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Showing drug card for Atorvastatin (DB01076)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:03:39
Primary Accession Number DB01076
Secondary Accession Number
  • APRD00055
Name Atorvastatin
Drug Type
  • Approved
  • Small Molecule
Description Atorvastatin (Lipitor) is a member of the drug class known as statins. It is used for lowering cholesterol. Atorvastatin inhibits the rate-determining enzyme located in hepatic tissue that produces mevalonate, a small molecule used in the synthesis of cholesterol and other mevalonate derivatives. This lowers the amount of cholesterol produced which in turn lowers the total amount of LDL cholesterol. Atorvastatin is a competitive inhibitor of HMG-CoA reductase.
Synonyms
  1. Atorvastatin calcium
Brand Names
  1. Atorpic
  2. Cardyl
  3. Lipitor
  4. Liprimar
  5. Sortis
  6. Sotis
  7. Torvacard
  8. Torvast
  9. Totalip
  10. Tozalip
  11. Tulip
  12. Xarator
  13. Xavator
Brand Mixtures Not Available
Chemical IUPAC Name (3R,5R)-7-[2-(4-fluorophenyl)-3-phenyl-4-(phenylcarbamoyl)-5-propan-2-ylpyrrol-1-yl]-3,5-dihydroxyheptanoic acid
Chemical Formula C33H35FN2O5
Chemical Structure Structure
CAS Registry Number 134523-00-5
InChI Identifier InChI=1/C33H35FN2O5/c1-21(2)31-30(33(41)35-25-11-7-4-8-12-25)29(22-9-5-3-6-10-22)32(23-13-15-24(34)16-14-23)36(31)18-17-26(37)19-27(38)20-28(39)40/h3-16,21,26-27,37-38H,17-20H2,1-2H3,(H,35,41)(H,39,40)/t26-,27-/m1/s1/f/h35,39H
InChI Key XUKUURHRXDUEBC-WPPSOWBEDM
KEGG Drug Not Available
KEGG Compound C06834 Link Image
PubChem Compound 60823 Link Image
PubChem Substance 205162 Link Image
ChEBI ID 2910 Link Image
PharmGKB ID PA448500 Link Image
HET ID 117 Link Image
GenBank ID Not Available
Drug ID Number [DIN] 02243097 Link Image
RxList Link http://www.rxlist.com/cgi/generic/atorvastatin.htm Link Image
PDRhealth Link http://www.pdrhealth.com/drug_info/rxdrugprofiles/drugs/lip1230.shtml Link Image
Wikipedia Link http://en.wikipedia.org/wiki/Atorvastatin Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference B.D. Roth, U.S. pat. 5,273, 995(1991, 1993)
Average Molecular Weight 558.6398
Monoisotopic Molecular Weight 558.2530
State Solid
Melting Point 159.2-160.7 oC
Experimental Water Solubility Sodium salt soluble in water, 20.4 ug/mL (pH 2.1), 1.23 mg/mL (pH 6.0) Source: PhysProp
Predicted Water Solubility 6.30e-04 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 5.7 Source: PhysProp
Predicted LogP 4.24 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -5.95 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Isomeric SMILES CC(C)C1=C(C(=O)NC2=CC=CC=C2)C(C2=CC=CC=C2)=C(N1CC[C@@H](O)C[C@@H](O)CC(O)=O)C1=CC=C(F)C=C1
Canonical SMILES CC(C)C1=C(C(=O)NC2=CC=CC=C2)C(C2=CC=CC=C2)=C(N1CCC(O)CC(O)CC(O)=O)C1=CC=C(F)C=C1
Drug Category
  • Anticholesteremic Agents
  • Hydroxymethylglutaryl-CoA Reductase Inhibitors
ATC Codes
AHFS Codes
  • 24:06.08
Indication For management as an adjunct to diet to reduce elevated total-C, LDL-C, apo B, and TG levels in patients with primary hypercholesterolemia and mixed dyslipidemia.
