTATTGCATGGACCACACC
TACACAACCATTCGGGTGCCAGTGGCCACTTCGGTGAAGGAAGTCATCAGTGCAGTTGCC
GACAAGCTGGGCTCCGGGGAGGGCCTGATCATAGTCAAGATGAGTTCCGGAGGAGAAAAG
GTGGTGCTCAAACCTAATGATGTTTCAGTATTTACGACGCTCACCATTAATGGACGCCTG
TTTGCTTGCCCGCGAGAGCAATTCGATTCACTGACTCCCTTACCAGAACAGGAAGGCCCA
ACTGTTGGAACAGTGGGAACTTTTGAACTGATGAGCTCCAAAGATTTAGCATACCAGATG
ACAATTTATGATTGGGAACTCTTCAACTGCGTGCATGAGCTGGAGCTAATCTATCACACA
TTTGGAAGGCATAATTTTAAAAAGACCACAGCAAACTTGGATTTGTTCCTGAGGAGATTT
AATGAAATTCAGTTTTGGGTCGTCACTGAGATCTGCCTTTGTTCTCAGCTCAGCAAGCGT
GTTCAGCTATTAAAAAAATTTATTAAGATAGCAGCCCACTGTAAGGAGTATAAAAATCTG
AATTCCTTTTTTGCCATCGTCATGGGACTAAGTAACGTTGCTGTGAGCCGCTTGGCACTA
ACGTGGGAGAAACTGCCAAGCAAGTTCAAGAAGTTCTATGCGGAGTTTGAAAGTTTAATG
GACCCTTCAAGGAACCACAGGGCCTACAGGCTGACAGTAGCTAAGCTGGAACCTCCTCTC
ATCCCCTTCATGCCTTTGCTCATTAAAGATATGACATTTACTCATGAGGGGAACAAGACG
TTCATTGACAATCTAGTAAACTTTGAAAAAATGCGCATGATTGCAAATACGGCCAGAACA
GTGAGATACTACAGGAGCCAACCCTTCAATCCTGATGCAGCTCAAGCTAATAAGAACCAT
CAGGATGTCCGGAGTTATGTACGGCAATTAAATGTGATTGACAACCAGAGAACTTTATCA
CAGATGTCACACAGATTAGAGCCTCGTCGACCATAG
Enzyme 72 GenBank Gene ID AB027471 Link Image
Enzyme 72 GeneCard ID RAPGEF4 Link Image
Enzyme 72 GenAtlas ID RAPGEF4 Link Image
Enzyme 72 HGNC ID HGNC:16626 Link Image
Enzyme 72 Chromosome Location 2
Enzyme 72 Locus 2q31-q32
Enzyme 72 SNPs SNPJam Report Link Image
Enzyme 72 General References
  1. Kawasaki H, Springett GM, Mochizuki N, Toki S, Nakaya M, Matsuda M, Housman DE, Graybiel AM: A family of cAMP-binding proteins that directly activate Rap1. Science. 1998 Dec 18;282(5397):2275-9. [PubMed Link Image]
  2. Ueno H, Shibasaki T, Iwanaga T, Takahashi K, Yokoyama Y, Liu LM, Yokoi N, Ozaki N, Matsukura S, Yano H, Seino S: Characterization of the gene EPAC2: structure, chromosomal localization, tissue expression, and identification of the liver-specific isoform. Genomics. 2001 Nov;78(1-2):91-8. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. de Rooij J, Rehmann H, van Triest M, Cool RH, Wittinghofer A, Bos JL: Mechanism of regulation of the Epac family of cAMP-dependent RapGEFs. J Biol Chem. 2000 Jul 7;275(27):20829-36. [PubMed Link Image]
Enzyme 72 Metabolite References Not Available
Enzyme 73 [top]
Enzyme 73 ID 8461
Enzyme 73 Name Steroidogenic factor 1
Enzyme 73 Synonyms
  1. SF-1
  2. STF-1
  3. Adrenal 4-binding protein
  4. Fushi tarazu factor homolog 1
  5. Nuclear receptor subfamily 5 group A member 1
  6. Steroid hormone receptor Ad4BP
Enzyme 73 Gene Name NR5A1
Enzyme 73 Protein Sequence >Steroidogenic factor 1
MDYSYDEDLDELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKHYTCTESQSCKIDKT
QRKRCPFCRFQKCLTVGMRLEAVRADRMRGGRNKFGPMYKRDRALKQQKKAQIRANGFKL
ETGPPMGVPPPPPPAPDYVLPPSLHGPEPKGLAAGPPAGPLGDFGAPALPMAVPGAHGPL
AGYLYPAFPGRAIKSEYPEPYASPPQPGLPYGYPEPFSGGPNVPELILQLLQLEPDEDQV
RARILGCLQEPTKSRPDQPAAFGLLCRMADQTFISIVDWARRCMVFKELEVADQMTLLQN
CWSELLVFDHIYRQVQHGKEGSILLVTGQEVELTTVATQAGSLLHSLVLRAQELVLQLLA
LQLDRQEFVCLKFIILFSLDLKFLNNHILVKDAQEKANAALLDYTLCHYPHCGDKFQQLL
LCLVEVRALSMQAKEYLYHKHLGNEMPRNNLLIEMLQAKQT
Enzyme 73 Number of Residues 461
Enzyme 73 Molecular Weight 51635.5
Enzyme 73 Theoretical pI 7.73
Enzyme 73 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • ligand-dependent nuclear receptor activity
  • metal ion binding
  • molecular transducer activity
  • nucleic acid binding
  • receptor activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
  • signal transducer activity
  • steroid hormone receptor activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 73 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 73 Specific Function Transcriptional activator. Seems to be essential for sexual differentiation and formation of the primary steroidogenic tissues. Binds to the Ad4 site found in the promoter region of steroidogenic P450 genes such as CYP11A, CYP11B and CYP21B. Also regulates the AMH/Muellerian inhibiting substance gene as well as the AHCH and STAR genes. 5'-YCAAGGYC-3' and 5'-RRAGGTCA-3' are the consensus sequences for the recognition by NR5A1. The SFPQ-NONO- NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. Binds phosphatidylcholine. Binds phospholipids with a phosphatidylinositol (PI) headgroup, in particular PI(3,4)P2 and PI(3,4,5)P3
Enzyme 73 Pathways Not Available
Enzyme 73 Reactions Not Available
Enzyme 73 Pfam Domain Function
Enzyme 73 Signals
  • None
Enzyme 73 Transmembrane Regions
  • None
Enzyme 73 Essentiality Not Available
Enzyme 73 GenBank ID Protein Not Available
Enzyme 73 UniProtKB/Swiss-Prot ID Q13285 Link Image
Enzyme 73 UniProtKB/Swiss-Prot Entry Name STF1_HUMAN Link Image
Enzyme 73 PDB ID 1YP0 Link Image
Enzyme 73 PDB File Show
Enzyme 73 3D Structure
Enzyme 73 Cellular Location Not Available
Enzyme 73 Gene Sequence >1386 bp
ATGGACTATTCGTACGACGAGGACCTGGACGAGCTGTGCCCCGTGTGCGGGGACAAGGTG
TCCGGCTACCACTACGGACTGCTCACGTGTGAGAGCTGCAAGGGCTTCTTCAAGCGCACG
GTGCAGAACAACAAGCACTACACGTGCACCGAGAGCCAGAGCTGCAAGATCGACAAGACG
CAGCGCAAGCGCTGTCCCTTCTGCCGCTTCCAGAAATGCCTGACGGTGGGGATGCGCCTG
GAAGCCGTGCGCGCTGACCGTATGAGGGGTGGCCGGAACAAGTTTGGGCCGATGTACAAG
CGGGACCGGGCCCTGAAACAGCAGAAGAAGGCACAGATTCGGGCCAATGGCTTCAAGCTG
GAGACAGGGCCCCCGATGGGGGTGCCCCCGCCGCCCCCTCCCGCACCGGACTACGTGCTG
CCTCCCAGCCTGCATGGGCCTGAGCCCAAGGGCCTGGCCGCCGGTCCACCTGCTGGGCCA
CTGGGCGACTTTGGGGCCCCAGCACTGCCCATGGCCGTGCCCGGTGCCCACGGGCCACTG
GCTGGCTACCTCTACCCTGCCTTTCCTGGCCGTGCCATCAAGTCTGAGTACCCGGAGCCT
TATGCCAGCCCCCCACAGCCTGGGCTGCCGTACGGCTACCCAGAGCCCTTCTCTGGAGGC
CCCAACGTGCCTGAGCTCATCCTGCAGCTGCTGCAGCTGGAGCCGGATGAGGACCAGGTG
CGGGCCCGCATCTTGGGCTGCCTGCAGGAGCCCACCAAAAGCCGCCCCGACCAGCCGGCG
GCCTTCGGCCTCCTGTGCAGAATGGCCGACCAGACCTTCATCTCCATCGTGGACTGGGCA
CGCAGGTGCATGGTCTTCAAGGAGCTGGAGGTGGCCGACCAGATGACGCTGCTGCAGAAC
TGCTGGAGCGAGCTGCTGGTGTTCGACCACATCTACCGCCAGGTCCAGCACGGCAAGGAG
GGCAGCATCCTGCTGGTCACCGGGCAGGAGGTGGAGCTGACCACAGTGGCCACCCAGGCG
GGCTCGCTGCTGCACAGCCTGGTGTTGCGGGCGCAGGAGCTGGTGCTGCAGCTGCTTGCG
CTGCAGCTGGACCGGCAGGAGTTTGTCTGCCTCAAGTTCATCATCCTCTTCAGCCTGGAT
TTGAAGTTCCTGAATAACCACATCCTGGTGAAAGACGCTCAGGAGAAGGCCAACGCCGCC
CTGCTTGACTACACCCTGTGCCACTACCCGCACTGCGGGGACAAATTCCAGCAGCTGCTG
CTGTGCCTGGTGGAGGTGCGGGCCCTGAGCATGCAGGCCAAGGAGTACCTGTACCACAAG
CACCTGGGCAACGAGATGCCCCGCAACAACCTGCTCATCGAAATGCTGCAAGCCAAGCAG
ACTTGA
Enzyme 73 GenBank Gene ID U76388 Link Image
Enzyme 73 GeneCard ID NR5A1 Link Image
Enzyme 73 GenAtlas ID NR5A1 Link Image
Enzyme 73 HGNC ID HGNC:7983 Link Image
Enzyme 73 Chromosome Location 9
Enzyme 73 Locus 9q33
Enzyme 73 SNPs SNPJam Report Link Image
Enzyme 73 General References
  1. Oba K, Yanase T, Nomura M, Morohashi K, Takayanagi R, Nawata H: Structural characterization of human Ad4bp (SF-1) gene. Biochem Biophys Res Commun. 1996 Sep 4;226(1):261-7. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Hammer GD, Krylova I, Zhang Y, Darimont BD, Simpson K, Weigel NL, Ingraham HA: Phosphorylation of the nuclear receptor SF-1 modulates cofactor recruitment: integration of hormone signaling in reproduction and stress. Mol Cell. 1999 Apr;3(4):521-6. [PubMed Link Image]
  5. Jacob AL, Lund J, Martinez P, Hedin L: Acetylation of steroidogenic factor 1 protein regulates its transcriptional activity and recruits the coactivator GCN5. J Biol Chem. 2001 Oct 5;276(40):37659-64. Epub 2001 Jul 30. [PubMed Link Image]
  6. Sewer MB, Nguyen VQ, Huang CJ, Tucker PW, Kagawa N, Waterman MR: Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, and SF-1, a complex that also participates in repression of transcription. Endocrinology. 2002 Apr;143(4):1280-90. [PubMed Link Image]
  7. Komatsu T, Mizusaki H, Mukai T, Ogawa H, Baba D, Shirakawa M, Hatakeyama S, Nakayama KI, Yamamoto H, Kikuchi A, Morohashi K: Small ubiquitin-like modifier 1 (SUMO-1) modification of the synergy control motif of Ad4 binding protein/steroidogenic factor 1 (Ad4BP/SF-1) regulates synergistic transcription between Ad4BP/SF-1 and Sox9. Mol Endocrinol. 2004 Oct;18(10):2451-62. Epub 2004 Jun 10. [PubMed Link Image]
  8. Li D, Urs AN, Allegood J, Leon A, Merrill AH Jr, Sewer MB: Cyclic AMP-stimulated interaction between steroidogenic factor 1 and diacylglycerol kinase theta facilitates induction of CYP17. Mol Cell Biol. 2007 Oct;27(19):6669-85. Epub 2007 Jul 30. [PubMed Link Image]
  9. Krylova IN, Sablin EP, Moore J, Xu RX, Waitt GM, MacKay JA, Juzumiene D, Bynum JM, Madauss K, Montana V, Lebedeva L, Suzawa M, Williams JD, Williams SP, Guy RK, Thornton JW, Fletterick RJ, Willson TM, Ingraham HA: Structural analyses reveal phosphatidyl inositols as ligands for the NR5 orphan receptors SF-1 and LRH-1. Cell. 2005 Feb 11;120(3):343-55. [PubMed Link Image]
  10. Wang W, Zhang C, Marimuthu A, Krupka HI, Tabrizizad M, Shelloe R, Mehra U, Eng K, Nguyen H, Settachatgul C, Powell B, Milburn MV, West BL: The crystal structures of human steroidogenic factor-1 and liver receptor homologue-1. Proc Natl Acad Sci U S A. 2005 May 24;102(21):7505-10. Epub 2005 May 16. [PubMed Link Image]
  11. Achermann JC, Ito M, Ito M, Hindmarsh PC, Jameson JL: A mutation in the gene encoding steroidogenic factor-1 causes XY sex reversal and adrenal failure in humans. Nat Genet. 1999 Jun;22(2):125-6. [PubMed Link Image]
  12. Biason-Lauber A, Schoenle EJ: Apparently normal ovarian differentiation in a prepubertal girl with transcriptionally inactive steroidogenic factor 1 (NR5A1/SF-1) and adrenocortical insufficiency. Am J Hum Genet. 2000 Dec;67(6):1563-8. Epub 2000 Oct 18. [PubMed Link Image]
  13. Achermann JC, Ozisik G, Ito M, Orun UA, Harmanci K, Gurakan B, Jameson JL: Gonadal determination and adrenal development are regulated by the orphan nuclear receptor steroidogenic factor-1, in a dose-dependent manner. J Clin Endocrinol Metab. 2002 Apr;87(4):1829-33. [PubMed Link Image]
  14. Lin L, Philibert P, Ferraz-de-Souza B, Kelberman D, Homfray T, Albanese A, Molini V, Sebire NJ, Einaudi S, Conway GS, Hughes IA, Jameson JL, Sultan C, Dattani MT, Achermann JC: Heterozygous missense mutations in steroidogenic factor 1 (SF1/Ad4BP, NR5A1) are associated with 46,XY disorders of sex development with normal adrenal function. J Clin Endocrinol Metab. 2007 Mar;92(3):991-9. Epub 2007 Jan 2. [PubMed Link Image]
  15. Kohler B, Lin L, Ferraz-de-Souza B, Wieacker P, Heidemann P, Schroder V, Biebermann H, Schnabel D, Gruters A, Achermann JC: Five novel mutations in steroidogenic factor 1 (SF1, NR5A1) in 46,XY patients with severe underandrogenization but without adrenal insufficiency. Hum Mutat. 2008 Jan;29(1):59-64. [PubMed Link Image]
  16. Lourenco D, Brauner R, Lin L, De Perdigo A, Weryha G, Muresan M, Boudjenah R, Guerra-Junior G, Maciel-Guerra AT, Achermann JC, McElreavey K, Bashamboo A: Mutations in NR5A1 associated with ovarian insufficiency. N Engl J Med. 2009 Mar 19;360(12):1200-10. Epub 2009 Feb 25. [PubMed Link Image]
Enzyme 73 Metabolite References Not Available
Enzyme 74 [top]
Enzyme 74 ID 8798
Enzyme 74 Name Sodium bicarbonate cotransporter 3
Enzyme 74 Synonyms
  1. Sodium bicarbonate cotransporter 2
  2. Sodium bicarbonate cotransporter 2b
  3. Bicarbonate transporter
  4. Solute carrier family 4 member 7
Enzyme 74 Gene Name SLC4A7
Enzyme 74 Protein Sequence >Sodium bicarbonate cotransporter 3
MERFRLEKKLPGPDEEAVVDLGKTSSTVNTKFEKEELESHRAVYIGVHVPFSKESRRRHR
HRGHKHHHRRRKDKESDKEDGRESPSYDTPSQRVQFILGTEDDDEEHIPHDLFTEMDELC
YRDGEEYEWKETARWLKFEEDVEDGGDRWSKPYVATLSLHSLFELRSCILNGTVMLDMRA
STLDEIADMVLDNMIASGQLDESIRENVREALLKRHHHQNEKRFTSRIPLVRSFADIGKK
HSDPHLLERNGEGLSASRHSLRTGLSASNLSLRGESPLSLLLGHLLPSSRAGTPAGSRCT
TPVPTPQNSPPSSPSISRLTSRSSQESQRQAPELLVSPASDDIPTVVIHPPEEDLEAALK
GEEQKNEENVDLTPGILASPQSAPGNLDNSKSGEIKGNGSGGSRENSTVDFSKVDMNFMR
KIPTGAEASNVLVGEVDFLERPIIAFVRLAPAVLLTGLTEVPVPTRFLFLLLGPAGKAPQ
YHEIGRSIATLMTDEIFHDVAYKAKDRNDLLSGIDEFLDQVTVLPPGEWDPSIRIEPPKS
VPSQEKRKIPVFHNGSTPTLGETPKEAAHHAGPELQRTGRLFGGLILDIKRKAPFFLSDF
KDALSLQCLASILFLYCACMSPVITFGGLLGEATEGRISAIESLFGASLTGIAYSLFAGQ
PLTILGSTGPVLVFEKILYKFCRDYQLSYLSLRTSIGLWTSFLCIVLVATDASSLVCYIT
RFTEEAFAALICIIFIYEALEKLFDLGETYAFNMHNNLDKLTSYSCVCTEPPNPSNETLA
QWKKDNITAHNISWRNLTVSECKKLRGVFLGSACGHHGPYIPDVLFWCVILFFTTFFLSS
FLKQFKTKRYFPTKVRSTISDFAVFLTIVIMVTIDYLVGVPSPKLHVPEKFEPTHPERGW
IISPLGDNPWWTLLIAAIPALLCTILIFMDQQITAVIINRKEHKLKKGAGYHLDLLMVGV
MLGVCSVMGLPWFVAATVLSISHVNSLKVESECSAPGEQPKFLGIREQRVTGLMIFILMG
LSVFMTSVLKFIPMPVLYGVFLYMGVSSLKGIQLFDRIKLFGMPAKHQPDLIYLRYVPLW
KVHIFTVIQLTCLVLLWVIKVSAAAVVFPMMVLALVFVRKLMDLCFTKRELSWLDDLMPE
SKKKKEDDKKKKEKEEAERMLQDDDDTVHLPFEGGSLLQIPVKALKYSPDKPVSVKISFE
DEPRKKYVDAETSL
Enzyme 74 Number of Residues 1214
Enzyme 74 Molecular Weight 136042.6
Enzyme 74 Theoretical pI 6.70
Enzyme 74 GO Classification
Function
  • anion transmembrane transporter activity
  • anion:anion antiporter activity
  • inorganic anion exchanger activity
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • anion transport
  • establishment of localization
  • ion transport
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 74 General Function Involved in anion transport
Enzyme 74 Specific Function Electroneutral sodium- and bicarbonate-dependent cotransporter with a Na(+):HCO3(-) 1:1 stoichiometry. Regulates intracellular pH and may play a role in bicarbonate salvage in secretory epithelia. May also have an associated sodium channel activity
Enzyme 74 Pathways Not Available
Enzyme 74 Reactions Not Available
Enzyme 74 Pfam Domain Function
Enzyme 74 Signals
  • None
Enzyme 74 Transmembrane Regions
  • 609-629 638-658 696-716 726-746 818-838 862-882 909-929 955-975 1012-1032 1035-1055 1093-1113
Enzyme 74 Essentiality Not Available
Enzyme 74 GenBank ID Protein 134288865 Link Image
Enzyme 74 UniProtKB/Swiss-Prot ID Q9Y6M7 Link Image
Enzyme 74 UniProtKB/Swiss-Prot Entry Name S4A7_HUMAN Link Image
Enzyme 74 PDB ID Not Available
Enzyme 74 Cellular Location Not Available
Enzyme 74 Gene Sequence >3645 bp
ATGGAAAGATTTCGTCTGGAGAAGAAGTTACCTGGTCCTGATGAAGAAGCTGTTGTGGAT
CTTGGCAAAACTAGCTCAACTGTGAACACCAAGTTTGAAAAAGAAGAACTAGAAAGTCAT
AGAGCTGTATATATTGGTGTTCACGTCCCGTTTAGTAAAGAGAGTCGTCGGCGTCATAGG
CATCGCGGACACAAACATCACCACCGGAGAAGAAAAGATAAAGAATCAGATAAAGAAGAT
GGACGGGAATCTCCTTCTTATGATACACCATCCCAGAGAGTTCAGTTTATCCTTGGTACT
GAAGATGATGATGAAGAACATATTCCCCATGATCTCTTCACGGAAATGGATGAACTGTGT
TACAGAGATGGAGAAGAATATGAATGGAAAGAAACTGCTAGATGGCTGAAATTTGAAGAG
GATGTTGAAGATGGCGGTGACCGATGGAGTAAACCTTATGTGGCAACTCTCTCTTTGCAC
AGTCTTTTTGAACTAAGGAGTTGCATCCTCAATGGAACAGTCATGCTGGATATGAGAGCA
AGCACTCTAGATGAAATAGCAGATATGGTATTAGACAACATGATAGCTTCTGGCCAATTA
GACGAGTCCATACGAGAGAATGTCAGAGAAGCTCTTCTGAAGAGACATCATCATCAGAAT
GAGAAAAGATTCACCAGTCGGATTCCTCTTGTTCGATCTTTTGCAGATATAGGCAAGAAA
CATTCTGACCCTCACTTGCTTGAAAGGAATGGGGAAGGCCTTTCAGCCTCCCGCCACTCT
TTGCGAACAGGTCTGTCTGCCTCAAACCTTTCCTTGAGAGGAGAATCACCTTTATCTCTT
CTTCTTGGTCATCTTCTTCCTTCTTCAAGAGCTGGAACCCCTGCAGGCTCAAGGTGTACA
ACCCCAGTACCCACCCCTCAAAACAGTCCTCCTTCTAGCCCTAGCATCAGCCGCCTGACC
TCCAGAAGTTCCCAAGAGAGTCAGCGTCAGGCCCCAGAACTACTGGTTTCACCTGCCAGT
GATGATATTCCCACAGTAGTAATTCATCCGCCTGAGGAAGACTTAGAAGCAGCGCTGAAA
GGCGAGGAGCAGAAGAATGAGGAAAATGTTGACTTAACTCCAGGTATTTTGGCCTCTCCC
CAGTCTGCTCCTGGAAACTTGGACAATAGTAAAAGTGGAGAAATTAAAGGTAATGGAAGT
GGTGGAAGCAGAGAAAATAGTACTGTTGACTTCAGCAAGGTTGATATGAATTTCATGAGA
AAAATTCCTACGGGTGCTGAGGCATCCAACGTCCTGGTGGGCGAAGTAGACTTTTTGGAA
AGGCCAATAATTGCATTTGTGAGACTGGCTCCTGCTGTCCTCCTTACAGGGTTGACTGAG
GTCCCTGTTCCAACCAGGTTTTTGTTTTTGTTATTGGGTCCAGCGGGCAAGGCACCACAG
TACCATGAAATTGGACGATCAATAGCCACTCTCATGACAGATGAGATTTTCCATGATGTA
GCTTATAAAGCAAAAGACAGAAATGACCTCTTATCTGGAATTGATGAATTTTTAGATCAA
GTAACTGTCCTACCTCCAGGAGAGTGGGATCCTTCTATACGCATAGAACCACCAAAAAGT
GTCCCTTCTCAGGAAAAGAGAAAGATTCCTGTGTTTCACAATGGATCTACCCCCACACTG
GGTGAGACTCCTAAAGAGGCCGCTCATCATGCTGGGCCTGAGCTACAGAGGACTGGACGG
CTTTTTGGTGGTTTGATACTTGACATCAAAAGGAAAGCACCTTTTTTCTTGAGTGACTTC
AAGGATGCATTAAGCCTGCAGTGCCTGGCCTCGATTCTTTTCCTATACTGTGCCTGTATG
TCTCCTGTAATCACTTTTGGAGGGCTGCTTGGAGAAGCTACAGAAGGCAGAATAAGTGCA
ATAGAGTCTCTTTTTGGAGCATCATTAACTGGGATTGCCTATTCATTGTTTGCTGGGCAA
CCTCTAACAATATTGGGGAGCACAGGTCCAGTTCTAGTGTTTGAAAAAATTTTATATAAA
TTCTGCAGAGATTATCAACTTTCTTATCTGTCTTTAAGAACCAGTATTGGTCTGTGGACT
TCTTTTTTGTGCATTGTTTTGGTTGCAACAGATGCAAGCAGCCTTGTGTGTTATATTACT
CGATTTACAGAAGAGGCTTTTGCAGCCCTTATTTGCATCATATTCATCTACGAGGCTTTG
GAGAAGCTCTTTGATTTAGGAGAAACATATGCATTTAATATGCACAACAACTTAGATAAA
CTGACCAGCTACTCATGTGTATGTACTGAACCTCCAAACCCCAGCAATGAAACTCTAGCA
CAATGGAAGAAAGATAATATAACAGCACACAATATTTCCTGGAGAAATCTTACTGTTTCT
GAATGTAAAAAACTTCGTGGTGTATTCTTGGGGTCAGCTTGTGGTCATCATGGACCTTAT
ATTCCAGATGTGCTCTTTTGGTGTGTCATCTTGTTTTTCACAACATTTTTTCTGTCTTCA
TTCCTCAAGCAATTTAAGACCAAGCGTTACTTTCCTACCAAGGTGCGATCGACAATCAGT
GATTTTGCTGTATTTCTCACAATAGTAATAATGGTTACAATTGACTACCTTGTAGGAGTT
CCATCTCCTAAACTTCATGTTCCTGAAAAATTTGAGCCTACTCATCCAGAGAGAGGGTGG
ATCATAAGCCCACTGGGAGATAATCCTTGGTGGACCTTATTAATAGCTGCTATTCCTGCT
TTGCTTTGTACCATTCTCATCTTTATGGATCAACAAATCACAGCTGTAATTATAAACAGA
AAGGAACACAAATTGAAGAAAGGAGCTGGCTATCACCTTGATTTGCTCATGGTTGGCGTT
ATGTTGGGAGTTTGCTCTGTCATGGGACTTCCATGGTTTGTGGCTGCAACAGTGTTGTCA
ATAAGTCATGTCAACAGCTTAAAAGTTGAATCTGAATGTTCTGCTCCAGGGGAACAACCC
AAGTTTTTGGGAATTCGTGAACAGCGGGTTACAGGGCTAATGATTTTTATTCTAATGGGC
CTCTCTGTGTTCATGACTTCAGTCCTAAAGTTTATTCCAATGCCTGTTCTGTATGGTGTT
TTCCTTTATATGGGAGTTTCCTCATTAAAAGGAATCCAGTTATTTGACCGTATAAAATTA
TTTGGAATGCCTGCTAAGCATCAGCCTGATTTGATATACCTCCGTTATGTGCCGCTCTGG
AAGGTCCATATTTTCACAGTCATTCAGCTTACTTGTTTGGTCCTTTTATGGGTGATAAAA
GTTTCAGCTGCTGCAGTGGTTTTTCCCATGATGGTTCTTGCATTAGTGTTTGTGCGCAAA
CTCATGGACCTGTGTTTCACGAAGAGAGAACTTAGTTGGCTTGATGATCTTATGCCAGAA
AGTAAGAAAAAGAAAGAAGATGACAAAAAGAAAAAAGAGAAAGAGGAAGCTGAACGGATG
CTTCAAGATGATGATGATACTGTGCACCTTCCATTTGAAGGGGGAAGTCTCTTGCAAATT
CCAGTCAAGGCCCTAAAATATAGTCCTGATAAACCTGTGAGTGTGAAAATAAGTTTTGAA
GATGAACCAAGAAAGAAATACGTGGATGCTGAAACTTCATTATAG
Enzyme 74 GenBank Gene ID NM_003615.3 Link Image
Enzyme 74 GeneCard ID SLC4A7 Link Image
Enzyme 74 GenAtlas ID SLC4A7 Link Image
Enzyme 74 HGNC ID HGNC:11033 Link Image
Enzyme 74 Chromosome Location 3
Enzyme 74 Locus 3p22
Enzyme 74 SNPs SNPJam Report Link Image
Enzyme 74 General References
  1. Ishibashi K, Sasaki S, Marumo F: Molecular cloning of a new sodium bicarbonate cotransporter cDNA from human retina. Biochem Biophys Res Commun. 1998 May 19;246(2):535-8. [PubMed Link Image]
  2. Pushkin A, Abuladze N, Lee I, Newman D, Hwang J, Kurtz I: Cloning, tissue distribution, genomic organization, and functional characterization of NBC3, a new member of the sodium bicarbonate cotransporter family. J Biol Chem. 1999 Jun 4;274(23):16569-75. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  5. Park M, Ko SB, Choi JY, Muallem G, Thomas PJ, Pushkin A, Lee MS, Kim JY, Lee MG, Muallem S, Kurtz I: The cystic fibrosis transmembrane conductance regulator interacts with and regulates the activity of the HCO3- salvage transporter human Na+-HCO3- cotransport isoform 3. J Biol Chem. 2002 Dec 27;277(52):50503-9. Epub 2002 Oct 25. [PubMed Link Image]
  6. Pushkin A, Abuladze N, Newman D, Muronets V, Sassani P, Tatishchev S, Kurtz I: The COOH termini of NBC3 and the 56-kDa H+-ATPase subunit are PDZ motifs involved in their interaction. Am J Physiol Cell Physiol. 2003 Mar;284(3):C667-73. Epub 2002 Nov 20. [PubMed Link Image]
  7. Loiselle FB, Morgan PE, Alvarez BV, Casey JR: Regulation of the human NBC3 Na+/HCO3- cotransporter by carbonic anhydrase II and PKA. Am J Physiol Cell Physiol. 2004 Jun;286(6):C1423-33. Epub 2004 Jan 21. [PubMed Link Image]
  8. Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC: Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. Anal Chem. 2004 May 15;76(10):2763-72. [PubMed Link Image]
  9. Reiners J, van Wijk E, Marker T, Zimmermann U, Jurgens K, te Brinke H, Overlack N, Roepman R, Knipper M, Kremer H, Wolfrum U: Scaffold protein harmonin (USH1C) provides molecular links between Usher syndrome type 1 and type 2. Hum Mol Genet. 2005 Dec 15;14(24):3933-43. Epub 2005 Nov 21. [PubMed Link Image]
  10. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  11. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  12. Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed Link Image]
  13. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 74 Metabolite References Not Available
Enzyme 75 [top]
Enzyme 75 ID 9716
Enzyme 75 Name Adenylate cyclase type 10
Enzyme 75 Synonyms
  1. AH-related protein
  2. Adenylate cyclase homolog
  3. Germ cell soluble adenylyl cyclase
  4. hsAC
  5. sAC
  6. Testicular soluble adenylyl cyclase
Enzyme 75 Gene Name ADCY10
Enzyme 75 Protein Sequence >Adenylate cyclase type 10
MNTPKEEFQDWPIVRIAAHLPDLIVYGHFSPERPFMDYFDGVLMFVDISGFTAMTEKFSS
AMYMDRGAEQLVEILNYHISAIVEKVLIFGGDILKFAGDALLALWRVERKQLKNIITVVI
KCSLEIHGLFETQEWEEGLDIRVKIGLAAGHISMLVFGDETHSHFLVIGQAVDDVRLAQN
MAQMNDVILSPNCWQLCDRSMIEIESVPDQRAVKVNFLKPPPNFNFDEFFTKCTTFMHYY
PSGEHKNLLRLACTLKPDPELEMSLQKYVMESILKQIDNKQLQGYLSELRPVTIVFVNLM
FEDQDKAEEIGPAIQDAYMHITSVLKIFQGQINKVFMFDKGCSFLCVFGFPGEKVPDELT
HALECAMDIFDFCSQVHKIQTVSIGVASGIVFCGIVGHTVRHEYTVIGQKVNLAARMMMY
YPGIVTCDSVTYNGSNLPAYFFKELPKKVMKGVADSGPLYQYWGRTEKVMFGMACLICNR
KEDYPLLGRNKEINYFMYTMKKFLISNSSQVLMYEGLPGYGKSQILMKIEYLAQGKNHRI
IAISLNKISFHQTFYTIQMFMANVLGLDTCKHYKERQTNLRNKVMTLLDEKFYCLLNDIF
HVQFPISREISRMSTLKKQKQLEILFMKILKLIVKEERIIFIIDEAQFVDSTSWRFMEKL
IRTLPIFIIMSLCPFVNIPCAAARAVIKNRNTTYIVIGAVQPNDISNKICLDLNVSCISK
ELDSYLGEGSCGIPFYCEELLKNLEHHEVLVFQQTESEEKTNRTWNNLFKYSIKLTEKLN
MVTLHSDKESEEVCHLTSGVRLKNLSPPTSLKEISLIQLDSMRLSHQMLVRCAAIIGLTF
TTELLFEILPCWNMKMMIKTLATLVESNIFYCFRNGKELQKALKQNDPSFEVHYRSLSLK
PSEGMDHGEEEQLRELENEVIECHRIRFCNPMMQKTAYELWLKDQRKAMHLKCARFLEED
AHRCDHCRGRDFIPYHHFTVNIRLNALDMDAIKKMAMSHGFKTEEKLILSNSEIPETSAF
FPENRSPEEIREKILNFFDHVLTKMKTSDEDIIPLESCQCEEILEIVILPLAHHFLALGE
NDKALYYFLEIASAYLIFCDNYMAYMYLNEGQKLLKTLKKDKSWSQTFESATFYSLKGEV
CFNMGQIVLAKKMLRKALKLLNRIFPYNLISLFLHIHVEKNRHFHYVNRQAQESPPPGKK
RLAQLYRQTVCLSLLWRIYSYSYLFHCKYYAHLAVMMQMNTALETQNCFQIIKAYLDYSL
YHHLAGYKGVWFKYEVMAMEHIFNLPLKGEGIEIVAYVAETLVFNKLIMGHLDLAIELGS
RALQMWALLQNPNRHYQSLCRLSRCLLLNSRYPQLIQVLGRLWELSVTQEHIFSKAFFYF
VCLDILLYSGFVYRTFEECLEFIHQYENNRILKFHSGLLLGLYSSVAIWYARLQEWDNFY
KFSNRAKNLLPRRTMTLTYYDGISRYMEGQVLHLQKQIKEQSENAQASGEELLKNLENLV
AQNTTGPVFCPRLYHLMAYVCILMGDGQKCGLFLNTALRLSETQGNILEKCWLNMNKESW
YSTSELKEDQWLQTILSLPSWEKIVAGRVNIQDLQKNKFLMRANTVDNHF
Enzyme 75 Number of Residues 1610
Enzyme 75 Molecular Weight 187147.5
Enzyme 75 Theoretical pI 7.32
Enzyme 75 GO Classification
Function
  • adenylate cyclase activity
  • binding
  • catalytic activity
  • cation binding
  • cyclase activity
  • ion binding
  • lyase activity
  • magnesium ion binding
  • metal ion binding
  • phosphorus-oxygen lyase activity
Process
  • cAMP biosynthetic process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • gamete generation
  • intracellular signaling pathway
  • male gamete generation
  • metabolic process
  • multicellular organismal reproductive process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • reproductive process
  • signaling
  • signaling pathway
  • spermatogenesis
Component
Enzyme 75 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 75 Specific Function Soluble adenylyl cyclase that has a critical role in mammalian spermatogenesis. Produces the cAMP which mediates in part the cAMP-responsive nuclear factors indispensable for maturation of sperm in the epididymis. Induces capacitation, the maturational process that sperm undergo prior to fertilization. May be the bicarbonate sensor. Involved in ciliary beat regulation
Enzyme 75 Pathways Not Available
Enzyme 75 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 75 Pfam Domain Function
Enzyme 75 Signals
  • None
Enzyme 75 Transmembrane Regions
  • None
Enzyme 75 Essentiality Not Available
Enzyme 75 GenBank ID Protein 7650188 Link Image
Enzyme 75 UniProtKB/Swiss-Prot ID Q96PN6 Link Image
Enzyme 75 UniProtKB/Swiss-Prot Entry Name ADCYA_HUMAN Link Image
Enzyme 75 PDB ID Not Available
Enzyme 75 Cellular Location Not Available
Enzyme 75 Gene Sequence >4833 bp
ATGAACACTCCAAAAGAAGAATTCCAGGACTGGCCCATAGTCAGAATAGCAGCTCATTTA
CCAGACCTCATTGTCTATGGACATTTCTCCCCAGAGCGACCCTTTATGGATTATTTTGAC
GGAGTCCTGATGTTTGTTGATATTTCAGGTTTTACTGCAATGACTGAGAAGTTCAGCAGT
GCCATGTACATGGACAGAGGGGCTGAGCAGTTGGTGGAGATCCTCAACTACCACATAAGT
GCAATAGTGGAGAAAGTGTTGATTTTTGGAGGAGACATCCTGAAATTTGCAGGTGATGCA
CTGCTAGCCCTGTGGAGGGTGGAGCGAAAGCAGCTGAAAAACATTATCACAGTGGTAATT
AAATGTAGCCTGGAGATCCATGGATTGTTTGAGACCCAGGAGTGGGAAGAAGGCCTAGAC
ATCCGAGTCAAGATAGGACTGGCTGCTGGCCACATCAGCATGTTGGTCTTTGGAGATGAA
ACACACAGCCACTTTCTGGTGATTGGTCAGGCAGTGGACGATGTGCGCCTTGCCCAGAAC
ATGGCTCAGATGAATGATGTTATTCTGTCACCAAACTGCTGGCAGCTCTGTGACCGGAGC
ATGATTGAAATTGAGAGTGTTCCAGATCAGAGAGCAGTTAAGGTTAACTTCTTAAAACCA
CCCCCCAATTTTAATTTTGATGAATTTTTCACAAAGTGTACGACCTTCATGCATTATTAT
CCTTCTGGTGAGCACAAAAACCTCCTGAGGCTTGCATGCACGCTGAAGCCTGATCCTGAA
CTGGAGATGTCCCTACAAAAGTATGTGATGGAAAGCATTTTGAAGCAGATTGATAACAAA
CAGCTTCAGGGCTATTTATCTGAGCTTCGCCCAGTGACGATTGTGTTTGTGAACCTGATG
TTTGAAGACCAAGACAAAGCAGAAGAGATAGGCCCAGCCATCCAGGATGCCTATATGCAC
ATCACTTCTGTCCTGAAGATCTTCCAAGGCCAAATCAATAAAGTCTTCATGTTTGACAAG
GGCTGCTCTTTCCTCTGTGTCTTTGGCTTCCCTGGGGAAAAGGTACCTGACGAGCTCACT
CATGCTCTGGAATGTGCTATGGATATATTTGACTTCTGCTCTCAAGTCCACAAAATCCAA
ACTGTATCCATCGGTGTTGCCAGTGGGATTGTCTTCTGTGGGATCGTTGGACACACTGTG
AGACACGAGTACACAGTCATTGGTCAAAAAGTCAACTTAGCTGCCAGGATGATGATGTAC
TACCCAGGAATTGTGACCTGCGACTCTGTCACCTACAATGGGAGCAACCTACCAGCGTAC
TTTTTTAAAGAGCTTCCAAAGAAAGTTATGAAAGGTGTTGCAGATTCTGGACCATTGTAT
CAGTATTGGGGCCGTACTGAGAAAGTCATGTTTGGTATGGCGTGCCTCATCTGCAACAGA
AAGGAGGATTACCCTTTGCTGGGACGTAATAAAGAGATCAACTACTTCATGTATACTATG
AAGAAATTTTTGATATCTAACAGCAGCCAAGTCTTAATGTATGAGGGATTACCAGGATAT
GGAAAAAGCCAGATACTTATGAAAATTGAGTACCTGGCCCAAGGTAAGAATCACAGGATT
ATTGCCATTTCATTGAATAAGATCAGCTTCCATCAAACTTTCTATACCATCCAGATGTTC
ATGGCCAATGTCCTAGGCCTAGACACTTGTAAACATTATAAAGAACGACAGACCAACCTT
CGAAATAAAGTCATGACACTGTTGGATGAAAAGTTCTACTGTCTTCTTAATGACATTTTC
CATGTTCAGTTCCCTATTTCTCGGGAGATTTCCAGGATGAGCACCTTGAAAAAGCAAAAA
CAATTGGAAATATTGTTTATGAAGATCTTGAAGCTGATAGTGAAAGAGGAAAGGATTATT
TTTATCATTGATGAGGCCCAGTTTGTGGATTCGACCTCCTGGAGATTTATGGAGAAGCTT
ATCCGGACTCTTCCTATCTTCATCATTATGTCCCTGTGTCCCTTCGTTAACATTCCCTGT
GCAGCTGCCAGGGCCGTAATAAAGAACAGGAACACCACCTACATTGTCGTTGGTGCAGTA
CAGCCTAACGACATCTCCAACAAGATCTGTCTTGACCTCAATGTGAGCTGCATCTCCAAA
GAACTGGACTCGTACCTGGGGGAGGGAAGCTGTGGGATTCCATTTTACTGTGAAGAATTG
CTTAAAAACCTGGAACATCATGAGGTACTCGTTTTCCAACAAACGGAGTCTGAGGAAAAG
ACAAATAGGACCTGGAATAACCTGTTCAAGTATTCCATTAAGCTAACAGAGAAGTTAAAC
ATGGTTACTCTCCATAGTGATAAGGAAAGTGAAGAAGTCTGTCACCTCACAAGTGGCGTC
AGACTGAAAAACCTGTCACCTCCAACGTCATTAAAAGAAATCTCTCTGATCCAGCTGGAT
AGCATGAGACTTTCCCACCAAATGCTGGTGAGATGTGCTGCCATCATTGGCCTGACCTTC
ACCACTGAGTTGTTGTTTGAGATTCTCCCCTGTTGGAATATGAAGATGATGATCAAGACC
CTGGCAACCCTAGTGGAATCTAACATTTTTTATTGTTTCCGGAATGGCAAGGAGCTTCAA
AAGGCCCTGAAACAGAATGATCCCTCATTTGAGGTGCACTATCGTTCCTTGTCTCTGAAG
CCCAGTGAAGGGATGGATCACGGTGAAGAGGAACAGCTTCGTGAACTGGAGAATGAGGTG
ATCGAGTGCCACAGGATTCGATTCTGTAACCCTATGATGCAGAAAACAGCCTACGAGCTG
TGGCTCAAGGACCAGAGAAAAGCCATGCACTTGAAATGTGCCCGCTTTTTAGAAGAAGAT
GCCCACAGATGTGACCACTGCCGAGGCAGGGACTTCATTCCCTATCATCACTTCACAGTG
AATATTCGGCTCAACGCTTTAGACATGGATGCCATTAAAAAGATGGCTATGTCTCATGGA
TTTAAAACTGAAGAAAAGCTTATCTTGTCCAACTCAGAGATTCCTGAGACATCTGCATTT
TTTCCTGAAAATCGCAGTCCTGAAGAAATAAGAGAAAAGATCTTGAATTTCTTTGACCAC
GTTTTAACAAAAATGAAGACATCTGACGAAGACATTATCCCTCTGGAATCTTGCCAGTGT
GAAGAAATCCTAGAGATTGTCATCTTGCCTCTGGCCCACCATTTTCTGGCTTTGGGAGAA
AATGACAAAGCCTTATATTACTTCTTAGAAATTGCATCTGCTTATCTCATCTTTTGTGAT
AACTACATGGCATACATGTATTTGAATGAAGGACAGAAGTTGCTAAAAACTCTCAAGAAG
GACAAATCTTGGAGCCAGACATTTGAGTCTGCCACCTTTTACAGCCTCAAAGGTGAGGTC
TGTTTCAATATGGGCCAGATAGTGCTTGCCAAGAAAATGCTGAGGAAGGCACTGAAGCTC
CTCAACCGAATCTTTCCTTACAACTTAATCTCCTTGTTTCTCCATATCCATGTCGAGAAA
AACAGACACTTTCATTATGTGAATCGGCAGGCCCAAGAGAGCCCACCTCCAGGGAAGAAG
AGGCTGGCACAACTTTACCGGCAAACTGTCTGCCTTTCCTTGCTGTGGCGCATCTATAGC
TACAGTTATCTTTTTCACTGCAAGTATTATGCCCACCTGGCAGTTATGATGCAAATGAAT
ACTGCACTGGAAACTCAAAATTGTTTCCAGATCATTAAGGCTTACCTAGACTATTCGCTA
TACCACCACCTGGCTGGCTACAAAGGTGTGTGGTTCAAATATGAAGTCATGGCCATGGAG
CACATCTTCAACCTCCCCCTGAAAGGCGAGGGCATTGAAATCGTGGCATACGTGGCTGAG
ACACTGGTCTTCAACAAGCTCATAATGGGACACCTGGATTTGGCCATTGAGTTAGGCTCC
CGAGCCCTTCAGATGTGGGCACTGCTCCAGAATCCCAACCGACATTATCAGTCCCTCTGC
AGACTTAGCAGATGTCTCCTTCTGAACAGCAGATACCCGCAATTGATCCAGGTGCTGGGG
CGGCTGTGGGAGCTTTCTGTAACACAGGAACACATCTTCAGCAAGGCATTTTTCTATTTT
GTCTGCTTGGACATCCTGCTTTATTCTGGTTTTGTTTATAGAACATTTGAAGAATGTTTG
GAATTCATACACCAATACGAAAACAACAGAATCCTCAAGTTCCACAGTGGACTCCTCCTG
GGACTTTATTCCTCTGTAGCTATCTGGTATGCCAGACTTCAGGAATGGGACAACTTTTAC
AAATTTTCCAATAGAGCTAAAAATCTTTTGCCAAGAAGAACCATGACACTTACTTACTAT
GACGGAATATCTAGGTACATGGAGGGGCAAGTTCTTCACCTTCAAAAACAAATCAAAGAA
CAGTCAGAGAATGCCCAAGCCAGTGGGGAGGAGCTACTCAAGAACTTGGAGAATCTGGTG
GCTCAAAATACCACTGGCCCTGTCTTTTGCCCAAGGCTCTACCACCTGATGGCTTACGTC
TGTATATTAATGGGAGATGGGCAGAAATGTGGCCTCTTCCTGAACACAGCCTTGCGGCTC
TCTGAAACACAGGGGAATATACTGGAGAAATGCTGGCTGAACATGAACAAAGAATCATGG
TACTCAACCTCTGAGTTAAAAGAAGACCAATGGCTTCAGACGATCTTGAGTCTCCCATCA
TGGGAAAAAATTGTAGCAGGCAGGGTAAACATTCAGGATCTTCAAAAAAACAAATTCCTG
ATGAGAGCTAATACCGTGGACAATCATTTCTAA
Enzyme 75 GenBank Gene ID AF176813 Link Image
Enzyme 75 GeneCard ID ADCY10 Link Image
Enzyme 75 GenAtlas ID ADCY10 Link Image
Enzyme 75 HGNC ID HGNC:21285 Link Image
Enzyme 75 Chromosome Location 1
Enzyme 75 Locus 1q24
Enzyme 75 SNPs SNPJam Report Link Image
Enzyme 75 General References
  1. Jaiswal BS, Conti M: Identification and functional analysis of splice variants of the germ cell soluble adenylyl cyclase. J Biol Chem. 2001 Aug 24;276(34):31698-708. Epub 2001 Jun 21. [PubMed Link Image]
  2. Reed BY, Gitomer WL, Heller HJ, Hsu MC, Lemke M, Padalino P, Pak CY: Identification and characterization of a gene with base substitutions associated with the absorptive hypercalciuria phenotype and low spinal bone density. J Clin Endocrinol Metab. 2002 Apr;87(4):1476-85. [PubMed Link Image]
  3. Litvin TN, Kamenetsky M, Zarifyan A, Buck J, Levin LR: Kinetic properties of "soluble" adenylyl cyclase. Synergism between calcium and bicarbonate. J Biol Chem. 2003 May 2;278(18):15922-6. Epub 2003 Feb 27. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Zippin JH, Chen Y, Nahirney P, Kamenetsky M, Wuttke MS, Fischman DA, Levin LR, Buck J: Compartmentalization of bicarbonate-sensitive adenylyl cyclase in distinct signaling microdomains. FASEB J. 2003 Jan;17(1):82-4. Epub 2002 Nov 15. [PubMed Link Image]
  7. Geng W, Wang Z, Zhang J, Reed BY, Pak CY, Moe OW: Cloning and characterization of the human soluble adenylyl cyclase. Am J Physiol Cell Physiol. 2005 Jun;288(6):C1305-16. Epub 2005 Jan 19. [PubMed Link Image]
  8. Schmid A, Sutto Z, Nlend MC, Horvath G, Schmid N, Buck J, Levin LR, Conner GE, Fregien N, Salathe M: Soluble adenylyl cyclase is localized to cilia and contributes to ciliary beat frequency regulation via production of cAMP. J Gen Physiol. 2007 Jul;130(1):99-109. [PubMed Link Image]
  9. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
Enzyme 75 Metabolite References Not Available
Enzyme 76 [top]
Enzyme 76 ID 9969
Enzyme 76 Name Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A
Enzyme 76 Synonyms
  1. cAMP and cGMP phosphodiesterase 11A
Enzyme 76 Gene Name PDE11A
Enzyme 76 Protein Sequence >Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A
MAASRLDFGEVETFLDRHPELFEDYLMRKGKQEMVEKWLQRHSQGQGALGPRPSLAGTSS
LAHSTCRGGSSVGGGTGPNGSAHSQPLPGGGDCGGVPLSPSWAGGSRGDGNLQRRASQKE
LRKSFARSKAIHVNRTYDEQVTSRAQEPLSSVRRRALLRKASSLPPTTAHILSALLESRV
NLPRYPPTAIDYKCHLKKHNERQFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSL
FLVEGAAAGKKTLVSKFFDVHAGTPLLPCSSTENSNEVQVPWGKGIIGYVGEHGETVNIP
DAYQDRRFNDEIDKLTGYKTKSLLCMPIRSSDGEIIGVAQAINKIPEGAPFTEDDEKVMQ
MYLPFCGIAISNAQLFAASRKEYERSRALLEVVNDLFEEQTDLEKIVKKIMHRAQTLLKC
ERCSVLLLEDIESPVVKFTKSFELMSPKCSADAENSFKESMEKSSYSDWLINNSIAELVA
STGLPVNISDAYQDPRFDAEADQISGFHIRSVLCVPIWNSNHQIIGVAQVLNRLDGKPFD
DADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQSVALDVLSYHATCSKAEVDKFKAANI
PLVSELAIDDIHFDDFSLDVDAMITAALRMFMELGMVQKFKIDYETLCRWLLTVRKNYRM
VLYHNWRHAFNVCQLMFAMLTTAGFQDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSG
SALAQLYGTSATLEHHHFNHAVMILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLY
FERRTEFFELVSKGEYDWNIKNHRDIFRSMLMTACDLGAVTKPWEISRQVAELVTSEFFE
QGDRERLELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNVKLKPMLDSVAT
NRSKWEELHQKRLLASTASSSPASVMVAKEDRN
Enzyme 76 Number of Residues 933
Enzyme 76 Molecular Weight 104750.6
Enzyme 76 Theoretical pI 6.57
Enzyme 76 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 76 General Function Involved in catalytic activity
Enzyme 76 Specific Function Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'- GMP, respectively
Enzyme 76 Pathways
Enzyme 76 Reactions
  • guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]
Enzyme 76 Pfam Domain Function
Enzyme 76 Signals
  • None
Enzyme 76 Transmembrane Regions
  • None
Enzyme 76 Essentiality Not Available
Enzyme 76 GenBank ID Protein 116536085 Link Image
Enzyme 76 UniProtKB/Swiss-Prot ID Q9HCR9 Link Image
Enzyme 76 UniProtKB/Swiss-Prot Entry Name PDE11_HUMAN Link Image
Enzyme 76 PDB ID Not Available
Enzyme 76 Cellular Location Not Available
Enzyme 76 Gene Sequence >2802 bp
ATGGCAGCCTCCCGCCTGGACTTTGGGGAGGTGGAAACTTTCCTGGACAGGCACCCAGAG
TTGTTTGAAGATTACTTGATGCGGAAGGGGAAGCAGGAGATGGTTGAAAAGTGGCTGCAG
AGGCACAGTCAGGGTCAGGGGGCTTTAGGTCCAAGGCCCTCTTTGGCTGGTACCAGCAGC
TTGGCTCACAGCACCTGCAGAGGTGGCAGCAGCGTTGGTGGTGGCACTGGACCAAATGGC
TCTGCCCACAGCCAGCCCCTTCCCGGTGGCGGGGACTGTGGTGGGGTTCCCTTGAGTCCC
AGCTGGGCCGGTGGCAGCAGGGGCGATGGGAACCTGCAGCGGAGAGCTTCTCAGAAAGAG
CTAAGGAAGAGTTTTGCCCGCTCCAAGGCCATCCACGTGAACAGGACCTACGATGAACAG
GTGACCTCCCGGGCTCAGGAACCCCTGAGTAGTGTACGACGGAGGGCACTTCTCCGGAAG
GCAAGCTCCCTGCCCCCCACCACAGCCCATATTCTCAGTGCGCTGCTGGAATCGAGAGTG
AATCTGCCTCGGTATCCCCCTACAGCCATCGACTACAAGTGCCATCTGAAAAAGCATAAT
GAGCGTCAGTTCTTTCTGGAATTGGTCAAAGATATCTCCAATGACCTTGACCTCACCAGC
CTGAGCTACAAGATTCTCATCTTTGTCTGCCTTATGGTGGATGCTGACCGCTGCTCTCTT
TTCCTGGTGGAAGGGGCAGCTGCTGGCAAGAAGACCTTGGTCTCCAAATTCTTTGATGTG
CATGCAGGAACACCTCTGCTGCCTTGCAGCAGCACAGAGAACTCAAATGAGGTGCAGGTC
CCCTGGGGCAAAGGTATCATTGGCTATGTCGGGGAGCATGGAGAAACGGTCAACATTCCT
GATGCCTACCAGGATCGACGATTCAATGATGAAATCGACAAGCTAACTGGATACAAGACA
AAATCATTATTGTGCATGCCTATCCGAAGCAGTGATGGTGAGATTATTGGTGTGGCCCAA
GCGATAAATAAGATTCCTGAAGGAGCTCCATTTACTGAAGATGATGAAAAAGTTATGCAG
ATGTATCTTCCATTTTGTGGAATCGCCATATCTAACGCTCAGCTCTTTGCTGCCTCAAGG
AAAGAATATGAAAGAAGCAGAGCTTTGCTAGAGGTGGTTAATGACCTCTTTGAAGAACAG
ACTGACCTGGAGAAAATTGTCAAGAAAATAATGCATCGGGCCCAAACTCTGCTGAAATGT
GAACGCTGTTCTGTTTTACTCCTAGAGGACATCGAATCACCAGTGGTGAAATTTACCAAA
TCCTTTGAATTGATGTCCCCAAAGTGCAGTGCTGATGCTGAGAACAGTTTCAAAGAAAGC
ATGGAGAAATCATCATACTCCGACTGGCTAATAAATAACAGCATTGCTGAGCTGGTTGCT
TCAACAGGCCTTCCAGTGAACATCAGTGATGCCTACCAGGATCCGCGCTTTGATGCAGAG
GCAGACCAGATATCTGGTTTTCACATAAGATCTGTTCTTTGTGTCCCTATTTGGAATAGC
AACCACCAAATAATTGGAGTGGCTCAAGTGTTAAACAGACTTGATGGGAAACCTTTTGAT
GATGCAGATCAACGACTTTTTGAGGCTTTTGTCATCTTTTGTGGACTTGGCATCAACAAC
ACAATTATGTATGATCAAGTGAAGAAGTCCTGGGCCAAGCAGTCTGTGGCTCTTGATGTG
CTATCATACCATGCAACATGTTCAAAAGCTGAAGTTGACAAGTTTAAGGCAGCCAACATC
CCTCTGGTGTCAGAACTTGCCATCGATGACATTCATTTTGATGACTTTTCTCTCGACGTT
GATGCCATGATCACAGCTGCTCTCCGGATGTTCATGGAGCTGGGGATGGTACAGAAATTT
AAAATTGACTATGAGACACTGTGTAGGTGGCTTTTGACAGTGAGGAAAAACTATCGGATG
GTTCTATACCACAACTGGAGACATGCCTTCAACGTGTGTCAGCTGATGTTCGCGATGTTA
ACCACTGCTGGGTTTCAAGACATTCTGACCGAGGTGGAAATTTTAGCGGTGATTGTGGGA
TGCCTGTGTCATGACCTCGACCACAGGGGAACCAACAATGCCTTCCAAGCTAAGAGTGGC
TCTGCCCTGGCCCAACTCTATGGAACCTCTGCTACCTTGGAGCATCACCATTTCAACCAC
GCCGTGATGATCCTTCAAAGTGAGGGTCACAATATCTTTGCTAACCTGTCCTCCAAGGAA
TATAGTGACCTTATGCAGCTTTTGAAGCAGTCAATATTGGCAACAGACCTCACGCTGTAC
TTTGAGAGGAGAACTGAATTCTTTGAACTTGTCAGTAAAGGAGAATACGATTGGAACATC
AAAAACCATCGTGATATATTTCGATCAATGTTAATGACAGCCTGTGACCTTGGAGCCGTG
ACCAAACCGTGGGAGATCTCCAGACAGGTGGCAGAACTTGTAACCAGTGAGTTCTTCGAA
CAAGGAGATCGGGAGAGATTAGAGCTCAAACTCACTCCTTCAGCAATTTTTGATCGGAAC
CGGAAGGATGAACTGCCTCGGTTGCAACTGGAGTGGATTGATAGCATCTGCATGCCTTTG
TATCAGGCACTGGTGAAGGTCAACGTGAAACTGAAGCCGATGCTAGATTCAGTAGCTACA
AACAGAAGTAAGTGGGAAGAGCTACACCAAAAACGACTGCTGGCCTCAACTGCCTCATCC
TCCCCTGCCAGTGTTATGGTAGCCAAGGAAGACAGGAACTAA
Enzyme 76 GenBank Gene ID NM_016953.3 Link Image
Enzyme 76 GeneCard ID PDE11A Link Image
Enzyme 76 GenAtlas ID PDE11A Link Image
Enzyme 76 HGNC ID HGNC:8773 Link Image
Enzyme 76 Chromosome Location 2
Enzyme 76 Locus 2q31.2
Enzyme 76 SNPs SNPJam Report Link Image
Enzyme 76 General References
  1. Yuasa K, Kotera J, Fujishige K, Michibata H, Sasaki T, Omori K: Isolation and characterization of two novel phosphodiesterase PDE11A variants showing unique structure and tissue-specific expression. J Biol Chem. 2000 Oct 6;275(40):31469-79. [PubMed Link Image]
  2. Fawcett L, Baxendale R, Stacey P, McGrouther C, Harrow I, Soderling S, Hetman J, Beavo JA, Phillips SC: Molecular cloning and characterization of a distinct human phosphodiesterase gene family: PDE11A. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3702-7. [PubMed Link Image]
  3. Hetman JM, Robas N, Baxendale R, Fidock M, Phillips SC, Soderling SH, Beavo JA: Cloning and characterization of two splice variants of human phosphodiesterase 11A. Proc Natl Acad Sci U S A. 2000 Nov 7;97(23):12891-5. [PubMed Link Image]
  4. Yuasa K, Kanoh Y, Okumura K, Omori K: Genomic organization of the human phosphodiesterase PDE11A gene. Evolutionary relatedness with other PDEs containing GAF domains. Eur J Biochem. 2001 Jan;268(1):168-78. [PubMed Link Image]
  5. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Loughney K, Taylor J, Florio VA: 3',5'-cyclic nucleotide phosphodiesterase 11A: localization in human tissues. Int J Impot Res. 2005 Jul-Aug;17(4):320-5. [PubMed Link Image]
  8. Francis SH: Phosphodiesterase 11 (PDE11): is it a player in human testicular function? Int J Impot Res. 2005 Sep-Oct;17(5):467-8. [PubMed Link Image]
  9. Gross-Langenhoff M, Hofbauer K, Weber J, Schultz A, Schultz JE: cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10 and cGMP for the tandem GAF domain of phosphodiesterase 11. J Biol Chem. 2006 Feb 3;281(5):2841-6. Epub 2005 Dec 5. [PubMed Link Image]
  10. Horvath A, Boikos S, Giatzakis C, Robinson-White A, Groussin L, Griffin KJ, Stein E, Levine E, Delimpasi G, Hsiao HP, Keil M, Heyerdahl S, Matyakhina L, Libe R, Fratticci A, Kirschner LS, Cramer K, Gaillard RC, Bertagna X, Carney JA, Bertherat J, Bossis I, Stratakis CA: A genome-wide scan identifies mutations in the gene encoding phosphodiesterase 11A4 (PDE11A) in individuals with adrenocortical hyperplasia. Nat Genet. 2006 Jul;38(7):794-800. Epub 2006 Jun 11. [PubMed Link Image]
Enzyme 76 Metabolite References Not Available
Enzyme 77 [top]
Enzyme 77 ID 10050
Enzyme 77 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
Enzyme 77 Synonyms
  1. Phosphoinositide phospholipase C-delta-3
  2. Phospholipase C-delta-3
  3. PLC-delta-3
Enzyme 77 Gene Name PLCD3
Enzyme 77 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
MLCGRWRRCRRPPEEPPVAAQVAAQVAAPVALPSPPTPSDGGTKRPGLRALKKMGLTEDE
DVRAMLRGSRLRKIRSRTWHKERLYRLQEDGLSVWFQRRIPRAPSQHIFFVQHIEAVREG
HQSEGLRRFGGAFAPARCLTIAFKGRRKNLDLAAPTAEEAQRWVRGLTKLRARLDAMSQR
ERLDHWIHSYLHRADSNQDSKMSFKEIKSLLRMVNVDMNDMYAYLLFKECDHSNNDRLEG
AEIEEFLRRLLKRPELEEIFHQYSGEDRVLSAPELLEFLEDQGEEGATLARAQQLIQTYE
LNETAKQHELMTLDGFMMYLLSPEGAALDNTHTCVFQDMNQPLAHYFISSSHNTYLTDSQ
IGGPSSTEAYVRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVVQAVRDHAFT
LSPYPVILSLENHCGLEQQAAMARHLCTILGDMLVTQALDSPNPEELPSPEQLKGRVLVK
GKKLPAARSEDGRALSDREEEEEDDEEEEEEVEAAAQRRLAKQISPELSALAVYCHATRL
RTLHPAPNAPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQ
EMWNSGCQLVALNFQTPGYEMDLNAGRFLVNGQCGYVLKPACLRQPDSTFDPEYPGPPRT
TLSIQVLTAQQLPKLNAEKPHSIVDPLVRIEIHGVPADCARQETDYVLNNGFNPRWGQTL
QFQLRAPELALVRFVVEDYDATSPNDFVGQFTLPLSSLKQGYRHIHLLSKDGASLSPATL
FIQIRIQRS
Enzyme 77 Number of Residues 789
Enzyme 77 Molecular Weight 89257.5
Enzyme 77 Theoretical pI 6.97
Enzyme 77 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 77 General Function Involved in calcium ion binding
Enzyme 77 Specific Function Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow
Enzyme 77 Pathways
Enzyme 77 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 77 Pfam Domain Function
Enzyme 77 Signals
  • None
Enzyme 77 Transmembrane Regions
  • None
Enzyme 77 Essentiality Not Available
Enzyme 77 GenBank ID Protein Not Available
Enzyme 77 UniProtKB/Swiss-Prot ID Q8N3E9 Link Image
Enzyme 77 UniProtKB/Swiss-Prot Entry Name PLCD3_HUMAN Link Image
Enzyme 77 PDB ID Not Available
Enzyme 77 Cellular Location Not Available
Enzyme 77 Gene Sequence >2370 bp
ATGCTGTGCGGCCGCTGGAGGCGTTGCCGCCGCCCGCCCGAGGAGCCCCCGGTGGCCGCC
CAGGTCGCAGCCCAAGTCGCGGCGCCGGTCGCTCTCCCGTCCCCGCCGACTCCCTCCGAT
GGCGGCACCAAGAGGCCCGGGCTGCGGGCGCTGAAGAAGATGGGCCTGACGGAGGACGAG
GACGTGCGCGCCATGCTGCGGGGCTCCCGGCTCCGCAAGATCCGCTCGCGCACGTGGCAC
AAGGAGCGGCTGTACCGGCTGCAGGAGGACGGCCTGAGCGTGTGGTTCCAGCGGCGCATC
CCGCGTGCGCCATCGCAGCACATCTTCTTCGTGCAGCACATCGAGGCGGTCCGCGAGGGC
CACCAGTCCGAGGGCCTGCGGCGCTTCGGGGGTGCCTTCGCGCCAGCGCGCTGCCTCACC
ATCGCCTTCAAGGGCCGCCGCAAGAACCTGGACCTGGCGGCGCCCACGGCTGAGGAAGCG
CAGCGCTGGGTGCGCGGTCTGACCAAGCTCCGCGCGCGCCTGGACGCCATGAGCCAGCGC
GAGCGGCTAGACCACTGGATCCACTCCTATCTGCACCGGGCTGACTCCAACCAGGACAGC
AAGATGAGCTTCAAGGAGATCAAGAGCCTGCTGAGAATGGTCAACGTGGACATGAACGAC
ATGTACGCCTACCTCCTCTTCAAGGAGTGTGACCACTCCAACAACGACCGTCTAGAGGGG
GCTGAGATCGAGGAGTTCCTGCGGCGGCTGCTGAAGCGGCCGGAGCTGGAGGAGATCTTC
CATCAGTACTCGGGCGAGGACCGCGTGCTGAGTGCCCCTGAGCTGCTGGAGTTCCTGGAG
GACCAGGGCGAGGAGGGCGCCACACTGGCCCGCGCCCAGCAGCTCATTCAGACCTATGAG
CTCAACGAGACAGCCAAGCAGCATGAGCTGATGACACTGGATGGCTTCATGATGTACCTG
TTGTCGCCGGAGGGGGCTGCCTTGGACAACACCCACACGTGTGTGTTCCAGGACATGAAC
CAGCCCCTTGCCCACTACTTCATCTCTTCCTCCCACAACACCTATCTGACTGACTCCCAG
ATCGGGGGGCCCAGCAGCACCGAGGCCTATGTTAGGGCCTTTGCCCAGGGATGCCGCTGC
GTGGAGCTGGACTGCTGGGAGGGGCCAGGAGGGGAGCCCGTCATCTATCATGGCCATACC
CTCACCTCCAAGATTCTCTTCCGGGACGTGGTCCAAGCCGTGCGCGACCATGCCTTCACG
CTGTCCCCTTACCCTGTCATCCTATCCCTGGAGAACCACTGCGGGCTGGAGCAGCAGGCT
GCCATGGCCCGCCACCTCTGCACCATCCTGGGGGACATGCTGGTGACACAGGCGCTGGAC
TCCCCAAATCCCGAGGAGCTGCCATCCCCAGAGCAGCTGAAGGGCCGGGTCCTGGTGAAG
GGAAAGAAGTTGCCCGCTGCTCGGAGCGAGGATGGCCGGGCTCTGTCGGATCGGGAGGAG
GAGGAGGAGGATGACGAGGAGGAAGAAGAGGAGGTGGAGGCTGCAGCGCAGAGGCGGCTG
GCCAAGCAGATCTCCCCGGAGCTGTCGGCCCTGGCTGTGTACTGCCACGCCACCCGCCTG
CGGACCCTGCACCCTGCCCCCAACGCCCCACAACCCTGCCAGGTCAGCTCCCTCAGCGAG
CGCAAAGCCAAGAAACTCATTCGGGAGGCAGGGAACAGCTTTGTCAGGCACAATGCCCGC
CAGCTGACCCGCGTGTACCCGCTGGGGCTGCGGATGAACTCAGCCAACTACAGTCCCCAG
GAGATGTGGAACTCGGGCTGTCAGCTGGTGGCCTTGAACTTCCAGACGCCAGGCTACGAG
ATGGACCTCAATGCCGGGCGCTTCCTAGTCAATGGGCAGTGTGGCTACGTCCTAAAACCT
GCCTGCCTGCGGCAACCTGACTCGACCTTTGACCCCGAGTACCCAGGACCTCCCAGAACC
ACTCTCAGCATCCAGGTGCTGACTGCACAGCAGCTGCCCAAGCTGAATGCCGAGAAGCCA
CACTCCATTGTGGACCCCCTGGTGCGCATTGAGATCCATGGGGTGCCCGCAGACTGTGCC
CGGCAGGAGACTGACTACGTGCTCAACAATGGCTTCAACCCCCGCTGGGGGCAGACCCTG
CAGTTCCAGCTGCGGGCTCCGGAGCTGGCACTGGTCCGGTTTGTGGTGGAAGATTATGAC
GCCACCTCCCCCAATGACTTTGTGGGCCAGTTTACACTGCCTCTTAGCAGCCTAAAGCAA
GGGTACCGCCACATACACCTGCTTTCCAAGGACGGGGCCTCACTGTCACCAGCCACGCTC
TTCATCCAAATCCGCATCCAGCGCTCCTGA
Enzyme 77 GenBank Gene ID AK074240 Link Image
Enzyme 77 GeneCard ID PLCD3 Link Image
Enzyme 77 GenAtlas ID PLCD3 Link Image
Enzyme 77 HGNC ID HGNC:9061 Link Image
Enzyme 77 Chromosome Location 1
Enzyme 77 Locus 17q21.31
Enzyme 77 SNPs SNPJam Report Link Image
Enzyme 77 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed Link Image]
  5. Pawelczyk T, Matecki A: Expression, purification and kinetic properties of human recombinant phospholipase C delta 3. Acta Biochim Pol. 1997;44(2):221-9. [PubMed Link Image]
  6. Ghosh S, Pawelczyk T, Lowenstein JM: Phospholipase C isoforms delta 1 and delta 3 from human fibroblasts. High-yield expression in Escherichia coli, simple purification, and properties. Protein Expr Purif. 1997 Mar;9(2):262-78. [PubMed Link Image]
  7. Pawelczyk T, Matecki A: Localization of phospholipase C delta3 in the cell and regulation of its activity by phospholipids and calcium. Eur J Biochem. 1998 Oct 1;257(1):169-77. [PubMed Link Image]
  8. Kim H, Suh PG, Ryu SH, Park SH: Assignment of the human PLC delta3 gene (PLCD3) to human chromosome band 17q21 by fluorescence in situ hybridization. Cytogenet Cell Genet. 1999;87(3-4):209-10. [PubMed Link Image]
  9. Pawelczyk T, Matecki A: Phospholipase C-delta3 binds with high specificity to phosphatidylinositol 4,5-bisphosphate and phosphatidic acid in bilayer membranes. Eur J Biochem. 1999 Jun;262(2):291-8. [PubMed Link Image]
  10. Lin FG, Cheng HF, Lee IF, Kao HJ, Loh SH, Lee WH: Downregulation of phospholipase C delta3 by cAMP and calcium. Biochem Biophys Res Commun. 2001 Aug 17;286(2):274-80. [PubMed Link Image]
  11. Ananthanarayanan B, Das S, Rhee SG, Murray D, Cho W: Membrane targeting of C2 domains of phospholipase C-delta isoforms. J Biol Chem. 2002 Feb 1;277(5):3568-75. Epub 2001 Nov 12. [PubMed Link Image]
  12. Landreville S, Coulombe S, Carrier P, Gelb MH, Guerin SL, Salesse C: Expression of phospholipases A2 and C in human corneal epithelial cells. Invest Ophthalmol Vis Sci. 2004 Nov;45(11):3997-4003. [PubMed Link Image]
  13. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  14. Naito Y, Okada M, Yagisawa H: Phospholipase C isoforms are localized at the cleavage furrow during cytokinesis. J Biochem. 2006 Dec;140(6):785-91. Epub 2006 Oct 14. [PubMed Link Image]
  15. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 77 Metabolite References Not Available
Enzyme 78 [top]
Enzyme 78 ID 12938
Enzyme 78 Name Lysophosphatidic acid receptor 6
Enzyme 78 Synonyms
  1. LPA receptor 6
  2. LPA-6
  3. Oleoyl-L-alpha-lysophosphatidic acid receptor
  4. P2Y purinoceptor 5
  5. P2Y5
  6. Purinergic receptor 5
  7. RB intron encoded G-protein coupled receptor
Enzyme 78 Gene Name LPAR6
Enzyme 78 Protein Sequence >Lysophosphatidic acid receptor 6
MVSVNSSHCFYNDSFKYTLYGCMFSMVFVLGLISNCVAIYIFICVLKVRNETTTYMINLA
MSDLLFVFTLPFRIFYFTTRNWPFGDLLCKISVMLFYTNMYGSILFLTCISVDRFLAIVY
PFKSKTLRTKRNAKIVCTGVWLTVIGGSAPAVFVQSTHSQGNNASEACFENFPEATWKTY
LSRIVIFIEIVGFFIPLILNVTCSSMVLKTLTKPVTLSRSKINKTKVLKMIFVHLIIFCF
CFVPYNINLILYSLVRTQTFVNCSVVAAVRTMYPITLCIAVSNCCFDPIVYYFTSDTIQN
SIKMKNWSVRRSDFRFSEVHGAENFIQHNLQTLKSKIFDNESAA
Enzyme 78 Number of Residues 344
Enzyme 78 Molecular Weight 39391.2
Enzyme 78 Theoretical pI 9.16
Enzyme 78 GO Classification
Function
  • G-protein coupled receptor activity
  • molecular transducer activity
  • nucleotide receptor activity, G-protein coupled
  • purinergic nucleotide receptor activity, G-protein coupled
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 78 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 78 Specific Function Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA). Intracellular cAMP is involved in the receptor activation. Important for the maintenance of hair growth and texture
Enzyme 78 Pathways Not Available
Enzyme 78 Reactions Not Available
Enzyme 78 Pfam Domain Function
Enzyme 78 Signals
  • None
Enzyme 78 Transmembrane Regions
  • 20-46 56-79 93-112 134-154 182-209 228-253 273-292
Enzyme 78 Essentiality Not Available
Enzyme 78 GenBank ID Protein 2232069 Link Image
Enzyme 78 UniProtKB/Swiss-Prot ID P43657 Link Image
Enzyme 78 UniProtKB/Swiss-Prot Entry Name LPAR6_HUMAN Link Image
Enzyme 78 PDB ID Not Available
Enzyme 78 Cellular Location Not Available
Enzyme 78 Gene Sequence >1035 bp
ATGGTAAGCGTTAACAGCTCCCACTGCTTCTATAATGACTCCTTTAAGTACACTTTGTAT
GGGTGCATGTTCAGCATGGTGTTTGTGCTTGGGTTAGTATCCAATTGTGTTGCCATATAC
ATTTTCATCTGCGTCCTCAAAGTCCGAAATGAAACTACAACTTACATGATTAACTTGGCA
ATGTCAGACTTGCTTTTTGTTTTTACTTTACCCTTCAGGATTTTTTACTTCACAACACGG
AATTGGCCATTTGGAGATTTACTTTGTAAGATTTCTGTGATGCTGTTTTATACCAACATG
TACGGAAGCATTCTGTTCTTAACCTGTATTAGTGTAGATCGATTTCTGGCAATTGTCTAC
CCATTTAAGTCAAAGACTCTAAGAACCAAAAGAAATGCAAAGATTGTTTGCACTGGCGTG
TGGTTAACTGTGATCGGAGGAAGTGCACCCGCCGTTTTTGTTCAGTCTACCCACTCTCAG
GGTAACAATGCCTCAGAAGCCTGCTTTGAAAATTTTCCAGAAGCCACATGGAAAACATAT
CTCTCAAGGATTGTAATTTTCATCGAAATAGTGGGATTTTTTATTCCTCTAATTTTAAAT
GTAACTTGTTCTAGTATGGTGCTAAAAACTTTAACCAAACCAGTTACATTAAGTAGAAGC
AAAATAAACAAAACTAAGGTTTTAAAAATGATTTTTGTACATTTGATCATATTCTGTTTC
TGTTTTGTTCCTTACAATATCAATCTTATTTTATATTCTCTTGTGAGAACACAAACATTT
GTTAATTGCTCAGTAGTGGCAGCAGTAAGGACAATGTACCCAATCACTCTCTGTATTGCT
GTTTCCAACTGTTGTTTTGACCCTATAGTTTACTACTTTACATCGGACACAATTCAGAAT
TCAATAAAAATGAAAAACTGGTCTGTCAGGAGAAGTGACTTCAGATTCTCTGAAGTTCAT
GGTGCAGAGAATTTTATTCAGCATAACCTACAGACCTTAAAAAGTAAGATATTTGACAAT
GAATCTGCTGCCTGA
Enzyme 78 GenBank Gene ID AF000546 Link Image
Enzyme 78 GeneCard ID LPAR6 Link Image
Enzyme 78 GenAtlas ID LPAR6 Link Image
Enzyme 78 HGNC ID HGNC:15520 Link Image
Enzyme 78 Chromosome Location 1
Enzyme 78 Locus 13q14
Enzyme 78 SNPs SNPJam Report Link Image
Enzyme 78 General References
  1. Toguchida J, McGee TL, Paterson JC, Eagle JR, Tucker S, Yandell DW, Dryja TP: Complete genomic sequence of the human retinoblastoma susceptibility gene. Genomics. 1993 Sep;17(3):535-43. [PubMed Link Image]
  2. Herzog H, Darby K, Hort YJ, Shine J: Intron 17 of the human retinoblastoma susceptibility gene encodes an actively transcribed G protein-coupled receptor gene. Genome Res. 1996 Sep;6(9):858-61. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Adrian K, Bernhard MK, Breitinger HG, Ogilvie A: Expression of purinergic receptors (ionotropic P2X1-7 and metabotropic P2Y1-11) during myeloid differentiation of HL60 cells. Biochim Biophys Acta. 2000 Jun 21;1492(1):127-38. [PubMed Link Image]
  8. Pasternack SM, von Kugelgen I, Aboud KA, Lee YA, Ruschendorf F, Voss K, Hillmer AM, Molderings GJ, Franz T, Ramirez A, Nurnberg P, Nothen MM, Betz RC: G protein-coupled receptor P2Y5 and its ligand LPA are involved in maintenance of human hair growth. Nat Genet. 2008 Mar;40(3):329-34. Epub 2008 Feb 24. [PubMed Link Image]
  9. Shimomura Y, Wajid M, Ishii Y, Shapiro L, Petukhova L, Gordon D, Christiano AM: Disruption of P2RY5, an orphan G protein-coupled receptor, underlies autosomal recessive woolly hair. Nat Genet. 2008 Mar;40(3):335-9. Epub 2008 Feb 24. [PubMed Link Image]
Enzyme 78 Metabolite References Not Available
Enzyme 79 [top]
Enzyme 79 ID 13091
Enzyme 79 Name Adenylate cyclase 1
Enzyme 79 Synonyms
  1. Brain
Enzyme 79 Gene Name ADCY1
Enzyme 79 Protein Sequence >Adenylate cyclase 1
MAGAPRGGGGGGGGAGEPGGAERAAGTSRRRGLRACDEEFACPELEALFRGYTLRLEQAA
TLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCVLFLALLVVTNVRSLQVPQLQ
QVGQLALLFSLTFALLCCPFALGGPARGSAGAAGGPATAEQGVWQLLLVTFVSYALLPVR
SLLAIGFGLVVAASHLLVTATLVPAKRPRLWRTLGANALLFVGVNMYGVFVRILTERSQR
KAFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHD
NVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGL
TQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWS
NDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGYGHERNSFLKTHNIETFFIVPSH
RRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALR
TASEKLRNRSSFSTNVVYTTPGTRVNRYISRLLEARQTELEMADLNFFTLKYKHVEREQK
YHQLQDEYFTSAVVLTLILAALFGLVYLLIFPQSVVVLLLLVFCICFLVACVLYLHITRV
QCFPGCLTIQIRTVLCIFIVVLIYSVAQGCVVGCLPWAWSSKPNSSLVVLSSGGQRTALP
TLPCESTHHALLCCLVGTLPLAIFFRVSSLPKMILLSGLTTSYILVLELSGYTRTGGGAV
SGRSYEPIVAILLFSCALALHARQVDIRLRLDYLWAAQAEEEREDMEKVKLDNRRILFNL
LPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEI
IADFDELMEKDFYKDIEKIKTIGSTYMAAVGLAPTSGTKAKKSISSHLSTLADFAIEMFD
VLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQV
TEEVHRLLRRCPYHFVCRGKVSVKGKGEMLTYFLEGRTDGNGSQIRSLGLDRKMCPFGRA
GLQGRRPPVCPMPGVSVRAGLPPHSPGQYLPSAAAGKEA
Enzyme 79 Number of Residues 1119
Enzyme 79 Molecular Weight 123442
Enzyme 79 Theoretical pI 8.49
Enzyme 79 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
Enzyme 79 General Function Signal transduction mechanisms
Enzyme 79 Specific Function Not Available
Enzyme 79 Pathways Not Available
Enzyme 79 Reactions Not Available
Enzyme 79 Pfam Domain Function
Enzyme 79 Signals
  • None
Enzyme 79 Transmembrane Regions
  • None
Enzyme 79 Essentiality Not Available
Enzyme 79 GenBank ID Protein Not Available
Enzyme 79 UniProtKB/Swiss-Prot ID A4D2L8 Link Image
Enzyme 79 UniProtKB/Swiss-Prot Entry Name A4D2L8_HUMAN Link Image
Enzyme 79 PDB ID Not Available
Enzyme 79 Cellular Location Not Available
Enzyme 79 Gene Sequence Not Available
Enzyme 79 GenBank Gene ID CH236960 Link Image
Enzyme 79 GeneCard ID A4D2L8 Link Image
Enzyme 79 GenAtlas ID Not Available
Enzyme 79 HGNC ID Not Available
Enzyme 79 Chromosome Location Not Available
Enzyme 79 Locus Not Available
Enzyme 79 SNPs SNPJam Report Link Image
Enzyme 79 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 79 Metabolite References Not Available
Enzyme 80 [top]
Enzyme 80 ID 13144
Enzyme 80 Name A-kinase anchor protein 7 isoforms alpha and beta
Enzyme 80 Synonyms
  1. AKAP-7 isoforms alpha and beta
  2. A-kinase anchor protein 18 kDa
  3. AKAP 18
  4. Protein kinase A-anchoring protein 7 isoforms alpha/beta
Enzyme 80 Gene Name AKAP7
Enzyme 80 Protein Sequence >A-kinase anchor protein 7 isoforms alpha and beta
MGQLCCFPFSRDEGKISELESSSSAVLQRYSKDIPSWSSGEKNGGEPDDAELVRLSKRLV
ENAVLKAVQQYLEETQNKNKPGEGSSVKTEAADQNGNDNENNRK
Enzyme 80 Number of Residues 104
Enzyme 80 Molecular Weight 11464.4
Enzyme 80 Theoretical pI 4.60
Enzyme 80 GO Classification Not Available
Enzyme 80 General Function Involved in protein kinase A binding
Enzyme 80 Specific Function Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel
Enzyme 80 Pathways Not Available
Enzyme 80 Reactions Not Available
Enzyme 80 Pfam Domain Function
Enzyme 80 Signals
  • None
Enzyme 80 Transmembrane Regions
  • None
Enzyme 80 Essentiality Not Available
Enzyme 80 GenBank ID Protein 20336196 Link Image
Enzyme 80 UniProtKB/Swiss-Prot ID O43687 Link Image
Enzyme 80 UniProtKB/Swiss-Prot Entry Name AKA7A_HUMAN Link Image
Enzyme 80 PDB ID Not Available
Enzyme 80 Cellular Location Not Available
Enzyme 80 Gene Sequence >315 bp
ATGGGCCAGCTTTGCTGCTTTCCTTTCTCAAGAGATGAAGGAAAAATCAGTGAGTTGGAA
AGCTCGTCCTCTGCAGTCCTACAGAGATACAGCAAGGATATACCCAGTTGGTCAAGTGGT
GAAAAGAACGGAGGGGAGCCCGATGACGCTGAACTAGTAAGGCTCAGTAAGAGGCTGGTG
GAGAACGCGGTGCTCAAGGCTGTCCAGCAGTATCTGGAGGAAACACAGAATAAAAACAAG
CCGGGGGAGGGGAGCTCTGTGAAAACCGAAGCAGCTGATCAGAATGGCAATGACAATGAG
AACAACAGGAAATGA
Enzyme 80 GenBank Gene ID NM_138633.1 Link Image
Enzyme 80 GeneCard ID AKAP7 Link Image
Enzyme 80 GenAtlas ID Not Available
Enzyme 80 HGNC ID Not Available
Enzyme 80 Chromosome Location 6
Enzyme 80 Locus 6q23
Enzyme 80 SNPs SNPJam Report Link Image
Enzyme 80 General References
  1. Fraser ID, Tavalin SJ, Lester LB, Langeberg LK, Westphal AM, Dean RA, Marrion NV, Scott JD: A novel lipid-anchored A-kinase Anchoring Protein facilitates cAMP-responsive membrane events. EMBO J. 1998 Apr 15;17(8):2261-72. [PubMed Link Image]
  2. Trotter KW, Fraser ID, Scott GK, Stutts MJ, Scott JD, Milgram SL: Alternative splicing regulates the subcellular localization of A-kinase anchoring protein 18 isoforms. J Cell Biol. 1999 Dec 27;147(7):1481-92. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 80 Metabolite References Not Available
Enzyme 81 [top]
Enzyme 81 ID 13145
Enzyme 81 Name A-kinase anchor protein 13
Enzyme 81 Synonyms
  1. AKAP-13
  2. AKAP-Lbc
  3. Breast cancer nuclear receptor-binding auxiliary protein
  4. Guanine nucleotide exchange factor Lbc
  5. Human thyroid-anchoring protein 31
  6. Lymphoid blast crisis oncogene
  7. LBC oncogene
  8. Non-oncogenic Rho GTPase-specific GTP exchange factor
  9. Protein kinase A-anchoring protein 13
  10. p47
Enzyme 81 Gene Name AKAP13
Enzyme 81 Protein Sequence >A-kinase anchor protein 13
MKLNPQQAPLYGDCVVTVLLAEEDKAEDDVVFYLVFLGSTLRHCTSTRKVSSDTLETIAP
GHDCCETVKVQLCASKEGLPVFVVAEEDFHFVQDEAYDAAQFLATSAGNQQALNFTRFLD
QSGPPSGDVNSLDKKLVLAFRHLKLPTEWNVLGTDQSLHDAGPRETLMHFAVRLGLLRLT
WFLLQKPGGRGALSIHNQEGATPVSLALERGYHKLHQLLTEENAGEPDSWSSLSYEIPYG
DCSVRHHRELDIYTLTSESDSHHEHPFPGDGCTGPIFKLMNIQQQLMKTNLKQMDSLMPL
MMTAQDPSSAPETDGQFLPCAPEPTDPQRLSSSEETESTQCCPGSPVAQTESPCDLSSIV
EEENTDRSCRKKNKGVERKGEEVEPAPIVDSGTVSDQDSCLQSLPDCGVKGTEGLSSCGN
RNEETGTKSSGMPTDQESLSSGDAVLQRDLVMEPGTAQYSSGGELGGISTTNVSTPDTAG
EMEHGLMNPDATVWKNVLQGGESTKERFENSNIGTAGASDVHVTSKPVDKISVPNCAPAA
SSLDGNKPAESSLAFSNEETSTEKTAETETSRSREESADAPVDQNSVVIPAAAKDKISDG
LEPYTLLAAGIGEAMSPSDLALLGLEEDVMPHQNSETNSSHAQSQKGKSSPICSTTGDDK
LCADSACQQNTVTSSGDLVAKLCDNIVSESESTTARQPSSQDPPDASHCEDPQAHTVTSD
PVRDTQERADFCPFKVVDNKGQRKDVKLDKPLTNMLEVVSHPHPVVPKMEKELVPDQAVI
SDSTFSLANSPGSESVTKDDALSFVPSQKEKGTATPELHTATDYRDGPDGNSNEPDTRPL
EDRAVGLSTSSTAAELQHGMGNTSLTGLGGEHEGPAPPAIPEALNIKGNTDSSLQSVGKA
TLALDSVLTEEGKLLVVSESSAAQEQDKDKAVTCSSIKENALSSGTLQEEQRTPPPGQDT
QQFHEKSISADCAKDKALQLSNSPGASSAFLKAETEHNKEVAPQVSLLTQGGAAQSLVPP
GASLATESRQEALGAEHNSSALLPCLLPDGSDGSDALNCSQPSPLDVGVKNTQSQGKTSA
CEVSGDVTVDVTGVNALQGMAEPRRENISHNTQDILIPNVLLSQEKNAVLGLPVALQDKA
VTDPQGVGTPEMIPLDWEKGKLEGADHSCTMGDAEEAQIDDEAHPVLLQPVAKELPTDME
LSAHDDGAPAGVREVMRAPPSGRERSTPSLPCMVSAQDAPLPKGADLIEEAASRIVDAVI
EQVKAAGALLTEGEACHMSLSSPELGPLTKGLESAFTEKVSTFPPGESLPMGSTPEEATG
SLAGCFAGREEPEKIILPVQGPEPAAEMPDVKAEDEVDFRASSISEEVAVGSIAATLKMK
QGPMTQAINRENWCTIEPCPDAASLLASKQSPECENFLDVGLGRECTSKQGVLKRESGSD
SDLFHSPSDDMDSIIFPKPEEEHLACDITGSSSSTDDTASLDRHSSHGSDVSLSQILKPN
RSRDRQSLDGFYSHGMGAEGRESESEPADPGDVEEEEMDSITEVPANCSVLRSSMRSLSP
FRRHSWGPGKNAASDAEMNHRSSMRVLGDVVRRPPIHRRSFSLEGLTGGAGVGNKPSSSL
EVSSANAEELRHPFSGEERVDSLVSLSEEDLESDQREHRMFDQQICHRSKQQGFNYCTSA
ISSPLTKSISLMTISHPGLDNSRPFHSTFHNTSANLTESITEENYNFLPHSPSKKDSEWK
SGTKVSRTFSYIKNKMSSSKKSKEKEKEKDKIKEKEKDSKDKEKDKKTVNGHTFSSIPVV
GPISCSQCMKPFTNKDAYTCANCSAFVHKGCRESLASCAKVKMKQPKGSLQAHDTSSLPT
VIMRNKPSQPKERPRSAVLLVDETATTPIFANRRSQQSVSLSKSVSIQNITGVGNDENMS
NTWKFLSHSTDSLNKISKVNESTESLTDEGVGTDMNEGQLLGDFEIESKQLEAESWSRII
DSKFLKQQKKDVVKRQEVIYELMQTEFHHVRTLKIMSGVYSQGMMADLLFEQQMVEKLFP
CLDELISIHSQFFQRILERKKESLVDKSEKNFLIKRIGDVLVNQFSGENAERLKKTYGKF
CGQHNQSVNYFKDLYAKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLFQRI
LQCTKDNEVEQEDLAQSLSLVKDVIGAVDSKVASYEKKVRLNEIYTKTDSKSIMRMKSGQ
MFAKEDLKRKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYIFASLDQKSTV
ISLKKLIVREVAHEEKGLFLISMGMTDPEMVEVHASSKEERNSWIQIIQDTINTLNRDED
EGIPSENEEEKKMLDTRARELKEQLHQKDQKILLLLEEKEMIFRDMAECSTPLPEDCSPT
HSPRVLFRSNTEEALKGGPLMKSAINEVEILQGLVSGNLGGTLGPTVSSPIEQDVVGPVS
LPRRAETFGGFDSHQMNASKGGEKEEGDDGQDLRRTESDSGLKKGGNANLVFMLKRNSEQ
VVQSVVHLYELLSALQGVVLQQDSYIEDQKLVLSERALTRSLSRPSSLIEQEKQRSLEKQ
RQDLANLQKQQAQYLEEKRRREREWEARERELREREALLAQREEEVQQGQQDLEKEREEL
QQKKGTYQYDLERLRAAQKQLEREQEQLRREAERLSQRQTERDLCQVSHPHTKLMRIPSF
FPSPEEPPSPSAPSIAKSGSLDSELSVSPKRNSISRTHKDKGPFHILSSTSQTNKGPEGQ
SQAPASTSASTRLFGLTKPKEKKEKKKKNKTSRSQPGDGPASEVSAEGEEIFC
Enzyme 81 Number of Residues 2813
Enzyme 81 Molecular Weight 307547.7
Enzyme 81 Theoretical pI 4.88
Enzyme 81 GO Classification
Function
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
  • biological regulation
  • intracellular signaling pathway
  • regulation of Ras protein signal transduction
  • regulation of Rho protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 81 General Function Involved in Rho guanyl-nucleotide exchange factor activity
Enzyme 81 Specific Function Anchors cAMP-dependent protein kinase (PKA) and acts as an adapter protein to selectively couple G alpha-13 and Rho. Augments gene activation by the estrogen receptor in an element- specific and ligand-dependent manner. Activates estrogen receptor beta by a p38 MAPK-dependent pathway. Isoform 6 stimulates exchange activity on Rho proteins in vitro, but not on CDC42, Ras or Rac and may bind calcium ions
Enzyme 81 Pathways Not Available
Enzyme 81 Reactions Not Available
Enzyme 81 Pfam Domain Function
Enzyme 81 Signals
  • None
Enzyme 81 Transmembrane Regions
  • None
Enzyme 81 Essentiality Not Available
Enzyme 81 GenBank ID Protein 15207794 Link Image
Enzyme 81 UniProtKB/Swiss-Prot ID Q12802 Link Image
Enzyme 81 UniProtKB/Swiss-Prot Entry Name AKP13_HUMAN Link Image
Enzyme 81 PDB ID Not Available
Enzyme 81 Cellular Location Not Available
Enzyme 81 Gene Sequence >8442 bp
ATGAAACTTAATCCACAGCAAGCTCCCTTATATGGTGATTGTGTTGTTACAGTGCTGCTT
GCTGAAGAGGACAAAGCTGAAGATGATGTAGTGTTTTACTTGGTATTTTTGGGTTCCACC
CTCCGTCACTGTACAAGTACTCGGAAGGTCAGTTCTGATACATTGGAGACCATTGCTCCT
GGTCATGATTGTTGTGAAACAGTGAAGGTGCAGCTCTGTGCTTCCAAAGAGGGCCTTCCC
GTGTTTGTGGTGGCTGAAGAAGACTTTCATTTCGTCCAGGATGAAGCGTATGATGCAGCT
CAATTCCTAGCAACCAGTGCTGGAAATCAGCAGGCTTTGAACTTTACCCGTTTTCTTGAC
CAGTCAGGACCCCCATCTGGGGATGTGAATTCCCTTGATAAGAAGTTGGTGCTGGCATTC
AGGCACCTGAAGCTGCCCACGGAGTGGAATGTATTGGGGACAGATCAGAGTTTGCATGAT
GCTGGCCCGCGAGAGACATTGATGCATTTTGCTGTGCGGCTGGGACTGCTGAGGTTGACG
TGGTTCCTGTTGCAGAAGCCAGGTGGCCGCGGAGCTCTCAGTATCCACAACCAGGAAGGG
GCGACGCCTGTGAGCTTGGCCTTGGAGCGAGGCTATCACAAGCTGCACCAGCTTCTAACC
GAGGAGAATGCTGGAGAACCAGACTCCTGGAGCAGTTTATCCTATGAAATACCGTATGGA
GACTGTTCTGTGAGGCATCATCGAGAGTTGGACATCTATACATTAACCTCTGAGTCTGAT
TCACATCATGAACACCCATTTCCTGGAGACGGTTGCACTGGACCAATTTTTAAACTTATG
AACATCCAACAGCAACTAATGAAAACAAACCTCAAGCAGATGGACAGTCTTATGCCCTTA
ATGATGACAGCACAGGATCCTTCCAGTGCCCCAGAGACAGATGGCCAGTTTCTTCCCTGT
GCACCGGAGCCCACGGACCCTCAGCGACTTTCTTCTTCTGAAGAGACTGAGAGCACTCAG
TGCTGCCCAGGGAGCCCTGTTGCACAGACTGAAAGTCCCTGTGATTTGTCAAGCATAGTT
GAGGAGGAGAATACAGACCGTTCCTGTAGGAAGAAAAATAAAGGCGTGGAAAGAAAAGGG
GAAGAGGTGGAGCCAGCACCTATTGTGGACTCTGGAACTGTATCTGATCAAGACAGCTGC
CTTCAGAGCTTGCCTGATTGTGGAGTAAAGGGCACGGAAGGCCTTTCGTCCTGTGGAAAC
AGAAATGAAGAAACTGGAACAAAATCTTCTGGAATGCCCACAGACCAGGAGTCCCTGAGC
AGTGGAGATGCTGTGCTTCAGAGAGACTTGGTCACGGAGCCAGGCACAGCCCAGTATTCC
TCTGGAGGTGAACTGGGAGGCATTTCAACAACAAATGTCAGTACCCCAGACACTGCAGGG
GAAATGGAACATGGGCTCATGAACCCAGATGCCACTGTTCGGAAGAATGTGCTTCAGGGA
GGGGAAAGTACAAAGGAAAGATTTGAGAACTCTAATATTGGCACAGCTGGAGCCTCTGAC
GTGCACGTCACAAGTAAGCCTGTGGATAAAATCAGTGTTCCAAACTGTGCCCCTGCCGCC
AGTTCCCTGGATGGTAACAAACCTGCTGAGTCTTCACTTGCATTTAGTAATGAAGAAACC
TCCACTGAAAAAACAGCAGAAACGGAAACTTCACGAAGTTGTGAGGAGAGTGCTGATGCT
CCAGTAGATCAGAATTCTGTGGTGATTCCAGCTGCTGCAAAAGACAAGATTTCAGATGGA
TTAGAACCTTATACTCTCTTAGCAGCAGGCATAGGTGAGGCAATGTCACCCTCAGATTTA
GCCCTTCTTGGGCTGGAAGAAGATGTAATGCCACACCAGAACTCAGAAACAAATTCATCT
CATGCTCAAAGCCAAAAGGGCAAATCCTCACCCATTTGTTCTACAACTGGAGACGATAAA
CTTTGTGCAGACTCTGCATGTCAACAGAACACAGTGACTTCTAGTGGCGATTTGGTTGCA
AAACTGTGTGATAACATAGTTAGCAAGTCCGAAAGCACCACAGCAAGGCAACCCAGCTCA
CAAGATCCACCCGATGCCTCCCACTGTGAAGACCCACAGGCTCATACAGTCACCTCTGAC
CCTGTAAGGGATACCCAGGAACGTGCGGATTTTTGTCCTTTCAAAGTGGTGGATAACAAA
GGCCAACGAAAAGATGTGAAACTAGATAAACCTTTAACAAATATGCTTGAGGTGGTTTCA
CATCCACATCCAGTTGTCCCTAAAATGGAGAAAGAACTGGTGCCAGACCAGGCAGTAATA
TCAGACAGTACTTTCTCTCTGGCAAACAGTCCAGGCAGTGAATCAGTAACCAAGGATGAC
GCACTTTCTTTTGTCCCCTCCCAGAAAGAAAAGGGAACAGCAACTCCTGAACTACATACA
GCTACAGATTATAGAGATGGCCCAGATGGAAATTCGAATGAGCCTGATACGCGGCCACTA
GAAGACAGGGCAGCAGGCCTGTCCACATCCTCCACTGCTGCAGAGCTTCAGCACGGGATG
GGGAATACCAGTCTCACAGGACTTGGTGGAGAGCATGAGGGTCCTGCCCCTCCAGCAATC
CCAGAAGCTCTGAATATCAAGGGGAACACTGACTCTTCCCTGCAAAGTATGGGTAAGGCC
ACTTTGGCTTTAGATTCAGTTTTGACTGAAGAAGGAAAACTTCTGGTGGTTTCAGAAAGC
TCTGCAGCTCAGGAACAAGATAAGGATAAAGCGGTGACCTGTTCCTCTATTAAGGAAAAT
GCTCTCTCTTCAGGAACTTTGCAGGAAGAGCAGAGAACACCACCTCCTGGACAAGATACT
CAACAATTTCATGAAAAATCAATCTCAGCTGACTGTGCCAAGGACAAAGCACTTCAGCTA
AGTAATTCACCGGGTGCATCCTCTGCCTTTCTTAAGGCAGAAACTGAACATAACAAGGAA
GTGGCCCCACAAGTCTCACTGCTGACTCAAGGTGGGGCTGCCCAGAGCCTGGTGCCACCA
GGAGCAAGTCTGGCCACAGAGTCAAGGCAGGAAGCCTTGGGGGCAGAGCACAACAGCTCC
GCTCTGTTGCCATGTCTGTTGCCAGATGGGTCTGATGGGTCCGATGCTCTTAACTGCAGT
CAGGCTTCTCCTCTGGATGTTGGAGTGAAGAACACTCAATCCCAGGGAAAAACTAGTGCC
TGTGAGGTGAGTGGAAATGTGACGGTGGATGTTACAGGGGTTAATGCTCTACAAGGTATG
GCTGAGCCCAGAAGAGAGAATATATCACACAACACCCAAGACATCCTGATTCCAAACGTC
TTGTTGAGCCAAGAGAAGAATGCCGTTCTAGGTTTGCCAGTGGCTCTACAGGACAAAGCT
GTGACTGACCCACAGGGAGTTGGAACCCCAGAGATGATACCTCTTGATTGGGAGAAAGGG
AAGCTGGAGGGAGCAGACCACAGCTGTACCATGGGTGACGCTGAGGAAGCCCAAATAGAC
GATGAAGCACATCCTGTCCTACTGCAGCCTGTTGCCAAGGAGCTCCCCACAGACATGGAG
CTCTCAGCCCATGATGATGGGGCCCCAGCTGGTGTGAGGGAAGTCACGCGAGCCCCGCCT
TCAGGCAGAGAAAGGAGCACTCCCTCTCTACCTTGCATGGTCTCTGCCCAGGACGCACCT
CTGCCTAAGGGGGCAGACTTGATAGAGGAGGCTGCCAGCCGTATAGTGGATGCTGTCATC
GAACAAGTCAAGGCCGCTGGAGCACTGCTTACTGAGGGGGAGGCCTGTCACATGTCACTG
TCCAGCCCTGAGTTGGGTCCTCTCACTAAAGGACTAGAGAGTGCTTTTACAGAAAAAGTG
AGTACTTTCCCACCTGGGGAGAGCCTACCAATGGGCAGTACTCCTGAGGAAGCCACGGGG
AGCCTTGCAGGATGTTTTGCTGGAAGGGAGGAGCCAGAGAAGATCATTTTACCTGTCCAG
GGGCCTGAGCCAGCAGCAGAAATGCCAGACGTGAAAGCTGAAGATGAAGTGGATTTTAGA
GCAAGTTCAATTTCTGAAGAAGTGGCTGTAGGGAGCATAGCTGCTACACTGAAGATGAAG
CAAGGCCCAATGACCCAGGCGATAAACCGAGAAAACTGGTGTACAATAGAGCCATGCCCT
GATGCAGCATCTCTTCTGGCTTCCAAGCAGAGCCCAGAATGTGAGAACTTCCTGGATGTT
GGACTGGGCAGAGAGTGTACCTCAAAACAAGGTGTACTTAAAAGAGAATCTGGGAGTGAT
TCTGACCTCTTTCACTCACCCAGTGATGACATGGACAGCATCATCTTCCCAAAGCCAGAG
GAAGAGCATTTGGCCTGTGATATCACCGGATCCAGTTCATCCACCGATGACACGGCTTCA
CTGGACCGACATTCTTCTCATGGCAGTGATGTGTCTCTCTCCCAGATTTTAAAGCCAAAC
AGGTCAAGAGATCGGCAAAGCCTTGATGGATTCTACAGCCATGGGATGGGAGCTGAGGGT
CGAGAAAGTGAGAGTGAGCCTGCTGACCCAGGCGACGTGGAGGAGGAGGAGATGGACAGT
ATCACTGAAGTGCCTGCAAACTGCTCTGTCCTAAGGAGCTCCATGCGCTCTCTTTCTCCC
TTCCGGAGGCACAGCTGGGGGCCTGGGAAAAATGCAGCCAGCGATGCAGAAATGAACCAC
CGGAGTTCAATGCGAGTTCTTGGGGATGTTGTCAGGAGACCTCCCATTCATAGGAGAAGT
TTCAGTCTAGAAGGCTTGACAGGAGGAGCTGGTGTCGGAAACAAGCCATCCTCATCTCTA
GAAGTAAGCTCTGCAAATGCCGAAGAGCTCAGACACCCATTCAGTGGTGAGGAACGGGTT
GACTCTTTGGTGTCACTTTCAGAAGAGGATCTGGAGTCAGACCAGAGAGAACATAGGATG
TTTGATCAGCAGATATGTCACAGATCTAAGCAGCAGGGATTTAATTACTGTACATCAGCC
ATTTCCTCTCCATTGACAAAATCCATCTCATTAATGACAATCAGCCATCCTGGATTGGAC
AATTCACGGCCCTTCCACAGTACCTTCCACAATACCAGTGCTAATCTGACTGAGAGTATA
ACAGAAGAGAACTATAATTTCCTGCCACATAGCCCCTCCAAGAAAGATTCTGAATGGAAG
AGTGGAACAAAAGTCAGTCGTACATTCAGCTACATCAAGAATAAAATGTCTAGCAGCAAG
AAGAGCAAAGAAAAGGAAAAAGAAAAAGATAAGATTAAGGAGAAGGAGAAAGATTCTAAA
GACAAGGAGAAAGATAAGAAGACTGTCAACGGGCACACTTTCAGTTCCATTCCTGTTGTG
GGTCCCATCAGCTGTAGCCAGTGTATGAAGCCCTTCACCAACAAAGATGCCTATACTTGT
GCAAATTGCAGTGCTTTTGTCCACAAAGGCTGCCGAGAAAGTCTAGCCTCCTGTGCAAAG
GTCAAAATGAAGCAGCCCAAAGGGAGCCTTCAGGCACATGACACATCATCACTGCCCACG
GTCATTATGAGAAACAAGCCCTCACAGCCCAAGGAGCGTCCTCGGTCCGCAGTCCTCCTG
GTGGATGAAACCGCTACCACCCCAATATTTGCCAATAGACGATCCCAGCAGAGTGTCTCG
CTCTCCAAAAGTGTCTCCATACAGAACATTACTGGAGTTGGCAATGATGAGAACATGTCA
AACACCTGGAAATTCCTGTCTCATTCAACAGACTCACTAAATAAAATCAGCAAGGTCAAT
GAGTCAACAGAATCACTTACTGATGAGGGAGTAGGTACAGACATGAATGAAGGACAACTA
CTGGGAGACTTTGAGATTGAGTCCAAACAGCTGGAAGCAGAGTCTTGGAGTCGGATAATA
GACAGCAAGTTTCTAAAACAGCAAAAGAAAGATGTGGTCAAACGGCAAGAAGTAATATAT
GAGTTGATGCAGACAGAGTTTCATCATGTCCGCACTCTCAAGATCATGAGTGGTGTGTAC
AGCCAGGGGATGATGGCGGATCTGCTTTTTGAGCAGCAGATGGTAGAAAAGCTGTTCCCC
TGTTTGGATGAGCTGATCAGTATCCATAGCCAATTCTTCCAGAGGATTCTGGAGCGGAAG
AAGGAGTCTCTGGTGGATAAAAGTGAAAAGAACTTTCTCATCAAGAGGATAGGGGATGTG
CTTGTAAATCAGTTTTCAGGTGAGAATGCAGAACGTTTAAAGAAGACATATGGCAAGTTT
TGTGGGCAACATAACCAGTCTGTAAACTACTTCAAAGACCTTTATGCCAAGGATAAGCGT
TTTCAAGCCTTTGTAAAGAAGAAGATGAGCAGTTCAGTTGTTAGAAGGCTTGGAATTCCA
GAGTGCATATTGCTTGTAACTCAGCGGATTACCAAGTACCCAGTTTTATTCCAAAGAATA
TTGCAGTGTACCAAAGACAATGAAGTGGAGCAGGAAGATCTAGCACAGTCCTTGAGCCTG
GTGAAGGATGTGATTGGAGCTGTAGACAGCAAAGTGGCAAGTTATGAAAAGAAAGTGCGT
CTCAATGAGATTTATACAAAGACAGATAGCAAGTCAATCATGAGGATGAAGAGTGGTCAG
ATGTTTGCCAAGGAAGATTTGAAACGGAAGAAGCTTGTACGTGATGGGAGTGTGTTTCTG
AAGAATGCAGCAGGAAGGTTGAAAGAGGTTCAAGCAGTTCTTCTCACTGACATTTTAGTT
TTCCTTCAAGAAAAAGACCAGAAGTACATCTTTGCATCATTGGACCAGAAGTCAACAGTG
ATCTCTTTAAAGAAGCTGATTGTGAGAGAAGTGGCACATGAGGAGAAAGGTTTATTCCTG
ATCAGCATGGGGATGACAGATCCAGAGATGGTAGAAGTCCATGCCAGCTCCAAAGAGGAA
CGAAACAGCTGGATTCAGATCATTCAGGACACAATCAACACCCTGAACAGAGATGAAGAT
GAAGGAATTCCTAGTGAGAATGAGGAAGAAAAGAAAATGTTGGACACCAGAGCCCGAGAA
TTAAAAGAACAACTTCACCAGAAGGACCAAAAAATCCTACTCTTGTTGGAAGAGAAGGAG
ATGATTTTCCGGGACATGGCTGAGTGCAGCACCCCTCTCCCAGAGGATTGCTCCCCAACA
CATAGCCCTAGAGTTCTCTTCCGCTCCAACACAGAAGAGGCTCTCAAAGGAGGACCTTTA
ATGAAAAGTGCAATAAATGAGGTGGAGATCCTTCAGGGTTTGGTGAGTGGAAATCTGGGA
GGCACACTTGGGCCGACTGTCAGCAGCCCCATTGAGCAAGATGTGGTCGGTCCCGTTTCC
CTGCCCCGGAGAGCAGAGACCTTTGGAGGATTTGACAGCCATCAGATGAATGCTTCAAAA
GGAGGCGAGAAGGAAGAGGGAGATGATGGCCAAGATCTTAGGAGAACGGAATCAGATAGT
GGCCTAAAAAAGGGTGGAAATGCTAACCTGGTATTTATGCTTAAAAGAAACAGTGAGCAG
GTTGTCCAGAGCGTTGTTCATCTCTACGAGCTCCTCAGCGCTCTGCAGGGTGTGGTGCTG
CAGCAGGACAGCTACATTGAGGACCAGAAACTGGTGCTGAGCGAGAGGGCGCTCACTCGC
AGCTTGTCCCGCCCGAGCTCCCTCATTGAGCAGGAGAAGCAGCGCAGCCTGGAGAAGCAG
CGCCAGGACCTGGCCAACCTGCAGAAGCAGCAGGCCCAGTACCTCGAGGAGAAGCGCAGG
CGCGAGCGTGAGTGGGAAGCTCGTGAGAGGGAGCTGCGGGAGCGGGAGGCCCTCCTGGCC
CAGCGCGAGGAGGAGGTGCAGCAGGGGCAGCAGGACCTGGAAAAGGAGCGGGAGGAGCTC
CAGCAGAAGAAGGGCACATACCAGTATGACCTGGAGCGACTGCGTGCTGCCCAGAAACAG
CTTGAGAGGGAACAGGAGCACGTGCGCCGGGAGGCAGAGCGGCTCAGCCAGCGGCAGACA
GAACGGGACCTGTGTCAGGTTTCCCATCCACATACCAAGCTGATGAGGATCCCATCGTTC
TTCCCCAGTCCTGAGGAGCCCCCCTCGCCATCTGCACCTTCCATAGCCAAATCAGGGTCA
TTGGACTCAGAACTTTCAGTGTCCCCAAAAAGGAACAGCATCTCTCGGACACACAAAGAT
AAGGGGCCTTTTCACATACTGAGTTCAACCAGCCAGACAAACAAAGGACCAGAAGGGCAG
AGCCAGGCCCCTGCGTCCACCTCTGCCTCTACCCGCCTGTTTGGGTTAACAAAGCCAAAG
GAAAAGAAGGAGAAAAAAAAGAAGAACAAAACCAGCCGCTCTCAGCCCGGTGATGGTCCC
GCGTCAGAAGTATCAGCAGAGGGTGAAGAGATCTTCTGCTGA
Enzyme 81 GenBank Gene ID AB055890 Link Image
Enzyme 81 GeneCard ID AKAP13 Link Image
Enzyme 81 GenAtlas ID AKAP13 Link Image
Enzyme 81 HGNC ID HGNC:371 Link Image
Enzyme 81 Chromosome Location 1
Enzyme 81 Locus 15q24-q25
Enzyme 81 SNPs SNPJam Report Link Image
Enzyme 81 General References
  1. Toksoz D, Williams DA: Novel human oncogene lbc detected by transfection with distinct homology regions to signal transduction products. Oncogene. 1994 Feb;9(2):621-8. [PubMed Link Image]
  2. Rubino D, Driggers P, Arbit D, Kemp L, Miller B, Coso O, Pagliai K, Gray K, Gutkind S, Segars J: Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action. Oncogene. 1998 May 14;16(19):2513-26. [PubMed Link Image]
  3. Sterpetti P, Hack AA, Bashar MP, Park B, Cheng SD, Knoll JH, Urano T, Feig LA, Toksoz D: Activation of the Lbc Rho exchange factor proto-oncogene by truncation of an extended C terminus that regulates transformation and targeting. Mol Cell Biol. 1999 Feb;19(2):1334-45. [PubMed Link Image]
  4. Klussmann E, Edemir B, Pepperle B, Tamma G, Henn V, Klauschenz E, Hundsrucker C, Maric K, Rosenthal W: Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling. FEBS Lett. 2001 Nov 2;507(3):264-8. [PubMed Link Image]
  5. Diviani D, Soderling J, Scott JD: AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation. J Biol Chem. 2001 Nov 23;276(47):44247-57. Epub 2001 Sep 6. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Carr DW, Hausken ZE, Fraser ID, Stofko-Hahn RE, Scott JD: Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain. J Biol Chem. 1992 Jul 5;267(19):13376-82. [PubMed Link Image]
  8. Driggers PH, Segars JH, Rubino DM: The proto-oncoprotein Brx activates estrogen receptor beta by a p38 mitogen-activated protein kinase pathway. J Biol Chem. 2001 Dec 14;276(50):46792-7. Epub 2001 Sep 28. [PubMed Link Image]
  9. Iwashita S, Fujii M, Mukai H, Ono Y, Miyamoto M: Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2. Biochem Biophys Res Commun. 2004 Aug 6;320(4):1063-8. [PubMed Link Image]
  10. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  11. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  12. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  14. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  15. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  16. Newlon MG, Roy M, Morikis D, Carr DW, Westphal R, Scott JD, Jennings PA: A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes. EMBO J. 2001 Apr 2;20(7):1651-62. [PubMed Link Image]
Enzyme 81 Metabolite References Not Available
Enzyme 82 [top]
Enzyme 82 ID 13325
Enzyme 82 Name Cyclic nucleotide-gated cation channel alpha-4
Enzyme 82 Synonyms
  1. Cyclic nucleotide-gated channel alpha-4
  2. CNG channel alpha-4
  3. CNG-4
  4. CNG4
Enzyme 82 Gene Name CNGA4
Enzyme 82 Protein Sequence >Cyclic nucleotide-gated cation channel alpha-4
MSQDTKVKTTESSPPAPSKARKLLPVLDPSGDYYYWWLNTMVFPVMYNLIILVCRACFPD
LQHGYLVAWLVLDYTSDLLYLLDMVVRFHTGFLEQGILVVDKGRISSRYVRTWSFFLDLA
SLMPTDVVYVRLGPHTPTLRLNRFLRAPRLFEAFDRTETRTAYPNAFRIAKLMLYIFVVI
HWNSCLYFALSRYLGFGRDAWVYPDPAQPGFERLRRQYLYSFYFSTLILTTVGDTPPPAR
EEEYLFMVGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNRKLE
RRVIDWYQHLQINKKMTNEVAILQHLPERLRAEVAVSVHLSTLSRVQIFQNCEASLLEEL
VLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVADDGITQYAVLGAGLYFGEISIIN
IKGNMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIMEEKGREILLKMNKLDV
NAEAAEIALQEATESRLRGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEWQTREWP
MPEDLAEADDEGVPEEGTSKDEEGRASQEGPPGPE
Enzyme 82 Number of Residues 575
Enzyme 82 Molecular Weight 65968.2
Enzyme 82 Theoretical pI 5.32
Enzyme 82 GO Classification
Function
  • ion channel activity
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 82 General Function Involved in ion channel activity
Enzyme 82 Specific Function Second messenger, cAMP, causes the opening of cation- selective cyclic nucleotide-gated (CNG) channels and depolarization of the neuron (olfactory sensory neurons, OSNs). CNGA4 is the modulatory subunit of this channel which is known to play a central role in the transduction of odorant signals and subsequent adaptation. By accelerating the calcium-mediated negative feedback in olfactory signaling it allows rapid adaptation to odor stimulation and extends its range of odor detection
Enzyme 82 Pathways Not Available
Enzyme 82 Reactions Not Available
Enzyme 82 Pfam Domain Function
Enzyme 82 Signals
  • None
Enzyme 82 Transmembrane Regions
  • 34-54 66-86 113-133 169-189 218-234 245-265
Enzyme 82 Essentiality Not Available
Enzyme 82 GenBank ID Protein 82617546 Link Image
Enzyme 82 UniProtKB/Swiss-Prot ID Q8IV77 Link Image
Enzyme 82 UniProtKB/Swiss-Prot Entry Name CNGA4_HUMAN Link Image
Enzyme 82 PDB ID Not Available
Enzyme 82 Cellular Location Not Available
Enzyme 82 Gene Sequence >1728 bp
ATGAGCCAGGACACCAAAGTGAAGACAACAGAGTCCAGTCCCCCAGCCCCATCCAAGGCC
AGGAAGTTGCTGCCTGTCCTGGACCCATCTGGGGATTACTACTACTGGTGGCTGAACACA
ATGGTCTTCCCAGTCATGTATAACCTCATCATCCTCGTGTGCAGAGCCTGCTTCCCCGAC
TTGCAGCACGGTTATCTGGTGGCCTGGTTGGTGCTGGACTACACGAGTGACCTGCTATAC
CTACTAGACATGGTGGTGCGCTTCCACACAGGATTCTTGGAACAGGGCATCCTGGTGGTG
GACAAGGGTAGGATCTCGAGTCGCTACGTTCGCACCTGGAGTTTCTTCTTGGACCTGGCT
TCCCTGATGCCCACAGATGTGGTCTACGTGCGGCTGGGCCCGCACACACCCACCCTGAGG
CTGAACCGCTTTCTCCGCGCGCCCCGCCTCTTCGAGGCCTTCGACCGCACAGAGACCCGC
ACAGCTTACCCAAATGCCTTTCGCATTGCCAAGCTGATGCTTTACATTTTTGTCGTCATC
CATTGGAACAGCTGCCTATACTTTGCCCTATCCCGGTACCTGGGCTTCGGGCGTGACGCA
TGGGTGTACCCGGACCCCGCGCAGCCTGGCTTTGAGCGCCTGCGGCGCCAGTACCTCTAT
AGCTTTTACTTCTCCACGCTGATACTGACTACAGTGGGCGATACACCGCCGCCAGCCAGG
GAAGAAGAGTACCTCTTCATGGTGGGCGACTTCCTGCTGGCCGTCATGGGTTTCGCCACC
ATCATGGGTAGCATGAGCTCTGTCATCTACAACATGAACACTGCAGATGCGGCTTTCTAC
CCAGATCATGCACTGGTGAAGAAGTACATGAAGCTGCAGCACGTCAACCGCAAGCTGGAG
CGGCGAGTTATTGACTGGTATCAGCACCTGCAGATCAACAAGAAGATGACCAACGAGGTA
GCCATCTTACAGCACTTGCCTGAGCGGCTGCGGGCAGAAGTGGCTGTGTCTGTGCACCTG
TCCACTCTGAGCCGGGTGCAGATCTTTCAGAACTGTGAGGCCAGCCTGCTGGAGGAGCTG
GTGCTGAAGCTGCAGCCCCAGACCTACTCACCAGGTGAATATGTATGCCGCAAAGGAGAC
ATTGGCCAAGAGATGTACATCATCCGAGAGGGTCAACTGGCCGTGGTGGCAGATGATGGT
ATCACACAGTATGCTGTGCTCGGTGCAGGGCTCTACTTTGGGGAGATCAGCATCATCAAC
ATCAAAGGGAACATGTCTGGGAACCGCCGCACAGCCAACATCAAGAGCCTAGGTTATTCA
GACCTATTCTGCCTGAGCAAGGAGGACCTGCGGGAGGTGCTGAGCGAGTATCCACAAGCA
CAGACCATCATGGAGGAGAAAGGACGTGAGATCCTGCTGAAAATGAACAAGTTGGACGTG
AATGCTGAGGCAGCTGAGATCGCCCTGCAGGAGGCCACAGAGTCCCGGCTACGAGGCCTA
GACCAGCAGCTGGATGATCTACAGACCAAGTTTGCTCGCCTCCTGGCTGAGCTGGAGTCC
AGCGCACTTAAGATTGCTTACCGCATTGAACGGCTGGAGTGGCAGACTCGAGAGTGGCCA
ATGCCCGAGGACCTGGCTGAGGCTGATGACGAGGGTGAGCCTGAGGAGGGAACTTCCAAA
GATGAAGAGGGCAGGGCCAGCCAGGAGGGACCCCCAGGTCCAGAGTGA
Enzyme 82 GenBank Gene ID NM_001037329 Link Image
Enzyme 82 GeneCard ID CNGA4 Link Image
Enzyme 82 GenAtlas ID CNGA4 Link Image
Enzyme 82 HGNC ID HGNC:2152 Link Image
Enzyme 82 Chromosome Location 1
Enzyme 82 Locus 11p15.4
Enzyme 82 SNPs SNPJam Report Link Image
Enzyme 82 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Bradley J, Bonigk W, Yau KW, Frings S: Calmodulin permanently associates with rat olfactory CNG channels under native conditions. Nat Neurosci. 2004 Jul;7(7):705-10. Epub 2004 Jun 13. [PubMed Link Image]
  5. Brady JD, Rich ED, Martens JR, Karpen JW, Varnum MD, Brown RL: Interplay between PIP3 and calmodulin regulation of olfactory cyclic nucleotide-gated channels. Proc Natl Acad Sci U S A. 2006 Oct 17;103(42):15635-40. Epub 2006 Oct 10. [PubMed Link Image]
Enzyme 82 Metabolite References Not Available
Enzyme 83 [top]
Enzyme 83 ID 13341
Enzyme 83 Name CREB-regulated transcription coactivator 1
Enzyme 83 Synonyms
  1. Mucoepidermoid carcinoma translocated protein 1
  2. Transducer of regulated cAMP response element-binding protein 1
  3. TORC-1
  4. Transducer of CREB protein 1
Enzyme 83 Gene Name CRTC1
Enzyme 83 Protein Sequence >CREB-regulated transcription coactivator 1
MATSNNPRKFSEKIALHNQKQAEETAAFEEVMKDLSLTRAARLQLQKSQYLQLGPSRGQY
YGGSLPNVNQIGSGTMDLPFQTPFQSSGLDTSRTTRHHGLVDRVYRERGRLGSPHRRPLS
VDKHGRQADSCPYGTMYLSPPADTSWRRTNSDSALHQSTMTPTQPESFSSGSQDVHQKRV
LLLTVPGMEETTSEADKNLSKQAWDTKKTGSRPKSCEVPGINIFPSADQENTTALIPATH
NTGGSLPDLTNIHFPSPLPTPLDPEEPTFPALSSSSSTGNLAANLTHLGIGGAGQGMSTP
GSSPQHRPAGVSPLSLSTEARRQQASPTLSPLSPITQAVAMDALSLEQQLPYAFFTQAGS
QQPPPQPQPPPPPPPASQQPPPPPPPQAPVRLPPGGPLLPSASLTRGPQPPPLAVTVPSS
LPQSPPENPGQPSMGIDIASAPALQQYRTSAGSPANQSPTSPVSNQGFSPGSSPQHTSTL
GSVFGDAYYEQQMAARQANALSHQLEQFNMMENAISSSSLYSPGSTLNYSQAAMMGLTGS
HGSLPDSQQLGYASHSGIPNIILTVTGESPPSLSKELTSSLAGVGDVSFDSDSQFPLDEL
KIDPLTLDGLHMLNDPDMVLADPATEDTFRMDRL
Enzyme 83 Number of Residues 634
Enzyme 83 Molecular Weight 67299.2
Enzyme 83 Theoretical pI 5.96
Enzyme 83 GO Classification Not Available
Enzyme 83 General Function Cell wall/membrane/envelope biogenesis
Enzyme 83 Specific Function Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PGC1alpha and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR). In the hippocampus, involved in late-phase long- term potentiation (L-LTP) maintenance at the Schaffer collateral- CA1 synapses
Enzyme 83 Pathways Not Available
Enzyme 83 Reactions Not Available
Enzyme 83 Pfam Domain Function Not Available
Enzyme 83 Signals
  • None
Enzyme 83 Transmembrane Regions
  • None
Enzyme 83 Essentiality Not Available
Enzyme 83 GenBank ID Protein 3327046 Link Image
Enzyme 83 UniProtKB/Swiss-Prot ID Q6UUV9 Link Image
Enzyme 83 UniProtKB/Swiss-Prot Entry Name CRTC1_HUMAN Link Image
Enzyme 83 PDB ID Not Available
Enzyme 83 Cellular Location Not Available
Enzyme 83 Gene Sequence >1906 bp
GCACAATCAGAAGCAGGCGGAGGAGACGGCGGCCTTCGAGGAGGTCATGAAGGACCTGAG
CCTGACGCGGGCCGCGCGGCTCCAGCTCCAGAAATCCCAGTACCTGCAACTGGGCCCCAG
CCGAGGCCAGTACTATGGCGGGTCCCTGCCCAACGTGAACCAGATCGGGAGTGGCACCAT
GGACCTGCCCTTCCAGCCCAGCGGATTTCTGGGGGAGGCCCTGGCAGCGGCTCCTGTCTC
TCTGACCCCCTTCCAATCCTCGGGCCTGGACACCAGCCGGACCACCCGGCACCATGGGCT
GGTGGACAGGGTGTACCGGGAGCGTGGCCGGCTCGGCTCCCCACACCGCCGGCCCCTGTC
AGTGGACAAACACGGACGGCAGGCCGACAGCTGCCCCTATGGCACCATGTACCTCTCACC
ACCCGCGGACACCAGCTGGAGAAGGACCAATTCTGACTCCGCCCTGCACCAGAGCACAAT
GACGCCCACGCAGCCAGAATCCTTTAGCAGTGGGTCCCAGGACGTGCACCAGAAAAGAGT
CTTACTGTTAACAGTCCCAGGAATGGAAGAGACCACATCAGAGGCAGACAAAAACCTTTC
CAAGCAAGCATGGGACACCAAGAAGACGGGGTCCAGGCCCAAGTCCTGTGAGGTCCCCGG
AATCAACATCTTCCCGTCTGCCGACCAGGAAAACACTACAGCCCTGATCCCCGCCACCCA
CAACACAGGGGGGTCCCTGCCCGACCTGACCAACATCCACTTCCCCTCCCCGCTCCCGAC
CCCGCTGGACCCCGAGGAGCCCACCTTCCCTGCACTGAGCAGCTCCAGCAGCACCGGCAA
CCTCGCGGCCAACCTGACGCACCTGGGCATCGGTGGCGCCGGCCAGGGAATGAGCACACC
TGGCTCCTCTCCACAGCACCGCCCAGCTGGCGTCAGCCCCCTGTCCCTGAGCACAGAGGC
AAGGCGTCAGCAGGCATCGCCCACCCTGTCTCCGCTGTCACCCATCACTCAGGCTGTAGC
CATGGACGCCCTGTCTCTGGAGCAGCAGCTGCCCTACGCCTTCTTCACCCAGGCGGGCTC
CCAGCAGCCACCGCCGCAGCCCCAGCCCCCGCCGCCTCCTCCACCCGCGTCCCAGCAGCC
ACCACCCCCGCCACCCCCACAGGCGCCCGTCCGCCTGCCCCCTGGTGGCCCCCTGTTGCC
CAGCGCCAGCCTGACTCGTGGGCCACAGCCGCCCCCGCTTGCAGTCACGGTACCGTCCTC
TCTCCCCCAGTCCCCCCCAGAGAACCCTGGCCAGCCATCGATGGGGATCGACATCGCCTC
GGCGCCGGCTCTGCAGCAGTACCGCACTAGCGCCGGCTCCCCGGCCAACCAGTCTCCCAC
CTCGCCAGTCTCCAATCAAGGCTTCTCCCCAGGGAGCTCCCCGCAACACACTTCCACCCT
GGGCAGCGTGTTTGGGGACGCGTACTATGAGCAGCAGATGGCGGCCAGGCAGGCCAATGC
TCTGTCCCACCAGCTGGAGCAGTTCAACATGATGGAGAACGCCATCAGCTCCAGCAGCCT
GTACAGCCCGGGCTCCACACTCAACTACTCGCAGGCGGCCATGATGGGCCTCACGGGCAG
CCACGGGAGCCTGCCGGACTCGCAGCAACTGGGATACGCCAGCCACAGTGGCATCCCCAA
CATCATCCTCACAGTGACAGGAGAGTCCCCCCCCAGCCTCTCTAAAGAACTGACCAGCTC
TCTGGCCGGGGTCGGCGACGTCAGCTTCGACTCCGACAGCCAGTTTCCCCTGGACGAACT
CAAGATCGACCCCCTGACCCTCGACGGACTGCACATGCTCAACGACCCCGACATGGTTCT
GGCCGACCCAGCCACCGAGGACACCTTCCGGATGGACCGCCTGTGA
Enzyme 83 GenBank Gene ID AB014516 Link Image
Enzyme 83 GeneCard ID CRTC1 Link Image
Enzyme 83 GenAtlas ID CRTC1 Link Image
Enzyme 83 HGNC ID HGNC:16062 Link Image
Enzyme 83 Chromosome Location 1
Enzyme 83 Locus 19p13.11
Enzyme 83 SNPs SNPJam Report Link Image
Enzyme 83 General References
  1. Iourgenko V, Zhang W, Mickanin C, Daly I, Jiang C, Hexham JM, Orth AP, Miraglia L, Meltzer J, Garza D, Chirn GW, McWhinnie E, Cohen D, Skelton J, Terry R, Yu Y, Bodian D, Buxton FP, Zhu J, Song C, Labow MA: Identification of a family of cAMP response element-binding protein coactivators by genome-scale functional analysis in mammalian cells. Proc Natl Acad Sci U S A. 2003 Oct 14;100(21):12147-52. Epub 2003 Sep 23. [PubMed Link Image]
  2. Tonon G, Modi S, Wu L, Kubo A, Coxon AB, Komiya T, O'Neil K, Stover K, El-Naggar A, Griffin JD, Kirsch IR, Kaye FJ: t(11;19)(q21;p13) translocation in mucoepidermoid carcinoma creates a novel fusion product that disrupts a Notch signaling pathway. Nat Genet. 2003 Feb;33(2):208-13. Epub 2003 Jan 21. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Enlund F, Behboudi A, Andren Y, Oberg C, Lendahl U, Mark J, Stenman G: Altered Notch signaling resulting from expression of a WAMTP1-MAML2 gene fusion in mucoepidermoid carcinomas and benign Warthin's tumors. Exp Cell Res. 2004 Jan 1;292(1):21-8. [PubMed Link Image]
  7. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Jun 30;5(3):169-76. [PubMed Link Image]
  8. Conkright MD, Canettieri G, Screaton R, Guzman E, Miraglia L, Hogenesch JB, Montminy M: TORCs: transducers of regulated CREB activity. Mol Cell. 2003 Aug;12(2):413-23. [PubMed Link Image]
  9. Bittinger MA, McWhinnie E, Meltzer J, Iourgenko V, Latario B, Liu X, Chen CH, Song C, Garza D, Labow M: Activation of cAMP response element-mediated gene expression by regulated nuclear transport of TORC proteins. Curr Biol. 2004 Dec 14;14(23):2156-61. [PubMed Link Image]
  10. Behboudi A, Winnes M, Gorunova L, van den Oord JJ, Mertens F, Enlund F, Stenman G: Clear cell hidradenoma of the skin-a third tumor type with a t(11;19)--associated TORC1-MAML2 gene fusion. Genes Chromosomes Cancer. 2005 Jun;43(2):202-5. [PubMed Link Image]
  11. Katoh Y, Takemori H, Lin XZ, Tamura M, Muraoka M, Satoh T, Tsuchiya Y, Min L, Doi J, Miyauchi A, Witters LA, Nakamura H, Okamoto M: Silencing the constitutive active transcription factor CREB by the LKB1-SIK signaling cascade. FEBS J. 2006 Jun;273(12):2730-48. [PubMed Link Image]
  12. Siu YT, Chin KT, Siu KL, Yee Wai Choy E, Jeang KT, Jin DY: TORC1 and TORC2 coactivators are required for tax activation of the human T-cell leukemia virus type 1 long terminal repeats. J Virol. 2006 Jul;80(14):7052-9. [PubMed Link Image]
  13. Wu Z, Huang X, Feng Y, Handschin C, Feng Y, Gullicksen PS, Bare O, Labow M, Spiegelman B, Stevenson SC: Transducer of regulated CREB-binding proteins (TORCs) induce PGC-1alpha transcription and mitochondrial biogenesis in muscle cells. Proc Natl Acad Sci U S A. 2006 Sep 26;103(39):14379-84. Epub 2006 Sep 15. [PubMed Link Image]
  14. Takemori H, Kanematsu M, Kajimura J, Hatano O, Katoh Y, Lin XZ, Min L, Yamazaki T, Doi J, Okamoto M: Dephosphorylation of TORC initiates expression of the StAR gene. Mol Cell Endocrinol. 2007 Feb;265-266:196-204. Epub 2007 Jan 8. [PubMed Link Image]
  15. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  16. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 83 Metabolite References Not Available
Enzyme 84 [top]
Enzyme 84 ID 13342
Enzyme 84 Name CREB-regulated transcription coactivator 2
Enzyme 84 Synonyms
  1. Transducer of regulated cAMP response element-binding protein 2
  2. TORC-2
  3. Transducer of CREB protein 2
Enzyme 84 Gene Name CRTC2
Enzyme 84 Protein Sequence >CREB-regulated transcription coactivator 2
MATSGANGPGSATASASNPRKFSEKIALQKQRQAEETAAFEEVMMDIGSTRLQAQKLRLA
YTRSSHYGGSLPNVNQIGSGLAEFQSPLHSPLDSSRSTRHHGLVERVQRDPRRMVSPLRR
YTRHIDSSPYSPAYLSPPPESSWRRTMAWGNFPAEKGQLFRLPSALNRTSSDSALHTSVM
NPSPQDTYPGPTPPSILPSRRGGILDGEMDPKVPAIEENLLDDKHLLKPWDAKKLSSSSS
RPRSCEVPGINIFPSPDQPANVPVLPPAMNTGGSLPDLTNLHFPPPLPTPLDPEETAYPS
LSGGNSTSNLTHTMTHLGISRGMGLGPGYDAPGLHSPLSHPSLQSSLSNPNLQASLSSPQ
PQLQGSHSHPSLPASSLARHVLPTTSLGHPSLSAPALSSSSSSSSTSSPVLGAPSYPAST
PGASPHHRRVPLSPLSLLAGPADARRSQQQLPKQFSPTMSPTLSSITQGVPLDTSKLSTD
QRLPPYPYSSPSLVLPTQPHTPKSLQQPGLPSQSCSVQSSGGQPPGRQSHYGTPYPPGPS
GHGQQSYHRPMSDFNLGNLEQFSMESPSASLVLDPPGFSEGPGFLGGEGPMGGPQDPHTF
NHQNLTHCSRHGSGPNIILTGDSSPGFSKEIAAALAGVPGFEVSAAGLELGLGLEDELRM
EPLGLEGLNMLSDPCALLPDPAVEESFRSDRLQ
Enzyme 84 Number of Residues 693
Enzyme 84 Molecular Weight 73301.0
Enzyme 84 Theoretical pI 7.11
Enzyme 84 GO Classification Not Available
Enzyme 84 General Function Involved in protein binding
Enzyme 84 Specific Function Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates gluconeogenesis as a component of the LKB1/AMPK/TORC2 signaling pathway. Regulates the expression of specific genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR)
Enzyme 84 Pathways Not Available
Enzyme 84 Reactions Not Available
Enzyme 84 Pfam Domain Function Not Available
Enzyme 84 Signals
  • None
Enzyme 84 Transmembrane Regions
  • None
Enzyme 84 Essentiality Not Available
Enzyme 84 GenBank ID Protein 62898850 Link Image
Enzyme 84 UniProtKB/Swiss-Prot ID Q53ET0 Link Image
Enzyme 84 UniProtKB/Swiss-Prot Entry Name CRTC2_HUMAN Link Image
Enzyme 84 PDB ID Not Available
Enzyme 84 Cellular Location Not Available
Enzyme 84 Gene Sequence >2082 bp
ATGGCGACGTCGGGGGCGAACGGGCCTGGTTCGGCCACGGCCTCGGCTTCCAATCCGCGC
AAATTTAGTGAGAAGATTGCGCTGCAGAAGCAGCGTCAGGCCGAGGAGACGGCGGCCTTC
GAGGAGGTGATGATGGACATCGGCTCCACCCGGTTACAGGCCCAAAAACTGCGACTGGCA
TACACAAGGAGCTCTCATTATGGTGGGTCTCTGCCCAATGTTAACCAGATTGGCTCTGGC
CTGGCCGAGTTCCAGAGCCCCCTCCACTCACCTTTGGATTCATCTCGGAGCACTCGGCAC
CATGGGCTGGTGGAACGGGTGCAGCGAGATCCTCGAAGAATGGTGTCCCCACTTCGCCGA
TACACCCGCCACATTGACAGCTCTCCCTATAGTCCTGCCTACTTATCTCCTCCCCCAGAG
TCTAGCTGGCGAAGGACGATGGCCTGGGGCAATTTCCCTGCAGAGAAGGGGCAGTTGTTT
CGACTACCATCTGCACTTAACAGGACAAGCTCTGACTCTGCCCTTCATACAAGTGTGATG
AACCCCAGTCCCCAGGATACCTACCCAGGCCCCACACCTCCCAGCATCCTGCCCAGCCGA
CGTGGGGGTATTCTGGATGGTGAAATGGACCCCAAAGTACCTGCTATTGAGGAGAACTTG
CTAGATGACAAGCATTTGCTGAAGCCATGGGATGCTAAGAAGCTATCCTCATCCTCTTCC
CGACCTCGGTCCTGTGAAGTCCCTGGAATTAACATCTTTCCATCTCCTGACCAGCCTGCC
AATGTGCCTGTCCTCCCACCTGCCATGAACACGGGGGGCTCCCTACCTGACCTCACCAAC
CTGCACTTTCCCCCACCACTGCCCACCCCCCTGGACCCTGAAGAGACAGCCTACCCTAGC
CTGAGTGGGGGCAACAGTACCTCCAATTTGACCCACACCATGACTCACCTGGGCATCAGC
AGGGGCATGGGCCTGGGCCCAGGCTATGATGCACCAGGACTTCATTCACCTCTCAGCCAC
CCATCCCTGCAGTCCTCCCTAAGCAATCCCAACCTCCAGGCTTCCCTGAGCAGTCCTCAG
CCCCAGCTTCAGGGCTCCCACAGCCACCCCTCTCTGCCTGCCTCCTCCTTGGCCCGCCAT
GTACTGCCCACCACCTCCCTGGGCCACCCCTCACTCAGTGCTCCGGCTCTCTCCTCCTCC
TCTTCCTCCTCCTCCACTTCATCTCCTGTTTTGGGCGCCCCTTCTTACCCTGCTTCTACC
CCTGGGGCCTCCCCCCACCACCGCCGTGTGCCCCTCAGCCCCCTGAGTTTGCTCGCGGGC
CCAGCCGACGCCAGAAGGTCCCAACAGCAGCTGCCCAAACAGTTTTCGCCAACAATGTCA
CCCACCTTGTCTTCCATCACTCAGGGCGTCCCCCTGGATACCAGTAAACTGTCCACTGAC
CAGCGGTTACCCCCATACCCATACAGCTCCCCAAGTCTGGTTCTGCCTACCCAGTCCCAC
ACCCCAAAGTCTCTACAGCAGCCAGGGCTGCCCTCTCAGTCTTGTTCAGTGCAGTCCTCA
GGTGGGCAGCCCCCAGGCAGGCAGTCTCATTATGGGACACCGTACCCACCTGGGCCCAGT
GGGCATGGGCAACAGTCTTACCACCGGCCAATGAGTGACTTCAACCTGGGGAATCTGGAG
CAGTTCAGCATGGAGAGCCCATCAGCCAGCCTGGTGCTGGATCCCCCTGGCTTTTCTGAA
GGGCCTGGATTTTTAGGGGGTGAGGGGCCAATGGGTGGCCCCCAGGATCCCCACACCTTC
AACCACCAGAACTTGACCCACTGTTCCCGCCATGGCTCAGGGCCTAACATCATCCTCACA
GGGGACTCCTCTCCAGGTTTCTCTAAGGAGATTGCAGCAGCCCTGGCCGGAGTGCCTGGC
TTTGAGGTGTCAGCAGCTGGATTGGAGCTAGGGCTTGGGCTAGAAGATGAGCTGCGCATG
GAGCCACTGGGCCTGGAAGGGCTAAACATGCTGAGTGACCCCTGTGCCCTGCTGCCTGAT
CCTGCTGTGGAGGAGTCATTCCGCAGTGACCGGCTCCAATGA
Enzyme 84 GenBank Gene ID AK223559 Link Image
Enzyme 84 GeneCard ID CRTC2 Link Image
Enzyme 84 GenAtlas ID CRTC2 Link Image
Enzyme 84 HGNC ID HGNC:27301 Link Image
Enzyme 84 Chromosome Location 1
Enzyme 84 Locus 1q21.3
Enzyme 84 SNPs SNPJam Report Link Image
Enzyme 84 General References
  1. Iourgenko V, Zhang W, Mickanin C, Daly I, Jiang C, Hexham JM, Orth AP, Miraglia L, Meltzer J, Garza D, Chirn GW, McWhinnie E, Cohen D, Skelton J, Terry R, Yu Y, Bodian D, Buxton FP, Zhu J, Song C, Labow MA: Identification of a family of cAMP response element-binding protein coactivators by genome-scale functional analysis in mammalian cells. Proc Natl Acad Sci U S A. 2003 Oct 14;100(21):12147-52. Epub 2003 Sep 23. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Conkright MD, Canettieri G, Screaton R, Guzman E, Miraglia L, Hogenesch JB, Montminy M: TORCs: transducers of regulated CREB activity. Mol Cell. 2003 Aug;12(2):413-23. [PubMed Link Image]
  5. Screaton RA, Conkright MD, Katoh Y, Best JL, Canettieri G, Jeffries S, Guzman E, Niessen S, Yates JR 3rd, Takemori H, Okamoto M, Montminy M: The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector. Cell. 2004 Oct 1;119(1):61-74. [PubMed Link Image]
  6. Bittinger MA, McWhinnie E, Meltzer J, Iourgenko V, Latario B, Liu X, Chen CH, Song C, Garza D, Labow M: Activation of cAMP response element-mediated gene expression by regulated nuclear transport of TORC proteins. Curr Biol. 2004 Dec 14;14(23):2156-61. [PubMed Link Image]
  7. Katoh Y, Takemori H, Lin XZ, Tamura M, Muraoka M, Satoh T, Tsuchiya Y, Min L, Doi J, Miyauchi A, Witters LA, Nakamura H, Okamoto M: Silencing the constitutive active transcription factor CREB by the LKB1-SIK signaling cascade. FEBS J. 2006 Jun;273(12):2730-48. [PubMed Link Image]
  8. Siu YT, Chin KT, Siu KL, Yee Wai Choy E, Jeang KT, Jin DY: TORC1 and TORC2 coactivators are required for tax activation of the human T-cell leukemia virus type 1 long terminal repeats. J Virol. 2006 Jul;80(14):7052-9. [PubMed Link Image]
  9. Wu Z, Huang X, Feng Y, Handschin C, Feng Y, Gullicksen PS, Bare O, Labow M, Spiegelman B, Stevenson SC: Transducer of regulated CREB-binding proteins (TORCs) induce PGC-1alpha transcription and mitochondrial biogenesis in muscle cells. Proc Natl Acad Sci U S A. 2006 Sep 26;103(39):14379-84. Epub 2006 Sep 15. [PubMed Link Image]
  10. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  11. Takemori H, Kanematsu M, Kajimura J, Hatano O, Katoh Y, Lin XZ, Min L, Yamazaki T, Doi J, Okamoto M: Dephosphorylation of TORC initiates expression of the StAR gene. Mol Cell Endocrinol. 2007 Feb;265-266:196-204. Epub 2007 Jan 8. [PubMed Link Image]
  12. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  14. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  15. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  16. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  17. Keshavarz P, Inoue H, Nakamura N, Yoshikawa T, Tanahashi T, Itakura M: Single nucleotide polymorphisms in genes encoding LKB1 (STK11), TORC2 (CRTC2) and AMPK alpha2-subunit (PRKAA2) and risk of type 2 diabetes. Mol Genet Metab. 2008 Feb;93(2):200-9. Epub 2007 Oct 18. [PubMed Link Image]
Enzyme 84 Metabolite References Not Available
Enzyme 85 [top]
Enzyme 85 ID 13422
Enzyme 85 Name Guanine nucleotide-binding protein G(t) subunit alpha-3
Enzyme 85 Synonyms
  1. Gustducin alpha-3 chain
Enzyme 85 Gene Name GNAT3
Enzyme 85 Protein Sequence >Guanine nucleotide-binding protein G(t) subunit alpha-3
MGSGISSESKESAKRSKELEKKLQEDAERDARTVKLLLLGAGESGKSTIVKQMKIIHKNG
YSEQECMEFKAVIYSNTLQSILAIVKAMTTLGIDYVNPRSAEDQRQLYAMANTLEDGGMT
PQLAEVIKRLWRDPGIQACFERASEYQLNDSAAYYLNDLDRITASGYVPNEQDVLHSRVK
TTGIIETQFSFKDLHFRMFDVGGQRSERKKWIHCFEGVTCIIFCAALSAYDMVLVEDEEV
NRMHESLHLFNSICNHKYFSTTSIVLFLNKKDIFQEKVTKVHLSICFPEYTGPNTFEDAG
NYIKNQFLDLNLKKEDKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF
Enzyme 85 Number of Residues 354
Enzyme 85 Molecular Weight 40356.7
Enzyme 85 Theoretical pI 5.87
Enzyme 85 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • molecular transducer activity
  • nucleotide binding
  • purine nucleotide binding
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • biological regulation
  • cell surface receptor linked signaling pathway
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 85 General Function Involved in signal transducer activity
Enzyme 85 Specific Function Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction. Transduction by this alpha subunit involves coupling of specific cell-surface receptors with a cGMP-phosphodiesterase; Activation of phosphodiesterase lowers intracellular levels of cAMP and cGMP which may open a cyclic nucleotide-suppressible cation channel leading to influx of calcium, ultimately leading to release of neurotransmitter. Indeed, denatonium and strychnine induce transient reduction in cAMP and cGMP in taste tissue, whereas this decrease is inhibited by GNAT3 antibody. Gustducin heterotrimer transduces response to bitter and sweet compounds via regulation of phosphodiesterase for alpha subunit, as well as via activation of phospholipase C for beta and gamma subunits, with ultimate increase inositol trisphosphate and increase of intracellular Calcium. GNAT3 can functionally couple to taste receptors to transmit intracellular signal:receptor heterodimer TAS1R2/TAS1R3 senses sweetness and TAS1R1/TAS1R3 transduces umami taste, whereas the T2R family GPCRs act as bitter sensors. Functions also as lumenal sugar sensors in the gut to control the expression of the Na+-glucose transporter SGLT1 in response to dietaty sugar, as well as the secretion of Glucagon-like peptide- 1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP. Thus, may modulate the gut capacity to absorb sugars, with implications in malabsorption syndromes and diet-related disorders including diabetes and obesity
Enzyme 85 Pathways Not Available
Enzyme 85 Reactions Not Available
Enzyme 85 Pfam Domain Function
Enzyme 85 Signals
  • None
Enzyme 85 Transmembrane Regions
  • None
Enzyme 85 Essentiality Not Available
Enzyme 85 GenBank ID Protein 156139155 Link Image
Enzyme 85 UniProtKB/Swiss-Prot ID A8MTJ3 Link Image
Enzyme 85 UniProtKB/Swiss-Prot Entry Name GNAT3_HUMAN Link Image
Enzyme 85 PDB ID Not Available
Enzyme 85 Cellular Location Not Available
Enzyme 85 Gene Sequence >1065 bp
ATGGGAAGTGGAATTAGTTCAGAGAGCAAGGAGTCAGCCAAAAGATCAAAAGAACTGGAG
AAAAAGCTTCAGGAGGATGCTGAGCGAGATGCAAGAACCGTAAAGCTGCTACTATTAGGA
GCAGGAGAATCTGGGAAAAGTACTATTGTTAAACAAATGAAGATCATCCATAAGAATGGT
TACAGTGAGCAAGAATGCATGGAGTTCAAAGCAGTAATTTACAGTAATACATTGCAATCC
ATCCTAGCTATTGTGAAAGCCATGACTACCCTTGGAATTGATTATGTAAATCCCAGAAGT
GCAGAGGACCAACGACAACTTTATGCAATGGCAAATACCCTGGAAGATGGTGGCATGACA
CCTCAACTGGCTGAGGTAATAAAACGGCTGTGGAGAGATCCAGGAATTCAGGCCTGCTTT
GAAAGGGCATCTGAATATCAGCTCAATGACTCAGCAGCTTACTACCTTAATGATTTAGAT
AGAATAACAGCATCTGGGTATGTGCCAAATGAACAAGATGTTCTCCATTCTCGAGTGAAA
ACGACTGGAATCATTGAAACTCAATTCTCCTTTAAAGACTTGCACTTCAGGATGTTTGAT
GTAGGTGGACAGAGATCTGAGAGAAAGAAGTGGATTCACTGCTTTGAAGGAGTTACATGC
ATTATATTTTGTGCTGCACTTAGTGCCTATGACATGGTCCTCGTGGAAGACGAAGAAGTG
AATAGAATGCATGAAAGCCTTCACCTGTTCAACAGTATCTGTAATCACAAGTATTTTTCA
ACAACCTCCATTGTCCTGTTCCTCAACAAAAAAGATATCTTTCAAGAAAAGGTAACCAAG
GTGCATCTTAGTATCTGCTTTCCAGAATACACTGGGCCAAATACATTTGAAGATGCAGGA
AACTACATCAAGAACCAGTTTCTAGACCTGAATTTAAAAAAAGAAGATAAGGAAATTTAT
TCCCACATGACCTGTGCTACTGACACCCAAAATGTCAAGTTTGTGTTTGACGCAGTTACA
GATATAATAATCAAAGAGAATCTAAAAGACTGTGGGCTTTTCTAA
Enzyme 85 GenBank Gene ID NM_001102386.1 Link Image
Enzyme 85 GeneCard ID GNAT3 Link Image
Enzyme 85 GenAtlas ID GNAT3 Link Image
Enzyme 85 HGNC ID HGNC:22800 Link Image
Enzyme 85 Chromosome Location 7
Enzyme 85 Locus 7q21.11
Enzyme 85 SNPs SNPJam Report Link Image
Enzyme 85 General References
  1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  2. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Takami S, Getchell TV, McLaughlin SK, Margolskee RF, Getchell ML: Human taste cells express the G protein alpha-gustducin and neuron-specific enolase. Brain Res Mol Brain Res. 1994 Mar;22(1-4):193-203. [PubMed Link Image]
  5. Li X, Staszewski L, Xu H, Durick K, Zoller M, Adler E: Human receptors for sweet and umami taste. Proc Natl Acad Sci U S A. 2002 Apr 2;99(7):4692-6. Epub 2002 Mar 26. [PubMed Link Image]
  6. Rozengurt N, Wu SV, Chen MC, Huang C, Sternini C, Rozengurt E: Colocalization of the alpha-subunit of gustducin with PYY and GLP-1 in L cells of human colon. Am J Physiol Gastrointest Liver Physiol. 2006 Nov;291(5):G792-802. Epub 2006 May 25. [PubMed Link Image]
  7. Fehr J, Meyer D, Widmayer P, Borth HC, Ackermann F, Wilhelm B, Gudermann T, Boekhoff I: Expression of the G-protein alpha-subunit gustducin in mammalian spermatozoa. J Comp Physiol A Neuroethol Sens Neural Behav Physiol. 2007 Jan;193(1):21-34. Epub 2006 Sep 22. [PubMed Link Image]
  8. Jang HJ, Kokrashvili Z, Theodorakis MJ, Carlson OD, Kim BJ, Zhou J, Kim HH, Xu X, Chan SL, Juhaszova M, Bernier M, Mosinger B, Margolskee RF, Egan JM: Gut-expressed gustducin and taste receptors regulate secretion of glucagon-like peptide-1. Proc Natl Acad Sci U S A. 2007 Sep 18;104(38):15069-74. Epub 2007 Aug 27. [PubMed Link Image]
  9. Margolskee RF, Dyer J, Kokrashvili Z, Salmon KS, Ilegems E, Daly K, Maillet EL, Ninomiya Y, Mosinger B, Shirazi-Beechey SP: T1R3 and gustducin in gut sense sugars to regulate expression of Na+-glucose cotransporter 1. Proc Natl Acad Sci U S A. 2007 Sep 18;104(38):15075-80. Epub 2007 Aug 27. [PubMed Link Image]
Enzyme 85 Metabolite References Not Available
Enzyme 86 [top]
Enzyme 86 ID 13664
Enzyme 86 Name Protein phosphatase 1 regulatory subunit 1A
Enzyme 86 Synonyms
  1. Protein phosphatase inhibitor 1
  2. I-1
  3. IPP-1
Enzyme 86 Gene Name PPP1R1A
Enzyme 86 Protein Sequence >Protein phosphatase 1 regulatory subunit 1A
MEQDNSPRKIQFTVPLLEPHLDPEAAEQIRRRRPTPATLVLTSDQSSPEIDEDRIPNPHL
KSTLAMSPRQRKKMTRITPTMKELQMMVEHHLGQQQQGEEPEGAAESTETQESRPPGIPD
TEVESRLGTSGTAKKTAECIPKTHERGSKEPSTKEPSTHIPPLDSKGANSV
Enzyme 86 Number of Residues 171
Enzyme 86 Molecular Weight 19011.2
Enzyme 86 Theoretical pI 6.25
Enzyme 86 GO Classification
Function
  • enzyme inhibitor activity
  • enzyme regulator activity
  • phosphatase inhibitor activity
  • phosphoprotein phosphatase inhibitor activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 86 General Function Involved in phosphoprotein phosphatase inhibitor activity
Enzyme 86 Specific Function Inhibitor of protein-phosphatase 1. This protein may be important in hormonal control of glycogen metabolism. Hormones that elevate intracellular cAMP increase I-1 activity in many tissues. I-1 activation may impose cAMP control over proteins that are not directly phosphorylated by PKA. Following a rise in intracellular calcium, I-1 is inactivated by calcineurin (or PP2B). Does not inhibit type-2 phosphatases
Enzyme 86 Pathways Not Available
Enzyme 86 Reactions Not Available
Enzyme 86 Pfam Domain Function
Enzyme 86 Signals
  • None
Enzyme 86 Transmembrane Regions
  • None
Enzyme 86 Essentiality Not Available
Enzyme 86 GenBank ID Protein 17978643 Link Image
Enzyme 86 UniProtKB/Swiss-Prot ID Q13522 Link Image
Enzyme 86 UniProtKB/Swiss-Prot Entry Name PPR1A_HUMAN Link Image
Enzyme 86 PDB ID Not Available
Enzyme 86 Cellular Location Not Available
Enzyme 86 Gene Sequence >516 bp
ATGGAGCAAGACAACAGCCCCCGAAAGATCCAGTTCACGGTCCCGCTGCTGGAGCCGCAC
CTTGACCCCGAGGCGGCGGAGCAGATTCGGAGGCGCCGCCCCACCCCTGCCACCCTCGTG
CTGACCGGTGACCAGTCATCCCCAGAGATAGATGAAGACCGGATCCCCAACCCACATCTC
AAGTCCACTTTGGCAATGTCTCCACGGCAACGGAAGAAGATGACAAGGATCACACCCACA
ATGAAAGAGCTCCAGATGATGGTTGAACATCACCTGGGGCAACAGCAGCAAGGAGAGGAA
CCTGAGGGGGCCGCTGAGAGCACAGGAACCCAGGAGTCCCGCCCACCTGGGATCCCAGAC
ACAGAAGTGGAGTCAAGGCTGGGCACCTCTGGGACAGCAAAAAAAACTGCAGAATGCATC
CCTAAAACTCATGAAAGAGGCAGTAAGGAACCCAGCACAAAAGAACCCTCAACCCATATA
CCACCACTGGATTCCAAGGGAGCTAACTCGGTCTGA
Enzyme 86 GenBank Gene ID AY063766 Link Image
Enzyme 86 GeneCard ID PPP1R1A Link Image
Enzyme 86 GenAtlas ID PPP1R1A Link Image
Enzyme 86 HGNC ID HGNC:9286 Link Image
Enzyme 86 Chromosome Location 1
Enzyme 86 Locus 12q13.2
Enzyme 86 SNPs SNPJam Report Link Image
Enzyme 86 General References
  1. Endo S, Zhou X, Connor J, Wang B, Shenolikar S: Multiple structural elements define the specificity of recombinant human inhibitor-1 as a protein phosphatase-1 inhibitor. Biochemistry. 1996 Apr 23;35(16):5220-8. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Connor JH, Weiser DC, Li S, Hallenbeck JM, Shenolikar S: Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1. Mol Cell Biol. 2001 Oct;21(20):6841-50. [PubMed Link Image]
Enzyme 86 Metabolite References Not Available
Enzyme 87 [top]
Enzyme 87 ID 13794
Enzyme 87 Name Transient receptor potential cation channel subfamily V member 2
Enzyme 87 Synonyms
  1. TrpV2
  2. Osm-9-like TRP channel 2
  3. OTRPC2
  4. Vanilloid receptor-like protein 1
  5. VRL-1
Enzyme 87 Gene Name TRPV2
Enzyme 87 Protein Sequence >Transient receptor potential cation channel subfamily V member 2
MTSPSSSPVFRLETLDGGQEDGSEADRGKLDFGSGLPPMESQFQGEDRKFAPQIRVNLNY
RKGTGASQPDPNRFDRDRLFNAVSRGVPEDLAGLPEYLSKTSKYLTDSEYTEGSTGKTCL
MKAVLNLKDGVNACILPLLQIDRDSGNPQPLVNAQCTDDYYRGHSALHIAIEKRSLQCVK
LLVENGANVHARACGRFFQKGQGTCFYFGELPLSLAACTKQWDVVSYLLENPHQPASLQA
TDSQGNTVLHALVMISDNSAENIALVTSMYDGLLQAGARLCPTVQLEDIRNLQDLTPLKL
AAKEGKIEIFRHILQREFSGLSHLSRKFTEWCYGPVRVSLYDLASVDSCEENSVLEIIAF
HCKSPHRHRMVVLEPLNKLLQAKWDLLIPKFFLNFLCNLIYMFIFTAVAYHQPTLKKQAA
PHLKAEVGNSMLLTGHILILLGGIYLLVGQLWYFWRRHVFIWISFIDSYFEILFLFQALL
TVVSQVLCFLAIEWYLPLLVSALVLGWLNLLYYTRGFQHTGIYSVMIQKVILRDLLRFLL
IYLVFLFGFAVALVSLSQEAWRPEAPTGPNATESVQPMEGQEDEGNGAQYRGILEASLEL
FKFTIGMGELAFQEQLHFRGMVLLLLLAYVLLTYILLLNMLIALMSETVNSVATDSWSIW
KLQKAISVLEMENGYWWCRKKQRAGVMLTVGTKPDGSPDERWCFRVEEVNWASWEQTLPT
LCEDPSGAGVPRTLENPVLASPPKEDEDGASEENYVPVQLLQSN
Enzyme 87 Number of Residues 764
Enzyme 87 Molecular Weight 85980.3
Enzyme 87 Theoretical pI 5.64
Enzyme 87 GO Classification
Function
  • ion channel activity
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 87 General Function Involved in ion channel activity
Enzyme 87 Specific Function Calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by IGF-I, PDGF and neuropeptide head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH
Enzyme 87 Pathways Not Available
Enzyme 87 Reactions Not Available
Enzyme 87 Pfam Domain Function
Enzyme 87 Signals
  • None
Enzyme 87 Transmembrane Regions
  • 391-411 435-455 472-492 494-514 538-558 622-642
Enzyme 87 Essentiality Not Available
Enzyme 87 GenBank ID Protein Not Available
Enzyme 87 UniProtKB/Swiss-Prot ID Q9Y5S1 Link Image
Enzyme 87 UniProtKB/Swiss-Prot Entry Name TRPV2_HUMAN Link Image
Enzyme 87 PDB ID Not Available
Enzyme 87 Cellular Location Not Available
Enzyme 87 Gene Sequence >2295 bp
ATGACCTCACCCTCCAGCTCTCCAGTTTTCAGGTTGGAGACATTAGATGGAGGCCAAGAA
GATGGCTCTGAGGCGGACAGAGGAAAGCTGGATTTTGGGAGCGGGCTGCCTCCCATGGAG
TCACAGTTCCAGGGCGAGGACCGGAAATTCGCCCCTCAGATAAGAGTCAACCTCAACTAC
CGAAAGGGAACAGGTGCCAGTCAGCCGGATCCAAACCGATTTGACCGAGATCGGCTCTTC
AATGCGGTCTCCCGGGGTGTCCCCGAGGATCTGGCTGGACTTCCAGAGTACCTGAGCAAG
ACCAGCAAGTACCTCACCGACTCGGAATACACAGAGGGCTCCACAGGTAAGACGTGCCTG
ATGAAGGCTGTGCTGAACCTTAAGGACGGAGTCAATGCCTGCATTCTGCCACTGCTGCAG
ATCGACAGGGACTCTGGCAATCCTCAGCCCCTGGTAAATGCCCAGTGCACAGATGACTAT
TACCGAGGCCACAGCGCTCTGCACATCGCCATTGAGAAGAGGAGTCTGCAGTGTGTGAAG
CTCCTGGTGGAGAATGGGGCCAATGTGCATGCCCGGGCCTGCGGCCGCTTCTTCCAGAAG
GGCCAAGGGACTTGCTTTTATTTCGGTGAGCTACCCCTCTCTTTGGCCGCTTGCACCAAG
CAGTGGGATGTGGTAAGCTACCTCCTGGAGAACCCACACCAGCCCGCCAGCCTGCAGGCC
ACTGACTCCCAGGGCAACACAGTCCTGCATGCCCTAGTGATGATCTCGGACAACTCAGCT
GAGAACATTGCACTGGTGACCAGCATGTATGATGGGCTCCTCCAAGCTGGGGCCCGCCTC
TGCCCTACCGTGCAGCTTGAGGACATCCGCAACCTGCAGGATCTCACGCCTCTGAAGCTG
GCCGCCAAGGAGGGCAAGATCGAGATTTTCAGGCACATCCTGCAGCGGGAGTTTTCAGGA
CTGAGCCACCTTTCCCGAAAGTTCACCGAGTGGTGCTATGGGCCTGTCCGGGTGTCGCTG
TATGACCTGGCTTCTGTGGACAGCTGTGAGGAGAACTCAGTGCTGGAGATCATTGCCTTT
CATTGCAAGAGCCCGCACCGACACCGAATGGTCGTTTTGGAGCCCCTGAACAAACTGCTG
CAGGCGAAATGGGATCTGCTCATCCCCAAGTTCTTCTTAAACTTCCTGTGTAATCTGATC
TACATGTTCATCTTCACCGCTGTTGCCTACCATCAGCCTACCCTGAAGAAGCAGGCCGCC
CCTCACCTGAAAGCGGAGGTTGGAAACTCCATGCTGCTGACGGGCCACATCCTTATCCTG
CTAGGGGGGATCTACCTCCTCGTGGGCCAGCTGTGGTACTTCTGGCGGCGCCACGTGTTC
ATCTGGATCTCGTTCATAGACAGCTACTTTGAAATCCTCTTCCTGTTCCAGGCCCTGCTC
ACAGTGGTGTCCCAGGTGCTGTGTTTCCTGGCCATCGAGTGGTACCTGCCCCTGCTTGTG
TCTGCGCTGGTGCTGGGCTGGCTGAACCTGCTTTACTATACACGTGGCTTCCAGCACACA
GGCATCTACAGTGTCATGATCCAGAAGGTCATCCTGCGGGACCTGCTGCGCTTCCTTCTG
ATCTACTTAGTCTTCCTTTTCGGCTTCGCTGTAGCCCTGGTGAGCCTGAGCCAGGAGGCT
TGGCGCCCCGAAGCTCCTACAGGCCCCAATGCCACAGAGTCAGTGCAGCCCATGGAGGGA
CAGGAGGACGAGGGCAACGGGGCCCAGTACAGGGGTATCCTGGAAGCCTCCTTGGAGCTC
TTCAAATTCACCATCGGCATGGGCGAGCTGGCCTTCCAGGAGCAGCTGCACTTCCGCGGC
ATGGTGCTGCTGCTGCTGCTGGCCTACGTGCTGCTCACCTACATCCTGCTGCTCAACATG
CTCATCGCCCTCATGAGCGAGACCGTCAACAGTGTCGCCACTGACAGCTGGAGCATCTGG
AAGCTGCAGAAAGCCATCTCTGTCCTGGAGATGGAGAATGGCTATTGGTGGTGCAGGAAG
AAGCAGCGGGCAGGTGTGATGCTGACCGTTGGCACTAAGCCAGATGGCAGCCCCGATGAG
CGCTGGTGCTTCAGGGTGGAGGAGGTGAACTGGGCTTCATGGGAGCAGACGCTGCCTACG
CTGTGTGAGGACCCGTCAGGGGCAGGTGTCCCTCGAACTCTCGAGAACCCTGTCCTGGCT
TCCCCTCCCAAGGAGGATGAGGATGGTGCCTCTGAGGAAAACTATGTGCCCGTCCAGCTC
CTCCAGTCCAACTGA
Enzyme 87 GenBank Gene ID AF129112 Link Image
Enzyme 87 GeneCard ID TRPV2 Link Image
Enzyme 87 GenAtlas ID TRPV2 Link Image
Enzyme 87 HGNC ID HGNC:18082 Link Image
Enzyme 87 Chromosome Location 1
Enzyme 87 Locus 17p11.2
Enzyme 87 SNPs SNPJam Report Link Image
Enzyme 87 General References
  1. Caterina MJ, Rosen TA, Tominaga M, Brake AJ, Julius D: A capsaicin-receptor homologue with a high threshold for noxious heat. Nature. 1999 Apr 1;398(6726):436-41. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  6. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  7. McCleverty CJ, Koesema E, Patapoutian A, Lesley SA, Kreusch A: Crystal structure of the human TRPV2 channel ankyrin repeat domain. Protein Sci. 2006 Sep;15(9):2201-6. Epub 2006 Aug 1. [PubMed Link Image]
Enzyme 87 Metabolite References Not Available
Enzyme 88 [top]
Enzyme 88 ID 13815
Enzyme 88 Name ATP-binding cassette sub-family C member 11
Enzyme 88 Synonyms
  1. Multidrug resistance-associated protein 8
Enzyme 88 Gene Name ABCC11
Enzyme 88 Protein Sequence >ATP-binding cassette sub-family C member 11
MTRKRTYWVPNSSGGLVNRGIDIGDDMVSGLIYKTYTLQDGPWSQQERNPEAPGRAAVPP
WGKYDAALRTMIPFRPKPRFPAPQPLDNAGLFSYLTVSWLTPLMIQSLRSRLDENTIPPL
SVHDASDKNVQRLHRLWEEEVSRRGIEKASVLLVMLRFQRTRLIFDALLGICFCIASVLG
PILIIPKILEYSEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSS
FAFEKLIQFKSVIHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIG
YTAFIAILCYLLVFPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKP
FAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAVWVLIHTSLKLKLTASMAFSM
LASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQESPVFYVQTLQDPSKALVFEEAT
LSWQQTCPGIVNGALELERNGHASEGMTRPRDALGPEEEGNSLGPELHKINLVVSKGMML
GVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDK
ARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDP
LSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELM
QKKGKYAQLIQKMHKEATSDMLQDTAKIAEKPKVESQALATSLEESLNGNAVPEHQLTQE
EEMEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSS
RESNGTMADLGNIADNPQLSFYQLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLF
NKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSP
YILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTED
FISQFKRLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMA
VNIVLQLASSFQATARIGLETEAQFTAVERILQYMKMCVSEAPLHMEGTSCPQGWPQHGE
IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRIL
IDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAI
SKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTI
REAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFAALMATATSS
LR
Enzyme 88 Number of Residues 1382
Enzyme 88 Molecular Weight 154299.6
Enzyme 88 Theoretical pI 8.15
Enzyme 88 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of substances
  • P-P-bond-hydrolysis-driven transmembrane transporter activity
  • active transmembrane transporter activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside binding
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • primary active transmembrane transporter activity
  • purine nucleoside binding
  • pyrophosphatase activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • transmembrane transport
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 88 General Function Involved in ATP binding
Enzyme 88 Specific Function Participates in physiological processes involving bile acids, conjugated steroids and cyclic nucleotides. Enhances the cellular extrusion of cAMP and cGMP. Stimulates the ATP-dependent uptake of a range of physiological and synthetic lipophilic anions, including the glutathione S-conjugates leukotriene C4 and dinitrophenyl S-glutathione, steroid sulfates such as dehydroepiandrosterone 3-sulfate (DHEAS) and estrone 3-sulfate, glucuronides such as estradiol 17-beta-D-glucuronide (E(2)17betaG), the monoanionic bile acids glycocholate and taurocholate, and methotrexate. Probably functions to secrete earwax
Enzyme 88 Pathways Not Available
Enzyme 88 Reactions Not Available
Enzyme 88 Pfam Domain Function
Enzyme 88 Signals
  • None
Enzyme 88 Transmembrane Regions
  • 164-184 195-215 271-291 297-317 384-404 418-438 807-827 864-884 931-951 1050-1070
Enzyme 88 Essentiality Not Available
Enzyme 88 GenBank ID Protein 15027829 Link Image
Enzyme 88 UniProtKB/Swiss-Prot ID Q96J66 Link Image
Enzyme 88 UniProtKB/Swiss-Prot Entry Name ABCCB_HUMAN Link Image
Enzyme 88 PDB ID Not Available
Enzyme 88 Cellular Location Not Available
Enzyme 88 Gene Sequence >4149 bp
ATGACTAGGAAGAGGACATACTGGGTGCCCAACTCTTCTGGTGGCCTCGTGAATCGTGGC
ATCGACATAGGCGATGACATGGTTTCAGGACTTATTTATAAAACCTATACTCTCCAAGAT
GGCCCCTGGAGTCAGCAAGAGAGAAATCCTGAGGCTCCAGGGAGGGCAGCTGTCCCACCG
TGGGGGAAGTATGATGCTGCCTTGAGAACCATGATTCCCTTCCGTCCCAAGCCGAGGTTT
CCTGCCCCCCAGCCCCTGGACAATGCTGGCCTGTTCTCCTACCTCACCGTGTCATGGCTC
ACCCCGCTCATGATCCAAAGCTTACGGAGTCGCTTAGATGAGAACACCATCCCTCCACTG
TCAGTCCATGATGCCTCAGACAAAAATGTCCAAAGGCTTCACCGCCTTTGGGAAGAAGAA
GTCTCAAGGCGAGGGATTGAAAAAGCTTCAGTGCTTCTGGTGATGCTGAGGTTCCAGAGA
ACAAGGTTGATTTTCGATGCACTTCTGGGCATCTGCTTCTGCATTGCCAGTGTACTCGGG
CCAATATTGATTATACCAAAGATCCTGGAATATTCAGAAGAGCAGTTGGGGAATGTTGTC
CATGGAGTGGGACTCTGCTTTGCCCTTTTTCTCTCCGAATGTGTGAAGTCTCTGAGTTTC
TCCTCCAGTTGGATCATCAACCAACGCACAGCCATCAGGTTCCGAGCAGCTGTTTCCTCC
TTTGCCTTTGAGAAGCTCATCCAATTTAAGTCTGTAATACACATCACCTCAGGAGAGGCC
ATCAGCTTCTTCACCGGTGATGTAAACTACCTGTTTGAAGGGGTGTGCTATGGACCCCTA
GTACTGATCACCTGCGCATCGCTGGTCATCTGCAGCATTTCTTCCTACTTCATTATTGGA
TACACTGCATTTATTGCCATCTTATGCTATCTCCTGGTTTTCCCACTGGCGGTATTCATG
ACAAGAATGGCTGTGAAGGCTCAGCATCACACATCTGAGGTCAGCGACCAGCGCATCCGT
GTGACCAGTGAAGTTCTCACTTGCATTAAGCTGATTAAAATGTACACATGGGAGAAACCA
TTTGCAAAAATCATTGAAGACCTAAGAAGGAAGGAAAGGAAACTATTGGAGAAGTGCGGG
CTTGTCCAGAGCCTGACAAGTATAACCTTGTTCATCATCCCCACAGTGGCCACAGCGGTC
TGGGTTCTCATCCACACATCCTTAAAGCTGAAACTCACAGCGTCAATGGCCTTCAGCATG
CTGGCCTCCTTGAATCTCCTTCGGCTGTCAGTGTTCTTTGTGCCTATTGCAGTCAAAGGT
CTCACGAATTCCAAGTCTGCAGTGATGAGGTTCAAGAAGTTTTTCCTCCAGGAGAGCCCT
GTTTTCTATGTCCAGACATTACAAGACCCCAGCAAAGCTCTGGTCTTTGAGGAGGCCACC
TTGTCATGGCAACAGACCTGTCCCGGGATCGTCAATGGGGCACTGGAGCTGGAGAGGAAC
GGGCATGCTTCTGAGGGGATGACCAGGCCTAGAGATGCCCTCGGGCCAGAGGAAGAAGGG
AACAGCCTGGGCCCAGAGTTGCACAAGATCAACCTGGTGGTGTCCAAGGGGATGATGTTA
GGGGTCTGCGGCAACACGGGGAGTGGTAAGAGCAGCCTGTTGTCAGCCATCCTGGAGGAG
ATGCACTTGCTCGAGGGCTCGGTGGGGGTGCAGGGAAGCCTGGCCTATGTCCCCCAGCAG
GCCTGGATCGTCAGCGGGAACATCAGGGAGAACATCCTCATGGGAGGCGCATATGACAAG
GCCCGATACCTCCAGGTGCTCCACTGCTGCTCCCTGAATCGGGACCTGGAACTTCTGCCC
TTTGGAGACATGACAGAGATTGGAGAGCGGGGCCTCAACCTCTCTGGGGGGCAGAAACAG
AGGATCAGCCTGGCCCGCGCCGTCTATTCCGACCGTCAGATCTACCTGCTGGACGACCCC
CTGTCTGCTGTGGACGCCCACGTGGGGAAGCACATTTTTGAGGAGTGCATTAAGAAGACA
CTCAGGGGGAAGACGGTCGTCCTGGTGACCCACCAGCTGCAGTACTTAGAATTTTGTGGC
CAGATCATTTTGTTGGAAAATGGGAAAATCTGTGAAAATGGAACTCACAGTGAGTTAATG
CAGAAAAAGGGGAAATATGCCCAACTTATCCAGAAGATGCACAAGGAAGCCACTTCGGAC
ATGTTGCAGGACACAGCAAAGATAGCAGAGAAGCCAAAGGTAGAAAGTCAGGCTCTGGCC
ACCTCCCTGGAAGAGTCTCTCAACGGAAATGCTGTGCCGGAGCATCAGCTCACACAGGAG
GAGGAGATGGAAGAAGGCTCCTTGAGTTGGAGGGTCTACCACCACTACATCCAGGCAGCT
GGAGGTTACATGGTCTCTTGCATAATTTTCTTCTTCGTGGTGCTGATCGTCTTCTTAACG
ATCTTCAGCTTCTGGTGGCTGAGCTACTGGTTGGAGCAGGGCTCGGGGACCAATAGCAGC
CGAGAGAGCAATGGAACCATGGCAGACCTGGGCAACATTGCAGACAATCCTCAACTGTCC
TTCTACCAGCTGGTGTACGGGCTCAACGCCCTGCTCCTCATCTGTGTGGGGGTCTGCTCC
TCAGGGATTTTCACCAAAGTCACGAGGAAGGCATCCACGGCCCTGCACAACAAGCTCTTC
AACAAGGTTTTCCGCTGCCCCATGAGTTTCTTTGACACCATCCCAATAGGCCGGCTTTTG
AACTGCTTCGCAGGGGACTTGGAACAGCTGGACCAGCTCTTGCCCATCTTTTCAGAGCAG
TTCCTGGTCCTGTCCTTAATGGTGATCGCCGTCCTGTTGATTGTCAGTGTGCTGTCTCCA
TATATCCTGTTAATGGGAGCCATAATCATGGTTATTTGCTTCATTTATTATATGATGTTC
AAGAAGGCCATCGGTGTGTTCAAGAGACTGGAGAACTATAGCCGGTCTCCTTTATTCTCC
CACATCCTCAATTCTCTGCAAGGCCTGAGCTCCATCCATGTCTATGGAAAAACTGAAGAC
TTCATCAGCCAGTTTAAGAGGCTGACTGATGCGCAGAATAACTACCTGCTGTTGTTTCTA
TCTTCCACACGATGGATGGCATTGAGGCTGGAGATCATGACCAACCTTGTGACCTTGGCT
GTTGCCCTGTTCGTGGCTTTTGGCATTTCCTCCACCCCCTACTCCTTTAAAGTCATGGCT
GTCAACATCGTGCTGCAGCTGGCGTCCAGCTTCCAGGCCACTGCCCGGATTGGCTTGGAG
ACAGAGGCACAGTTCACGGCTGTAGAGAGGATACTGCAGTACATGAAGATGTGTGTCTCG
GAAGCTCCTTTACACATGGAAGGCACAAGTTGTCCCCAGGGGTGGCCACAGCATGGGGAA
ATCATATTTCAGGATTATCACATGAAATACAGAGACAACACACCCACCGTGCTTCACGGC
ATCAACCTGACCATCCGCGGCCACGAAGTGGTGGGCATCGTGGGAAGGACGGGCTCTGGG
AAGTCCTCCTTGGGCATGGCTCTCTTCCGCCTGGTGGAGCCCATGGCAGGCCGGATTCTC
ATTGACGGCGTGGACATTTGCAGCATCGGCCTGGAGGACTTGCGGTCCAAGCTCTCAGTG
ATCCCTCAAGATCCAGTGCTGCTCTCAGGAACCATCAGATTCAACCTAGATCCCTTTGAC
CGTCACACTGACCAGCAGATCTGGGATGCCTTGGAGAGGACATTCCTGACCAAGGCCATC
TCAAAGTTCCCCAAAAAGCTGCATACAGATGTGGTGGAAAACGGTGGAAACTTCTCTGTG
GGGGAGAGGCAGCTGCTCTGCATTGCCAGGGCTGTGCTTCGCAACTCCAAGATCATCCTT
ATCGATGAAGCCACAGCCTCCATTGACATGGAGACAGACACCCTGATCCAGCGCACAATC
CGTGAAGCCTTCCAGGGCTGCACCGTGCTCGTCATTGCCCACCGTGTCACCACTGTGCTG
AACTGTGACCACATCCTGGTTATGGGCAATGGGAAGGTGGTAGAATTTGATCGGCCGGAG
GTACTGCGGAAGAAGCCTGGGTCATTGTTCGCAGCCCTCATGGCCACAGCCACTTCTTCA
CTGAGATAA
Enzyme 88 GenBank Gene ID AY040219 Link Image
Enzyme 88 GeneCard ID ABCC11 Link Image
Enzyme 88 GenAtlas ID ABCC11 Link Image
Enzyme 88 HGNC ID HGNC:14639 Link Image
Enzyme 88 Chromosome Location 1
Enzyme 88 Locus 16q12.1
Enzyme 88 SNPs SNPJam Report Link Image
Enzyme 88 General References
  1. Tammur J, Prades C, Arnould I, Rzhetsky A, Hutchinson A, Adachi M, Schuetz JD, Swoboda KJ, Ptacek LJ, Rosier M, Dean M, Allikmets R: Two new genes from the human ATP-binding cassette transporter superfamily, ABCC11 and ABCC12, tandemly duplicated on chromosome 16q12. Gene. 2001 Jul 25;273(1):89-96. [PubMed Link Image]
  2. Yabuuchi H, Shimizu H, Takayanagi S, Ishikawa T: Multiple splicing variants of two new human ATP-binding cassette transporters, ABCC11 and ABCC12. Biochem Biophys Res Commun. 2001 Nov 9;288(4):933-9. [PubMed Link Image]
  3. Bera TK, Lee S, Salvatore G, Lee B, Pastan I: MRP8, a new member of ABC transporter superfamily, identified by EST database mining and gene prediction program, is highly expressed in breast cancer. Mol Med. 2001 Aug;7(8):509-16. [PubMed Link Image]
  4. Guo Y, Kotova E, Chen ZS, Lee K, Hopper-Borge E, Belinsky MG, Kruh GD: MRP8, ATP-binding cassette C11 (ABCC11), is a cyclic nucleotide efflux pump and a resistance factor for fluoropyrimidines 2',3'-dideoxycytidine and 9'-(2'-phosphonylmethoxyethyl)adenine. J Biol Chem. 2003 Aug 8;278(32):29509-14. Epub 2003 May 22. [PubMed Link Image]
  5. Chen ZS, Guo Y, Belinsky MG, Kotova E, Kruh GD: Transport of bile acids, sulfated steroids, estradiol 17-beta-D-glucuronide, and leukotriene C4 by human multidrug resistance protein 8 (ABCC11). Mol Pharmacol. 2005 Feb;67(2):545-57. Epub 2004 Nov 10. [PubMed Link Image]
  6. Yoshiura K, Kinoshita A, Ishida T, Ninokata A, Ishikawa T, Kaname T, Bannai M, Tokunaga K, Sonoda S, Komaki R, Ihara M, Saenko VA, Alipov GK, Sekine I, Komatsu K, Takahashi H, Nakashima M, Sosonkina N, Mapendano CK, Ghadami M, Nomura M, Liang DS, Miwa N, Kim DK, Garidkhuu A, Natsume N, Ohta T, Tomita H, Kaneko A, Kikuchi M, Russomando G, Hirayama K, Ishibashi M, Takahashi A, Saitou N, Murray JC, Saito S, Nakamura Y, Niikawa N: A SNP in the ABCC11 gene is the determinant of human earwax type. Nat Genet. 2006 Mar;38(3):324-30. Epub 2006 Jan 29. [PubMed Link Image]
Enzyme 88 Metabolite References Not Available
Enzyme 89 [top]
Enzyme 89 ID 13816
Enzyme 89 Name ADM2
Enzyme 89 Synonyms
  1. Intermedin
  2. Adrenomedullin-2
  3. AM2
  4. Intermedin-long
  5. IMDL
  6. Intermedin-short
  7. IMDS
Enzyme 89 Gene Name ADM2
Enzyme 89 Protein Sequence >ADM2
MARIPTAALGCISLLCLQLPGSLSRSLGGDPRPVKPREPPARSPSSSLQPRHPAPRPVVW
KLHRALQAQRGAGLAPVMGQPLRDGGRQHSGPRRHSGPRRTQAQLLRVGCVLGTCQVQNL
SHRLWQLMGPAGRQDSAPVDPSSPHSYG
Enzyme 89 Number of Residues 148
Enzyme 89 Molecular Weight 15865.2
Enzyme 89 Theoretical pI 12.31
Enzyme 89 GO Classification
Function
  • binding
  • hormone activity
  • protein binding
  • receptor binding
Process
Component
  • extracellular region
Enzyme 89 General Function Involved in hormone activity
Enzyme 89 Specific Function IMDL and IMDS may play a role as physiological regulators of gastrointestinal, cardiovascular bioactivities mediated by the CALCRL/RAMPs receptor complexes. Activates the cAMP-dependent pathway
Enzyme 89 Pathways Not Available
Enzyme 89 Reactions Not Available
Enzyme 89 Pfam Domain Function
Enzyme 89 Signals
  • 1-24
Enzyme 89 Transmembrane Regions
  • None
Enzyme 89 Essentiality Not Available
Enzyme 89 GenBank ID Protein 41016726 Link Image
Enzyme 89 UniProtKB/Swiss-Prot ID Q7Z4H4 Link Image
Enzyme 89 UniProtKB/Swiss-Prot Entry Name ADM2_HUMAN Link Image
Enzyme 89 PDB ID Not Available
Enzyme 89 Cellular Location Not Available
Enzyme 89 Gene Sequence >447 bp
ATGGCCCGGATCCCGACGGCCGCCCTGGGTTGCATCAGCCTCCTCTGCCTGCAGCTCCCT
GGCTCGCTGTCCCGCAGCCTGGGCGGGGACCCGCGACCCGTCAAACCCAGGGAGCCCCCA
GCCCGGAGCCCTTCCAGCAGCCTGCAGCCCAGGCACCCCGCACCCCGACCTGTGGTCTGG
AAGCTTCACCGGGCCCTCCAGGCACAGAGGGGTGCCGGCCTGGCCCCTGTTATGGGTCAG
CCTCTCCGGGATGGTGGCCGCCAACACTCGGGCCCCCGAAGACACTCGGGCCCCCGCAGG
ACCCAAGCCCAGCTCCTGCGAGTGGGCTGTGTGCTGGGCACCTGCCAGGTGCAGAATCTC
AGCCACCGCCTGTGGCAACTCATGGGACCGGCCGGCCGGCAGGACTCAGCTCCTGTGGAC
CCCAGCAGCCCCCACAGCTATGGCTGA
Enzyme 89 GenBank Gene ID AB121034 Link Image
Enzyme 89 GeneCard ID ADM2 Link Image
Enzyme 89 GenAtlas ID ADM2 Link Image
Enzyme 89 HGNC ID HGNC:28898 Link Image
Enzyme 89 Chromosome Location 2
Enzyme 89 Locus 22q13.33
Enzyme 89 SNPs SNPJam Report Link Image
Enzyme 89 General References
  1. Roh J, Chang CL, Bhalla A, Klein C, Hsu SY: Intermedin is a calcitonin/calcitonin gene-related peptide family peptide acting through the calcitonin receptor-like receptor/receptor activity-modifying protein receptor complexes. J Biol Chem. 2004 Feb 20;279(8):7264-74. Epub 2003 Nov 13. [PubMed Link Image]
  2. Takei Y, Inoue K, Ogoshi M, Kawahara T, Bannai H, Miyano S: Identification of novel adrenomedullin in mammals: a potent cardiovascular and renal regulator. FEBS Lett. 2004 Jan 2;556(1-3):53-8. [PubMed Link Image]
  3. Takahashi K, Kikuchi K, Maruyama Y, Urabe T, Nakajima K, Sasano H, Imai Y, Murakami O, Totsune K: Immunocytochemical localization of adrenomedullin 2/intermedin-like immunoreactivity in human hypothalamus, heart and kidney. Peptides. 2006 Jun;27(6):1383-9. Epub 2005 Dec 15. [PubMed Link Image]
  4. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 89 Metabolite References Not Available
Enzyme 90 [top]
Enzyme 90 ID 13817
Enzyme 90 Name A-kinase anchor protein 7 isoform gamma
Enzyme 90 Synonyms
  1. AKAP-7 isoform gamma
  2. A-kinase anchor protein 18 kDa
  3. AKAP 18
  4. Protein kinase A-anchoring protein 7 isoform gamma
Enzyme 90 Gene Name AKAP7
Enzyme 90 Protein Sequence >A-kinase anchor protein 7 isoform gamma
MSEEFEANTMDSLVDMPFATVDIQDDCGITDEPQINLKRSQENEWVKSDQVKKRKKKRKD
YQPNYFLSIPITNKEIIKGIKILQNAIIQQDERLAKAMVSDGSFHITLLVMQLLNEDEVN
IGIDALLELKPFIEELLQGKHLTLPFQGIGTFGNQVGFVKLAEGDHVNSLLEIAETANRT
FQEKGILVGESRSFKPHLTFMKLSKSPWLRKNGVKKIDPDLYEKFISHRFGEEILYRIDL
CSMLKKKQSNGYYHCESSIVIGEKNGGEPDDAELVRLSKRLVENAVLKAVQQYLEETQNK
NKPGEGSSVKTEAADQNGNDNENNRK
Enzyme 90 Number of Residues 326
Enzyme 90 Molecular Weight 37058.9
Enzyme 90 Theoretical pI 5.76
Enzyme 90 GO Classification
Function
  • catalytic activity
Process
  • RNA metabolic process
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
Component
  • cell part
  • intracellular
Enzyme 90 General Function Involved in catalytic activity
Enzyme 90 Specific Function Probably targets cAMP-dependent protein kinase (PKA) to the cellular membrane or cytoskeletal structures
Enzyme 90 Pathways Not Available
Enzyme 90 Reactions Not Available
Enzyme 90 Pfam Domain Function
Enzyme 90 Signals
  • None
Enzyme 90 Transmembrane Regions
  • None
Enzyme 90 Essentiality Not Available
Enzyme 90 GenBank ID Protein 6759917 Link Image
Enzyme 90 UniProtKB/Swiss-Prot ID Q9P0M2 Link Image
Enzyme 90 UniProtKB/Swiss-Prot Entry Name AKA7G_HUMAN Link Image
Enzyme 90 PDB ID Not Available
Enzyme 90 Cellular Location Not Available
Enzyme 90 Gene Sequence >981 bp
ATGTCAGAGGAATTTGAAGCCAATACTATGGATTCTCTGGTAGACATGCCATTTGCTACT
GTAGATATTCAGGATGACTGTGGAATCACTGATGAACCTCAAATAAATTTGAAGAGAAGT
CAAGAAAATGAATGGGTCAAGAGTGATCAAGTAAAGAAGAGGAAAAAAAAGAGAAAAGAT
TATCAACCCAACTATTTCCTGTCCATTCCAATCACCAACAAAGAGATTATAAAAGGAATT
AAGATCCTGCAGAATGCAATAATACAACAAGATGAGCGACTGGCCAAAGCAATGGTCAGT
GATGGTTCCTTTCATATTACCCTGCTGGTGATGCAATTATTAAATGAAGATGAAGTAAAC
ATTGGTATTGATGCTCTTTTGGAATTGAAACCATTCATAGAAGAACTCCTCCAGGGAAAA
CATTTGACTTTGCCCTTTCAAGGGATTGGTACTTTTGGAAATCAGGTTGGATTTGTGAAG
CTGGCAGAAGGAGATCATGTAAACTCACTTTTGGAGATAGCAGAGACTGCAAATAGGACA
TTTCAAGAAAAAGGCATCCTGGTAGGAGAGAGCAGAAGTTTTAAACCTCATTTGACCTTC
ATGAAGTTGTCAAAATCACCGTGGCTCCGTAAGAATGGAGTGAAAAAAATAGATCCTGAT
TTATATGAAAAGTTTATCAGTCACAGATTTGGAGAAGAAATATTATATCGCATAGATCTT
TGCTCCATGCTGAAGAAAAAACAAAGTAATGGTTATTATCACTGTGAATCTTCCATTGTG
ATTGGTGAAAAGAACGGAGGGGAGCCCGATGACGCTGAACTAGTAAGGCTCAGTAAGAGG
CTGGTGGAGAACGCGGTGCTCAAGGCTGTCCAGCAGTATCTGGAGGAAACACAGAATAAA
AACAAGCCGGGGGAGGGGAGCTCTGTGAAAACCGAAGCAGCTGATCAGAATGGCAATGAC
AATGAGAACAACAGGAAATGA
Enzyme 90 GenBank Gene ID AF152929 Link Image
Enzyme 90 GeneCard ID AKAP7 Link Image
Enzyme 90 GenAtlas ID AKAP7 Link Image
Enzyme 90 HGNC ID HGNC:377 Link Image
Enzyme 90 Chromosome Location 6
Enzyme 90 Locus 6q23
Enzyme 90 SNPs SNPJam Report Link Image
Enzyme 90 General References
  1. Trotter KW, Fraser ID, Scott GK, Stutts MJ, Scott JD, Milgram SL: Alternative splicing regulates the subcellular localization of A-kinase anchoring protein 18 isoforms. J Cell Biol. 1999 Dec 27;147(7):1481-92. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 90 Metabolite References Not Available
Enzyme 91 [top]
Enzyme 91 ID 13818
Enzyme 91 Name A-kinase anchor protein 2
Enzyme 91 Synonyms
  1. AKAP-2
  2. AKAP-KL
  3. Protein kinase A-anchoring protein 2
  4. PRKA2
Enzyme 91 Gene Name AKAP2
Enzyme 91 Protein Sequence >A-kinase anchor protein 2
MEIEVSVAECKSVPGITSTPHPMDHPSAFYSPPHNGLLTDHHESLDNDVAREIRYLDEVL
EANCCDSAVDGTYNGTSSPEPGAVVLVGGLSPPVHEATQPEPTERTASRQAPPHIELSNS
SPDPMAEAERTNGHSPSQPRDALGDSLQVPVSPSSTTSSRCSSRDGEFTLTTLKKEAKFE
LRAFHEDKKPSKLFEDDEHEKEQYCIRKVRPSEEMLELEKERRELIRSQAVKKNPGIAAK
WWNPPQEKTIEEQLDEEHLESHKKYKERKERRAQQEQLLLQKQLQQQQQQPPSQLCTAPA
SSHERASMIDKAKEDIVTEQIDFSAARKQFQLMENSRQAVAKGQSTPRLFSIKPFYRPLG
SVNSDKPLTNPRPPSVGGPPEDSGASAAKGQKSPGALETPSAAGSQGNTASQGKEGPYSE
PSKRGPLSKLWAEDGEFTSARAVLTVVKDDDHGILDQFSRSVNVSLTQEELDSGLDELSV
RSQDTTVLETLSNDFSMDNISDSGASNETTNALQENSLADFSLPQTPQTDNPSEGRGEGV
SKSFSDHGFYSPSSTLGDSPLVDDPLEYQAGLLVQNAIQQAIAEQVDKAVSKTSRDGAEQ
QGPEATVEEAEAAAFGSEKPQSMFEPPQVSSPVQEKRDVLPKILPAEDRALRERGPPQPL
PAVQPSGPINMEETRPEGSYFSKYSEAAELRSTASLLATQESDVMVGPFKLRSRKQRTLS
MIEEEIRAAQEREEELKRQRQVLQSTQSPRTKNAPSLPSRTCYKTAPGKIEKVKPPPSPT
TEGPSLQPDLAPEEAAGTQRPKNLMQTLMEDYETHKSKRRERMDDSSVLEATRVNRRKSA
LALRWEAGIYANQEEEDNE
Enzyme 91 Number of Residues 859
Enzyme 91 Molecular Weight 94659.7
Enzyme 91 Theoretical pI 4.76
Enzyme 91 GO Classification Not Available
Enzyme 91 General Function Involved in enzyme binding
Enzyme 91 Specific Function Binds to regulatory subunit (RII) of protein kinase A. May be involved in establishing polarity in signaling systems or in integrating PKA-RII isoforms with downstream effectors to capture, amplify and focus diffuse, trans-cellular signals carried by cAMP
Enzyme 91 Pathways Not Available
Enzyme 91 Reactions Not Available
Enzyme 91 Pfam Domain Function
Enzyme 91 Signals
  • None
Enzyme 91 Transmembrane Regions
  • None
Enzyme 91 Essentiality Not Available
Enzyme 91 GenBank ID Protein 194390790 Link Image
Enzyme 91 UniProtKB/Swiss-Prot ID Q9Y2D5 Link Image
Enzyme 91 UniProtKB/Swiss-Prot Entry Name AKAP2_HUMAN Link Image
Enzyme 91 PDB ID Not Available
Enzyme 91 Cellular Location Not Available
Enzyme 91 Gene Sequence >2580 bp
ATGGAAATTGAGGTGTCTGTTGCAGAATGTAAAAGTGTTCCTGGAATCACCTCTACCCCA
CATCCCATGGACCATCCCTCCGCTTTCTATTCACCCCCGCATAATGGCCTCCTTACTGAT
CACCACGAATCCCTGGATAATGATGTTGCCAGAGAGATCCGCTATCTAGATGAGGTGCTA
GAGGCCAACTGCTGTGATTCTGCTGTGGATGGAACGTACAATGGAACATCCTCCCCAGAG
CCTGGTGCAGTGGTTCTGGTGGGCGGCCTAAGCCCCCCTGTCCACGAGGCGACCCAGCCA
GAACCCACTGAAAGAACAGCTAGCCGGCAGGCACCTCCTCACATCGAGCTCAGTAATAGC
AGCCCTGACCCCATGGCAGAGGCAGAAAGAACAAATGGCCATTCCCCCAGCCAGCCTAGA
GATGCGCTGGGGGACAGCCTGCAGGTGCCTGTCAGCCCCAGCTCCACAACCAGCTCACGG
TGTTCTTCCCGAGATGGAGAGTTCACTCTCACCACACTGAAAAAGGAGGCCAAGTTTGAG
CTGCGTGCCTTCCATGAGGACAAGAAGCCCTCCAAGCTCTTTGAGGATGACGAGCATGAG
AAAGAACAATACTGCATTAGAAAAGTGAGGCCTTCAGAGGAGATGCTGGAGCTGGAAAAG
GAGAGGAGAGAGCTCATCCGCAGCCAGGCCGTCAAGAAGAATCCTGGCATTGCAGCAAAA
TGGTGGAATCCCCCGCAGGAAAAAACCATCGAGGAGCAGCTGGACGAGGAACATCTGGAG
TCGCACAAAAAGTACAAGGAGCGCAAAGAGAGAAGGGCACAGCAGGAACAGTTGCTGCTG
CAGCAGCAGTTACAGCAGCAGCAGCAGCAGCCCCCATCGCAGCTCTGCACAGCCCCTGCC
TCTTCTCATGAACGCGCAAGCATGATTGACAAAGCAAAGGAGGACATTGTCACAGAGCAG
ATAGATTTCTCTGCTGCTCGCAAACAATTTCAGCTGATGGAGAATTCCAGGCAAGCGGTG
GCCAAGGGCCAGAGTACACCCAGGCTGTTCTCCATCAAGCCTTTCTACAGGCCTCTGGGG
TCAGTCAACTCAGACAAGCCACTGACTAATCCGAGACCACCTTCTGTCGGGGGACCTCCA
GAAGACAGTGGTGCCTCAGCCGCCAAGGGACAGAAATCCCCCGGTGCCCTGGAGACCCCA
TCGGCAGCAGGAAGCCAGGGCAACACAGCCTCTCAGGGGAAGGAAGGGCCCTACAGCGAG
CCTTCTAAACGTGGGCCCTTATCTAAACTGTGGGCTGAGGATGGAGAATTTACGAGCGCC
CGGGCTGTCCTCACTGTGGTCAAGGATGATGACCATGGGATTTTGGATCAGTTCTCAAGA
TCTGTCAATGTCTCCTTGACCCAAGAGGAGCTTGACTCTGGTCTGGACGAATTGTCGGTG
AGGTCTCAGGATACCACAGTCCTGGAGACCCTATCCAATGATTTCAGCATGGACAACATC
AGTGACAGCGGGGCATCCAATGAGACAACCAATGCCCTCCAGGAAAATTCACTGGCTGAT
TTTTCTCTGCCCCAGACACCACAAACTGACAACCCCTCAGAGGGCCGAGGAGAAGGCGTC
TCCAAGTCATTTAGTGATCATGGTTTCTATTCCCCTTCCTCCACGCTGGGGGACTCTCCG
TTGGTTGATGACCCCTTGGAGTATCAGGCTGGCCTCCTGGTGCAGAATGCCATTCAACAA
GCCATAGCCGAGCAGGTGGATAAAGCTGTGTCCAAAACCAGCAGGGATGGAGCAGAGCAA
CAGGGACCTGAAGCGACTGTAGAGGAAGCTGAAGCTGCGGCTTTCGGCTCAGAAAAGCCT
CAGAGCATGTTTGAGCCACCTCAGGTGTCTTCTCCTGTTCAAGAGAAAAGGGATGTATTA
CCAAAGATTCTGCCTGCTGAAGACAGGGCGCTCAGGGAAAGGGGGCCCCCCCAGCCACTG
CCAGCTGTGCAGCCCAGTGGCCCGATTAACATGGAGGAGACCAGGCCCGAAGGAAGCTAT
TTCAGCAAGTACTCGGAGGCAGCTGAGCTGAGAAGCACAGCCTCCCTCCTGGCCACTCAA
GAATCTGACGTGATGGTTGGGCCTTTCAAGCTGAGGTCCAGGAAACAGCGGACTTTGTCC
ATGATTGAGGAAGAGATCCGAGCAGCTCAGGAAAGGGAAGAGGAGCTGAAGAGGCAGAGA
CAAGTCTTGCAGAGTACGCAGAGCCCCAGGACAAAGAATGCCCCATCGCTGCCCTCCAGA
ACATGCTACAAAACTGCTCCAGGGAAAATAGAGAAAGTCAAACCTCCTCCATCCCCCACC
ACTGAAGGCCCCAGCTTGCAGCCTGACTTAGCCCCTGAAGAGGCTGCCGGAACCCAGCGG
CCCAAGAATCTGATGCAGACCCTCATGGAAGACTATGAGACACACAAATCTAAAAGGCGC
GAGAGAATGGATGATAGTAGTGTCCTCGAGGCCACACGGGTTAATCGAAGAAAGAGCGCA
CTGGCTTTGCGCTGGGAAGCAGGGATCTATGCCAACCAGGAGGAAGAAGACAACGAATAA
Enzyme 91 GenBank Gene ID AK300427 Link Image
Enzyme 91 GeneCard ID AKAP2 Link Image
Enzyme 91 GenAtlas ID AKAP2 Link Image
Enzyme 91 HGNC ID HGNC:372 Link Image
Enzyme 91 Chromosome Location 9
Enzyme 91 Locus 9q31.3
Enzyme 91 SNPs SNPJam Report Link Image
Enzyme 91 General References
  1. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Hu B, Copeland NG, Gilbert DJ, Jenkins NA, Kilimann MW: The paralemmin protein family: identification of paralemmin-2, an isoform differentially spliced to AKAP2/AKAP-KL, and of palmdelphin, a more distant cytosolic relative. Biochem Biophys Res Commun. 2001 Aug 3;285(5):1369-76. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  9. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  12. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 91 Metabolite References Not Available
Enzyme 92 [top]
Enzyme 92 ID 13819
Enzyme 92 Name A-kinase anchor protein 5
Enzyme 92 Synonyms
  1. AKAP-5
  2. A-kinase anchor protein 79 kDa
  3. AKAP 79
  4. H21
  5. cAMP-dependent protein kinase regulatory subunit II high affinity-binding protein
Enzyme 92 Gene Name AKAP5
Enzyme 92 Protein Sequence >A-kinase anchor protein 5
METTISEIHVENKDEKRSAEGSPGAERQKEKASMLCFKRRKKAAKALKPKAGSEAADVAR
KCPQEAGASDQPEPTRGAWASLKRLVTRRKRSESSKQQKPLEGEMQPAINAEDADLSKKK
AKSRLKIPCIKFPRGPKRSNHSKIIEDSDCSIKVQEEAEILDIQTQTPLNDQATKAKSTQ
DLSEGISRKDGDEVCESNVSNSTTSGEKVISVELGLDNGHSAIQTGTLILEEIETIKEKQ
DVQPQQASPLETSETDHQQPVLSDVPPLPAIPDQQIVEEASNSTLESAPNGKDYESTEIV
AEETKPKDTELSQESDFKENGITEEKSKSEESKRMEPIAIIITDTEISEFDVTKSKNVPK
QFLISAENEQVGVFANDNGFEDRTSEQYETLLIETASSLVKNAIQLSIEQLVNEMASDDN
KINNLLQ
Enzyme 92 Number of Residues 427
Enzyme 92 Molecular Weight 47087.8
Enzyme 92 Theoretical pI 4.58
Enzyme 92 GO Classification
Function
  • binding
  • protein binding
Process
  • biological regulation
  • establishment of localization
  • intracellular protein transport
  • protein targeting
  • protein transport
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • transport
Component
Enzyme 92 General Function Involved in protein binding
Enzyme 92 Specific Function May anchor the PKA protein to cytoskeletal and/or organelle-associated proteins, targeting the signal carried by cAMP to specific intracellular effectors. Association with to the beta2-adrenergic receptor (beta2-AR) not only regulates beta2-AR signaling pathway, but also the activation by PKA by switching off the beta2-AR signaling cascade
Enzyme 92 Pathways Not Available
Enzyme 92 Reactions Not Available
Enzyme 92 Pfam Domain Function
Enzyme 92 Signals
  • None
Enzyme 92 Transmembrane Regions
  • None
Enzyme 92 Essentiality Not Available
Enzyme 92 GenBank ID Protein 158187521 Link Image
Enzyme 92 UniProtKB/Swiss-Prot ID P24588 Link Image
Enzyme 92 UniProtKB/Swiss-Prot Entry Name AKAP5_HUMAN Link Image
Enzyme 92 PDB ID Not Available
Enzyme 92 Cellular Location Not Available
Enzyme 92 Gene Sequence >1284 bp
ATGGAAACCACAATTTCAGAAATTCATGTAGAAAACAAGGATGAGAAGAGATCAGCAGAA
GGTAGTCCTGGGGCTGAAAGGCAGAAGGAAAAGGCATCCATGCTTTGCTTCAAGAGAAGA
AAGAAAGCAGCCAAAGCACTGAAGCCCAAAGCTGGCTCTGAAGCTGCTGATGTGGCAAGG
AAGTGTCCACAAGAAGCAGGAGCTTCTGATCAGCCAGAGCCCACACGGGGGGCCTGGGCC
TCACTCAAACGTCTTGTAACACGCAGGAAAAGGTCAGAGTCTTCAAAGCAGCAAAAGCCA
TTGGAGGGTGAAATGCAACCTGCAATAAATGCTGAGGATGCTGATCTTTCTAAGAAAAAG
GCAAAATCTAGACTTAAGATTCCCTGCATAAAATTCCCAAGAGGGCCAAAAAGGAGTAAT
CATTCCAAAATTATAGAAGACTCAGACTGCAGCATCAAAGTCCAGGAAGAAGCTGAAATT
TTGGATATACAAACACAGACCCCATTGAATGATCAGGCAACAAAGGCTAAGTCAACCCAG
GATCTAAGTGAAGGCATCTCACGGAAAGATGGTGATGAGGTCTGTGAATCAAATGTGAGC
AATAGCACAACTTCTGGAGAGAAAGTGATTTCAGTAGAACTTGGATTAGATAATGGGCAT
TCTGCTATTCAAACGGGAACTCTAATCCTTGAAGAAATTGAAACGATCAAGGAAAAACAA
GATGTTCAACCCCAGCAAGCAAGCCCACTTGAAACTTCAGAAACAGACCATCAGCAGCCA
GTACTTTCTGATGTTCCTCCTTTACCTGCAATTCCAGATCAACAAATTGTGGAAGAAGCC
AGTAACAGTACCCTAGAAAGTGCACCAAATGGAAAAGACTATGAAAGTACAGAGATTGTA
GCTGAAGAAACTAAGCCAAAAGATACTGAATTGAGCCAAGAATCAGATTTTAAAGAAAAT
GGGATCACTGAAGAGAAATCCAAATCAGAAGAAAGCAAAAGAATGGAGCCAATTGCTATT
ATTATTACAGACACTGAAATCAGTGAATTTGATGTTACAAAATCTAAAAATGTCCCTAAG
CAATTCTTAATTTCAGCTGAAAATGAGCAAGTAGGGGTTTTTGCTAATGATAATGGTTTT
GAGGATAGAACTTCAGAACAATATGAAACACTCTTAATTGAAACAGCCTCTTCTCTAGTC
AAGAATGCTATTCAGTTGTCAATAGAACAGCTGGTTAATGAAATGGCCTCTGATGATAAT
AAAATAAACAATCTTCTACAGTGA
Enzyme 92 GenBank Gene ID NM_004857.3 Link Image
Enzyme 92 GeneCard ID AKAP5 Link Image
Enzyme 92 GenAtlas ID AKAP5 Link Image
Enzyme 92 HGNC ID HGNC:375 Link Image
Enzyme 92 Chromosome Location 1
Enzyme 92 Locus 14q21-q24
Enzyme 92 SNPs SNPJam Report Link Image
Enzyme 92 General References
  1. Carr DW, Stofko-Hahn RE, Fraser ID, Cone RD, Scott JD: Localization of the cAMP-dependent protein kinase to the postsynaptic densities by A-kinase anchoring proteins. Characterization of AKAP 79. J Biol Chem. 1992 Aug 25;267(24):16816-23. [PubMed Link Image]
  2. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  3. Hirsch AH, Glantz SB, Li Y, You Y, Rubin CS: Cloning and expression of an intron-less gene for AKAP 75, an anchor protein for the regulatory subunit of cAMP-dependent protein kinase II beta. J Biol Chem. 1992 Feb 5;267(4):2131-4. [PubMed Link Image]
Enzyme 92 Metabolite References Not Available
Enzyme 93 [top]
Enzyme 93 ID 13820
Enzyme 93 Name A-kinase anchor protein 8
Enzyme 93 Synonyms
  1. AKAP-8
  2. A-kinase anchor protein 95 kDa
  3. AKAP 95
Enzyme 93 Gene Name AKAP8
Enzyme 93 Protein Sequence >A-kinase anchor protein 8
MDQGYGGYGAWSAGPANTQGAYGTGVASWQGYENYNYYGAQNTSVTTGATYSYGPASWEA
AKANDGGLAAGAPAMHMASYGPEPCTDNSDSLIAKINQRLDMMSKEGGRGGSGGGGEGIQ
DRESSFRFQPFESYDSRPCLPEHNPYRPSYSYDYEFDLGSDRNGSFGGQYSECRDPARER
GSLDGFMRGRGQGRFQDRSNPGTFMRSDPFVPPAASSEPLSTPWNELNYVGGRGLGGPSP
SRPPPSLFSQSMAPDYGVMGMQGAGGYDSTMPYGCGRSQPRMRDRDRPKRRGFDRFGPDG
TGRKRKQFQLYEEPDTKLARVDSEGDFSENDDAAGDFRSGDEEFKGEDELCDSGRQRGEK
EDEDEDVKKRREKQRRRDRTRDRAADRIQFACSVCKFRSFDDEEIQKHLQSKFHKETLRF
ISTKLPDKTVEFLQEYIVNRNKKIEKRRQELMEKETAKPKPDPFKGIGQEHFFKKIEAAH
CLACDMLIPAQPQLLQRHLHSVDHNHNRRLAAEQFKKTSLHVAKSVLNNRHIVKMLEKYL
KGEDPFTSETVDPEMEGDDNLGGEDKKETPEEVAADVLAEVITAAVRAVDGEGAPAPESS
GEPAEDEGPTDTAEAGSDPQAEQLLEEQVPCGTAHEKGVPKARSEAAEAGNGAETMAAEA
ESAQTRVAPAPAAADAEVEQTDAESKDAVPTE
Enzyme 93 Number of Residues 692
Enzyme 93 Molecular Weight 76107.7
Enzyme 93 Theoretical pI 4.77
Enzyme 93 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • nucleic acid binding
  • transition metal ion binding
  • zinc ion binding
Process
Component
  • cell part
  • intracellular
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 93 General Function Involved in DNA binding
Enzyme 93 Specific Function Anchoring protein that mediates the subcellular compartmentation of cAMP-dependent protein kinase (PKA type II)
Enzyme 93 Pathways Not Available
Enzyme 93 Reactions Not Available
Enzyme 93 Pfam Domain Function
Enzyme 93 Signals
  • None
Enzyme 93 Transmembrane Regions
  • None
Enzyme 93 Essentiality Not Available
Enzyme 93 GenBank ID Protein 3702291 Link Image
Enzyme 93 UniProtKB/Swiss-Prot ID O43823 Link Image
Enzyme 93 UniProtKB/Swiss-Prot Entry Name AKAP8_HUMAN Link Image
Enzyme 93 PDB ID Not Available
Enzyme 93 Cellular Location Not Available
Enzyme 93 Gene Sequence >2079 bp
ATGGACCAGGGCTACGGAGGCTACGGGGCGTGGAGTGCTGGACCTGCCAACACCCAGGGT
GCATATGGAACTGGTGTGGCCAGCTGGCAAGGTTATGAAAACTACAATTACTATGGCGCC
CAGAACACCAGTGTCACCACAGGCGCAACCTACAGCTACGGCCCAGCCTCGTGGGAGGCC
GCCAAGGCCAATGATGGCGGCCTGGCGGCCGGGGCCCCTGCCATGCACATGGCCTCTTAC
GGCCCAGAGCCATGCACCGACAATTCCGACTCCCTCATTGCCAAGATCAACCAGCGTTTG
GACATGATGTCCAAGGAAGGAGGCAGGGGCGGGAGCGGCGGCGGTGGGGAGGGCATACAG
GACCGGGAGAGCTCCTTCCGCTTCCAGCCGTTCGAGTCCTATGACTCCAGGCCCTGCCTG
CCGGAGCACAACCCCTACCGCCCCAGCTACAGCTACGACTATGAGTTCGACCTGGGGTCC
GACCGCAATGGCAGCTTTGGGGGGCAGTACAGTGAATGCCGAGACCCAGCCCGGGAGCGG
GGCTCCCTTGATGGCTTCATGCGGGGCCGGGGCCAGGGCCGCTTCCAGGACCGGAGCAAC
CCTGGCACCTTCATGCGCAGCGACCCCTTCGTGCCCCCCGCTGCGTCCTCTGAGCCCCTG
TCCACGCCCTGGAACGAGCTGAACTACGTGGGTGGACGGGGCCTGGGAGGGCCCTCCCCC
AGCCGGCCACCTCCGTCCCTCTTCTCCCAGTCCATGGCTCCCGACTACGGCGTGATGGGC
ATGCAGGGGGCGGGCGGCTATGACAGCACCATGCCCTACGGATGTGGCCGCTCGCAGCCT
CGGATGCGGGATCGGGATCGGCCCAAGAGGAGAGGGTTTGACCGCTTCGGACCAGATGGC
ACGGGCAGGAAACGGAAGCAGTTCCAACTTTACGAGGAGCCAGACACCAAACTGGCCCGG
GTTGACAGTGAAGGAGATTTCTCCGAAAATGATGACGCAGCTGGTGACTTCCGCTCAGGA
GATGAAGAATTCAAGGGTGAGGATGAACTCTGCGACTCTGGGAGGCAAAGAGGAGAGAAG
GAGGACGAGGACGAGGATGTGAAGAAGAGAAGGGAAAAGCAAAGGAGAAGAGACAGGACG
CGGGACCGTGCAGCCGACAGAATTCAGTTTGCCTGTTCTGTATGCAAGTTCCGTAGCTTT
GATGACGAAGAGATCCAGAAGCATCTGCAAAGCAAATTTCACAAAGAGACCCTGCGGTTC
ATAAGCACCAAGCTGCCCGACAAGACCGTGGAGTTCCTCCAGGAATACATTGTAAACAGA
AATAAGAAAATTGAGAAGCGGCGTCAGGAATTGATGGAGAAAGAAACCGCAAAACCAAAA
CCAGATCCTTTCAAAGGGATTGGCCAGGAGCACTTCTTCAAGAAGATCGAGGCTGCTCAC
TGCCTGGCCTGCGACATGCTAATTCCTGCACAGCCGCAGCTCCTCCAGCGGCACCTGCAC
TCCGTGGACCACAATCACAACCGCAGGTTGGCTGCTGAACAGTTCAAGAAAACCAGTCTC
CATGTGGCTAAGAGTGTTTTGAACAACAGACATATAGTGAAGATGCTGGAAAAATACCTC
AAGGGTGAGGACCCTTTCACCAGTGAAACTGTTGATCCAGAAATGGAAGGAGATGACAAT
TTAGGAGGTGAGGATAAGAAAGAGACACCTGAGGAGGTGGCCGCGGACGTCTTAGCAGAG
GTGATTACAGCAGCAGTGAGGGCCGTAGATGGGGAAGGAGCGCCCGCTCCAGAGAGCAGC
GGGGAGCCGGCTGAGGACGAAGGCCCCACGGACACAGCGGAGGCCGGTAGTGATCCTCAA
GCCGAACAGCTGCTGGAAGAGCAGGTGCCCTGTGGAACGGCACATGAGAAGGGCGTCCCC
AAGGCCAGAAGTGAGGCTGCAGAGGCTGGAAATGGCGCCGAGACAATGGCAGCAGAGGCA
GAAAGTGCCCAAACCAGAGTTGCTCCTGCCCCAGCTGCCGCGGATGCTGAAGTGGAACAA
ACTGATGCAGAGTCTAAAGACGCTGTTCCCACAGAATGA
Enzyme 93 GenBank Gene ID AC005785 Link Image
Enzyme 93 GeneCard ID AKAP8 Link Image
Enzyme 93 GenAtlas ID AKAP8 Link Image
Enzyme 93 HGNC ID HGNC:378 Link Image
Enzyme 93 Chromosome Location 1
Enzyme 93 Locus 19p13.1
Enzyme 93 SNPs SNPJam Report Link Image
Enzyme 93 General References
  1. Eide T, Coghlan V, Orstavik S, Holsve C, Solberg R, Skalhegg BS, Lamb NJ, Langeberg L, Fernandez A, Scott JD, Jahnsen T, Tasken K: Molecular cloning, chromosomal localization, and cell cycle-dependent subcellular distribution of the A-kinase anchoring protein, AKAP95. Exp Cell Res. 1998 Feb 1;238(2):305-16. [PubMed Link Image]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  3. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  4. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  5. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  9. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  10. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  11. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 93 Metabolite References Not Available
Enzyme 94 [top]
Enzyme 94 ID 13821
Enzyme 94 Name Agouti-signaling protein
Enzyme 94 Synonyms
  1. ASP
  2. Agouti switch protein
Enzyme 94 Gene Name ASIP
Enzyme 94 Protein Sequence >Agouti-signaling protein
MDVTRLLLATLLVFLCFFTANSHLPPEEKLRDDRSLRSNSSVNLLDVPSVSIVALNKKSK
QIGRKAAEKKRSSKKEASMKKVVRPRTPLSAPCVATRNSCKPPAPACCDPCASCQCRFFR
SACSCRVLSLNC
Enzyme 94 Number of Residues 132
Enzyme 94 Molecular Weight 14514.9
Enzyme 94 Theoretical pI 10.34
Enzyme 94 GO Classification
Function
Process
  • hormone-mediated signaling pathway
  • signaling
  • signaling pathway
Component
  • extracellular region
Enzyme 94 General Function Involved in hormone-mediated signaling pathway
Enzyme 94 Specific Function Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment). In higher primates, agouti may affect the quality of hair pigmentation rather than its pattern of deposition. Could well play a role in neuroendocrine aspects of melanocortin action. May have some functional role in regulating the lipid metabolism with adipocytes
Enzyme 94 Pathways Not Available
Enzyme 94 Reactions Not Available
Enzyme 94 Pfam Domain Function
Enzyme 94 Signals
  • 1-22
Enzyme 94 Transmembrane Regions
  • None
Enzyme 94 Essentiality Not Available
Enzyme 94 GenBank ID Protein 8953446 Link Image
Enzyme 94 UniProtKB/Swiss-Prot ID P42127 Link Image
Enzyme 94 UniProtKB/Swiss-Prot Entry Name ASIP_HUMAN Link Image
Enzyme 94 PDB ID 1Y7K Link Image
Enzyme 94 PDB File Show
Enzyme 94 3D Structure
Enzyme 94 Cellular Location Not Available
Enzyme 94 Gene Sequence >399 bp
ATGGATGTCACCCGCTTACTCCTGGCCACCCTGCTGGTCTTCCTCTGCTTCTTCACTGCC
AACAGCCACCTGCCACCTGAGGAGAAGCTCCGAGATGACAGGAGCCTGAGAAGCAACTCC
TCTGTGAACCTACTGGATGTCCCTTCTGTCTCTATTGTGGCGCTGAACAAGAAATCCAAA
CAGATCGGCAGAAAAGCAGCAGAAAAGAAAAGATCTTCTAAGAAGGAGGCTTCGATGAAG
AAAGTGGTGCGGCCCCGGACCCCCCTATCTGCGCCCTGCGTGGCCACCCGCAACAGCTGC
AAGCCGCCGGCACCCGCCTGCTGCGACCCGTGCGCCTCCTGCCAGTGCCGCTTCTTCCGC
AGCGCCTGCTCCTGCCGCGTGCTCAGCCTCAACTGCTGA
Enzyme 94 GenBank Gene ID AL035458 Link Image
Enzyme 94 GeneCard ID ASIP Link Image
Enzyme 94 GenAtlas ID ASIP Link Image
Enzyme 94 HGNC ID HGNC:745 Link Image
Enzyme 94 Chromosome Location 2
Enzyme 94 Locus 20q11.2-q12
Enzyme 94 SNPs SNPJam Report Link Image
Enzyme 94 General References
  1. Kwon HY, Bultman SJ, Loffler C, Chen WJ, Furdon PJ, Powell JG, Usala AL, Wilkison W, Hansmann I, Woychik RP: Molecular structure and chromosomal mapping of the human homolog of the agouti gene. Proc Natl Acad Sci U S A. 1994 Oct 11;91(21):9760-4. [PubMed Link Image]
  2. Wilson BD, Ollmann MM, Kang L, Stoffel M, Bell GI, Barsh GS: Structure and function of ASP, the human homolog of the mouse agouti gene. Hum Mol Genet. 1995 Feb;4(2):223-30. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. McNulty JC, Jackson PJ, Thompson DA, Chai B, Gantz I, Barsh GS, Dawson PE, Millhauser GL: Structures of the agouti signaling protein. J Mol Biol. 2005 Mar 4;346(4):1059-70. Epub 2005 Jan 25. [PubMed Link Image]
  6. Kanetsky PA, Swoyer J, Panossian S, Holmes R, Guerry D, Rebbeck TR: A polymorphism in the agouti signaling protein gene is associated with human pigmentation. Am J Hum Genet. 2002 Mar;70(3):770-5. Epub 2002 Feb 6. [PubMed Link Image]
Enzyme 94 Metabolite References Not Available
Enzyme 95 [top]
Enzyme 95 ID 13822
Enzyme 95 Name Cyclic AMP-dependent transcription factor ATF-1
Enzyme 95 Synonyms
  1. cAMP-dependent transcription factor ATF-1
  2. Activating transcription factor 1
  3. Protein TREB36
Enzyme 95 Gene Name ATF1
Enzyme 95 Protein Sequence >Cyclic AMP-dependent transcription factor ATF-1
MEDSHKSTTSETAPQPGSAVQGAHISHIAQQVSSLSESEESQDSSDSIGSSQKAHGILAR
RPSYRKILKDLSSEDTRGRKGDGENSGVSAAVTSMSVPTPIYQTSSGQYIAIAPNGALQL
ASPGTDGVQGLQTLTMTNSGSTQQGTTILQYAQTSDGQQILVPSNQVVVQTASGDMQTYQ
IRTTPSATSLPQTVVMTSPVTLTSQTTKTDDPQLKREIRLMKNREAARECRRKKKEYVKC
LENRVAVLENQNKTLIEELKTLKDLYSNKSV
Enzyme 95 Number of Residues 271
Enzyme 95 Molecular Weight 29232.4
Enzyme 95 Theoretical pI 8.64
Enzyme 95 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
  • protein binding
  • protein dimerization activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 95 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 95 Specific Function This protein binds the cAMP response element (CRE) (consensus:5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Binds to the Tax-responsive element (TRE) of HTLV-I. Mediates PKA-induced stimulation of CRE-reporter genes
Enzyme 95 Pathways Not Available
Enzyme 95 Reactions Not Available
Enzyme 95 Pfam Domain Function
Enzyme 95 Signals
  • None
Enzyme 95 Transmembrane Regions
  • None
Enzyme 95 Essentiality Not Available
Enzyme 95 GenBank ID Protein 20810445 Link Image
Enzyme 95 UniProtKB/Swiss-Prot ID P18846 Link Image
Enzyme 95 UniProtKB/Swiss-Prot Entry Name ATF1_HUMAN Link Image
Enzyme 95 PDB ID Not Available
Enzyme 95 Cellular Location Not Available
Enzyme 95 Gene Sequence >816 bp
ATGGAAGATTCCCACAAGAGTACCACGTCAGAGACAGCACCTCAACCTGGTTCAGCAGTT
CAGGGAGCTCACATTTCTCATATTGCTCAACAGGTATCATCTTTATCAGAAAGTGAGGAG
TCCCAGGACTCATCCGACAGCATAGGCTCCTCACAGAAAGCCCACGGGATCCTAGCACGG
CGCCCATCTTACAGAAAAATTTTGAAAGACTTATCTTCTGAAGATACACGGGGCAGAAAA
GGAGACGGAGAAAATTCTGGAGTTTCTGCTGCTGTCACTTCTATGTCTGTTCCAACTCCC
ATCTATCAGACTAGCAGCGGACAGTATATTGCCATTGCCCCAAATGGAGCCTTACAGTTG
GCAAGTCCAGGCACAGATGGAGTACAGGGACTTCAGACATTAACCATGACAAATTCAGGC
AGTACTCAGCAAGGTACAACTATTCTTCAGTATGCACAGACCTCTGATGGACAGCAGATA
CTTGTGCCCAGCAATCAGGTGGTCGTACAAACTGCATCAGGAGATATGCAAACATATCAG
ATCCGAACTACACCTTCAGCTACTTCTCTGCCACAAACTGTGGTGATGACATCTCCTGTG
ACTCTCACCTCTCAGACAACTAAGACAGATGACCCCCAATTGAAAAGAGAAATAAGGTTA
ATGAAAAACAGAGAAGCTGCTCGAGAATGTCGCAGAAAGAAGAAAGAATATGTGAAATGC
CTGGAAAACCGAGTTGCAGTCCTGGAAAATCAAAATAAAACTCTAATAGAAGAGTTAAAA
ACTTTGAAGGATCTTTATTCCAATAAAAGTGTTTGA
Enzyme 95 GenBank Gene ID BC029619 Link Image
Enzyme 95 GeneCard ID ATF1 Link Image
Enzyme 95 GenAtlas ID ATF1 Link Image
Enzyme 95 HGNC ID HGNC:783 Link Image
Enzyme 95 Chromosome Location 1
Enzyme 95 Locus 12q13
Enzyme 95 SNPs SNPJam Report Link Image
Enzyme 95 General References
  1. Yoshimura T, Fujisawa J, Yoshida M: Multiple cDNA clones encoding nuclear proteins that bind to the tax-dependent enhancer of HTLV-1: all contain a leucine zipper structure and basic amino acid domain. EMBO J. 1990 Aug;9(8):2537-42. [PubMed Link Image]
  2. Rehfuss RP, Walton KM, Loriaux MM, Goodman RH: The cAMP-regulated enhancer-binding protein ATF-1 activates transcription in response to cAMP-dependent protein kinase A. J Biol Chem. 1991 Oct 5;266(28):18431-4. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Hai TW, Liu F, Coukos WJ, Green MR: Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers. Genes Dev. 1989 Dec;3(12B):2083-90. [PubMed Link Image]
  5. Waters BL, Panagopoulos I, Allen EF: Genetic characterization of angiomatoid fibrous histiocytoma identifies fusion of the FUS and ATF-1 genes induced by a chromosomal translocation involving bands 12q13 and 16p11. Cancer Genet Cytogenet. 2000 Sep;121(2):109-16. [PubMed Link Image]
  6. Sun P, Lou L, Maurer RA: Regulation of activating transcription factor-1 and the cAMP response element-binding protein by Ca2+/calmodulin-dependent protein kinases type I, II, and IV. J Biol Chem. 1996 Feb 9;271(6):3066-73. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Hallor KH, Mertens F, Jin Y, Meis-Kindblom JM, Kindblom LG, Behrendtz M, Kalen A, Mandahl N, Panagopoulos I: Fusion of the EWSR1 and ATF1 genes without expression of the MITF-M transcript in angiomatoid fibrous histiocytoma. Genes Chromosomes Cancer. 2005 Sep;44(1):97-102. [PubMed Link Image]
  9. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 95 Metabolite References Not Available
Enzyme 96 [top]
Enzyme 96 ID 13823
Enzyme 96 Name Cyclic AMP-dependent transcription factor ATF-2
Enzyme 96 Synonyms
  1. cAMP-dependent transcription factor ATF-2
  2. Activating transcription factor 2
  3. Cyclic AMP-responsive element-binding protein 2
  4. CREB-2
  5. cAMP-responsive element-binding protein 2
  6. HB16
  7. cAMP response element-binding protein CRE-BP1
Enzyme 96 Gene Name ATF2
Enzyme 96 Protein Sequence >Cyclic AMP-dependent transcription factor ATF-2
MKFKLHVNSARQYKDLWNMSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARN
DSVIVADQTPTPTRFLKNCEEVGLFNELASPFENEFKKASEDDIKKMPLDLSPLATPIIR
SKIEEPSVVETTHQDSPLPHPESTTSDEKEVPLAQTAQPTSAIVRPASLQVPNVLLTSSD
SSVIIQQAVPSPTSSTVITQAPSSNRPIVPVPGPFPLLLHLPNGQTMPVAIPASITSSNV
HVPAAVPLVRPVTMVPSVPGIPGPSSPQPVQSEAKMRLKAALTQQHPPVTNGDTVKGHGS
GLVRTQSEESRPQSLQQPATSTTETPASPAHTTPQTQSTSGRRRRAANEDPDEKRRKFLE
RNRAAASRCRQKRKVWVQSLEKKAEDLSSLNGQLQSEVTLLRNEVAQLKQLLLAHKDCPV
TAMQKKSGYHTADKDDSSEDISVPSSPHTEAIQHSSVSTSNGVSSTSKAEAVATSVLTQM
ADQSTEPALSQIVMAPSSQSQPSGS
Enzyme 96 Number of Residues 505
Enzyme 96 Molecular Weight 54536.9
Enzyme 96 Theoretical pI 8.01
Enzyme 96 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • nucleic acid binding
  • protein binding
  • protein dimerization activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • cell part
  • intracellular
Enzyme 96 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 96 Specific Function Transcriptional activator, probably constitutive, which binds to the cAMP-responsive element (CRE) (consensus:5'- GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Interaction with JUN redirects JUN to bind to CRES preferentially over the 12-O-tetradecanoylphorbol-13-acetate response elements (TRES) as part of an ATF2/JUN complex
Enzyme 96 Pathways Not Available
Enzyme 96 Reactions Not Available
Enzyme 96 Pfam Domain Function
Enzyme 96 Signals
  • None
Enzyme 96 Transmembrane Regions
  • None
Enzyme 96 Essentiality Not Available
Enzyme 96 GenBank ID Protein 30215 Link Image
Enzyme 96 UniProtKB/Swiss-Prot ID P15336 Link Image
Enzyme 96 UniProtKB/Swiss-Prot Entry Name ATF2_HUMAN Link Image
Enzyme 96 PDB ID 1T2K Link Image
Enzyme 96 PDB File Show
Enzyme 96 3D Structure
Enzyme 96 Cellular Location Not Available
Enzyme 96 Gene Sequence >1518 bp
ATGAAATTCAAGTTACATGTGAATTCTGCCAGGCAATACAAGGACCTGTGGAATATGAGT
GATGACAAACCCTTTCTATGTACTGCGCCTGGATGTGGCCAGCGTTTTACCAACGAGGAT
CATTTGGCTGTCCATAAACATAAACATGAGATGACACTGAAATTTGGTCCAGCACGTAAT
GACAGTGTCATTGTGGCTGATCAGACCCCAACACCAACAAGATTCTTGAAAAACTGTGAA
GAAGTGGGTTTGTTTAATGAGTTGGCGAGTCCATTTGAGAATGAATTCAAGAAAGCTTCA
GAAGATGACATTAAAAAAATGCCTCTAGATTTATCCCCTCTTGCAACACCTATCATAAGA
AGCAAAATTGAGGAGCCTTCTGTTGTAGAAACAACTCACCAGGATAGTCCTTTACCTCAC
CCAGAGTCTACTACCAGTGATGAGAAGGAAGTACCATTGGCACAAACTGCACAGCCCACA
TCAGCTATTGTTCGTCCAGCATCATTACAGGTTCCCAATGTGCTGCTTACAAGTTCTGAC
TCAAGTGTAATTATTCAGCAGGCAGTACCTTCACCAACCTCAAGTACTGTAATCACCCAG
GCACCATCCTCTAACAGGCCAATTGTCCCTGTACCAGGCCCATTTCCTCTTCTGTTACAT
CTTCCTAGTGGACAAACCATGCCTGTTGCTATTCCTGCATCAATTACAAGTTCTAATGTG
CATGTTCCAGCTGCAGTCCCACTCGTTCGACCAGTCACCATGGTGCCTAGTGTTCCAGGA
ATCCCAGGTCCTTCCTCTCCCCAACCAGTACAGTCAGAAGCAAAAATGAGATTAAAAGCT
GCTTTGACCCAGCAACATCCTCCAGTTACCAATGGTGATACTGTCAAAGGTCATGGTAGC
GGATTGGTTAGGACTCAGTCAGAGGAATCTCGACCGCAGTCATTACAACAGCCAGCCACA
TCCACTACAGAAACTCCGGCTTCTCCAGCTCACACAACTCCACAGACCCAAAGTACAAGT
GGTCGTCGGAGAAGAGCAGCTAACGAAGATCCTGATGAAAAAAGGAGAAAGTTTTTAGAG
CGAAATAGAGCAGCAGCTTCAAGATGCCGACAAAAAAGGAAAGTCTGGGTTCAGTCTTTA
GAGAAGAAAGCTGAAGACTTGAGTTCATTAAATGGTCAGCTGCAGAGTGAAGTCACCCTG
CTGAGAAATGAAGTGGCACAGCTGAAACAGCTTCTTCTGGCTCATAAAGATTGCCCTGTA
ACCGCCATGCAGAAGAAATCTGGCTATCATACTGCTGATAAAGATGATAGTTCAGAAGAC
ATTTCAGTGCCGAGTAGTCCACATACGGAAGCTATACAGCATAGTTCGGTCAGCACATCC
AATGGAGTCAGTTCAACCTCCAAGGCAGAAGCTGTAGCCACTTCAGTCCTCACCCAGATG
GCGGACCAGAGTACAGAGCCTGCTCTTTCACAGATCGTTATGGCTCCTTCCTCCCAGTCA
CAGCCCTCAGGAAGTTGA
Enzyme 96 GenBank Gene ID X15875 Link Image
Enzyme 96 GeneCard ID ATF2 Link Image
Enzyme 96 GenAtlas ID ATF2 Link Image
Enzyme 96 HGNC ID HGNC:784 Link Image
Enzyme 96 Chromosome Location 2
Enzyme 96 Locus 2q32
Enzyme 96 SNPs SNPJam Report Link Image
Enzyme 96 General References
  1. Maekawa T, Sakura H, Kanei-Ishii C, Sudo T, Yoshimura T, Fujisawa J, Yoshida M, Ishii S: Leucine zipper structure of the protein CRE-BP1 binding to the cyclic AMP response element in brain. EMBO J. 1989 Jul;8(7):2023-8. [PubMed Link Image]
  2. Yang L, Lanier ER, Kraig E: Identification of a novel, spliced variant of CREB that is preferentially expressed in the thymus. J Immunol. 1997 Mar 15;158(6):2522-5. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Kara CJ, Liou HC, Ivashkiv LB, Glimcher LH: A cDNA for a human cyclic AMP response element-binding protein which is distinct from CREB and expressed preferentially in brain. Mol Cell Biol. 1990 Apr;10(4):1347-57. [PubMed Link Image]
  6. Fukushima A, Okuda A, Nishimoto M, Seki N, Hori TA, Muramatsu M: Characterization of functional domains of an embryonic stem cell coactivator UTF1 which are conserved and essential for potentiation of ATF-2 activity. J Biol Chem. 1998 Oct 2;273(40):25840-9. [PubMed Link Image]
  7. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  12. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  13. Nagadoi A, Nakazawa K, Uda H, Okuno K, Maekawa T, Ishii S, Nishimura Y: Solution structure of the transactivation domain of ATF-2 comprising a zinc finger-like subdomain and a flexible subdomain. J Mol Biol. 1999 Apr 2;287(3):593-607. [PubMed Link Image]
  14. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 96 Metabolite References Not Available
Enzyme 97 [top]
Enzyme 97 ID 13824
Enzyme 97 Name Cyclic AMP-dependent transcription factor ATF-3
Enzyme 97 Synonyms
  1. cAMP-dependent transcription factor ATF-3
  2. Activating transcription factor 3
Enzyme 97 Gene Name ATF3
Enzyme 97 Protein Sequence >Cyclic AMP-dependent transcription factor ATF-3
MMLQHPGQVSASEVSASAIVPCLSPPGSLVFEDFANLTPFVKEELRFAIQNKHLCHRMSS
ALESVTVSDRPLGVSITKAEVAPEEDERKKRRRERNKIAAAKCRNKKKEKTECLQKESEK
LESVNAELKAQIEELKNEKQHLIYMLNLHRPTCIVRAQNGRTPEDERNLFIQQIKEGTLQ
S
Enzyme 97 Number of Residues 181
Enzyme 97 Molecular Weight 20575.4
Enzyme 97 Theoretical pI 8.76
Enzyme 97 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
  • protein binding
  • protein dimerization activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 97 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 97 Specific Function This protein binds the cAMP response element (CRE) (consensus:5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Represses transcription from promoters with ATF sites. It may repress transcription by stabilizing the binding of inhibitory cofactors at the promoter. Isoform 2 activates transcription presumably by sequestering inhibitory cofactors away from the promoters
Enzyme 97 Pathways Not Available
Enzyme 97 Reactions Not Available
Enzyme 97 Pfam Domain Function
Enzyme 97 Signals
  • None
Enzyme 97 Transmembrane Regions
  • None
Enzyme 97 Essentiality Not Available
Enzyme 97 GenBank ID Protein 37574508 Link Image
Enzyme 97 UniProtKB/Swiss-Prot ID P18847 Link Image
Enzyme 97 UniProtKB/Swiss-Prot Entry Name ATF3_HUMAN Link Image
Enzyme 97 PDB ID Not Available
Enzyme 97 Cellular Location Not Available
Enzyme 97 Gene Sequence >546 bp
ATGATGCTTCAACACCCAGGCCAGGTCTCTGCCTCGGAAGTGAGTGCTTCTGCCATCGTC
CCCTGCCTGTCCCCTCCTGGGTCACTGGTGTTTGAGGATTTTGCTAACCTGACGCCCTTT
GTCAAGGAAGAGCTGAGGTTTGCCATCCAGAACAAGCACCTCTGCCACCGGATGTCCTCT
GCGCTGGAATCAGTCACTGTCAGCGACAGACCCCTCGGGGTGTCCATCACAAAAGCCGAG
GTAGCCCCTGAAGAAGATGAAAGGAAAAAGAGGCGACGAGAAAGAAATAAGATTGCAGCT
GCAAAGTGCCGAAACAAGAAGAAGGAGAAGACGGAGTGCCTGCAGAAAGAGTCGGAGAAG
CTGGAAAGTGTGAATGCTGAACTGAAGGCTCAGATTGAGGAGCTCAAGAACGAGAAGCAG
CATTTGATATACATGCTCAACCTTCATCGGCCCACGTGTATTGTCCGGGCTCAGAATGGG
AGGACTCCAGAAGATGAGAGAAACCTCTTTATCCAACAGATAAAAGAAGGAACATTGCAG
AGCTAA
Enzyme 97 GenBank Gene ID AY426987 Link Image
Enzyme 97 GeneCard ID ATF3 Link Image
Enzyme 97 GenAtlas ID ATF3 Link Image
Enzyme 97 HGNC ID HGNC:785 Link Image
Enzyme 97 Chromosome Location 1
Enzyme 97 Locus 1q32.3
Enzyme 97 SNPs SNPJam Report Link Image
Enzyme 97 General References
  1. Chen BP, Liang G, Whelan J, Hai T: ATF3 and ATF3 delta Zip. Transcriptional repression versus activation by alternatively spliced isoforms. J Biol Chem. 1994 Jun 3;269(22):15819-26. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Hai TW, Liu F, Coukos WJ, Green MR: Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers. Genes Dev. 1989 Dec;3(12B):2083-90. [PubMed Link Image]
  4. Hillman RT, Green RE, Brenner SE: An unappreciated role for RNA surveillance. Genome Biol. 2004;5(2):R8. Epub 2004 Feb 2. [PubMed Link Image]
Enzyme 97 Metabolite References Not Available
Enzyme 98 [top]
Enzyme 98 ID 13825
Enzyme 98 Name Cyclic AMP-dependent transcription factor ATF-4
Enzyme 98 Synonyms
  1. cAMP-dependent transcription factor ATF-4
  2. Activating transcription factor 4
  3. Cyclic AMP-responsive element-binding protein 2
  4. CREB-2
  5. cAMP-responsive element-binding protein 2
  6. DNA-binding protein TAXREB67
  7. Tax-responsive enhancer element-binding protein 67
  8. TaxREB67
Enzyme 98 Gene Name ATF4
Enzyme 98 Protein Sequence >Cyclic AMP-dependent transcription factor ATF-4
MTEMSFLSSEVLVGDLMSPFDQSGLGAEESLGLLDDYLEVAKHFKPHGFSSDKAKAGSSE
WLAVDGLVSPSNNSKEDAFSGTDWMLEKMDLKEFDLDALLGIDDLETMPDDLLTTLDDTC
DLFAPLVQETNKQPPQTVNPIGHLPESLTKPDQVAPFTFLQPLPLSPGVLSSTPDHSFSL
ELGSEVDITEGDRKPDYTAYVAMIPQCIKEEDTPSDNDSGICMSPESYLGSPQHSPSTRG
SPNRSLPSPGVLCGSARPKPYDPPGEKMVAAKVKGEKLDKKLKKMEQNKTAATRYRQKKR
AEQEALTGECKELEKKNEALKERADSLAKEIQYLKDLIEEVRKARGKKRVP
Enzyme 98 Number of Residues 351
Enzyme 98 Molecular Weight 38589.1
Enzyme 98 Theoretical pI 4.58
Enzyme 98 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
  • protein binding
  • protein dimerization activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
Enzyme 98 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 98 Specific Function Transcriptional activator. Binds the cAMP response element (CRE) (consensus:5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. It binds to a Tax- responsive enhancer element in the long terminal repeat of HTLV-I
Enzyme 98 Pathways Not Available
Enzyme 98 Reactions Not Available
Enzyme 98 Pfam Domain Function
Enzyme 98 Signals
  • None
Enzyme 98 Transmembrane Regions
  • None
Enzyme 98 Essentiality Not Available
Enzyme 98 GenBank ID Protein 5102567 Link Image
Enzyme 98 UniProtKB/Swiss-Prot ID P18848 Link Image
Enzyme 98 UniProtKB/Swiss-Prot Entry Name ATF4_HUMAN Link Image
Enzyme 98 PDB ID 1CI6 Link Image
Enzyme 98 PDB File Show
Enzyme 98 3D Structure
Enzyme 98 Cellular Location Not Available
Enzyme 98 Gene Sequence >1056 bp
ATGACCGAAATGAGCTTCCTGAGCAGCGAGGTGTTGGTGGGGGACTTGATGTCCCCCTTC
GACCAGTCGGGTTTGGGGGCTGAAGAAAGCCTAGGTCTCTTAGATGATTACCTGGAGGTG
GCCAAGCACTTCAAACCTCATGGGTTCTCCAGCGACAAGGCTAAGGCGGGCTCCTCCGAA
TGGCTGGCTGTGGATGGGTTGGTCAGTCCCTCCAACAACAGCAAGGAGGATGCCTTCTCC
GGGACAGATTGGATGTTGGAGAAAATGGATTTGAAGGAGTTCGACTTGGATGCCCTGTTG
GGTATAGATGACCTGGAAACCATGCCAGATGACCTTCTGACCACGTTGGATGACACTTGT
GATCTCTTTGCCCCCCTAGTCCAGGAGACTAATAAGCAGCCCCCCCAGACGGTGAACCCA
ATTGGCCATCTCCCAGAAAGTTTAACAAAACCCGACCAGGTTGCCCCCTTCACCTTCTTA
CAACCTCTTCCCCTTTCCCCAGGGGTCCTGTCCTCCACTCCAGATCATTCCTTTAGTTTA
GAGCTGGGCAGTGAAGTGGATATCACTGAAGGAGATAGGAAGCCAGACTACACTGCTTAC
GTTGCCATGATCCCTCAGTGCATAAAGGAGGAAGACACCCCTTCAGATAATGATAGTGGC
ATCTGTATGAGCCCAGAGTCCTATCTGGGGTCTCCTCAGCACAGCCCCTCTACCAGGGGC
TCTCCAAATAGGAGCCTCCCATCTCCAGGTGTTCTCTGTGGGTCTGCCCGTCCCAAACCT
TACGATCCTCCTGGAGAGAAGATGGTAGCAGCAAAAGTAAAGGGTGAGAAACTGGATAAG
AAGCTGAAAAAAATGGAGCAAAACAAGACAGCAGCCACTAGGTACCGCCAGAAGAAGAGG
GCGGAGCAGGAGGCTCTTACTGGTGAGTGCAAAGAGCTGGAAAAGAAGAACGAGGCTCTA
AAAGAGAGGGCGGATTCCCTGGCCAAGGAGATCCAGTACCTGAAAGATTTGATAGAAGAG
GTCCGCAAGGCAAGGGGGAAGAAAAGGGTCCCCTAG
Enzyme 98 GenBank Gene ID AL022312 Link Image
Enzyme 98 GeneCard ID ATF4 Link Image
Enzyme 98 GenAtlas ID ATF4 Link Image
Enzyme 98 HGNC ID HGNC:786 Link Image
Enzyme 98 Chromosome Location 2
Enzyme 98 Locus 22q13.1
Enzyme 98 SNPs SNPJam Report Link Image
Enzyme 98 General References
  1. Tsujimoto A, Nyunoya H, Morita T, Sato T, Shimotohno K: Isolation of cDNAs for DNA-binding proteins which specifically bind to a tax-responsive enhancer element in the long terminal repeat of human T-cell leukemia virus type I. J Virol. 1991 Mar;65(3):1420-6. [PubMed Link Image]
  2. Karpinski BA, Morle GD, Huggenvik J, Uhler MD, Leiden JM: Molecular cloning of human CREB-2: an ATF/CREB transcription factor that can negatively regulate transcription from the cAMP response element. Proc Natl Acad Sci U S A. 1992 Jun 1;89(11):4820-4. [PubMed Link Image]
  3. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Hai TW, Liu F, Coukos WJ, Green MR: Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers. Genes Dev. 1989 Dec;3(12B):2083-90. [PubMed Link Image]
  6. Yu VW, Ambartsoumian G, Verlinden L, Moir JM, Prud'homme J, Gauthier C, Roughley PJ, St-Arnaud R: FIAT represses ATF4-mediated transcription to regulate bone mass in transgenic mice. J Cell Biol. 2005 May 23;169(4):591-601. [PubMed Link Image]
  7. Sayer JA, Otto EA, O'Toole JF, Nurnberg G, Kennedy MA, Becker C, Hennies HC, Helou J, Attanasio M, Fausett BV, Utsch B, Khanna H, Liu Y, Drummond I, Kawakami I, Kusakabe T, Tsuda M, Ma L, Lee H, Larson RG, Allen SJ, Wilkinson CJ, Nigg EA, Shou C, Lillo C, Williams DS, Hoppe B, Kemper MJ, Neuhaus T, Parisi MA, Glass IA, Petry M, Kispert A, Gloy J, Ganner A, Walz G, Zhu X, Goldman D, Nurnberg P, Swaroop A, Leroux MR, Hildebrandt F: The centrosomal protein nephrocystin-6 is mutated in Joubert syndrome and activates transcription factor ATF4. Nat Genet. 2006 Jun;38(6):674-81. Epub 2006 May 7. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  9. Podust LM, Krezel AM, Kim Y: Crystal structure of the CCAAT box/enhancer-binding protein beta activating transcription factor-4 basic leucine zipper heterodimer in the absence of DNA. J Biol Chem. 2001 Jan 5;276(1):505-13. [PubMed Link Image]
Enzyme 98 Metabolite References Not Available
Enzyme 99 [top]
Enzyme 99 ID 13826
Enzyme 99 Name Cyclic AMP-dependent transcription factor ATF-5
Enzyme 99 Synonyms
  1. cAMP-dependent transcription factor ATF-5
  2. Activating transcription factor 5
  3. Transcription factor ATFx
Enzyme 99 Gene Name ATF5
Enzyme 99 Protein Sequence >Cyclic AMP-dependent transcription factor ATF-5
MSLLATLGLELDRALLPASGLGWLVDYGKLPPAPAPLAPYEVLGGALEGGLPVGGEPLAG
DGFSDWMTERVDFTALLPLEPPLPPGTLPQPSPTPPDLEAMASLLKKELEQMEDFFLDAP
PLPPPSPPPLPPPPLPPAPSLPLSLPSFDLPQPPVLDTLDLLAIYCRNEAGQEEVGMPPL
PPPQQPPPPSPPQPSRLAPYPHPATTRGDRKQKKRDQNKSAALRYRQRKRAEGEALEGEC
QGLEARNRELKERAESVEREIQYVKDLLIEVYKARSQRTRSC
Enzyme 99 Number of Residues 282
Enzyme 99 Molecular Weight 30673.9
Enzyme 99 Theoretical pI 4.61
Enzyme 99 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
  • protein binding
  • protein dimerization activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
Enzyme 99 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 99 Specific Function Transcriptional activator which binds the cAMP response element (CRE) (consensus:5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters and blocks the differentiation of neuroprogenitor cells into neurons. Its transcriptional activity is enhanced by CCND3 and slightly inhibited by CDK4
Enzyme 99 Pathways Not Available
Enzyme 99 Reactions Not Available
Enzyme 99 Pfam Domain Function
Enzyme 99 Signals
  • None
Enzyme 99 Transmembrane Regions
  • None
Enzyme 99 Essentiality Not Available
Enzyme 99 GenBank ID Protein 12583650 Link Image
Enzyme 99 UniProtKB/Swiss-Prot ID Q9Y2D1 Link Image
Enzyme 99 UniProtKB/Swiss-Prot Entry Name ATF5_HUMAN Link Image
Enzyme 99 PDB ID Not Available
Enzyme 99 Cellular Location Not Available
Enzyme 99 Gene Sequence >849 bp
ATGTCACTCCTGGCGACCCTGGGGCTGGAGCTGGACAGGGCCCTGCTCCCAGCTAGTGGG
CTGGGATGGCTCGTAGACTATGGGAAACTCCCCCCGGCCCCTGCCCCCCTGGCTCCCTAT
GAGGTCCTTGGGGGAGCCCTGGAGGGCGGGCTTCCAGTGGGGGGAGAGCCCCTGGCAGGT
GATGGCTTCTCTGACTGGATGACTGAGCGAGTTGATTTCACAGCTCTCCTCCCTCTGGAG
CCTCCCCTACCCCCCGGCACCCTCCCCCAACCTTCCCCAACCCCACCTGACCTGGAAGCT
ATGGCCTCCCTCCTCAAGAAGGAGCTGGAACAGATGGAAGACTTCTTCCTAGATGCCCCG
CCCCTCCCACCACCCTCCCCGCCGCCACTACCACCACCACCACTACCACCAGCCCCCTCC
CTCCCCCTGTCCCTCCCCTCCTTTGACCTCCCCCAGCCCCCTGTCTTGGATACTCTGGAC
TTGCTGGCCATCTACTGCCGCAACGAGGCCGGGCAGGAGGAAGTGGGGATGCCGCCTCTG
CCCCCGCCACAGCAGCCCCCTCCTCCTTCTCCACCTCAACCTTCTCGCCTGGCCCCCTAC
CCACATCCTGCCACCACCCGAGGGGACCGCAAGCAAAAGAAGAGAGACCAGAACAAGTCG
GCGGCTCTGAGGTACCGCCAGCGGAAGCGGGCAGAGGGTGAGGCCCTGGAGGGCGAGTGC
CAGGGGCTGGAGGCACGGAATCGCGAGCTGAAGGAACGGGCAGAGTCCGTGGAGCGCGAG
ATCCAGTACGTCAAGGACCTGCTCATCGAGGTTTACAAGGCCCGGAGCCAGAGGACCCGT
AGCTGCTAG
Enzyme 99 GenBank Gene ID AB021663 Link Image
Enzyme 99 GeneCard ID ATF5 Link Image
Enzyme 99 GenAtlas ID ATF5 Link Image
Enzyme 99 HGNC ID HGNC:790 Link Image
Enzyme 99 Chromosome Location 1
Enzyme 99 Locus 19q13.3
Enzyme 99 SNPs SNPJam Report Link Image
Enzyme 99 General References
  1. White JH, McIllhinney RA, Wise A, Ciruela F, Chan WY, Emson PC, Billinton A, Marshall FH: The GABAB receptor interacts directly with the related transcription factors CREB2 and ATFx. Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13967-72. [PubMed Link Image]
  2. Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Pati D, Meistrich ML, Plon SE: Human Cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors of cyclic AMP-induced transcription for proteolysis. Mol Cell Biol. 1999 Jul;19(7):5001-13. [PubMed Link Image]
  7. Liu W, Sun M, Jiang J, Shen X, Sun Q, Liu W, Shen H, Gu J: Cyclin D3 interacts with human activating transcription factor 5 and potentiates its transcription activity. Biochem Biophys Res Commun. 2004 Sep 3;321(4):954-60. [PubMed Link Image]
Enzyme 99 Metabolite References Not Available
Enzyme 100 [top]
Enzyme 100 ID 13827
Enzyme 100 Name Cyclic AMP-dependent transcription factor ATF-7
Enzyme 100 Synonyms
  1. cAMP-dependent transcription factor ATF-7
  2. Activating transcription factor 7
  3. Transcription factor ATF-A
Enzyme 100 Gene Name ATF7
Enzyme 100 Protein Sequence >Cyclic AMP-dependent transcription factor ATF-7
MGDDRPFVCNAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARTDSVIIADQTPTPTRFLKN
CEEVGLFNELASSFEHEFKKAADEDEKKARSRTVAKKLVAAAGPLDMSLPSTPDIKIKEE
EPVEVDSSPPDSPASSPCSPPLKEKEVTPKPVLISTPTPTIVRPGSLPLHLGYDPLHPTL
PSPTSVITQAPPSNRQMGSPTGSLPLVMHLANGQTMPVLPGPPVQMPSVISLARPVSMVP
NIPGIPGPPVNSSGSISPSGHPIPSEAKMRLKATLTHQVSSINGGCGMVVGTASTMVTAR
PEQSQILIQHPDAPSPAQPQVSPAQPTPSTGGRRRRTVDEDPDERRQRFLERNRAAASRC
RQKRKLWVSSLEKKAEELTSQNIQLSNEVTLLRNEVAQLKQLLLAHKDCPVTALQKKTQG
YLESPKESSEPTGSPAPVIQHSSATAPSNGLSVRSAAEAVATSVLTQMASQRTELSMPIQ
SHVIMTPQSQSAGR
Enzyme 100 Number of Residues 494
Enzyme 100 Molecular Weight 52966.9
Enzyme 100 Theoretical pI 8.89
Enzyme 100 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • nucleic acid binding
  • protein binding
  • protein dimerization activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • cell part
  • intracellular
Enzyme 100 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 100 Specific Function Isoform 4/ATF-A0 acts as a dominant repressor of the E- selectin/NF-ELAM1/delta-A promoter
Enzyme 100 Pathways Not Available
Enzyme 100 Reactions Not Available
Enzyme 100 Pfam Domain Function
Enzyme 100 Signals
  • None
Enzyme 100 Transmembrane Regions
  • None
Enzyme 100 Essentiality Not Available
Enzyme 100 GenBank ID Protein 194385140 Link Image
Enzyme 100 UniProtKB/Swiss-Prot ID P17544 Link Image
Enzyme 100 UniProtKB/Swiss-Prot Entry Name ATF7_HUMAN Link Image
Enzyme 100 PDB ID Not Available
Enzyme 100 Cellular Location Not Available
Enzyme 100 Gene Sequence >1485 bp
ATGGGAGACGACAGACCGTTTGTGTGCAATGCCCCGGGCTGTGGACAGAGATTTACAAAC
GAGGACCACCTGGCAGTTCATAAACACAAGCATGAGATGACATTGAAATTTGGCCCAGCC
CGAACTGACTCAGTCATCATTGCAGATCAAACGCCTACTCCAACTAGATTCCTGAAGAAC
TGTGAGGAGGTGGGACTCTTCAATGAACTAGCTAGCTCCTTTGAACATGAATTCAAGAAA
GCTGCAGATGAGGATGAGAAAAAGGCAAGAAGCAGGACTGTTGCCAAAAAACTGGTGGCT
GCTGCTGGGCCCCTTGACATGTCTCTGCCTTCCACACCAGACATCAAAATCAAAGAAGAA
GAGCCAGTGGAGGTAGACTCATCCCCACCTGATAGCCCTGCCTCTAGTCCCTGTTCCCCA
CCACTGAAGGAGAAGGAGGTTACCCCAAAGCCTGTTCTGATCTCTACCCCCACACCCACC
ATTGTACGTCCTGGCTCCCTGCCTCTCCACTTGGGCTATGATCCACTTCATCCAACCCTT
CCCTCCCCAACCTCTGTCATCACACAGGCTCCACCATCCAACAGGCAAATGGGGTCTCCC
ACTGGCTCCCTCCCTCTTGTCATGCATCTTGCTAATGGACAGACCATGCCTGTGTTGCCA
GGGCCTCCAGTACAGATGCCGTCTGTTATATCGCTGGCCAGACCTGTGTCCATGGTGCCC
AACATTCCTGGTATCCCTGGCCCACCAGTTAACAGTAGTGGCTCCATTTCTCCCTCTGGC
CACCCTATACCATCAGAAGCCAAGATGAGACTGAAAGCCACCCTAACTCACCAAGTCTCC
TCAATCAATGGTGGTTGTGGAATGGTGGTGGGTACTGCCAGCACCATGGTGACAGCCCGC
CCAGAGCAGAGCCAGATTCTCATCCAGCACCCTGATGCCCCATCCCCTGCCCAGCCACAG
GTCTCACCAGCTCAGCCCACCCCTAGTACTGGGGGGCGACGGCGGCGCACAGTAGATGAA
GATCCAGATGAGCGACGGCAGCGCTTTCTGGAGCGCAACCGGGCTGCAGCCTCCCGCTGC
CGCCAAAAGCGAAAGCTGTGGGTGTCCTCCCTAGAGAAGAAGGCCGAAGAACTCACTTCT
CAGAACATTCAGCTGAGTAATGAAGTCACATTACTACGCAATGAGGTGGCCCAGTTGAAA
CAGCTACTGTTAGCTCATAAAGACTGCCCAGTCACTGCACTACAGAAAAAGACTCAAGGC
TATTTAGAAAGCCCCAAGGAAAGCTCAGAGCCAACGGGTTCTCCAGCCCCTGTGATTCAG
CACAGCTCAGCAACAGCCCCTAGCAATGGCCTCAGTGTTCGCTCTGCAGCTGAAGCTGTG
GCCACCTCGGTCCTCACTCAGATGGCCAGCCAAAGGACAGAACTGAGCATGCCGATACAA
TCGCATGTAATCATGACCCCACAGTCCCAGTCTGCGGGCAGATGA
Enzyme 100 GenBank Gene ID AK298853 Link Image
Enzyme 100 GeneCard ID ATF7 Link Image
Enzyme 100 GenAtlas ID ATF7 Link Image
Enzyme 100 HGNC ID HGNC:792 Link Image
Enzyme 100 Chromosome Location 1
Enzyme 100 Locus 12q13
Enzyme 100 SNPs SNPJam Report Link Image
Enzyme 100 General References
  1. Gaire M, Chatton B, Kedinger C: Isolation and characterization of two novel, closely related ATF cDNA clones from HeLa cells. Nucleic Acids Res. 1990 Jun 25;18(12):3467-73. [PubMed Link Image]
  2. Pescini R, Kaszubska W, Whelan J, DeLamarter JF, Hooft van Huijsduijnen R: ATF-a0, a novel variant of the ATF/CREB transcription factor family, forms a dominant transcription inhibitor in ATF-a heterodimers. J Biol Chem. 1994 Jan 14;269(2):1159-65. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hai T, Curran T: Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3720-4. [PubMed Link Image]
  5. Chatton B, Bocco JL, Gaire M, Hauss C, Reimund B, Goetz J, Kedinger C: Transcriptional activation by the adenovirus larger E1a product is mediated by members of the cellular transcription factor ATF family which can directly associate with E1a. Mol Cell Biol. 1993 Jan;13(1):561-70. [PubMed Link Image]
  6. Chatton B, Bocco JL, Goetz J, Gaire M, Lutz Y, Kedinger C: Jun and Fos heterodimerize with ATFa, a member of the ATF/CREB family and modulate its transcriptional activity. Oncogene. 1994 Feb;9(2):375-85. [PubMed Link Image]
  7. De Graeve F, Bahr A, Sabapathy KT, Hauss C, Wagner EF, Kedinger C, Chatton B: Role of the ATFa/JNK2 complex in Jun activation. Oncogene. 1999 Jun 10;18(23):3491-500. [PubMed Link Image]
  8. Hamard PJ, Dalbies-Tran R, Hauss C, Davidson I, Kedinger C, Chatton B: A functional interaction between ATF7 and TAF12 that is modulated by TAF4. Oncogene. 2005 May 12;24(21):3472-83. [PubMed Link Image]
  9. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  10. Hamard PJ, Boyer-Guittaut M, Camuzeaux B, Dujardin D, Hauss C, Oelgeschlager T, Vigneron M, Kedinger C, Chatton B: Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity. Nucleic Acids Res. 2007;35(4):1134-44. Epub 2007 Jan 30. [PubMed Link Image]
  11. Camuzeaux B, Diring J, Hamard PJ, Oulad-Abdelghani M, Donzeau M, Vigneron M, Kedinger C, Chatton B: p38beta2-mediated phosphorylation and sumoylation of ATF7 are mutually exclusive. J Mol Biol. 2008 Dec 26;384(4):980-91. Epub 2008 Oct 11. [PubMed Link Image]
  12. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  14. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  15. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 100 Metabolite References Not Available
Enzyme 101 [top]
Enzyme 101 ID 13828
Enzyme 101 Name Basic leucine zipper transcriptional factor ATF-like
Enzyme 101 Synonyms
  1. B-cell-activating transcription factor
  2. B-ATF
  3. SF-HT-activated gene 2 protein
  4. SFA-2
Enzyme 101 Gene Name BATF
Enzyme 101 Protein Sequence >Basic leucine zipper transcriptional factor ATF-like
MPHSSDSSDSSFSRSPPPGKQDSSDDVRRVQRREKNRIAAQKSRQRQTQKADTLHLESED
LEKQNAALRKEIKQLTEELKYFTSVLNSHEPLCSVLAASTPSPPEVVYSAHAFHQPHVSS
PRFQP
Enzyme 101 Number of Residues 125
Enzyme 101 Molecular Weight 14119.5
Enzyme 101 Theoretical pI 9.17
Enzyme 101 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
  • protein binding
  • protein dimerization activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 101 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 101 Specific Function Functions as a negative regulator of AP-1 mediated transcription by binding to Jun proteins. Jun/B-ATF heterodimers bind DNA preferentially at the 12-O-tetradecanoylphorbol-13- acetate response element (TRE) (consensus:5'-TGA[CG]TCA-3') and weaker at the cAMP-responsive region (CRE) (consensus:5'- GTGACGT[AC][AG]-3'), but are transcriptionally inert
Enzyme 101 Pathways Not Available
Enzyme 101 Reactions Not Available
Enzyme 101 Pfam Domain Function
Enzyme 101 Signals
  • None
Enzyme 101 Transmembrane Regions
  • None
Enzyme 101 Essentiality Not Available
Enzyme 101 GenBank ID Protein 5764706 Link Image
Enzyme 101 UniProtKB/Swiss-Prot ID Q16520 Link Image
Enzyme 101 UniProtKB/Swiss-Prot Entry Name BATF_HUMAN Link Image
Enzyme 101 PDB ID Not Available
Enzyme 101 Cellular Location Not Available
Enzyme 101 Gene Sequence >378 bp
ATGCCTCACAGCTCCGACAGCAGTGACTCCAGCTTCAGCCGCTCTCCTCCCCCTGGCAAA
CAGGACTCATCTGATGATGTGAGAAGAGTTCAGAGGAGGGAGAAAAATCGTATTGCCGCC
CAGAAGAGCCGACAGAGGCAGACACAGAAGGCCGACACCCTGCACCTGGAGAGCGAAGAC
CTGGAGAAACAGAACGCGGCTCTACGCAAGGAGATCAAGCAGCTCACAGAGGAACTGAAG
TACTTCACGTCGGTGCTGAACAGCCACGAGCCCCTGTGCTCGGTGCTGGCCGCCAGCACG
CCCTCGCCCCCCGAGGTGGTGTACAGCGCCCACGCATTCCACCAACCTCATGTCAGCTCC
CCGCGCTTCCAGCCCTGA
Enzyme 101 GenBank Gene ID AC007182 Link Image
Enzyme 101 GeneCard ID BATF Link Image
Enzyme 101 GenAtlas ID BATF Link Image
Enzyme 101 HGNC ID HGNC:958 Link Image
Enzyme 101 Chromosome Location 1
Enzyme 101 Locus 14q24.3
Enzyme 101 SNPs SNPJam Report Link Image
Enzyme 101 General References
  1. Dorsey MJ, Tae HJ, Sollenberger KG, Mascarenhas NT, Johansen LM, Taparowsky EJ: B-ATF: a novel human bZIP protein that associates with members of the AP-1 transcription factor family. Oncogene. 1995 Dec 7;11(11):2255-65. [PubMed Link Image]
  2. Hasegawa H, Utsunomiya Y, Kishimoto K, Tange Y, Yasukawa M, Fujita S: SFA-2, a novel bZIP transcription factor induced by human T-cell leukemia virus type I, is highly expressed in mature lymphocytes. Biochem Biophys Res Commun. 1996 May 6;222(1):164-70. [PubMed Link Image]
  3. Meyer NP, Johansen LM, Tae HJ, Budde PP, Williams KL, Taparowsky EJ: Genomic organization of human B-ATF, a target for regulation by EBV and HTLV-1. Mamm Genome. 1998 Oct;9(10):849-52. [PubMed Link Image]
  4. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Echlin DR, Tae HJ, Mitin N, Taparowsky EJ: B-ATF functions as a negative regulator of AP-1 mediated transcription and blocks cellular transformation by Ras and Fos. Oncogene. 2000 Mar 30;19(14):1752-63. [PubMed Link Image]
  7. Wang X, Johansen LM, Tae HJ, Taparowsky EJ: IFP 35 forms complexes with B-ATF, a member of the AP1 family of transcription factors. Biochem Biophys Res Commun. 1996 Dec 4;229(1):316-22. [PubMed Link Image]
Enzyme 101 Metabolite References Not Available
Enzyme 102 [top]
Enzyme 102 ID 13829
Enzyme 102 Name Cyclic nucleotide-gated olfactory channel
Enzyme 102 Synonyms
  1. Cyclic nucleotide-gated cation channel 2
  2. Cyclic nucleotide-gated channel alpha-2
  3. CNG channel alpha-2
  4. CNG-2
  5. CNG2
Enzyme 102 Gene Name CNGA2
Enzyme 102 Protein Sequence >Cyclic nucleotide-gated olfactory channel
MTEKTNGVKSSPANNHNHHAPPAIKANGKDDHRTSSRPHSAADDDTSSELQRLADVDAPQ
QGRSGFRRIVRLVGIIREWANKNFREEEPRPDSFLERFRGPELQTVTTQEGDGKGDKDGE
DKGTKKKFELFVLDPAGDWYYCWLFVIAMPVLYNWCLLVARACFSDLQKGYYLVWLVLDY
VSDVVYIADLFIRLRTGFLEQGLLVKDTKKLRDNYIHTLQFKLDVASIIPTDLIYFAVDI
HSPEVRFNRLLHFARMFEFFDRTETRTNYPNIFRISNLVLYILVIIHWNACIYYAISKSI
GFGVDTWVYPNITDPEYGYLAREYIYCLYWSTLTLTTIGETPPPVKDEEYLFVIFDFLIG
VLIFATIVGNVGSMISNMNATRAEFQAKIDAVKHYMQFRKVSKGMEAKVIRWFDYLWTNK
KTVDEREILKNLPAKLRAEIAINVHLSTLKKVRIFHDCEAGLLVELVLKLRPQVFSPGDY
ICRKGDIGKEMYIIKEGKLAVVADDGVTQYALLSAGSCFGEISILNIKGSKMGNRRTANI
RSLGYSDLFCLSKDDLMEAVTEYPDAKKVLEERGREILMKEGLLDENEVATSMEVDVQEK
LGQLETNMETLYTRFGRLLAEYTGAQQKLKQRITVLETKMKQNNEDDYLSDGMNSPELAA
ADEP
Enzyme 102 Number of Residues 664
Enzyme 102 Molecular Weight 76047.5
Enzyme 102 Theoretical pI 6.14
Enzyme 102 GO Classification
Function
  • ion channel activity
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 102 General Function Involved in ion channel activity
Enzyme 102 Specific Function Odorant signal transduction is probably mediated by a G- protein coupled cascade using cAMP as second messenger. The olfactory channel can be shown to be activated by cyclic nucleotides which leads to a depolarization of olfactory sensory neurons
Enzyme 102 Pathways Not Available
Enzyme 102 Reactions Not Available
Enzyme 102 Pfam Domain Function
Enzyme 102 Signals
  • None
Enzyme 102 Transmembrane Regions
  • 139-159 172-192 225-245 275-295 351-371 454-474
Enzyme 102 Essentiality Not Available
Enzyme 102 GenBank ID Protein 116496687 Link Image
Enzyme 102 UniProtKB/Swiss-Prot ID Q16280 Link Image
Enzyme 102 UniProtKB/Swiss-Prot Entry Name CNGA2_HUMAN Link Image
Enzyme 102 PDB ID Not Available
Enzyme 102 Cellular Location Not Available
Enzyme 102 Gene Sequence >1995 bp
ATGACCGAAAAAACCAATGGTGTGAAGAGCTCCCCAGCCAATAATCACAACCATCATGCA
CCTCCTGCCATCAAGGCCAATGGCAAAGATGACCACAGGACAAGCAGCAGGCCACACTCT
GCAGCTGACGATGACACCTCCTCAGAACTGCAGAGGCTGGCAGACGTGGATGCCCCACAG
CAGGGAAGGAGTGGCTTCCGCAGGATAGTTCGCCTGGTGGGGATCATCAGAGAATGGGCC
AACAAGAATTTCCGAGAGGAGGAACCTAGGCCTGACTCATTCCTCGAGCGTTTTCGTGGG
CCTGAACTCCAGACTGTGACCACACAGGAGGGGGATGGCAAAGGCGACAAGGATGGCGAG
GACAAAGGCACCAAGAAGAAATTTGAACTATTTGTCTTGGACCCAGCTGGGGATTGGTAC
TACTGCTGGCTATTTGTCATTGCCATGCCCGTCCTTTACAACTGGTGCCTGCTGGTGGCC
AGAGCCTGCTTCAGTGACCTACAGAAAGGCTACTACCTGGTGTGGCTGGTGCTGGATTAT
GTCTCAGATGTGGTCTACATTGCGGACCTCTTCATCCGATTGCGCACAGGTTTCCTGGAG
CAGGGGCTGCTGGTCAAAGATACCAAGAAACTGCGAGACAACTACATCCACACCCTGCAG
TTCAAGCTGGATGTGGCTTCCATCATCCCCACTGACCTGATCTATTTTGCTGTGGACATC
CACAGCCCTGAGGTGCGCTTCAACCGCCTGCTGCACTTTGCCCGCATGTTTGAGTTCTTT
GACCGGACAGAGACACGCACCAACTACCCTAACATCTTCCGCATCAGCAACCTTGTCCTC
TACATCTTGGTCATCATCCACTGGAATGCCTGCATCTATTATGCCATCTCCAAATCCATA
GGCTTTGGGGTCGACACCTGGGTTTACCCAAACATCACTGACCCTGAGTATGGCTACCTG
GCTAGGGAATACATCTATTGCCTTTACTGGTCCACACTGACTCTCACTACCATTGGGGAG
ACACCACCCCCTGTAAAGGATGAGGAGTACCTATTTGTCATCTTTGACTTCCTGATTGGC
GTCCTCATCTTTGCCACCATCGTGGGAAATGTGGGCTCCATGATCTCCAACATGAATGCC
ACCCGGGCAGAGTTCCAGGCTAAGATCGATGCCGTGAAACACTACATGCAGTTCCGAAAG
GTCAGCAAGGGGATGGAAGCCAAGGTCATTAGGTGGTTTGACTACTTGTGGACCAATAAG
AAGACAGTGGATGAGCGAGAAATTCTCAAGAATCTGCCAGCCAAGCTCAGGGCTGAGATA
GCCATCAATGTCCACTTGTCCACACTCAAGAAAGTGCGCATCTTCCATGATTGTGAGGCT
GGCCTGCTGGTAGAGCTGGTACTGAAACTCCGTCCTCAGGTCTTCAGTCCTGGGGATTAC
ATTTGCCGCAAAGGGGACATCGGCAAGGAGATGTACATCATTAAGGAGGGCAAACTGGCA
GTGGTGGCTGATGATGGTGTGACTCAGTATGCTCTGCTGTCGGCTGGAAGCTGCTTTGGC
GAGATCAGTATCCTTAACATTAAGGGCAGTAAAATGGGCAATCGACGCACAGCTAATATC
CGCAGCCTGGGCTACTCAGATCTCTTCTGCTTGTCCAAGGATGATCTTATGGAAGCTGTG
ACTGAGTACCCTGATGCCAAGAAAGTCCTAGAAGAGAGGGGTCGGGAGATCCTCATGAAG
GAGGGACTGCTGGATGAGAACGAAGTGGCAACCAGCATGGAGGTCGACGTGCAGGAGAAG
CTAGGGCAGCTGGAGACCAACATGGAAACCTTGTACACTCGCTTTGGCCGCCTGCTGGCT
GAGTACACGGGGGCCCAGCAGAAGCTCAAGCAGCGCATCACAGTTCTGGAAACCAAGATG
AAACAGAACAATGAAGATGACTACCTGTCTGATGGGATGAACAGCCCTGAGCTGGCTGCT
GCTGACGAGCCATAA
Enzyme 102 GenBank Gene ID BC126302 Link Image
Enzyme 102 GeneCard ID CNGA2 Link Image
Enzyme 102 GenAtlas ID CNGA2 Link Image
Enzyme 102 HGNC ID HGNC:2149 Link Image
Enzyme 102 Chromosome Location Not Available
Enzyme 102 Locus Not Available
Enzyme 102 SNPs SNPJam Report Link Image
Enzyme 102 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Distler M, Biel M, Flockerzi V, Hofmann F: Expression of cyclic nucleotide-gated cation channels in non-sensory tissues and cells. Neuropharmacology. 1994 Nov;33(11):1275-82. [PubMed Link Image]
  3. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 102 Metabolite References Not Available
Enzyme 103 [top]
Enzyme 103 ID 13830
Enzyme 103 Name Cyclic AMP-responsive element-binding protein 3-like protein 1
Enzyme 103 Synonyms
  1. cAMP-responsive element-binding protein 3-like protein 1
  2. Old astrocyte specifically-induced substance
  3. OASIS
  4. Processed cyclic AMP-responsive element-binding protein 3-like protein 1
Enzyme 103 Gene Name CREB3L1
Enzyme 103 Protein Sequence >Cyclic AMP-responsive element-binding protein 3-like protein 1
MDAVLEPFPADRLFPGSSFLDLGDLNESDFLNNAHFPEHLDHFTENMEDFSNDLFSSFFD
DPVLDEKSPLLDMELDSPTPGIQAEHSYSLSGDSAPQSPLVPIKMEDTTQDAEHGAWALG
HKLCSIMVKQEQSPELPVDPLAAPSAMAAAAAMATTPLLGLSPLSRLPIPHQAPGEMTQL
PVIKAEPLEVNQFLKVTPEDLVQMPPTPPSSHGSDSDGSQSPRSLPPSSPVRPMARSSTA
ISTSPLLTAPHKLQGTSGPLLLTEEEKRTLIAEGYPIPTKLPLTKAEEKALKRVRRKIKN
KISAQESRRKKKEYVECLEKKVETFTSENNELWKKVETLENANRTLLQQLQKLQTLVTNK
ISRPYKMAATQTGTCLMVAALCFVLVLGSLVPCLPEFSSGSQTVKEDPLAADGVYTASQM
PSRSLLFYDDGAGLWEDGRSTLLPMEPPDGWEINPGGPAEQRPRDHLQHDHLDSTHETTK
YLSEAWPKDGGNGTSPDFSHSKEWFHDRDLGPNTTIKLS
Enzyme 103 Number of Residues 519
Enzyme 103 Molecular Weight 57004.8
Enzyme 103 Theoretical pI 4.81
Enzyme 103 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
  • protein binding
  • protein dimerization activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 103 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 103 Specific Function Transcription factor that acts during endoplasmic reticulum stress by activating unfolded protein response target genes. Specifically involved in ER-stress response in astrocytes in the central nervous system (By similartity). May play a role in gliosis. In vitro, binds to box-B element, cAMP response element (CRE) and CRE-like sequences, and activates transcription through box-B element but not through CRE
Enzyme 103 Pathways Not Available
Enzyme 103 Reactions Not Available
Enzyme 103 Pfam Domain Function
Enzyme 103 Signals
  • None
Enzyme 103 Transmembrane Regions
  • 375-395
Enzyme 103 Essentiality Not Available
Enzyme 103 GenBank ID Protein 21668502 Link Image
Enzyme 103 UniProtKB/Swiss-Prot ID Q96BA8 Link Image
Enzyme 103 UniProtKB/Swiss-Prot Entry Name CR3L1_HUMAN Link Image
Enzyme 103 PDB ID Not Available
Enzyme 103 Cellular Location Not Available
Enzyme 103 Gene Sequence >1560 bp
ATGGACGCCGTCTTGGAACCCTTCCCGGCCGACAGGCTGTTCCCCGGATCCAGCTTCCTG
GACTTGGGGGATCTGAACGAGTCGGACTTCCTCAACAATGCGCACTTTCCTGAGCACCTG
GACCACTTTACGGAGAACATGGAGGACTTCTCCAATGACCTGTTCAGCAGCTTCTTTGAT
GACCCTGTGCTGGATGAGAAGAGCCCTCTATTGGACATGGAACTGGACTCCCCTACGCCA
GGCATCCAGGCGGAGCACAGCTACTCCCTGAGCGGCGACTCAGCGCCCCAGAGCCCCCTT
GTGCCCATCAAGATGGAGGACACCACCCAAGATGCAGAGCATGGAGCATGGGCGCTGGGA
CACAAACTGTGCTCCATCATGGTGAAGCAGGAGCAGAGCCCGGAGCTGCCCGTGGACCCT
CTGGCTGCCCCCTCGGCCATGGCTGCCGCGGCCGCCATGGCCACCACCCCGCTGCTGGGC
CTCAGCCCCTTGTCCAGGCTGCCCATCCCCCACCAGGCCCCGGGAGAGATGACTCAGCTG
CCAGTGATCAAAGCAGAGCCTCTGGAGGTGAACCAGTTCCTCAAAGTGACACCGGAGGAC
CTGGTGCAGATGCCTCCGACGCCCCCCAGCAGCCATGGCAGTGACAGCGACGGCTCCCAG
AGTCCCCGCTCTCTGCCCCCCTCCAGCCCTGTCAGGCCCATGGCGCGCTCCTCCACGGCC
ATCTCCACCTCCCCACTCCTCACTGCCCCTCACAAATTACAGGGGACATCAGGGCCACTG
CTCCTGACAGAGGAGGAGAAGCGGACCCTGATTGCTGAGGGCTACCCCATCCCCACAAAA
CTCCCCCTCACCAAAGCCGAGGAGAAGGCCTTGAAGAGAGTCCGGAGGAAAATCAAGAAC
AAGATCTCAGCCCAGGAGAGCCGTCGTAAGAAGAAGGAGTATGTGGAGTGTCTAGAAAAG
AAGGTGGAGACATTTACATCTGAGAACAATGAACTGTGGAAGAAGGTGGAGACCCTGGAG
AATGCCAACAGGACCCTGCTCCAGCAGCTGCAGAAACTCCAGACTCTGGTCACCAACAAG
ATCTCCAGACCTTACAAGATGGCCGCCACCCAGACTGGGACCTGCCTCATGGTGGCAGCC
TTGTGCTTTGTTCTGGTGCTGGGCTCCCTCGTGCCCTGCCTTCCCGAGTTCTCCTCCGGC
TCCCAGACTGTGAAGGAAGACCCCCTGGCCGCAGACGGCGTCTACACGGCCAGCCAGATG
CCCTCCCGAAGCCTCCTATTCTACGATGACGGGGCAGGCTTATGGGAAGATGGCCGCAGC
ACCCTGCTGCCCATGGAGCCCCCAGATGGCTGGGAAATCAACCCCGGGGGGCCGGCAGAG
CAGCGGCCCCGGGACCACCTGCAGCATGATCACCTGGACAGCACCCACGAGACCACCAAG
TACCTGAGTGAGGCCTGGCCTAAAGACGGTGGAAACGGCACCAGCCCCGACTTCTCCCAC
TCCAAGGAGTGGTTCCACGACAGGGATCTGGGCCCCAACACCACCATCAAACTCTCCTAG
Enzyme 103 GenBank Gene ID AB063321 Link Image
Enzyme 103 GeneCard ID CREB3L1 Link Image
Enzyme 103 GenAtlas ID CREB3L1 Link Image
Enzyme 103 HGNC ID HGNC:18856 Link Image
Enzyme 103 Chromosome Location 1
Enzyme 103 Locus 11p11.2
Enzyme 103 SNPs SNPJam Report Link Image
Enzyme 103 General References
  1. Omori Y, Imai J, Suzuki Y, Watanabe S, Tanigami A, Sugano S: OASIS is a transcriptional activator of CREB/ATF family with a transmembrane domain. Biochem Biophys Res Commun. 2002 Apr 26;293(1):470-7. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Murakami T, Kondo S, Ogata M, Kanemoto S, Saito A, Wanaka A, Imaizumi K: Cleavage of the membrane-bound transcription factor OASIS in response to endoplasmic reticulum stress. J Neurochem. 2006 Feb;96(4):1090-100. Epub 2006 Jan 17. [PubMed Link Image]
Enzyme 103 Metabolite References Not Available
Enzyme 104 [top]
Enzyme 104 ID 13831
Enzyme 104 Name Cyclic AMP-responsive element-binding protein 3-like protein 2
Enzyme 104 Synonyms
  1. cAMP-responsive element-binding protein 3-like protein 2
  2. BBF2 human homolog on chromosome 7
  3. Processed cyclic AMP-responsive element-binding protein 3-like protein 2
Enzyme 104 Gene Name CREB3L2
Enzyme 104 Protein Sequence >Cyclic AMP-responsive element-binding protein 3-like protein 2
MEVLESGEQGVLQWDRKLSELSEPGDGEALMYHTHFSELLDEFSQNVLGQLLNDPFLSEK
SVSMEVEPSPTSPAPLIQAEHSYSLCEEPRAQSPFTHITTSDSFNDDEVESEKWYLSTDF
PSTSIKTEPVTDEPPPGLVPSVTLTITAISTPLEKEEPPLEMNTGVDSSCQTIIPKIKLE
PHEVDQFLNFSPKEAPVDHLHLPPTPPSSHGSDSEGSLSPNPRLHPFSLPQTHSPSRAAP
RAPSALSSSPLLTAPHKLQGSGPLVLTEEEKRTLIAEGYPIPTKLPLSKSEEKALKKIRR
KIKNKISAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNRTLLQQLQKLQTL
VMGKVSRTCKLAGTQTGTCLMVVVLCFAVAFGSFFQGYGPYPSATKMALPSQHSLQEPYT
ASVVRSRNLLIYEEHSPPEESSSPGSAGELGGWDRGSSLLRVSGLESRPDVDLPHFIISN
ETSLEKSVLLELQQHLVSAKLEGNETLKVVELDRRVNTTF
Enzyme 104 Number of Residues 520
Enzyme 104 Molecular Weight 57414.3
Enzyme 104 Theoretical pI 5.13
Enzyme 104 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
  • protein binding
  • protein dimerization activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
Enzyme 104 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 104 Specific Function Transcriptional activator which is processed and activated during endoplasmic reticulum stress late phase. Binds to the cAMP response element (CRE) and activates transcription through CRE. Regulates the transcription of unfolded protein response target genes, preventing accumulation of unfolded proteins in damaged neurons. Also regulates the expression of SEC23A, accelerating protein trafficking from the ER to the Golgi thereby playing a key role in chondrocyte differentiation and formation of epiphyseal cartilage
Enzyme 104 Pathways Not Available
Enzyme 104 Reactions Not Available
Enzyme 104 Pfam Domain Function
Enzyme 104 Signals
  • None
Enzyme 104 Transmembrane Regions
  • 380-400
Enzyme 104 Essentiality Not Available
Enzyme 104 GenBank ID Protein 56550067 Link Image
Enzyme 104 UniProtKB/Swiss-Prot ID Q70SY1 Link Image
Enzyme 104 UniProtKB/Swiss-Prot Entry Name CR3L2_HUMAN Link Image
Enzyme 104 PDB ID Not Available
Enzyme 104 Cellular Location Not Available
Enzyme 104 Gene Sequence >1563 bp
ATGGAGGTGCTGGAGAGCGGGGAGCAGGGCGTGCTGCAGTGGGACCGCAAGCTGAGCGAG
CTGTCAGAGCCCGGGGACGGCGAGGCCCTCATGTACCACACGCACTTCTCAGAACTTCTG
GATGAGTTTTCCCAGAACGTCTTGGGTCAGCTCCTGAATGATCCTTTCCTCTCAGAGAAG
AGTGTGTCAATGGAGGTGGAACCTTCCCCGACGTCCCCGGCGCCTCTCATCCAGGCTGAG
CACAGCTACTCCCTGTGCGAGGAGCCTCGGGCCCAGTCGCCCTTCACCCACATTACCACC
AGTGACAGCTTCAATGACGATGAGGTGGAAAGTGAGAAATGGTACCTGTCTACAGACTTC
CCTTCAACATCCATCAAGACAGAGCCAGTTACAGACGAACCACCCCCAGGACTCGTTCCG
TCTGTCACTCTGACCATCACAGCCATCTCCACCCCGTTGGAAAAGGAGGAACCTCCTCTG
GAAATGAACACTGGGGTTGATTCCTCGTGCCAGACCATTATTCCTAAAATTAAGCTGGAG
CCTCATGAAGTGGATCAGTTTCTAAACTTCTCTCCTAAAGAAGCCCCAGTGGACCACCTG
CATTTGCCGCCCACCCCTCCGAGCAGTCACGGCAGTGACTCAGAGGGCAGCCTGAGTCCC
AACCCACGCCTGCACCCCTTCAGCCTGCCTCAGACCCACAGCCCCTCCAGAGCTGCACCC
CGGGCCCCCTCCGCCCTCTCCAGCTCCCCTCTCCTCACGGCTCCTCATAAACTGCAGGGA
TCAGGCCCTCTGGTCCTGACAGAGGAGGAGAAGAGGACCCTGATCGCTGAGGGCTATCCC
ATCCCCACCAAATTGCCCCTGTCAAAATCAGAGGAGAAGGCCCTGAAGAAAATTCGGAGG
AAGATCAAGAATAAGATTTCTGCTCAGGAAAGTAGGAGAAAGAAGAAAGAATACATGGAC
AGCCTGGAGAAAAAAGTGGAGTCTTGTTCAACTGAGAACTTGGAGCTTCGGAAGAAGGTA
GAGGTTCTAGAGAACACTAATAGGACTCTCCTTCAGCAACTCCAGAAGCTTCAGACTTTG
GTGATGGGCAAGGTTTCTCGAACCTGCAAGTTAGCTGGCACGCAGACTGGCACCTGCCTC
ATGGTTGTGGTGCTGTGCTTTGCCGTTGCATTCGGCAGCTTCTTTCAAGGCTACGGGCCC
TATCCTTCTGCCACCAAGATGGCTCTGCCCAGCCAGCATTCCCTGCAGGAGCCCTACACA
GCCTCCGTGGTGAGATCCAGAAACCTGCTGATCTACGAGGAACATTCTCCCCCAGAGGAG
TCATCCAGCCCGGGCTCGGCTGGGGAGCTGGGGGGCTGGGATAGAGGTTCCTCCCTGCTC
AGGGTGTCAGGGCTGGAGTCCAGGCCGGATGTGGATCTTCCCCATTTCATTATCTCGAAT
GAGACCAGCCTGGAGAAGTCAGTGCTTTTGGAGCTGCAGCAGCACCTGGTCAGCGCCAAA
CTGGAGGGGAATGAAACACTAAAAGTTGTAGAACTCGACAGAAGAGTGAACACCACTTTC
TAA
Enzyme 104 GenBank Gene ID NM_194071.2 Link Image
Enzyme 104 GeneCard ID CREB3L2 Link Image
Enzyme 104 GenAtlas ID CREB3L2 Link Image
Enzyme 104 HGNC ID HGNC:23720 Link Image
Enzyme 104 Chromosome Location 7
Enzyme 104 Locus 7q34
Enzyme 104 SNPs SNPJam Report Link Image
Enzyme 104 General References
  1. Storlazzi CT, Mertens F, Nascimento A, Isaksson M, Wejde J, Brosjo O, Mandahl N, Panagopoulos I: Fusion of the FUS and BBF2H7 genes in low grade fibromyxoid sarcoma. Hum Mol Genet. 2003 Sep 15;12(18):2349-58. Epub 2003 Jul 22. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Panagopoulos I, Storlazzi CT, Fletcher CD, Fletcher JA, Nascimento A, Domanski HA, Wejde J, Brosjo O, Rydholm A, Isaksson M, Mandahl N, Mertens F: The chimeric FUS/CREB3l2 gene is specific for low-grade fibromyxoid sarcoma. Genes Chromosomes Cancer. 2004 Jul;40(3):218-28. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Kondo S, Saito A, Hino S, Murakami T, Ogata M, Kanemoto S, Nara S, Yamashita A, Yoshinaga K, Hara H, Imaizumi K: BBF2H7, a novel transmembrane bZIP transcription factor, is a new type of endoplasmic reticulum stress transducer. Mol Cell Biol. 2007 Mar;27(5):1716-29. Epub 2006 Dec 18. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 104 Metabolite References Not Available
Enzyme 105 [top]
Enzyme 105 ID 13832
Enzyme 105 Name Cyclic AMP-responsive element-binding protein 3-like protein 3
Enzyme 105 Synonyms
  1. cAMP-responsive element-binding protein 3-like protein 3
  2. Transcription factor CREB-H
  3. Processed cyclic AMP-responsive element-binding protein 3-like protein 3
Enzyme 105 Gene Name CREB3L3
Enzyme 105 Protein Sequence >Cyclic AMP-responsive element-binding protein 3-like protein 3
MNTDLAAGKMASAACSMDPIDSFELLDLLFDRQDGILRHVELGEGWGHVKDQQVLPNPDS
DDFLSSILGSGDSLPSSPLWSPEGSDSGISEDLPSDPQDTPPRSGPATSPAGCHPAQPGK
GPCLSYHPGNSCSTTTPGPVIQVPEASVTIDLEMWSPGGRICAEKPADPVDLSPRCNLTV
KDLLLSGSSGDLQQHHLGASYLLRPGAGHCQELVLTEDEKKLLAKEGITLPTQLPLTKYE
ERVLKKIRRKIRNKQSAQESRKKKKEYIDGLETRMSACTAQNQELQRKVLHLEKQNLSLL
EQLKKLQAIVVQSTSKSAQTGTCVAVLLLSFALIILPSISPFGPNKTESPGDFAPVRVFS
RTLHNDAASRVAADAVPGSEAPGPRPEADTTREESPGSPGADWGFQDTANLTNSTEELDN
ATLVLRNATEGLGQVALLDWVAPGPSTGSGRAGLEAAGDEL
Enzyme 105 Number of Residues 461
Enzyme 105 Molecular Weight 49076.6
Enzyme 105 Theoretical pI 4.76
Enzyme 105 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
  • protein binding
  • protein dimerization activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
Enzyme 105 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 105 Specific Function Transcription factor that may act during endoplasmic reticulum stress by activating unfolded protein response target genes. Activated in response to cAMP stimulation. In vitro, binds to the cAMP response element (CRE) and box-B element. Activates transcription through box-B element. Activates transcription through CRE. Seems to function synergistically with ATF6. In acute inflammatory response, may activate expression of acute phase response (APR) genes. May be involved in growth suppression
Enzyme 105 Pathways Not Available
Enzyme 105 Reactions Not Available
Enzyme 105 Pfam Domain Function
Enzyme 105 Signals
  • None
Enzyme 105 Transmembrane Regions
  • 323-343
Enzyme 105 Essentiality Not Available
Enzyme 105 GenBank ID Protein 13990957 Link Image
Enzyme 105 UniProtKB/Swiss-Prot ID Q68CJ9 Link Image
Enzyme 105 UniProtKB/Swiss-Prot Entry Name CR3L3_HUMAN Link Image
Enzyme 105 PDB ID Not Available
Enzyme 105 Cellular Location Not Available
Enzyme 105 Gene Sequence >1386 bp
ATGAATACGGATTTAGCTGCTGGAAAGATGGCTTCTGCTGCCTGCTCCATGGACCCCATC
GACAGCTTTGAGCTCCTGGATCTCCTGTTTGACCGGCAGGACGGCATCCTGAGACACGTG
GAGCTGGGCGAGGGCTGGGGTCACGTCAAGGACCAGCAGGTCCTGCCAAACCCCGACTCT
GACGACTTCCTCAGCTCCATCCTGGGCTCTGGAGACTCACTGCCCAGCTCCCCACTCTGG
TCCCCCGAAGGCAGTGATAGTGGCATCTCCGAAGACCTCCCCTCCGACCCCCAGGACACC
CCTCCACGCAGCGGACCAGCCACCTCCCCCGCCGGCTGCCATCCTGCCCAGCCTGGCAAG
GGGCCCTGCCTCTCCTATCATCCTGGCAACTCTTGCTCCACCACAACCCCAGGGCCAGTG
ATCCAAGTACCTGAAGCCTCTGTGACCATAGACCTGGAAATGTGGAGCCCAGGAGGAAGG
ATCTGTGCTGAGAAGCCGGCTGATCCGGTGGACCTGTCCCCACGATGCAATCTCACCGTG
AAAGACCTCCTCCTTTCGGGCAGCAGTGGGGACCTGCAACAGCATCACCTGGGGGCCTCC
TACCTCCTGCGACCTGGGGCTGGGCACTGTCAGGAGCTGGTGCTCACCGAGGATGAGAAG
AAGCTGCTGGCTAAAGAAGGCATCACCCTGCCCACTCAGCTGCCCCTCACTAAGTACGAG
GAGCGAGTGCTGAAAAAAATCCGCCGGAAAATCCGGAACAAGCAGTCGGCGCAAGAAAGC
AGGAAGAAGAAGAAGGAATATATCGATGGCCTGGAGACTCGGATGTCAGCTTGCACTGCT
CAGAATCAGGAGTTACAGAGGAAAGTCTTGCATCTCGAGAAGCAAAACCTGTCCCTCTTG
GAGCAACTGAAGAAACTCCAGGCCATTGTGGTGCAGTCCACCAGCAAGTCAGCCCAGACA
GGCACCTGTGTCGCAGTCCTGTTGCTGTCCTTTGCCCTCATCATCCTCCCCTCCATCAGC
CCTTTTGGCCCCAACAAAACCGAGAGCCCTGGGGACTTTGCGCCTGTACGAGTGTTCTCC
AGAACTTTGCACAACGATGCTGCCTCCCGCGTGGCTGCTGATGCTGTGCCAGGCTCCGAG
GCCCCAGGACCCCGACCCGAGGCTGACACAACCCGAGAAGAGTCTCCAGGAAGCCCCGGG
GCAGACTGGGGCTTCCAGGACACCGCGAACCTGACCAATTCGACGGAGGAGCTGGACAAC
GCCACCCTGGTCCTGAGGAATGCAACAGAGGGGCTGGGCCAGGTCGCCCTGCTGGACTGG
GTGGCGCCTGGGCCGAGCACTGGCTCAGGACGTGCAGGGCTGGAGGCGGCGGGAGACGAG
CTGTGA
Enzyme 105 GenBank Gene ID AB050902 Link Image
Enzyme 105 GeneCard ID CREB3L3 Link Image
Enzyme 105 GenAtlas ID CREB3L3 Link Image
Enzyme 105 HGNC ID HGNC:18855 Link Image
Enzyme 105 Chromosome Location 1
Enzyme 105 Locus 19p13.3
Enzyme 105 SNPs SNPJam Report Link Image
Enzyme 105 General References
  1. Omori Y, Imai J, Watanabe M, Komatsu T, Suzuki Y, Kataoka K, Watanabe S, Tanigami A, Sugano S: CREB-H: a novel mammalian transcription factor belonging to the CREB/ATF family and functioning via the box-B element with a liver-specific expression. Nucleic Acids Res. 2001 May 15;29(10):2154-62. [PubMed Link Image]
  2. Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Chin KT, Zhou HJ, Wong CM, Lee JM, Chan CP, Qiang BQ, Yuan JG, Ng IO, Jin DY: The liver-enriched transcription factor CREB-H is a growth suppressor protein underexpressed in hepatocellular carcinoma. Nucleic Acids Res. 2005 Mar 30;33(6):1859-73. Print 2005. [PubMed Link Image]
  6. Zhang K, Shen X, Wu J, Sakaki K, Saunders T, Rutkowski DT, Back SH, Kaufman RJ: Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell. 2006 Feb 10;124(3):587-99. [PubMed Link Image]
  7. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
Enzyme 105 Metabolite References Not Available
Enzyme 106 [top]
Enzyme 106 ID 13833
Enzyme 106 Name Cyclic AMP-responsive element-binding protein 3
Enzyme 106 Synonyms
  1. CREB-3
  2. cAMP-responsive element-binding protein 3
  3. Luman
  4. Transcription factor LZIP-alpha
  5. Processed cyclic AMP-responsive element-binding protein 3
Enzyme 106 Gene Name CREB3
Enzyme 106 Protein Sequence >Cyclic AMP-responsive element-binding protein 3
MELELDAGDQDLLAFLLEESGDLGTAPDEAVRAPLDWALPLSEVPSDWEVDDLLCSLLSP
PASLNILSSSNPCLVHHDHTYSLPRETVSMDLGECEISLTGRTGFMGLAIHTFPFAESES
CRKEGTQMTPQHMEELAEQEIARLVLTDEEKSLLEKEGLILPETLPLTKTEEQILKRVRR
KIRNKRSAQESRRKKKVYVGGLESRVLKYTAQNMELQNKVQLLEEQNLSLLDQLRKLQAM
VIEISNKTSSSSTCILVLLVSFCLLLVPAMYSSDTRGSLPAEHGVLSRQLRALPSEDPYQ
LELPALQSEVPKDSTHQWLDGSDCVLQAPGNTSCLLHYMPQAPSAEPPLEWPFPDLFSEP
LCRGPILPLQANLTRKGGWLPTGSPSVILQDRYSG
Enzyme 106 Number of Residues 395
Enzyme 106 Molecular Weight 43916.7
Enzyme 106 Theoretical pI 4.57
Enzyme 106 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
  • protein binding
  • protein dimerization activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
Enzyme 106 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 106 Specific Function Transcription factors activated upon intramembrane proteolysis (RIP), binds the cAMP response element (CRE) (consensus:5'-GTGACGT[AG][AG]-3'), a sequence present in many viral and cellular promoters. Binds to and requires HCFC1 as a coactivator. Activity and expression are suppressed when the HCFC1-CREB3 complex binds with CREBZF. Participates in LKN- 1/CCL15-induced chemotaxis signaling
Enzyme 106 Pathways Not Available
Enzyme 106 Reactions Not Available
Enzyme 106 Pfam Domain Function
Enzyme 106 Signals
  • None
Enzyme 106 Transmembrane Regions
  • 255-271
Enzyme 106 Essentiality Not Available
Enzyme 106 GenBank ID Protein 2911282 Link Image
Enzyme 106 UniProtKB/Swiss-Prot ID O43889 Link Image
Enzyme 106 UniProtKB/Swiss-Prot Entry Name CREB3_HUMAN Link Image
Enzyme 106 PDB ID Not Available
Enzyme 106 Cellular Location Not Available
Enzyme 106 Gene Sequence >1188 bp
ATGGAGCTGGAATTGGATGCTGGTGACCAAGACCTGCTGGCCTTCCTGCTAGAGGAAAGT
GGAGATTTGGGGACGGCACCCGATGAGGCCGTGAGGGCCCCACTGGACTGGGCGCTGCCG
CTTTCTGAGGTACCGAGCGACTGGGAAGTAGATGATTTGCTGTGCTCCCTGCTGAGTCCC
CCAGCGTCGTTGAACATTCTCAGCTCCTCCAACCCCTGCCTTGTCCACCATGACCACACC
TACTCCCTCCCACGGGAAACTGTCTCTATGGATCTAGGTGAGTGTGAAATAAGTTTGACG
GGGAGGACAGGGTTCATGGGCCTGGCTATTCATACTTTCCCTTTTGCAGAGAGTGAGAGC
TGTAGAAAAGAGGGGACCCAGATGACTCCACAGCATATGGAGGAGCTGGCAGAGCAGGAG
ATTGCTAGGCTAGTACTGACAGATGAGGAGAAGAGTCTATTGGAGAAGGAGGGGCTTATT
CTGCCTGAGACACTTCCTCTCACTAAGACAGAGGAACAAATTCTGAAACGTGTGCGGAGG
AAGATTCGAAATAAAAGATCTGCTCAAGAGAGCCGCAGGAAAAAGAAGGTGTATGTTGGG
GGTTTAGAGAGCAGGGTCTTGAAATACACAGCCCAGAATATGGAGCTTCAGAACAAAGTA
CAGCTTCTGGAGGAACAGAATTTGTCCCTTCTAGATCAACTGAGGAAACTCCAGGCCATG
GTGATTGAGATATCAAACAAAACCAGCAGCAGCAGCACCTGCATCTTGGTCCTACTAGTC
TCCTTCTGCCTCCTCCTTGTACCTGCTATGTACTCCTCTGACACAAGGGGGAGCCTGCCA
GCTGAGCATGGAGTGTTGTCCCGCCAGCTTCGTGCCCTCCCCAGTGAGGACCCTTACCAG
CTGGAGCTGCCTGCCCTGCAGTCAGAAGTGCCGAAAGACAGCACACACCAGTGGTTGGAC
GGCTCAGACTGTGTACTCCAGGCCCCTGGCAACACTTCCTGCCTGCTGCATTACATGCCT
CAGGCTCCCAGTGCAGAGCCTCCCCTGGAGTGGCCATTCCCTGACCTCTTCTCAGAGCCT
CTCTGCCGAGGTCCCATCCTCCCCCTGCAGGCAAATCTCACAAGGAAGGGAGGATGGCTT
CCTACTGGTAGCCCCTCTGTCATTTTGCAGGACAGATACTCAGGCTAG
Enzyme 106 GenBank Gene ID U88528 Link Image
Enzyme 106 GeneCard ID CREB3 Link Image
Enzyme 106 GenAtlas ID CREB3 Link Image
Enzyme 106 HGNC ID HGNC:2347 Link Image
Enzyme 106 Chromosome Location 9
Enzyme 106 Locus 9p13.3
Enzyme 106 SNPs SNPJam Report Link Image
Enzyme 106 General References
  1. Lu R, Yang P, O'Hare P, Misra V: Luman, a new member of the CREB/ATF family, binds to herpes simplex virus VP16-associated host cellular factor. Mol Cell Biol. 1997 Sep;17(9):5117-26. [PubMed Link Image]
  2. Freiman RN, Herr W: Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP. Genes Dev. 1997 Dec 1;11(23):3122-7. [PubMed Link Image]
  3. Jin DY, Wang HL, Zhou Y, Chun AC, Kibler KV, Hou YD, Kung H, Jeang KT: Hepatitis C virus core protein-induced loss of LZIP function correlates with cellular transformation. EMBO J. 2000 Feb 15;19(4):729-40. [PubMed Link Image]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Lu R, Misra V: Potential role for luman, the cellular homologue of herpes simplex virus VP16 (alpha gene trans-inducing factor), in herpesvirus latency. J Virol. 2000 Jan;74(2):934-43. [PubMed Link Image]
  7. Luciano RL, Wilson AC: N-terminal transcriptional activation domain of LZIP comprises two LxxLL motifs and the host cell factor-1 binding motif. Proc Natl Acad Sci U S A. 2000 Sep 26;97(20):10757-62. [PubMed Link Image]
  8. Raggo C, Rapin N, Stirling J, Gobeil P, Smith-Windsor E, O'Hare P, Misra V: Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis. Mol Cell Biol. 2002 Aug;22(16):5639-49. [PubMed Link Image]
  9. Mahajan SS, Wilson AC: Mutations in host cell factor 1 separate its role in cell proliferation from recruitment of VP16 and LZIP. Mol Cell Biol. 2000 Feb;20(3):919-28. [PubMed Link Image]
  10. Ko J, Jang SW, Kim YS, Kim IS, Sung HJ, Kim HH, Park JY, Lee YH, Kim J, Na DS: Human LZIP binds to CCR1 and differentially affects the chemotactic activities of CCR1-dependent chemokines. FASEB J. 2004 May;18(7):890-2. Epub 2004 Mar 4. [PubMed Link Image]
  11. Misra V, Rapin N, Akhova O, Bainbridge M, Korchinski P: Zhangfei is a potent and specific inhibitor of the host cell factor-binding transcription factor Luman. J Biol Chem. 2005 Apr 15;280(15):15257-66. Epub 2005 Feb 9. [PubMed Link Image]
Enzyme 106 Metabolite References Not Available
Enzyme 107 [top]
Enzyme 107 ID 13834
Enzyme 107 Name Luc7-like protein 3
Enzyme 107 Synonyms
  1. Cisplatin resistance-associated-overexpressed protein
  2. Luc7A
  3. Okadaic acid-inducible phosphoprotein OA48-18
  4. cAMP regulatory element-associated protein 1
  5. CRE-associated protein 1
  6. CREAP-1
Enzyme 107 Gene Name LUC7L3
Enzyme 107 Protein Sequence >Luc7-like protein 3
MISAAQLLDELMGRDRNLAPDEKRSNVRWDHESVCKYYLCGFCPAELFTNTRSDLGPCEK
IHDENLRKQYEKSSRFMKVGYERDFLRYLQSLLAEVERRIRRGHARLALSQNQQSSGAAG
PTGKNEEKIQVLTDKIDVLLQQIEELGSEGKVEEAQGMMKLVEQLKEERELLRSTTSTIE
SFAAQEKQMEVCEVCGAFLIVGDAQSRVDDHLMGKQHMGYAKIKATVEELKEKLRKRTEE
PDRDERLKKEKQEREEREKEREREREERERKRRREEEEREKERARDRERRKRSRSRSRHS
SRTSDRRCSRSRDHKRSRSRERRRSRSRDRRRSRSHDRSERKHRSRSRDRRRSKSRDRKS
YKHRSKSRDREQDRKSKEKEKRGSDDKKSSVKSGSREKQSEDTNTESKESDTKNEVNGTS
EDIKSEGDTQSN
Enzyme 107 Number of Residues 432
Enzyme 107 Molecular Weight 51465.7
Enzyme 107 Theoretical pI 10.46
Enzyme 107 GO Classification Not Available
Enzyme 107 General Function Involved in DNA binding
Enzyme 107 Specific Function Binds cAMP regulatory element DNA sequence. May play a role in RNA splicing
Enzyme 107 Pathways Not Available
Enzyme 107 Reactions Not Available
Enzyme 107 Pfam Domain Function
Enzyme 107 Signals
  • None
Enzyme 107 Transmembrane Regions
  • None
Enzyme 107 Essentiality Not Available
Enzyme 107 GenBank ID Protein 6899846 Link Image
Enzyme 107 UniProtKB/Swiss-Prot ID O95232 Link Image
Enzyme 107 UniProtKB/Swiss-Prot Entry Name LC7L3_HUMAN Link Image
Enzyme 107 PDB ID Not Available
Enzyme 107 Cellular Location Not Available
Enzyme 107 Gene Sequence >1299 bp
ATGATTTCGGCCGCGCAGTTGTTGGATGAGTTAATGGGCCGGGACCGAAACCTAGCCCCG
GACGAGAAGCGCAGCAACGTGCGGTGGGACCACGAGAGCGTTTGTAAATATTATCTCTGT
GGTTTTTGTCCTGCGGAATTGTTCACAAATACACGTTCTGATCTTGGTCCGTGTGAAAAA
ATTCATGATGAAAATCTACGAAAACAGTATGAGAAGAGCTCTCGTTTCATGAAAGTTGGC
TATGAAAGAGATTTTTTGCGATACTTACAGAGCTTACTTGCAGAAGTAGAACGTAGGATC
AGACGAGGCCATGCTCGTTTGGCATTATCTCAAAACCAGCAGTCTTCTGGGGCCGCTGGC
CCAACAGGCAAAAATGAAGAAAAAATTCAGGTTCTAACAGACAAAATTGATGTACTTCTG
CAACAGATTGAAGAATTAGGGTCTGAAGGAAAAGTAGAAGAAGCCCAGGGGATGATGAAA
TTAGTTGAGCAATTAAAAGAAGAGAGAGAACTGCTAAGGTCCACAACGTCGACAATTGAA
AGCTTTGCTGCACAAGAAAAACAAATGGAAGTTTGTGAAGTATGTGGAGCCTTTTTAATA
GTAGGAGATGCCCAGTCCCGGGTAGATGACCATTTGATGGGAAAACAACACATGGGCTAT
GCCAAAATTAAAGCTACTGTAGAAGAATTAAAAGAAAAGTTAAGGAAAAGAACCGAAGAA
CCTGATCGTGATGAGCGTCTAAAAAAGGAGAAGCAAGAAAGAGAAGAAAGAGAAAAAGAA
CGGGAGAGAGAAAGGGAAGAAAGAGAAAGGAAAAGACGAAGGGAAGAGGAAGAAAGAGAA
AAAGAAAGGGCTCGTGACAGAGAAAGAAGAAAGAGAAGTCGTTCACGAAGTAGACACTCA
AGCCGAACATCAGACAGAAGATGCAGCAGGTCTCGGGACCACAAAAGGTCACGAAGTAGA
GAAAGAAGGCGGAGCAGAAGTAGAGATCGACGAAGAAGCAGAAGCCATGATCGATCAGAA
AGAAAACACAGATCTCGAAGTCGGGATCGAAGAAGATCAAAAAGCCGGGATCGAAAGTCA
TATAAGCACAGGAGCAAAAGTCGGGACAGAGAACAAGATAGAAAATCCAAGGAGAAAGAA
AAGAGGGGATCTGATGATAAAAAAAGTAGTGTGAAGTCCGGTAGTCGAGAAAAGCAGAGT
GAAGACACAAACACTGAATCGAAGGAAAGTGATACTAAGAATGAGGTCAATGGGACCAGT
GAAGACATTAAATCTGAAGGTGACACTCAGTCCAATTAA
Enzyme 107 GenBank Gene ID AB034205 Link Image
Enzyme 107 GeneCard ID LUC7L3 Link Image
Enzyme 107 GenAtlas ID LUC7L3 Link Image
Enzyme 107 HGNC ID HGNC:24309 Link Image
Enzyme 107 Chromosome Location 1
Enzyme 107 Locus 17q21.33
Enzyme 107 SNPs SNPJam Report Link Image
Enzyme 107 General References
  1. Nishii Y, Morishima M, Kakehi Y, Umehara K, Kioka N, Terano Y, Amachi T, Ueda K: CROP/Luc7A, a novel serine/arginine-rich nuclear protein, isolated from cisplatin-resistant cell line. FEBS Lett. 2000 Jan 14;465(2-3):153-6. [PubMed Link Image]
  2. Shipman KL, Robinson PJ, King BR, Smith R, Nicholson RC: Identification of a family of DNA-binding proteins with homology to RNA splicing factors. Biochem Cell Biol. 2006 Feb;84(1):9-19. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Chin LS, Singh SK, Wang Q, Murray SF: Identification of okadaic-acid-induced genes by mRNA differential display in glioma cells. J Biomed Sci. 2000 Mar-Apr;7(2):152-9. [PubMed Link Image]
  6. Umehara H, Nishii Y, Morishima M, Kakehi Y, Kioka N, Amachi T, Koizumi J, Hagiwara M, Ueda K: Effect of cisplatin treatment on speckled distribution of a serine/arginine-rich nuclear protein CROP/Luc7A. Biochem Biophys Res Commun. 2003 Feb 7;301(2):324-9. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  9. Zhou A, Ou AC, Cho A, Benz EJ Jr, Huang SC: Novel splicing factor RBM25 modulates Bcl-x pre-mRNA 5' splice site selection. Mol Cell Biol. 2008 Oct;28(19):5924-36. Epub 2008 Jul 28. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  12. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  13. Webby CJ, Wolf A, Gromak N, Dreger M, Kramer H, Kessler B, Nielsen ML, Schmitz C, Butler DS, Yates JR 3rd, Delahunty CM, Hahn P, Lengeling A, Mann M, Proudfoot NJ, Schofield CJ, Bottger A: Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing. Science. 2009 Jul 3;325(5936):90-3. [PubMed Link Image]
  14. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 107 Metabolite References Not Available
Enzyme 108 [top]
Enzyme 108 ID 13835
Enzyme 108 Name CREB-regulated transcription coactivator 3
Enzyme 108 Synonyms
  1. Transducer of regulated cAMP response element-binding protein 3
  2. TORC-3
  3. Transducer of CREB protein 3
Enzyme 108 Gene Name CRTC3
Enzyme 108 Protein Sequence >CREB-regulated transcription coactivator 3
MAASPGSGSANPRKFSEKIALHTQRQAEETRAFEQLMTDLTLSRVQFQKLQQLRLTQYHG
GSLPNVSQLRSSASEFQPSFHQADNVRGTRHHGLVERPSRNRFHPLHRRSGDKPGRQFDG
SAFGANYSSQPLDESWPRQQPPWKDEKHPGFRLTSALNRTNSDSALHTSALSTKPQDPYG
GGGQSAWPAPYMGFCDGENNGHGEVASFPGPLKEENLLNVPKPLPKQLWETKEIQSLSGR
PRSCDVGGGNAFPHNGQNLGLSPFLGTLNTGGSLPDLTNLHYSTPLPASLDTTDHHFGSM
SVGNSVNNIPAAMTHLGIRSSSGLQSSRSNPSIQATLNKTVLSSSLNNHPQTSVPNASAL
HPSLRLFSLSNPSLSTTNLSGPSRRRQPPVSPLTLSPGPEAHQGFSRQLSSTSPLAPYPT
SQMVSSDRSQLSFLPTEAQAQVSPPPPYPAPQELTQPLLQQPRAPEAPAQQPQAASSLPQ
SDFQLLPAQGSSLTNFFPDVGFDQQSMRPGPAFPQQVPLVQQGSRELQDSFHLRPSPYSN
CGSLPNTILPEDSSTSLFKDLNSALAGLPEVSLNVDTPFPLEEELQIEPLSLDGLNMLSD
SSMGLLDPSVEETFRADRL
Enzyme 108 Number of Residues 619
Enzyme 108 Molecular Weight 66958.7
Enzyme 108 Theoretical pI 6.83
Enzyme 108 GO Classification Not Available
Enzyme 108 General Function Involved in interspecies interaction between organisms
Enzyme 108 Specific Function Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR)
Enzyme 108 Pathways Not Available
Enzyme 108 Reactions Not Available
Enzyme 108 Pfam Domain Function Not Available
Enzyme 108 Signals
  • None
Enzyme 108 Transmembrane Regions
  • None
Enzyme 108 Essentiality Not Available
Enzyme 108 GenBank ID Protein 110431354 Link Image
Enzyme 108 UniProtKB/Swiss-Prot ID Q6UUV7 Link Image
Enzyme 108 UniProtKB/Swiss-Prot Entry Name CRTC3_HUMAN Link Image
Enzyme 108 PDB ID Not Available
Enzyme 108 Cellular Location Not Available
Enzyme 108 Gene Sequence >1860 bp
ATGGCCGCCTCGCCGGGCTCGGGCAGCGCCAACCCGCGGAAGTTCAGTGAGAAGATCGCG
CTGCACACGCAGAGACAGGCCGAGGAGACGCGGGCCTTCGAGCAGCTCATGACCGACCTC
ACCCTGTCGCGGGTTCAATTTCAGAAGCTTCAGCAACTGCGCCTTACACAGTACCATGGA
GGATCCTTACCAAATGTGAGCCAGCTGCGGAGCAGTGCGTCAGAGTTTCAGCCGTCATTT
CACCAAGCTGATAATGTTCGGGGAACCCGCCATCACGGGCTGGTGGAGAGGCCATCCAGG
AACCGCTTCCACCCCCTCCACCGAAGGTCTGGGGACAAGCCAGGGCGACAATTTGATGGT
AGTGCTTTTGGAGCCAATTATTCCTCACAGCCTCTGGATGAGAGTTGGCCAAGGCAGCAG
CCTCCTTGGAAAGACGAAAAGCATCCTGGGTTCAGGCTGACATCTGCACTTAACAGGACC
AATTCTGATTCTGCTCTTCACACGAGTGCTCTGAGTACCAAGCCCCAGGACCCCTATGGA
GGAGGGGGCCAGTCGGCCTGGCCTGCCCCATACATGGGTTTCTGTGATGGTGAGAATAAT
GGACATGGGGAAGTAGCATCTTTCCCTGGCCCATTGAAAGAAGAGAATCTGTTAAATGTT
CCGAAGCCACTGCCAAAACAACTGTGGGAGACCAAGGAGATTCAGTCCCTGTCAGGACGC
CCTCGATCCTGTGATGTTGGAGGTGGCAATGCTTTTCCACATAATGGTCAAAACCTAGGC
CTCTCACCCTTCTTGGGGACCTTGAACACTGGAGGGTCATTGCCAGATCTAACCAACCTC
CACTACTCGACACCCCTGCCAGCCTCCCTGGACACCACCGACCACCACTTTGGCAGTATG
AGTGTGGGGAATAGTGTGAACAACATCCCAGCTGCTATGACCCACCTGGGTATAAGAAGC
TCCTCTGGTCTCCAGAGTTCTCGGAGTAACCCCTCCATCCAAGCCACGCTCAATAAGACT
GTGCTTTCCTCTTCCTTAAATAACCACCCACAGACATCTGTTCCCAACGCATCTGCTCTT
CACCCTTCGCTCCGTCTGTTTTCCCTTAGCAACCCATCTCTTTCCACCACAAACCTGAGC
GGCCCGTCTCGGCGTCGGCAGCCTCCCGTCAGCCCTCTCACGCTTTCTCCTGGCCCTGAA
GCACATCAAGGTTTCAGCAGACAGCTGTCTTCAACCAGCCCACTGGCCCCATATCCTACC
TCCCAGATGGTGTCCTCAGACCGAAGCCAACTTTCCTTTCTGCCCACAGAAGCTCAAGCC
CAGGTGTCGCCGCCACCCCCTTACCCTGCACCCCAGGAGCTCACCCAGCCCCTCCTGCAG
CAGCCCCGCGCCCCTGAGGCCCCTGCCCAGCAGCCCCAGGCAGCCTCCTCACTGCCACAG
TCAGACTTTCAGCTTCTCCCGGCCCAGGGCTCATCTTTGACCAACTTCTTCCCAGATGTG
GGTTTTGACCAGCAGTCCATGAGGCCAGGCCCTGCCTTTCCTCAACAGGTGCCTCTGGTG
CAACAAGGTTCCCGAGAACTGCAGGACTCTTTTCATTTGAGACCAAGCCCGTATTCCAAC
TGCGGGAGTCTCCCGAACACCATCCTGCCAGAAGACTCCAGCACCAGCCTGTTCAAAGAC
CTCAACAGTGCGCTGGCAGGCCTGCCTGAGGTCAGCCTGAACGTGGACACTCCATTTCCA
CTGGAAGAGGAGCTGCAGATTGAACCCCTGAGCCTGGACGGACTCAACATGTTAAGTGAC
TCCAGCATGGGCCTGCTGGACCCCTCTGTTGAAGAGACGTTTCGAGCTGACAGACTGTGA
Enzyme 108 GenBank Gene ID NM_022769.3 Link Image
Enzyme 108 GeneCard ID CRTC3 Link Image
Enzyme 108 GenAtlas ID CRTC3 Link Image
Enzyme 108 HGNC ID HGNC:26148 Link Image
Enzyme 108 Chromosome Location 1
Enzyme 108 Locus 15q26.1
Enzyme 108 SNPs SNPJam Report Link Image
Enzyme 108 General References
  1. Iourgenko V, Zhang W, Mickanin C, Daly I, Jiang C, Hexham JM, Orth AP, Miraglia L, Meltzer J, Garza D, Chirn GW, McWhinnie E, Cohen D, Skelton J, Terry R, Yu Y, Bodian D, Buxton FP, Zhu J, Song C, Labow MA: Identification of a family of cAMP response element-binding protein coactivators by genome-scale functional analysis in mammalian cells. Proc Natl Acad Sci U S A. 2003 Oct 14;100(21):12147-52. Epub 2003 Sep 23. [PubMed Link Image]
  2. Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Conkright MD, Canettieri G, Screaton R, Guzman E, Miraglia L, Hogenesch JB, Montminy M: TORCs: transducers of regulated CREB activity. Mol Cell. 2003 Aug;12(2):413-23. [PubMed Link Image]
  6. Screaton RA, Conkright MD, Katoh Y, Best JL, Canettieri G, Jeffries S, Guzman E, Niessen S, Yates JR 3rd, Takemori H, Okamoto M, Montminy M: The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector. Cell. 2004 Oct 1;119(1):61-74. [PubMed Link Image]
  7. Koga H, Ohshima T, Shimotohno K: Enhanced activation of tax-dependent transcription of human T-cell leukemia virus type I (HTLV-I) long terminal repeat by TORC3. J Biol Chem. 2004 Dec 17;279(51):52978-83. Epub 2004 Oct 4. [PubMed Link Image]
  8. Bittinger MA, McWhinnie E, Meltzer J, Iourgenko V, Latario B, Liu X, Chen CH, Song C, Garza D, Labow M: Activation of cAMP response element-mediated gene expression by regulated nuclear transport of TORC proteins. Curr Biol. 2004 Dec 14;14(23):2156-61. [PubMed Link Image]
  9. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  10. Katoh Y, Takemori H, Lin XZ, Tamura M, Muraoka M, Satoh T, Tsuchiya Y, Min L, Doi J, Miyauchi A, Witters LA, Nakamura H, Okamoto M: Silencing the constitutive active transcription factor CREB by the LKB1-SIK signaling cascade. FEBS J. 2006 Jun;273(12):2730-48. [PubMed Link Image]
  11. Siu YT, Chin KT, Siu KL, Yee Wai Choy E, Jeang KT, Jin DY: TORC1 and TORC2 coactivators are required for tax activation of the human T-cell leukemia virus type 1 long terminal repeats. J Virol. 2006 Jul;80(14):7052-9. [PubMed Link Image]
  12. Wu Z, Huang X, Feng Y, Handschin C, Feng Y, Gullicksen PS, Bare O, Labow M, Spiegelman B, Stevenson SC: Transducer of regulated CREB-binding proteins (TORCs) induce PGC-1alpha transcription and mitochondrial biogenesis in muscle cells. Proc Natl Acad Sci U S A. 2006 Sep 26;103(39):14379-84. Epub 2006 Sep 15. [PubMed Link Image]
  13. Hishiki T, Ohshima T, Ego T, Shimotohno K: BCL3 acts as a negative regulator of transcription from the human T-cell leukemia virus type 1 long terminal repeat through interactions with TORC3. J Biol Chem. 2007 Sep 28;282(39):28335-43. Epub 2007 Jul 20. [PubMed Link Image]
  14. Takemori H, Kanematsu M, Kajimura J, Hatano O, Katoh Y, Lin XZ, Min L, Yamazaki T, Doi J, Okamoto M: Dephosphorylation of TORC initiates expression of the StAR gene. Mol Cell Endocrinol. 2007 Feb;265-266:196-204. Epub 2007 Jan 8. [PubMed Link Image]
  15. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  16. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  17. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  18. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 108 Metabolite References Not Available
Enzyme 109 [top]
Enzyme 109 ID 13836
Enzyme 109 Name Dematin
Enzyme 109 Synonyms
  1. Erythrocyte membrane protein band 4.9
Enzyme 109 Gene Name EPB49
Enzyme 109 Protein Sequence >Dematin
MERLQKQPLTSPGSVSPSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPD
LMIYEPHFTYSLLEHVELPRSRERSLSPKSTSPPPSPEVWADSRSPGIISQASAPRTTGT
PRTSLPHFHHPETSRPDSNIYKKPPIYKQRESVGGSPQTKHLIEDLIIESSKFPAAQPPD
PNQPAKIETDYWPCPPSLAVVETEWRKRKASRRGAEEEEEEEDDDSGEEMKALRERQREE
LSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHQGTSKSSSLPAYGRTTLSR
LQSTEFSPSGSETGSPGLQNGEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNKGRTKLPP
GVDRMRLERHLSAEDFSRVFAMSPEEFGKLALWKRNELKKKASLF
Enzyme 109 Number of Residues 405
Enzyme 109 Molecular Weight 45513.9
Enzyme 109 Theoretical pI 9.36
Enzyme 109 GO Classification
Function
  • actin binding
  • binding
  • cytoskeletal protein binding
  • protein binding
Process
  • cellular component organization at cellular level
  • cellular process
  • cytoskeleton organization
  • organelle organization
Component
Enzyme 109 General Function Involved in actin binding
Enzyme 109 Specific Function Actin-bundling protein. May function in mitogen- activated protein kinase pathway
Enzyme 109 Pathways Not Available
Enzyme 109 Reactions Not Available
Enzyme 109 Pfam Domain Function
Enzyme 109 Signals
  • None
Enzyme 109 Transmembrane Regions
  • None
Enzyme 109 Essentiality Not Available
Enzyme 109 GenBank ID Protein 166706877 Link Image
Enzyme 109 UniProtKB/Swiss-Prot ID Q08495 Link Image
Enzyme 109 UniProtKB/Swiss-Prot Entry Name DEMA_HUMAN Link Image
Enzyme 109 PDB ID 1QZP Link Image
Enzyme 109 PDB File Show
Enzyme 109 3D Structure
Enzyme 109 Cellular Location Not Available
Enzyme 109 Gene Sequence >1218 bp
ATGGAACGGCTGCAGAAGCAACCACTTACCTCCCCCGGGAGCGTGAGCCCCTCCCGAGAT
TCCAGTGTGCCTGGCTCTCCCTCCAGCATCGTGGCCAAGATGGACAATCAGGTGCTGGGC
TACAAGGACCTGGCTGCCATCCCCAAGGACAAGGCCATCCTGGACATCGAGCGGCCCGAC
CTCATGATCTACGAGCCTCACTTCACTTATTCCCTCCTGGAACACGTGGAGCTGCCTCGC
AGCCGCGAGCGCTCGCTGTCACCCAAATCCACATCCCCCCCACCATCCCCAGAGGTGTGG
GCGGACAGCCGGTCGCCTGGAATCATCTCTCAGGCCTCGGCCCCCAGAACCACTGGAACC
CCCCGGACCAGCCTGCCCCATTTCCACCACCCTGAGACCTCCCGCCCAGATTCCAACATC
TACAAGAAGCCTCCCATCTATAAGCAGAGAGAGTCCGTGGGAGGCAGCCCTCAGACCAAG
CACCTCATCGAGGATCTCATCATCGAGTCATCCAAGTTTCCTGCAGCCCAGCCCCCAGAC
CCCAACCAGCCAGCCAAAATCGAAACCGACTACTGGCCATGCCCCCCGTCTCTGGCTGTT
GTGGAGACAGAATGGAGGAAGCGGAAGGCGTCTCGGAGGGGAGCAGAGGAAGAGGAGGAG
GAGGAAGATGACGACTCTGGAGAGGAGATGAAGGCTCTCAGGGAGCGTCAGAGAGAGGAA
CTCAGTAAGGTTACTTCCAACTTGGGAAAGATGATCTTGAAAGAAGAGATGGAAAAGTCA
TTGCCGATCCGAAGGAAAACCCGCTCTCTGCCTGACCGGACACCCTTCCATACCTCCTTG
CACCAGGGAACGTCTAAATCTTCCTCTCTCCCCGCCTATGGCAGGACCACCCTGAGCCGG
CTACAGTCCACAGAGTTCAGCCCATCAGGGAGTGAGACTGGAAGCCCAGGCCTGCAGAAC
GGAGAGGGCCAGAGGGGGAGGATGGACCGGGGGAACTCCCTGCCCTGTGTGCTGGAGCAG
AAGATCTATCCCTATGAAATGCTAGTGGTGACCAACAAGGGGCGAACCAAGCTGCCACCG
GGGGTGGATCGGATGCGGCTTGAGAGGCATCTGTCTGCCGAGGACTTCTCAAGGGTATTT
GCCATGTCCCCTGAAGAGTTTGGCAAGCTGGCTCTGTGGAAGCGGAATGAGCTCAAGAAG
AAGGCCTCTCTCTTCTGA
Enzyme 109 GenBank Gene ID NM_001114135.2 Link Image
Enzyme 109 GeneCard ID EPB49 Link Image
Enzyme 109 GenAtlas ID EPB49 Link Image
Enzyme 109 HGNC ID HGNC:3382 Link Image
Enzyme 109 Chromosome Location 8
Enzyme 109 Locus 8p21.1
Enzyme 109 SNPs SNPJam Report Link Image
Enzyme 109 General References
  1. Rana AP, Ruff P, Maalouf GJ, Speicher DW, Chishti AH: Cloning of human erythroid dematin reveals another member of the villin family. Proc Natl Acad Sci U S A. 1993 Jul 15;90(14):6651-5. [PubMed Link Image]
  2. Azim AC, Knoll JH, Beggs AH, Chishti AH: Isoform cloning, actin binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily. J Biol Chem. 1995 Jul 21;270(29):17407-13. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Lutchman M, Kim AC, Cheng L, Whitehead IP, Oh SS, Hanspal M, Boukharov AA, Hanada T, Chishti AH: Dematin interacts with the Ras-guanine nucleotide exchange factor Ras-GRF2 and modulates mitogen-activated protein kinase pathways. Eur J Biochem. 2002 Jan;269(2):638-49. [PubMed Link Image]
  6. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  7. Carrascal M, Ovelleiro D, Casas V, Gay M, Abian J: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. J Proteome Res. 2008 Dec;7(12):5167-76. [PubMed Link Image]
  8. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
  9. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 109 Metabolite References Not Available
Enzyme 110 [top]
Enzyme 110 ID 13837
Enzyme 110 Name Erythrocyte membrane protein band 4.2
Enzyme 110 Synonyms
  1. Erythrocyte protein 4.2
  2. P4.2
Enzyme 110 Gene Name EPB42
Enzyme 110 Protein Sequence >Erythrocyte membrane protein band 4.2
MGQALGIKSCDFQAARNNEEHHTKALSSRRLFVRRGQPFTIILYFRAPVRAFLPALKKVA
LTAQTGEQPSKINRTQATFPISSLGDRKWWSAVVEERDAQSWTISVTTPADAVIGHYSLL
LQVSGRKQLLLGQFTLLFNPWNREDAVFLKNEAQRMEYLLNQNGLIYLGTADCIQAESWD
FGQFEGDVIDLSLRLLSKDKQVEKWSQPVHVARVLGALLHFLKEQRVLPTPQTQATQEGA
LLNKRRGSVPILRQWLTGRGRPVYDGQAWVLAAVACTVLRCLGIPARVVTTFASAQGTGG
RLLIDEYYNEEGLQNGEGQRGRIWIFQTSTECWMTRPALPQGYDGWQILHPSAPNGGGVL
GSCDLVPVRAVKEGTLGLTPAVSDLFAAINASCVVWKCCEDGTLELTDSNTKYVGNNIST
KGVGSDRCEDITQNYKYPEGSLQEKEVLERVEKEKMEREKDNGIRPPSLETASPLYLLLK
APSSLPLRGDAQISVTLVNHSEQEKAVQLAIGVQAVHYNGVLAAKLWRKKLHLTLSANLE
KIITIGLFFSNFERNPPENTFLRLTAMATHSESNLSCFAQEDIAICRPHLAIKMPEKAEQ
YQPLTASVSLQNSLDAPMEDCVISILGRGLIHRERSYRFRSVWPENTMCAKFQFTPTHVG
LQRLTVEVDCNMFQNLTNYKSVTVVAPELSA
Enzyme 110 Number of Residues 691
Enzyme 110 Molecular Weight 77008.5
Enzyme 110 Theoretical pI 8.17
Enzyme 110 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
Enzyme 110 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 110 Specific Function Probably plays an important role in the regulation of erythrocyte shape and mechanical properties
Enzyme 110 Pathways Not Available
Enzyme 110 Reactions Not Available
Enzyme 110 Pfam Domain Function
Enzyme 110 Signals
  • None
Enzyme 110 Transmembrane Regions
  • None
Enzyme 110 Essentiality Not Available
Enzyme 110 GenBank ID Protein 166362737 Link Image
Enzyme 110 UniProtKB/Swiss-Prot ID P16452 Link Image
Enzyme 110 UniProtKB/Swiss-Prot Entry Name EPB42_HUMAN Link Image
Enzyme 110 PDB ID Not Available
Enzyme 110 Cellular Location Not Available
Enzyme 110 Gene Sequence >2076 bp
ATGGGACAGGCCCTGGGTATCAAGAGCTGTGACTTTCAGGCAGCAAGAAACAATGAGGAG
CACCACACCAAGGCCCTCAGCTCCCGGCGCCTCTTTGTGAGGAGGGGGCAGCCCTTCACC
ATCATCCTGTACTTCCGCGCTCCAGTCCGTGCATTTCTGCCTGCCCTGAAGAAGGTGGCC
CTCACTGCACAAACTGGAGAGCAGCCTTCCAAGATCAACAGGACCCAAGCCACATTCCCA
ATTTCCAGTCTGGGGGACCGAAAGTGGTGGAGTGCAGTGGTGGAGGAGAGAGATGCCCAG
TCCTGGACCATCTCTGTGACCACACCTGCGGACGCTGTCATTGGCCACTACTCGCTTCTG
CTGCAGGTCTCAGGCAGGAAGCAACTCCTCTTGGGTCAGTTCACACTGCTTTTTAACCCC
TGGAATAGAGAGGATGCTGTGTTCCTGAAGAATGAGGCTCAGCGCATGGAGTACTTGTTG
AACCAGAATGGTCTCATCTACCTGGGTACAGCTGACTGCATCCAGGCAGAGTCCTGGGAC
TTTGGCCAGTTCGAGGGGGATGTCATTGACCTCAGCCTGCGCTTGCTGAGCAAGGACAAG
CAGGTAGAGAAGTGGAGCCAGCCGGTGCACGTGGCCCGTGTGTTGGGTGCCTTGCTGCAT
TTTCTCAAGGAGCAGAGGGTCCTGCCCACCCCGCAGACCCAGGCCACCCAGGAAGGGGCC
TTGCTGAACAAGCGCCGGGGCAGCGTGCCCATCCTGCGGCAGTGGCTCACCGGCCGAGGC
CGACCTGTGTATGATGGCCAGGCCTGGGTGTTGGCTGCTGTTGCTTGCACAGTGCTGCGA
TGCCTGGGAATCCCTGCCCGCGTGGTGACCACGTTTGCCTCAGCACAGGGCACCGGTGGG
CGTCTTCTCATAGATGAATACTATAATGAGGAGGGACTTCAGAACGGAGAAGGCCAGAGA
GGCAGAATCTGGATCTTCCAGACTTCCACAGAGTGCTGGATGACGCGGCCTGCCTTGCCC
CAGGGTTATGATGGATGGCAGATTCTGCACCCAAGTGCTCCTAATGGAGGTGGAGTCCTG
GGGTCCTGTGATCTGGTGCCGGTCAGAGCAGTCAAGGAGGGGACGCTGGGGCTGACCCCA
GCAGTGTCAGACCTTTTTGCTGCCATAAATGCCTCATGTGTGGTCTGGAAGTGCTGTGAG
GATGGGACACTGGAGTTGACTGACTCCAACACAAAGTATGTTGGCAACAACATCAGCACC
AAGGGTGTGGGCAGTGACCGCTGCGAGGACATCACTCAGAACTACAAGTATCCTGAAGGG
TCTCTTCAGGAAAAAGAGGTGCTGGAGAGAGTCGAGAAAGAGAAAATGGAACGTGAGAAA
GACAACGGCATCCGTCCTCCCAGTCTCGAGACTGCCAGTCCTCTGTACCTGCTCTTGAAA
GCACCCAGCTCCCTACCCCTGAGAGGGGATGCCCAGATCTCAGTGACGCTGGTTAATCAC
AGTGAGCAGGAGAAGGCAGTGCAGCTGGCAATTGGGGTCCAGGCTGTACACTACAACGGT
GTCCTTGCTGCCAAGCTCTGGAGGAAGAAGCTGCACCTCACGCTCAGTGCCAACCTGGAA
AAGATAATAACCATCGGCCTGTTCTTCTCCAATTTTGAGCGAAACCCACCCGAGAACACC
TTCCTTAGACTCACCGCCATGGCAACACACTCTGAATCCAACCTTAGCTGCTTTGCTCAG
GAAGACATTGCCATTTGTAGACCACACCTTGCCATCAAGATGCCAGAGAAAGCAGAGCAG
TATCAACCCCTCACAGCCTCAGTCAGCCTCCAGAACTCCCTAGATGCCCCCATGGAGGAC
TGTGTGATCTCCATCCTGGGAAGGGGGCTCATTCACAGAGAGAGGAGCTACAGATTCCGT
TCAGTGTGGCCTGAAAACACCATGTGTGCCAAGTTCCAGTTCACGCCAACACATGTGGGG
CTCCAGAGACTCACTGTGGAAGTGGACTGCAACATGTTCCAGAACCTAACCAACTATAAA
AGCGTCACCGTGGTAGCCCCTGAACTATCAGCTTAA
Enzyme 110 GenBank Gene ID NM_001114134.1 Link Image
Enzyme 110 GeneCard ID EPB42 Link Image
Enzyme 110 GenAtlas ID EPB42 Link Image
Enzyme 110 HGNC ID HGNC:3381 Link Image
Enzyme 110 Chromosome Location 1
Enzyme 110 Locus 15q15-q21
Enzyme 110 SNPs SNPJam Report Link Image
Enzyme 110 General References
  1. Korsgren C, Cohen CM: Organization of the gene for human erythrocyte membrane protein 4.2: structural similarities with the gene for the a subunit of factor XIII. Proc Natl Acad Sci U S A. 1991 Jun 1;88(11):4840-4. [PubMed Link Image]
  2. Korsgren C, Lawler J, Lambert S, Speicher D, Cohen CM: Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2. Proc Natl Acad Sci U S A. 1990 Jan;87(2):613-7. [PubMed Link Image]
  3. Sung LA, Chien S, Chang LS, Lambert K, Bliss SA, Bouhassira EE, Nagel RL, Schwartz RS, Rybicki AC: Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane. Proc Natl Acad Sci U S A. 1990 Feb;87(3):955-9. [PubMed Link Image]
  4. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Risinger MA, Dotimas EM, Cohen CM: Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated. J Biol Chem. 1992 Mar 15;267(8):5680-5. [PubMed Link Image]
  7. Dotimas E, Speicher DW, GuptaRoy B, Cohen CM: Structural domain mapping and phosphorylation of human erythrocyte pallidin (band 4.2). Biochim Biophys Acta. 1993 May 14;1148(1):19-29. [PubMed Link Image]
  8. Bouhassira EE, Schwartz RS, Yawata Y, Ata K, Kanzaki A, Qiu JJ, Nagel RL, Rybicki AC: An alanine-to-threonine substitution in protein 4.2 cDNA is associated with a Japanese form of hereditary hemolytic anemia (protein 4.2NIPPON). Blood. 1992 Apr 1;79(7):1846-54. [PubMed Link Image]
  9. Takaoka Y, Ideguchi H, Matsuda M, Sakamoto N, Takeuchi T, Fukumaki Y: A novel mutation in the erythrocyte protein 4.2 gene of Japanese patients with hereditary spherocytosis (protein 4.2 Fukuoka). Br J Haematol. 1994 Nov;88(3):527-33. [PubMed Link Image]
  10. Hayette S, Morle L, Bozon M, Ghanem A, Risinger M, Korsgren C, Tanner MJ, Fattoum S, Cohen CM, Delaunay J: A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia. Br J Haematol. 1995 Apr;89(4):762-70. [PubMed Link Image]
  11. Kanzaki A, Yasunaga M, Okamoto N, Inoue T, Yawata A, Wada H, Andoh A, Hodohara K, Fujiyama Y, Bamba T, et al.: Band 4.2 Shiga: 317 CGC-->TGC in compound heterozygotes with 142 GCT-->ACT results in band 4.2 deficiency and microspherocytosis. Br J Haematol. 1995 Oct;91(2):333-40. [PubMed Link Image]
  12. Kanzaki A, Yawata Y, Yawata A, Inoue T, Okamoto N, Wada H, Harano T, Harano K, Wilmotte R, Hayette S, et al.: Band 4.2 Komatsu: 523 GAT-->TAT (175 Asp-->Tyr) in exon 4 of the band 4.2 gene associated with total deficiency of band 4.2, hemolytic anemia with ovalostomatocytosis and marked disruption of the cytoskeletal network. Int J Hematol. 1995 Jun;61(4):165-78. [PubMed Link Image]
  13. Perrotta S, Iolascon A, Polito R, d'Urzo G, Conte ML, Miraglia del Giudice E: 4.2 Nippon mutation in a non-Japanese patient with hereditary spherocytosis. Haematologica. 1999 Jul;84(7):660-2. [PubMed Link Image]
Enzyme 110 Metabolite References Not Available
Enzyme 111 [top]
Enzyme 111 ID 13838
Enzyme 111 Name FERM, RhoGEF and pleckstrin domain-containing protein 1
Enzyme 111 Synonyms
  1. Chondrocyte-derived ezrin-like protein
  2. Pleckstrin homology domain-containing family C member 2
  3. PH domain-containing family C member 2
Enzyme 111 Gene Name FARP1
Enzyme 111 Protein Sequence >FERM, RhoGEF and pleckstrin domain-containing protein 1
MGEIEQRPTPGSRLGAPENSGISTLERGQKPPPTPSGKLVSIKIQMLDDTQEAFEVPQRA
PGKVLLDAVCNHLNLVEGDYFGLEFPDHKKITVWLDLLKPIVKQIRRPKHVVVKFVVKFF
PPDHTQLQEELTRYLFALQVKQDLAQGRLTCNDTSAALLISHIVQSEIGDFDEALDREHL
AKNKYIPQQDALEDKIVEFHHNHIGQTPAESDFQLLEIARRLEMYGIRLHPAKDREGTKI
NLAVANTGILVFQGFTKINAFNWAKVRKLSFKRKRFLIKLRPDANSAYQDTLEFLMASRD
FCKSFWKICVEHHAFFRLFEEPKPKPKPVLFSRGSSFRFSGRTQKQVLDYVKEGGHKKVQ
FERKHSKIHSIRSLASQPTELNSEVLEQSQQSTSLTFGEGAESPGGQSCRRGKEPKVSAG
EPGSHPSPAPRRSPAGNKQADGAASAPTEEEEEVVKDRTQQSKPQPPQPSTGSLTGSPHL
SELSVNSQGGVAPANVTLSPNLSPDTKQASPLISPLLNDQACPRTDDEDEGRRKRFPTDK
AYFIAKEVSTTERTYLKDLEVITSWFQSTVSKEDAMPEALKSLIFPNFEPLHKFHTNFLK
EIEQRLALWEGRSNAQIRDYQRIGDVMLKNIQGMKHLAAHLWKHSEALEALENGIKSSRR
LENFCRDFELQKVCYLPLNTFLLRPLHRLMHYKQVLERLCKHHPPSHADFRDCRAALAEI
TEMVAQLHGTMIKMENFQKLHELKKDLIGIDNLVVPGREFIRLGSLSKLSGKGLQQRMFF
LFNDVLLYTSRGLTASNQFKVHGQLPLYGMTIEESEDEWGVPHCLTLRGQRQSIIVAASS
RSEMEKWVEDIQMAIDLAEKSSSPAPEFLASSPPDNKSPDEATAADQESEDDLSASRTSL
ERQAPHRGNTMVHVCWHRNTSVSMVDFSIAVENQLSGNLLRKFKNSNGWQKLWVVFTNFC
LFFYKSHQDNHPLASLPLLGYSLTIPSESENIQKDYVFKLHFKSHVYYFRAESEYTFERW
MEVIRSATSSASRPHVLSHKESLVY
Enzyme 111 Number of Residues 1045
Enzyme 111 Molecular Weight 118631.9
Enzyme 111 Theoretical pI 8.27
Enzyme 111 GO Classification
Function
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • binding
  • cytoskeletal protein binding
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • protein binding
  • small GTPase regulator activity
Process
  • biological regulation
  • regulation of Ras protein signal transduction
  • regulation of Rho protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
Component
  • cell part
  • cytoplasm
  • cytoskeleton
  • extrinsic to membrane
  • intracellular
  • intracellular non-membrane-bounded organelle
  • intracellular part
  • membrane part
  • non-membrane-bounded organelle
  • organelle
Enzyme 111 General Function Involved in Rho guanyl-nucleotide exchange factor activity
Enzyme 111 Specific Function May function as Rho-guanine nucleotide exchange factor
Enzyme 111 Pathways Not Available
Enzyme 111 Reactions Not Available
Enzyme 111 Pfam Domain Function
Enzyme 111 Signals
  • None
Enzyme 111 Transmembrane Regions
  • None
Enzyme 111 Essentiality Not Available
Enzyme 111 GenBank ID Protein 2766165 Link Image
Enzyme 111 UniProtKB/Swiss-Prot ID Q9Y4F1 Link Image
Enzyme 111 UniProtKB/Swiss-Prot Entry Name FARP1_HUMAN Link Image
Enzyme 111 PDB ID Not Available
Enzyme 111 Cellular Location Not Available
Enzyme 111 Gene Sequence >3138 bp
ATGGGAGAAATAGAGCAGAGGCCGACCCCAGGATCACGACTGGGGGCCCCGGAAAATTCG
GGGATCAGTACCTTGGAACGTGGACAGAAGCCGCCCCCAACACCTTCAGGAAAACTCGTG
TCCATCAAAATCCAGATGCTGGATGACACCCAGGAGGCATTTGAAGTTCCACAAAGAGCT
CCTGGGAAGGTGCTGCTGGATGCAGTTTGCAACCACCTCAACCTCGTGGAAGGTGACTAT
TTTGGCCTCGAGTTTCCTGATCACAAAAAGATCACGGTGTGGCTGGATCTCCTAAAACCC
ATTGTGAAACAGATTAGAAGGCCAAAGCACGTTGTTGTTAAGTTTGTGGTGAAATTCTTT
CCGCCTGACCACACACAACTCCAAGAAGAACTCACAAGGTACCTGTTCGCGCTGCAGGTG
AAGCAGGACTTGGCTCAAGGCAGGTTGACGTGTAATGACACCAGCGCAGCTCTCTTGATT
TCACACATTGTGCAATCTGAGATTGGGGATTTTGATGAAGCCTTGGACAGAGAGCACTTA
GCAAAAAATAAATACATACCTCAGCAAGACGCACTAGAGGACAAAATCGTGGAATTTCAC
CATAACCACATTGGACAAACACCAGCAGAATCAGATTTCCAGCTCCTAGAGATTGCCCGT
CGGCTAGAGATGTATGGAATCCGGTTGCACCCGGCCAAGGACAGGGAAGGCACGAAGATC
AATCTGGCCGTTGCCAACACGGGAATTCTAGTGTTTCAGGGTTTCACTAAGATCAATGCC
TTCAACTGGGCCAAGGTGCGGAAGCTGAGCTTCAAGAGGAAGCGCTTTCTCATCAAGCTC
CGGCCAGATGCCAATAGTGCGTACCAGGATACCTTGGAATTCCTGATGGCCAGTCGGGAT
TTCTGCAAGTCCTTCTGGAAAATCTGTGTTGAACATCATGCCTTCTTTAGACTTTTTGAA
GAGCCCAAACCAAAGCCCAAGCCCGTCCTCTTTAGCCGGGGGTCATCATTTCGGTTCAGT
GGTCGGACTCAGAAGCAGGTTCTCGACTATGTTAAAGAAGGAGGACATAAGAAGGTGCAG
TTTGAAAGGAAGCACAGCAAGATTCATTCTATCCGGAGCCTTGCTTCACAGCCTACAGAA
CTGAATTCGGAAGTGCTGGAGCAGTCTCAGCAGAGCACCAGCCTTACATTTGGAGAAGGT
GCCGAATCTCCAGGGGGCCAGAGCTGCCGGCGAGGAAAGGAACCGAAGGTTTCCGCCGGG
GAGCCGGGGTCGCACCCGAGCCCTGCGCCGAGGAGAAGCCCCGCGGGTAACAAGCAGGCG
GACGGAGCCGCCTCGGCGCCCACGGAGGAAGAGGAGGAGGTCGTTAAGGATAGGACCCAG
CAGAGTAAACCTCAGCCCCCGCAGCCAAGCACAGGCTCCCTGACTGGCAGTCCTCACCTT
TCCGAGCTGTCTGTGAACTCGCAGGGGGGAGTGGCCCCTGCCAACGTGACCTTGTCTCCC
AACCTGAGCCCCGACACCAAGCAGGCCTCTCCCTTGATCAGCCCGCTGCTGAATGACCAG
GCCTGCCCCCGGACGGACGATGAGGATGAGGGCCGGAGGAAGAGATTCCCAACTGATAAA
GCGTACTTCATAGCTAAGGAAGTGTCTACCACCGAGCGAACATATCTGAAGGATCTCGAA
GTTATCACTTCGTGGTTTCAGAGCACAGTGAGCAAAGAGGACGCCATGCCGGAAGCACTG
AAAAGTCTCATATTCCCGAATTTTGAACCTTTGCACAAATTTCATACTAATTTTCTCAAG
GAAATTGAGCAACGACTTGCCCTGTGGGAAGGCCGCTCAAATGCCCAAATCAGAGATTAC
CAAAGAATCGGCGATGTCATGCTGAAGAACATTCAGGGCATGAAGCACCTGGCGGCTCAC
CTGTGGAAGCACAGCGAGGCCTTGGAGGCCCTGGAGAATGGAATCAAGAGCTCCCGGCGG
CTGGAGAACTTCTGCAGAGACTTTGAGCTGCAGAAGGTGTGTTACCTACCGCTCAACACC
TTCCTCCTGCGGCCACTGCACCGGCTCATGCACTACAAGCAGGTCCTGGAGCGGCTGTGC
AAACACCACCCGCCGAGCCACGCCGACTTCAGGGACTGCCGAGCCGCTTTGGCAGAGATC
ACGGAGATGGTGGCACAGCTCCACGGTACGATGATCAAGATGGAGAATTTCCAGAAGCTG
CACGAACTCAAGAAAGATTTGATTGGCATTGACAATCTTGTGGTTCCGGGAAGGGAGTTC
ATCCGTCTGGGCAGCCTCAGCAAGCTCTCGGGGAAGGGGCTCCAGCAGCGCATGTTCTTC
CTGTTCAACGACGTCCTGCTATACACGAGCCGGGGGCTGACGGCCTCCAATCAGTTTAAA
GTCCACGGGCAGCTCCCGCTCTATGGCATGACGATTGAGGAGAGCGAAGACGAGTGGGGG
GTGCCCCACTGCCTGACCCTCCGGGGCCAGCGGCAGTCCATCATCGTGGCCGCCAGTTCT
CGGTCCGAGATGGAGAAGTGGGTTGAGGACATCCAGATGGCCATTGACCTGGCGGAGAAG
AGCAGCAGCCCCGCCCCTGAGTTCCTGGCCAGCAGCCCCCCTGACAACAAGTCCCCTGAT
GAAGCCACCGCGGCTGACCAGGAGTCAGAGGATGACCTGAGCGCCTCGCGCACATCGCTG
GAGCGCCAGGCCCCGCACCGCGGCAACACAATGGTGCACGTGTGCTGGCACCGCAACACC
AGCGTCTCCATGGTGGACTTCAGCATCGCAGTGGAGAATCAGTTGTCTGGAAACCTGCTG
AGGAAATTCAAAAACAGCAACGGGTGGCAGAAGCTGTGGGTGGTGTTCACAAACTTCTGC
CTGTTCTTCTACAAATCACACCAGGACAATCATCCCCTTGCCAGCCTGCCTCTGCTCGGC
TACTCGCTCACCATCCCCTCTGAGTCCGAGAACATCCAGAAAGACTACGTGTTCAAGCTG
CACTTCAAGTCCCACGTCTACTACTTCAGGGCGGAAAGCGAGTACACGTTCGAAAGGTGG
ATGGAAGTGATCCGCAGTGCCACCAGCTCTGCCTCGCGACCCCACGTGTTGAGCCACAAA
GAGTCTCTTGTGTATTGA
Enzyme 111 GenBank Gene ID AB008430 Link Image
Enzyme 111 GeneCard ID FARP1 Link Image
Enzyme 111 GenAtlas ID FARP1 Link Image
Enzyme 111 HGNC ID HGNC:3591 Link Image
Enzyme 111 Chromosome Location 1
Enzyme 111 Locus 13q32.2
Enzyme 111 SNPs SNPJam Report Link Image
Enzyme 111 General References
  1. Koyano Y, Kawamoto T, Shen M, Yan W, Noshiro M, Fujii K, Kato Y: Molecular cloning and characterization of CDEP, a novel human protein containing the ezrin-like domain of the band 4.1 superfamily and the Dbl homology domain of Rho guanine nucleotide exchange factors. Biochem Biophys Res Commun. 1997 Dec 18;241(2):369-75. [PubMed Link Image]
  2. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  5. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  6. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  10. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 111 Metabolite References Not Available
Enzyme 112 [top]
Enzyme 112 ID 13839
Enzyme 112 Name G-protein coupled bile acid receptor 1
Enzyme 112 Synonyms
  1. G-protein coupled receptor GPCR19
  2. hGPCR19
  3. Membrane-type receptor for bile acids
  4. M-BAR
  5. hBG37
  6. BG37
Enzyme 112 Gene Name GPBAR1
Enzyme 112 Protein Sequence >G-protein coupled bile acid receptor 1
MTPNSTGEVPSPIPKGALGLSLALASLIITANLLLALGIAWDRRLRSPPAGCFFLSLLLA
GLLTGLALPTLPGLWNQSRRGYWSCLLVYLAPNFSFLSLLANLLLVHGERYMAVLRPLQP
PGSIRLALLLTWAGPLLFASLPALGWNHWTPGANCSSQAIFPAPYLYLEVYGLLLPAVGA
AAFLSVRVLATAHRQLQDICRLERAVCRDEPSALARALTWRQARAQAGAMLLFGLCWGPY
VATLLLSVLAYEQRPPLGPGTLLSLLSLGSASAAAVPVAMGLGDQRYTAPWRAAAQRCLQ
GLWGRASRDSPGPSIAYHPSSQSSVDLDLN
Enzyme 112 Number of Residues 330
Enzyme 112 Molecular Weight 35247.8
Enzyme 112 Theoretical pI 9.62
Enzyme 112 GO Classification
Function
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 112 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 112 Specific Function Receptor for bile acid. Bile acid-binding induces its internalization, activation of extracellular signal-regulated kinase and intracellular cAMP production. May be involved in the suppression of macrophage functions by bile acids
Enzyme 112 Pathways Not Available
Enzyme 112 Reactions Not Available
Enzyme 112 Pfam Domain Function
Enzyme 112 Signals
  • None
Enzyme 112 Transmembrane Regions
  • 20-40 51-71 86-106 126-146 166-186 229-249 262-282
Enzyme 112 Essentiality Not Available
Enzyme 112 GenBank ID Protein 20152266 Link Image
Enzyme 112 UniProtKB/Swiss-Prot ID Q8TDU6 Link Image
Enzyme 112 UniProtKB/Swiss-Prot Entry Name GPBAR_HUMAN Link Image
Enzyme 112 PDB ID Not Available
Enzyme 112 Cellular Location Not Available
Enzyme 112 Gene Sequence >993 bp
ATGACGCCCAACAGCACTGGCGAGGTGCCCAGCCCCATTCCCAAGGGGGCTTTGGGGCTC
TCCCTGGCCCTGGCAAGCCTCATCATCACCGCGAACCTGCTCCTAGCCCTGGGCATCGCC
TGGGACCGCCGCCTGCGCAGCCCACCTGCTGGCTGCTTCTTCCTGAGCCTACTGCTGGCT
GGGCTGCTCACGGGTCTGGCATTGCCCACATTGCCAGGGCTGTGGAACCAGAGTCGCCGG
GGTTACTGGTCCTGCCTCCTCGTCTACTTGGCTCCCAACTTCTCCTTCCTCTCCCTGCTT
GCCAACCTCTTGCTGGTGCACGGGGAGCGCTACATGGCAGTCCTGAGGCCACTCCAGCCC
CCTGGGAGCATTCGGCTGGCCCTGCTCCTCACCTGGGCTGGTCCCCTGCTCTTTGCCAGT
CTGCCCGCTCTGGGGTGGAACCACTGGACCCCTGGTGCCAACTGCAGCTCCCAGGCTATC
TTCCCAGCCCCCTACCTGTACCTCGAAGTCTATGGGCTCCTGCTGCCCGCCGTGGGTGCT
GCTGCCTTCCTCTCTGTCCGCGTGCTGGCCACTGCCCACCGCCAGCTGCAGGACATCTGC
CGGCTGGAGCGGGCAGTGTGCCGCGATGAGCCCTCCGCCCTGGCCCGGGCCCTTACCTGG
AGGCAGGCAAGGGCACAGGCTGGAGCCATGCTGCTCTTCGGGCTGTGCTGGGGGCCCTAC
GTGGCCACACTGCTCCTCTCAGTCCTGGCCTATGAGCAGCGCCCGCCACTGGGGCCTGGG
ACACTGTTGTCCCTCCTCTCCCTAGGAAGTGCCAGTGCAGCGGCAGTGCCCGTAGCCATG
GGGCTGGGCGATCAGCGCTACACAGCCCCCTGGAGGGCAGCCGCCCAAAGGTGCCTGCAG
GGGCTGTGGGGAAGAGCCTCCCGGGACAGTCCCGGCCCCAGCATTGCCTACCACCCAAGC
AGCCAAAGCAGTGTCGACCTGGACTTGAACTAA
Enzyme 112 GenBank Gene ID AB083601 Link Image
Enzyme 112 GeneCard ID GPBAR1 Link Image
Enzyme 112 GenAtlas ID GPBAR1 Link Image
Enzyme 112 HGNC ID HGNC:19680 Link Image
Enzyme 112 Chromosome Location 2
Enzyme 112 Locus 2q35
Enzyme 112 SNPs SNPJam Report Link Image
Enzyme 112 General References
  1. Maruyama T, Miyamoto Y, Nakamura T, Tamai Y, Okada H, Sugiyama E, Nakamura T, Itadani H, Tanaka K: Identification of membrane-type receptor for bile acids (M-BAR). Biochem Biophys Res Commun. 2002 Nov 15;298(5):714-9. [PubMed Link Image]
  2. Kawamata Y, Fujii R, Hosoya M, Harada M, Yoshida H, Miwa M, Fukusumi S, Habata Y, Itoh T, Shintani Y, Hinuma S, Fujisawa Y, Fujino M: A G protein-coupled receptor responsive to bile acids. J Biol Chem. 2003 Mar 14;278(11):9435-40. Epub 2003 Jan 10. [PubMed Link Image]
  3. Takeda S, Kadowaki S, Haga T, Takaesu H, Mitaku S: Identification of G protein-coupled receptor genes from the human genome sequence. FEBS Lett. 2002 Jun 5;520(1-3):97-101. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 112 Metabolite References Not Available
Enzyme 113 [top]
Enzyme 113 ID 13840
Enzyme 113 Name Glycoprotein hormone alpha-2
Enzyme 113 Synonyms
  1. Putative secreted protein Zsig51
  2. Thyrostimulin subunit alpha
Enzyme 113 Gene Name GPHA2
Enzyme 113 Protein Sequence >Glycoprotein hormone alpha-2
MPMASPQTLVLYLLVLAVTEAWGQEAVIPGCHLHPFNVTVRSDRQGTCQGSHVAQACVGH
CESSAFPSRYSVLVASGYRHNITSVSQCCTISGLKKVKVQLQCVGSRREELEIFTARACQ
CDMCRLSRY
Enzyme 113 Number of Residues 129
Enzyme 113 Molecular Weight 14163.3
Enzyme 113 Theoretical pI 8.27
Enzyme 113 GO Classification
Function
  • binding
  • hormone activity
  • protein binding
  • receptor binding
Process
Component
  • extracellular region
Enzyme 113 General Function Involved in hormone activity
Enzyme 113 Specific Function Stimulates the thyroid. Binds and activates THSR, leads to increased cAMP production
Enzyme 113 Pathways Not Available
Enzyme 113 Reactions Not Available
Enzyme 113 Pfam Domain Function Not Available
Enzyme 113 Signals
  • 1-23
Enzyme 113 Transmembrane Regions
  • None
Enzyme 113 Essentiality Not Available
Enzyme 113 GenBank ID Protein 14009506 Link Image
Enzyme 113 UniProtKB/Swiss-Prot ID Q96T91 Link Image
Enzyme 113 UniProtKB/Swiss-Prot Entry Name GPHA2_HUMAN Link Image
Enzyme 113 PDB ID Not Available
Enzyme 113 Cellular Location Not Available
Enzyme 113 Gene Sequence >390 bp
ATGCCTATGGCGTCCCCTCAAACCCTGGTCCTCTATCTGCTGGTCCTGGCAGTCACTGAA
GCCTGGGGCCAGGAGGCAGTCATCCCAGGCTGCCACTTGCACCCCTTCAATGTGACAGTG
CGAAGTGACCGCCAAGGCACCTGCCAGGGCTCCCACGTGGCACAGGCCTGTGTGGGCCAC
TGTGAGTCCAGCGCCTTCCCTTCTCGGTACTCTGTGCTGGTGGCCAGTGGTTACCGACAC
AACATCACCTCCGTCTCTCAGTGCTGCACCATCAGTGGCCTGAAGAAGGTCAAAGTACAG
CTGCAGTGTGTGGGGAGCCGGAGGGAGGAGCTCGAGATCTTCACGGCCAGGGCCTGCCAG
TGTGACATGTGTCGCCTCTCTCGCTACTAG
Enzyme 113 GenBank Gene ID AF260739 Link Image
Enzyme 113 GeneCard ID GPHA2 Link Image
Enzyme 113 GenAtlas ID GPHA2 Link Image
Enzyme 113 HGNC ID HGNC:18054 Link Image
Enzyme 113 Chromosome Location 1
Enzyme 113 Locus 11q13.1
Enzyme 113 SNPs SNPJam Report Link Image
Enzyme 113 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Nakabayashi K, Matsumi H, Bhalla A, Bae J, Mosselman S, Hsu SY, Hsueh AJ: Thyrostimulin, a heterodimer of two new human glycoprotein hormone subunits, activates the thyroid-stimulating hormone receptor. J Clin Invest. 2002 Jun;109(11):1445-52. [PubMed Link Image]
  3. Hsu SY, Nakabayashi K, Bhalla A: Evolution of glycoprotein hormone subunit genes in bilateral metazoa: identification of two novel human glycoprotein hormone subunit family genes, GPA2 and GPB5. Mol Endocrinol. 2002 Jul;16(7):1538-51. [PubMed Link Image]
Enzyme 113 Metabolite References Not Available
Enzyme 114 [top]
Enzyme 114 ID 13841
Enzyme 114 Name Glycoprotein hormone beta-5
Enzyme 114 Synonyms
  1. Thyrostimulin subunit beta
Enzyme 114 Gene Name GPHB5
Enzyme 114 Protein Sequence >Glycoprotein hormone beta-5
MKLAFLFLGPMALLLLAGYGCVLGASSGNLRTFVGCAVREFTFLAKKPGCRGLRITTDAC
WGRCETWEKPILEPPYIEAHHRVCTYNETKQVTVKLPNCAPGVDPFYTYPVAIRCDCGAC
STATTECETI
Enzyme 114 Number of Residues 130
Enzyme 114 Molecular Weight 14231.5
Enzyme 114 Theoretical pI 7.82
Enzyme 114 GO Classification
Function
  • binding
  • hormone activity
  • protein binding
  • receptor binding
Process
Component
  • extracellular region
Enzyme 114 General Function Involved in hormone activity
Enzyme 114 Specific Function Stimulates the thyroid. Binds and activates THSR, leading to increased cAMP production
Enzyme 114 Pathways Not Available
Enzyme 114 Reactions Not Available
Enzyme 114 Pfam Domain Function
Enzyme 114 Signals
  • 1-24
Enzyme 114 Transmembrane Regions
  • None
Enzyme 114 Essentiality Not Available
Enzyme 114 GenBank ID Protein 21427594 Link Image
Enzyme 114 UniProtKB/Swiss-Prot ID Q86YW7 Link Image
Enzyme 114 UniProtKB/Swiss-Prot Entry Name GPHB5_HUMAN Link Image
Enzyme 114 PDB ID Not Available
Enzyme 114 Cellular Location Not Available
Enzyme 114 Gene Sequence >393 bp
ATGAAGCTGGCATTCCTCTTCCTTGGCCCCATGGCCCTCCTCCTTCTGGCTGGCTATGGC
TGTGTCCTCGGTGCCTCCAGTGGGAACCTGCGCACCTTTGTGGGCTGTGCCGTGAGGGAG
TTTACTTTCCTGGCCAAGAAGCCAGGCTGCAGGGGCCTTCGGATCACCACGGATGCCTGC
TGGGGTCGCTGTGAGACCTGGCAGAAACCCATTCTGGAACCCCCCTATATTGAAGCCCAT
CATCGAGTCTGTACCTACAACGAGACCAAACAGGTGACTGTCAAGCTGCCCAACTGTGCC
CCGGGAGTCGACCCCTTCTACACCTATCCCGTGCCATCCGCTGTGACTGCGGAGCCTGCT
CCACTGGCCACCACGGAGTGTGAGACCATCTGA
Enzyme 114 GenBank Gene ID AF403430 Link Image
Enzyme 114 GeneCard ID GPHB5 Link Image
Enzyme 114 GenAtlas ID GPHB5 Link Image
Enzyme 114 HGNC ID HGNC:18055 Link Image
Enzyme 114 Chromosome Location 1
Enzyme 114 Locus 14q23.2
Enzyme 114 SNPs SNPJam Report Link Image
Enzyme 114 General References
  1. Nakabayashi K, Matsumi H, Bhalla A, Bae J, Mosselman S, Hsu SY, Hsueh AJ: Thyrostimulin, a heterodimer of two new human glycoprotein hormone subunits, activates the thyroid-stimulating hormone receptor. J Clin Invest. 2002 Jun;109(11):1445-52. [PubMed Link Image]
  2. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Hsu SY, Nakabayashi K, Bhalla A: Evolution of glycoprotein hormone subunit genes in bilateral metazoa: identification of two novel human glycoprotein hormone subunit family genes, GPA2 and GPB5. Mol Endocrinol. 2002 Jul;16(7):1538-51. [PubMed Link Image]
  5. Okada SL, Ellsworth JL, Durnam DM, Haugen HS, Holloway JL, Kelley ML, Lewis KE, Ren H, Sheppard PO, Storey HM, Waggie KS, Wolf AC, Yao LY, Webster PJ: A glycoprotein hormone expressed in corticotrophs exhibits unique binding properties on thyroid-stimulating hormone receptor. Mol Endocrinol. 2006 Feb;20(2):414-25. Epub 2005 Oct 6. [PubMed Link Image]
Enzyme 114 Metabolite References Not Available
Enzyme 115 [top]
Enzyme 115 ID 13842
Enzyme 115 Name Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
Enzyme 115 Synonyms Not Available
Enzyme 115 Gene Name HCN4
Enzyme 115 Protein Sequence >Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
MDKLPPSMRKRLYSLPQQVGAKAWIMDEEEDAEEEGAGGRQDPSRRSIRLRPLPSPSPSA
AAGGTESRSSALGAADSEGPARGAGKSSTNGDCRRFRGSLASLGSRGGGSGGTGSGSSHG
HLHDSAEERRLIAEGDASPGEDRTPPGLAAEPERPGASAQPAASPPPPQQPPQPASASCE
QPSVDTAIKVEGGAAAGDQILPEAEVRLGQAGFMQRQFGAMLQPGVNKFSLRMFGSQKAV
EREQERVKSAGFWIIHPYSDFRFYWDLTMLLLMVGNLIIIPVGITFFKDENTTPWIVFNV
VSDTFFLIDLVLNFRTGIVVEDNTEIILDPQRIKMKYLKSWFMVDFISSIPVDYIFLIVE
TRIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIVN
LIGMMLLLCHWDGCLQFLVPMLQDFPDDCWVSINNMVNNSWGKQYSYALFKAMSHMLCIG
YGRQAPVGMSDVWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSF
HKLPPDTRQRIHDYYEHRYQGKMFDEESILGELSEPLREEIINFNCRKLVASMPLFANAD
PNFVTSMLTKLRFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKETKLADGSYFGE
ICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVALDRLDRIGKKNSI
LLHKVQHDLNSGVFNYQENEIIQQIVQHDREMAHCAHRVQAAASATPTPTPVIWTPLIQA
PLQAAAATTSVAIALTHHPRLPAAIFRPPPGSGLGNLGAGQTPRHLKRLQSLIPSALGSA
SPASSPSQVDTPSSSSFHIQQLAGFSAPAGLSPLLPSSSSSPPPGACGSPSAPTPSAGVA
ATTIAGFGHFHKALGGSLSSSDSPLLTPLQPGARSPQAAQPSPAPPGARGGLGLPEHFLP
PPPSSRSPSSSPGQLGQPPGELSLGLATGPLSTPETPPRQPEPPSLVAGASGGASPVGFT
PRGGLSPPGHSPGPPRTFPSAPPRASGSHGSLLLPPASSPPPPQVPQRRGTPPLTPGRLT
QDLKLISASQPALPQDGAQTLRRASPHSSGESMAAFPLFPRAGGGSGGSGSSGGLGPPGR
PYGAIPGQHVTLPRKTSSGSLPPPLSLFGARATSSGGPPLTAGPQREPGARPEPVRSKLP
SNL
Enzyme 115 Number of Residues 1203
Enzyme 115 Molecular Weight 129040.7
Enzyme 115 Theoretical pI 9.15
Enzyme 115 GO Classification
Function
  • cation channel activity
  • ion channel activity
  • ion transmembrane transporter activity
  • potassium channel activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
  • voltage-gated potassium channel activity
Process
  • cation transport
  • establishment of localization
  • ion transport
  • monovalent inorganic cation transport
  • potassium ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 115 General Function Involved in ion channel activity
Enzyme 115 Specific Function Hyperpolarization-activated ion channel with very slow activation and inactivation exhibiting weak selectivity for potassium over sodium ions. May contribute to the native pacemaker currents in heart (If) and in neurons (Ih). Activated by cAMP. May mediate responses to sour stimuli
Enzyme 115 Pathways Not Available
Enzyme 115 Reactions Not Available
Enzyme 115 Pfam Domain Function
Enzyme 115 Signals
  • None
Enzyme 115 Transmembrane Regions
  • 267-287 294-314 341-361 369-389 421-441 497-517
Enzyme 115 Essentiality Not Available
Enzyme 115 GenBank ID Protein 4775353 Link Image
Enzyme 115 UniProtKB/Swiss-Prot ID Q9Y3Q4 Link Image
Enzyme 115 UniProtKB/Swiss-Prot Entry Name HCN4_HUMAN Link Image
Enzyme 115 PDB ID 1Q3E Link Image
Enzyme 115 PDB File Show
Enzyme 115 3D Structure
Enzyme 115 Cellular Location Not Available
Enzyme 115 Gene Sequence >3612 bp
ATGGACAAGCTGCCGCCGTCCATGCGCAAGCGGCTCTACAGCCTCCCGCAGCAGGTGGGG
GCCAAGGCGTGGATCATGGACGAGGAAGAGGACGCCGAGGAGGAGGGGGCCGGGGGCCGC
CAAGACCCCAGCCGCAGGAGCATCCGGCTGCGGCCACTGCCCTCGCCCTCCCCCTCGGCG
GCCGCGGGTGGCACGGAGTCCCGGAGCTCGGCCCTCGGGGCAGCGGACAGCGAAGGGCCG
GCCCGCGGCGCGGGCAAGTCCAGCACGAACGGCGACTGCAGGCGCTTCCGCGGGAGCCTG
GCCTCGCTGGGCAGCCGGGGCGGCGGCAGCGGCGGCACGGGGAGCGGCAGCAGTCACGGA
CACCTGCATGACTCCGCGGAGGAGCGGCGGCTCATCGCCGAGGGCGACGCGTCCCCCGGC
GAGGACAGGACGCCCCCAGGCCTGGCGGCCGAGCCCGAGCGCCCCGGCGCCTCGGCGCAG
CCCGCAGCCTCGCCGCCGCCGCCCCAGCAGCCACCGCAGCCGGCCTCCGCCTCCTGCGAG
CAGCCCTCGGTGGACACCGCTATCAAAGTGGAGGGAGGCGCGGCTGCCGGCGACCAGATC
CTCCCGGAGGCCGAGGTGCGCCTGGGCCAGGCCGGCTTCATGCAGCGCCAGTTCGGGGCC
ATGCTCCAACCCGGGGTCAACAAATTCTCCCTAAGGATGTTCGGCAGCCAGAAAGCCGTG
GAGCGCGAACAGGAGAGGGTCAAGTCGGCCGGATTTTGGATTATCCACCCCTACAGTGAC
TTCAGATTTTACTGGGACCTGACCATGCTGCTGCTGATGGTGGGAAACCTGATTATCATT
CCTGTGGGCATCACCTTCTTCAAGGATGAGAACACCACACCCTGGATTGTCTTCAATGTG
GTGTCAGACACATTCTTCCTCATCGACTTGGTCCTCAACTTCCGCACAGGGATCGTGGTG
GAGGACAACACAGAGATCATCCTGGACCCGCAGCGGATTAAAATGAAGTACCTGAAAAGC
TGGTTCATGGTAGATTTCATTTCCTCCATCCCCGTGGACTACATCTTCCTCATTGTGGAG
ACACGCATCGACTCGGAGGTCTACAAGACTGCCCGGGCCCTGCGCATTGTCCGCTTCACG
AAGATCCTCAGCCTCTTACGCCTGTTACGCCTCTCCCGCCTCATTCGATATATTCACCAG
TGGGAAGAGATCTTCCACATGACCTACGACCTGGCCAGCGCCGTGGTGCGCATCGTGAAC
CTCATCGGCATGATGCTCCTGCTCTGCCACTGGGACGGCTGCCTGCAGTTCCTGGTACCC
ATGCTACAGGACTTCCCTGACGACTGCTGGGTGTCCATCAACAACATGGTGAACAACTCC
TGGGGGAAGCAGTACTCCTACGCGCTCTTCAAGGCCATGAGCCACATGCTGTGCATCGGC
TACGGGCGGCAGGCGCCCGTGGGCATGTCCGACGTCTGGCTCACCATGCTCAGCATGATC
GTGGGTGCCACCTGCTACGCCATGTTCATTGGCCACGCCACTGCCCTCATCCAGTCCCTG
GACTCCTCCCGGCGCCAGTACCAGGAAAAGTACAAGCAGGTGGAGCAGTACATGTCCTTT
CACAAGCTCCCGCCCGACACCCGGCAGCGCATCCACGACTACTACGAGCACCGCTACCAG
GGCAAGATGTTCGACGAGGAGAGCATCCTGGGCGAGCTAAGCGAGCCCCTGCGGGAGGAG
ATCATCAACTTTAACTGTCGGAAGCTGGTGGCCTCCATGCCACTGTTTGCCAATGCGGAC
CCCAACTTCGTGACGTCCATGCTGACCAAGCTGCGTTTCGAGGTCTTCCAGCCTGGGGAC
TACATCATCCGGGAAGGCACCATTGGCAAGAAGATGTACTTCATCCAGCATGGCGTGGTC
AGCGTGCTCACCAAGGGCAACAAGGAGACCAAGCTGGCCGACGGCTCCTACTTTGGAGAG
ATCTGCCTGCTGACCCGGGGCCGGCGCACAGCCAGCGTGAGGGCCGACACCTACTGCCGC
CTCTACTCGCTGAGCGTGGACAACTTCAATGAGGTGCTGGAGGAGTACCCCATGATGCGA
AGGGCCTTCGAGACCGTGGCGCTGGACCGCCTGGACCGCATTGGCAAGAAGAACTCCATC
CTCCTCCACAAAGTCCAGCACGACCTCAACTCCGGCGTCTTCAACTACCAGGAGAATGAG
ATCATCCAGCAGATTGTGCAGCATGACCGGGAGATGGCCCACTGCGCGCACCGCGTCCAG
GCTGCTGCCTCTGCCACCCCAACCCCCACGCCCGTCATCTGGACCCCGCTGATCCAGGCA
CCACTGCAGGCTGCCGCTGCCACCACTTCTGTGGCCATAGCCCTCACCCACCACCCTCGC
CTGCCTGCTGCCATCTTCCGCCCTCCCCCAGGATCTGGGCTGGGCAACCTCGGTGCCGGG
CAGACGCCAAGGCACCTGAAACGGCTGCAGTCCCTGATCCCTTCTGCGCTGGGCTCCGCC
TCGCCCGCCAGCAGCCCGTCCCAGGTGGACACACCGTCTTCATCCTCCTTCCACATCCAA
CAGCTGGCTGGATTCTCTGCCCCCGCTGGACTGAGCCCACTCCTGCCCTCATCCAGCTCC
TCCCCACCCCCCGGGGCCTGTGGCTCCCCCTCGGCTCCCACACCATCAGCTGGCGTAGCC
GCCACCACCATAGCCGGGTTTGGCCACTTCCACAAGGCGCTGGGTGGCTCCCTGTCCTCC
TCCGACTCTCCCCTGCTCACCCCGCTGCAGCCAGGCGCCCGCTCCCCGCAGGCTGCCCAG
CCATCTCCCGCGCCACCCGGGGCCCGGGGAGGCCTGGGACTCCCGGAGCACTTCCTGCCA
CCCCCACCCTCATCCAGATCCCCGTCATCTAGCCCCGGGCAGCTGGGCCAGCCTCCCGGG
GAGTTGTCCCTAGGTCTGGCCACTGGCCCACTGAGCACGCCAGAGACACCCCCACGGCAG
CCTGAGCCGCCGTCCCTTGTGGCAGGGGCCTCTGGGGGGGCTTCCCCTGTAGGCTTTACT
CCCCGAGGAGGTCTCAGCCCCCCTGGCCACAGCCCAGGCCCCCCAAGAACCTTCCCGAGT
GCCCCGCCCCGGGCCTCTGGCTCCCACGGATCCTTGCTCCTGCCACCTGCATCCAGCCCC
CCACCACCCCAGGTCCCCCAGCGCCGGGGCACACCCCCGCTCACCCCCGGCCGCCTCACC
CAGGACCTCAAGCTCATCTCCGCGTCTCAGCCAGCCCTGCCTCAGGACGGGGCGCAGACT
CTCCGCAGAGCCTCCCCGCACTCCTCAGGGGAGTCCATGGCTGCCTTCCCGCTCTTCCCC
AGGGCTGGGGGTGGCAGCGGGGGCAGTGGGAGCAGCGGGGGCCTCGGTCCCCCTGGGAGG
CCCTATGGTGCCATCCCCGGCCAGCACGTCACTCTGCCTCGGAAGACATCCTCAGGTTCT
TTGCCACCCCCTCTGTCTTTGTTTGGGGCAAGAGCCACCTCTTCTGGGGGGCCCCCTCTG
ACTGCTGGACCCCAGAGGGAACCTGGGGCCAGGCCTGAGCCAGTGCGCTCCAAACTGCCA
TCCAATCTATGA
Enzyme 115 GenBank Gene ID AJ132429 Link Image
Enzyme 115 GeneCard ID HCN4 Link Image
Enzyme 115 GenAtlas ID HCN4 Link Image
Enzyme 115 HGNC ID HGNC:16882 Link Image
Enzyme 115 Chromosome Location 1
Enzyme 115 Locus 15q24.1
Enzyme 115 SNPs SNPJam Report Link Image
Enzyme 115 General References
  1. Ludwig A, Zong X, Stieber J, Hullin R, Hofmann F, Biel M: Two pacemaker channels from human heart with profoundly different activation kinetics. EMBO J. 1999 May 4;18(9):2323-9. [PubMed Link Image]
  2. Seifert R, Scholten A, Gauss R, Mincheva A, Lichter P, Kaupp UB: Molecular characterization of a slowly gating human hyperpolarization-activated channel predominantly expressed in thalamus, heart, and testis. Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):9391-6. [PubMed Link Image]
  3. Ueda K, Hirano Y, Higashiuesato Y, Aizawa Y, Hayashi T, Inagaki N, Tana T, Ohya Y, Takishita S, Muratani H, Hiraoka M, Kimura A: Role of HCN4 channel in preventing ventricular arrhythmia. J Hum Genet. 2009 Feb;54(2):115-21. Epub 2009 Jan 23. [PubMed Link Image]
  4. Ueda K, Nakamura K, Hayashi T, Inagaki N, Takahashi M, Arimura T, Morita H, Higashiuesato Y, Hirano Y, Yasunami M, Takishita S, Yamashina A, Ohe T, Sunamori M, Hiraoka M, Kimura A: Functional characterization of a trafficking-defective HCN4 mutation, D553N, associated with cardiac arrhythmia. J Biol Chem. 2004 Jun 25;279(26):27194-8. Epub 2004 Apr 30. [PubMed Link Image]
  5. Milanesi R, Baruscotti M, Gnecchi-Ruscone T, DiFrancesco D: Familial sinus bradycardia associated with a mutation in the cardiac pacemaker channel. N Engl J Med. 2006 Jan 12;354(2):151-7. [PubMed Link Image]
Enzyme 115 Metabolite References Not Available
Enzyme 116 [top]
Enzyme 116 ID 13843
Enzyme 116 Name Histamine H4 receptor
Enzyme 116 Synonyms
  1. H4R
  2. HH4R
  3. AXOR35
  4. G-protein coupled receptor 105
  5. GPRv53
  6. Pfi-013
  7. SP9144
Enzyme 116 Gene Name HRH4
Enzyme 116 Protein Sequence >Histamine H4 receptor
MPDTNSTINLSLSTRVTLAFFMSLVAFAIMLGNALVILAFVVDKNLRHRSSYFFLNLAIS
DFFVGVISIPLYIPHTLFEWDFGKEICVFWLTTDYLLCTASVYNIVLISYDRYLSVSNAV
SYRTQHTGVLKIVTLMVAVWVLAFLVNGPMILVSESWKDEGSECEPGFFSEWYILAITSF
LEFVIPVILVAYFNMNIYWSLWKRDHLSRCQSHPGLTAVSSNICGHSFRGRLSSRRSLSA
STEVPASFHSERQRRKSSLMFSSRTKMNSNTIASKMGSFSQSDSVALHQREHVELLRARR
LAKSLAILLGVFAVCWAPYSLFTIVLSFYSSATGPKSVWYRIAFWLQWFNSFVNPLLYPL
CHKRFQKAFLKIFCIKKQPLPSQHSRSVSS
Enzyme 116 Number of Residues 390
Enzyme 116 Molecular Weight 44495.4
Enzyme 116 Theoretical pI 9.92
Enzyme 116 GO Classification
Function
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 116 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 116 Specific Function The H4 subclass of histamine receptors could mediate the histamine signals in peripheral tissues. Displays a significant level of constitutive activity (spontaneous activity in the absence of agonist)
Enzyme 116 Pathways Not Available
Enzyme 116 Reactions Not Available
Enzyme 116 Pfam Domain Function
Enzyme 116 Signals
  • None
Enzyme 116 Transmembrane Regions
  • 20-40 53-73 88-108 132-152 173-193 305-325 342-362
Enzyme 116 Essentiality Not Available
Enzyme 116 GenBank ID Protein 10241847 Link Image
Enzyme 116 UniProtKB/Swiss-Prot ID Q9H3N8 Link Image
Enzyme 116 UniProtKB/Swiss-Prot Entry Name HRH4_HUMAN Link Image
Enzyme 116 PDB ID Not Available
Enzyme 116 Cellular Location Not Available
Enzyme 116 Gene Sequence >1173 bp
ATGCCAGATACTAATAGCACAATCAATTTATCACTAAGCACTCGTGTTACTTTAGCATTT
TTTATGTCCTTAGTAGCTTTTGCTATAATGCTAGGAAATGCTTTGGTCATTTTAGCTTTT
GTGGTGGACAAAAACCTTAGACATCGAAGTAGTTATTTTTTTCTTAACTTGGCCATCTCT
GACTTCTTTGTGGGTGTGATCTCCATTCCTTTGTACATCCCTCACACGCTGTTCGAATGG
GATTTTGGAAAGGAAATCTGTGTATTTTGGCTCACTACTGACTATCTGTTATGTACAGCA
TCTGTATATAACATTGTCCTCATCAGCTATGATCGATACCTGTCAGTCTCAAATGCTGTG
TCTTATAGAACTCAACATACTGGGGTCTTGAAGATTGTTACTCTGATGGTGGTCGTTTGG
GTGCTGGCCTTCTTAGTGAATGGGCCAATGATTCTAGTTTCAGAGTCTTGGAAGGATGAA
GGTAGTGAATGTGAACCTGGATTTTTTTCGGAATGGTACATCCTTGCCATCACATCATTC
TTGGAATTCGTGATCCCAGTCATCTTAGTCGCTTATTTCAACATGAATATTTATTGGAGC
CTGTGGAAGCGTGATCGTCTCAGTAGGTGCCAAAGCCATCCTGGACTGACTGCTGTCTCT
TCCAACATCTGTGGACACTCATTCAGAGGTAGACTATCTTCAAGGAGATCTCTTTCTGCA
TCGACAGAAGTTCCTGCATCCTTTCATTCAGAGAGACGGAGGAGAAAGAGTAGTCTCATG
TTTTCCTCAAGAACCAAGATGAATAGCAATACAATTGCTTCCAAAATGGGTTCCTTCTCC
CAATCAGATTCTGTAGCTCTTCACCAAAGGGAACATGTTGAACTGCTTAGAGCCAGGAGA
TTAGCCAAGTCACTGGCCATTCTCTTAGGGGTTTTTGCTGTTTGCTGGGCTCCATATTCT
CTGTTCACAATTGTCCTTTCATTTTATTCCTCAGCAACAGGTCCTAAATCAGTTTGGTAT
AGAATTGCATTTTGGCTTCAGTGGTTCAATTCCTTTGTCAATCCTCTTTTGTATCCATTG
TGTCACAAGCGCTTTCAAAAGGCTTTCTTGAAAATATTTTGTATAAAAAAGCAACCTCTA
CCATCACAACACAGTCGGTCAGTATCTTCTTAA
Enzyme 116 GenBank Gene ID AB044934 Link Image
Enzyme 116 GeneCard ID HRH4 Link Image
Enzyme 116 GenAtlas ID HRH4 Link Image
Enzyme 116 HGNC ID HGNC:17383 Link Image
Enzyme 116 Chromosome Location 1
Enzyme 116 Locus 18q11.2
Enzyme 116 SNPs SNPJam Report Link Image
Enzyme 116 General References
  1. Oda T, Morikawa N, Saito Y, Masuho Y, Matsumoto S: Molecular cloning and characterization of a novel type of histamine receptor preferentially expressed in leukocytes. J Biol Chem. 2000 Nov 24;275(47):36781-6. [PubMed Link Image]
  2. Nakamura T, Itadani H, Hidaka Y, Ohta M, Tanaka K: Molecular cloning and characterization of a new human histamine receptor, HH4R. Biochem Biophys Res Commun. 2000 Dec 20;279(2):615-20. [PubMed Link Image]
  3. Liu C, Ma X, Jiang X, Wilson SJ, Hofstra CL, Blevitt J, Pyati J, Li X, Chai W, Carruthers N, Lovenberg TW: Cloning and pharmacological characterization of a fourth histamine receptor (H(4)) expressed in bone marrow. Mol Pharmacol. 2001 Mar;59(3):420-6. [PubMed Link Image]
  4. Morse KL, Behan J, Laz TM, West RE Jr, Greenfeder SA, Anthes JC, Umland S, Wan Y, Hipkin RW, Gonsiorek W, Shin N, Gustafson EL, Qiao X, Wang S, Hedrick JA, Greene J, Bayne M, Monsma FJ Jr: Cloning and characterization of a novel human histamine receptor. J Pharmacol Exp Ther. 2001 Mar;296(3):1058-66. [PubMed Link Image]
  5. Zhu Y, Michalovich D, Wu H, Tan KB, Dytko GM, Mannan IJ, Boyce R, Alston J, Tierney LA, Li X, Herrity NC, Vawter L, Sarau HM, Ames RS, Davenport CM, Hieble JP, Wilson S, Bergsma DJ, Fitzgerald LR: Cloning, expression, and pharmacological characterization of a novel human histamine receptor. Mol Pharmacol. 2001 Mar;59(3):434-41. [PubMed Link Image]
  6. O'Reilly M, Alpert R, Jenkinson S, Gladue RP, Foo S, Trim S, Peter B, Trevethick M, Fidock M: Identification of a histamine H4 receptor on human eosinophils--role in eosinophil chemotaxis. J Recept Signal Transduct Res. 2002 Feb-Nov;22(1-4):431-48. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 116 Metabolite References Not Available
Enzyme 117 [top]
Enzyme 117 ID 13844
Enzyme 117 Name cAMP-dependent protein kinase inhibitor alpha
Enzyme 117 Synonyms
  1. PKI-alpha
  2. cAMP-dependent protein kinase inhibitor, muscle/brain isoform
Enzyme 117 Gene Name PKIA
Enzyme 117 Protein Sequence >cAMP-dependent protein kinase inhibitor alpha
MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSS
TEQSGEAQGEAAKSES
Enzyme 117 Number of Residues 76
Enzyme 117 Molecular Weight 7988.4
Enzyme 117 Theoretical pI 4.18
Enzyme 117 GO Classification
Function
  • cAMP-dependent protein kinase inhibitor activity
  • enzyme inhibitor activity
  • enzyme regulator activity
  • kinase inhibitor activity
  • protein kinase inhibitor activity
  • protein serine/threonine kinase inhibitor activity
Process
  • biological regulation
  • negative regulation of kinase activity
  • negative regulation of protein kinase activity
  • regulation of biological process
  • regulation of cellular metabolic process
  • regulation of kinase activity
  • regulation of metabolic process
  • regulation of phosphate metabolic process
  • regulation of phosphorus metabolic process
  • regulation of phosphorylation
Component
Enzyme 117 General Function Involved in cAMP-dependent protein kinase inhibitor activity
Enzyme 117 Specific Function Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains
Enzyme 117 Pathways Not Available
Enzyme 117 Reactions Not Available
Enzyme 117 Pfam Domain Function
Enzyme 117 Signals
  • None
Enzyme 117 Transmembrane Regions
  • None
Enzyme 117 Essentiality Not Available
Enzyme 117 GenBank ID Protein 7208450 Link Image
Enzyme 117 UniProtKB/Swiss-Prot ID P61925 Link Image
Enzyme 117 UniProtKB/Swiss-Prot Entry Name IPKA_HUMAN Link Image
Enzyme 117 PDB ID 1CMK Link Image
Enzyme 117 PDB File Show
Enzyme 117 3D Structure
Enzyme 117 Cellular Location Not Available
Enzyme 117 Gene Sequence >231 bp
ATGACTGATGTGGAAACTACATATGCAGATTTTATTGCTTCAGGAAGAACAGGTAGAAGA
AATGCAATACATGATATCCTGGTTTCCTCTGCAAGTGGCAACAGCAATGAATTAGCCTTG
AAATTAGCAGGTCTTGATATCAACAAGACAGAAGGTGAAGAAGATGCACAACGAAGTTCT
ACAGAACAAAGTGGGGAAGCCCAGGGAGAAGCAGCAAAATCTGAAAGCTAA
Enzyme 117 GenBank Gene ID AF234641 Link Image
Enzyme 117 GeneCard ID PKIA Link Image
Enzyme 117 GenAtlas ID PKIA Link Image
Enzyme 117 HGNC ID HGNC:9017 Link Image
Enzyme 117 Chromosome Location 8
Enzyme 117 Locus 8q21.12
Enzyme 117 SNPs SNPJam Report Link Image
Enzyme 117 General References
  1. Olsen SR, Uhler MD: Inhibition of protein kinase-A by overexpression of the cloned human protein kinase inhibitor. Mol Endocrinol. 1991 Sep;5(9):1246-56. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 117 Metabolite References Not Available
Enzyme 118 [top]
Enzyme 118 ID 13845
Enzyme 118 Name cAMP-dependent protein kinase inhibitor beta
Enzyme 118 Synonyms
  1. PKI-beta
Enzyme 118 Gene Name PKIB
Enzyme 118 Protein Sequence >cAMP-dependent protein kinase inhibitor beta
MRTDSSKMTDVESGVANFASSARAGRRNALPDIQSSAATDGTSDLPLKLEALSVKEDAKE
KDEKTTQDQLEKPQNEEK
Enzyme 118 Number of Residues 78
Enzyme 118 Molecular Weight 8468.2
Enzyme 118 Theoretical pI 4.50
Enzyme 118 GO Classification
Function
  • cAMP-dependent protein kinase inhibitor activity
  • enzyme inhibitor activity
  • enzyme regulator activity
  • kinase inhibitor activity
  • protein kinase inhibitor activity
  • protein serine/threonine kinase inhibitor activity
Process
  • biological regulation
  • negative regulation of kinase activity
  • negative regulation of protein kinase activity
  • regulation of biological process
  • regulation of cellular metabolic process
  • regulation of kinase activity
  • regulation of metabolic process
  • regulation of phosphate metabolic process
  • regulation of phosphorus metabolic process
  • regulation of phosphorylation
Component
Enzyme 118 General Function Involved in cAMP-dependent protein kinase inhibitor activity
Enzyme 118 Specific Function Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains
Enzyme 118 Pathways Not Available
Enzyme 118 Reactions Not Available
Enzyme 118 Pfam Domain Function
Enzyme 118 Signals
  • None
Enzyme 118 Transmembrane Regions
  • None
Enzyme 118 Essentiality Not Available
Enzyme 118 GenBank ID Protein 20086435 Link Image
Enzyme 118 UniProtKB/Swiss-Prot ID Q9C010 Link Image
Enzyme 118 UniProtKB/Swiss-Prot Entry Name IPKB_HUMAN Link Image
Enzyme 118 PDB ID Not Available
Enzyme 118 Cellular Location Not Available
Enzyme 118 Gene Sequence >237 bp
ATGAGGACAGATTCATCAAAAATGACTGACGTGGAGTCTGGGGTCGCCAATTTTGCATCT
TCAGCAAGGGCAGGCCGCCGGAATGCCTTACCAGACATCCAGAGTTCAGCTGCCACAGAC
GGAACCTCAGATTTGCCCCTCAAACTGGAGGCTCTCTCCGTGAAGGAAGATGCAAAAGAG
AAAGATGAAAAAACAACACAAGACCAATTGGAAAAGCCTCAAAATGAAGAAAAATGA
Enzyme 118 GenBank Gene ID AF087873 Link Image
Enzyme 118 GeneCard ID PKIB Link Image
Enzyme 118 GenAtlas ID PKIB Link Image
Enzyme 118 HGNC ID HGNC:9018 Link Image
Enzyme 118 Chromosome Location 6
Enzyme 118 Locus 6q22.31
Enzyme 118 SNPs SNPJam Report Link Image
Enzyme 118 General References
  1. Zheng L, Yu L, Tu Q, Zhang M, He H, Chen W, Gao J, Yu J, Wu Q, Zhao S: Cloning and mapping of human PKIB and PKIG, and comparison of tissue expression patterns of three members of the protein kinase inhibitor family, including PKIA. Biochem J. 2000 Jul 15;349(Pt 2):403-7. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Naka