Pharmacology Atorvastatin, a selective, competitive HMG-CoA reductase inhibitor, is used to lower cholesterol and triglycerides in patients with hypercholesterolemia and mixed dyslipidemia and in the treatment of homozygous familial hypercholesterolemia. Atorvastatin has a unique structure, long half-life, and hepatic selectivity, explaining its greater LDL-lowering potency compared to other HMG-CoA reductase inhibitors.
Mechanism of Action Atorvastatin selectively and competitively inhibits the hepatic enzyme hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase. As HMG-CoA reductase is responsible for converting HMG-CoA to mevalonate, this results in a decrease in mevalonate, a precursor of cholesterol, and a subsequent decrease in hepatic cholesterol levels and increase in uptake of LDL cholesterol.
Absorption Atorvastatin is rapidly absorbed after oral administration. The absolute bioavailability of atorvastatin (parent drug) is approximately 14% and the systemic availability of HMG-CoA reductase inhibitory activity is approximately 30%.
Toxicity Symptoms of overdose include rhabdomyolysis, eye hemorrhages, and liver problems.
Protein Binding 98%
Biotransformation Atorvastatin is extensively metabolized to ortho- and parahydroxylated derivatives and various beta-oxidation products. In vitro inhibition of HMG-CoA reductase by ortho- and parahydroxylated metabolites is equivalent to that of atorvastatin. Approximately 70% of circulating inhibitory activity for HMG-CoA reductase is attributed to active metabolites.
Half Life 14 hours
Dosage Forms
Form Route
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Amprenavir Amprenavir can possibly increase the statin
Atazanavir Atazanavir increases the effect and toxicity of the statin
Bezafibrate Increased risk of myopathy/rhabdomyolysis
Bosentan Bosentan could decrease atorvastatin
Carbamazepine Carbamazepine decreases the effect of the statin
Clarithromycin The macrolide possibly increases the statin toxicity
Colchicine Increased risk of rhadbomyolysis with this combination
Cyclosporine Possible myopathy and rhabdomyolysis
Delavirdine The NNRT inhibitor increases the effect and toxicity of the statin
Diltiazem Diltiazem increases the effect and toxicity of atorvastatin
Efavirenz The NNRT inhibitor increases the effect and toxicity of the statin
Erythromycin The macrolide possibly increases the statin toxicity
Fenofibrate Increased risk of myopathy/rhabdomyolysis
Fluconazole Increased risk of myopathy/rhabdomyolysis
Fosamprenavir Amprenavir can possibly increase the statin toxicity
Gemfibrozil Increased risk of myopathy/rhabdomyolysis
Imatinib Imatinib increases the effect and toxicity of atorvastatin
Indinavir Indinavir increases the effect and toxicity of atorvastatin
Itraconazole Increased risk of myopathy/rhabdomyolysis
Josamycin The macrolide possibly increases the statin toxicity
Ketoconazole Increased risk of myopathy/rhabdomyolysis
Nefazodone Nefazodone increases the effect and toxicity of the statin drug
Nelfinavir Nelfinavir increases the effect and toxicity of the statin
Nevirapine The NNRT inhibitor increases the effect and toxicity of the statin
Quinupristin This combination presents an increased risk of toxicity
Rifabutin The rifamycin decreases the effect of the statin drug
Rifampin The rifamycin decreases the effect of the statin drug
Ritonavir Ritonavir increases the effect and toxicity of the statin
Saquinavir Saquinavir increases the effect and toxicity of atorvastatin
Tacrolimus Tacrolimus increases the effect and toxicity of the statin
Telithromycin Telithromycin may possibly increase statin toxicity
Verapamil Verapamil increases the effect and toxicity of the statin
Food Interactions
  • Avoid alcohol.
  • Avoid drastic changes in dietary habit.
  • Avoid taking grapefruit or grapefruit juice throughout treatment.
  • Food may decrease maximum plasma levels and area under the curve, but this is inconsequential according to the manufacturer.
  • Grapefruit can significantly increase serum levels of this product.
  • Take with low fat meal.
Pathways
Name SMPDB Link KEGG Link
Atorvastatin Pathway SMP00131 Link Image
General References
  1. Maggon K: Best-selling human medicines 2002-2004. Drug Discov Today. 2005 Jun 1;10(11):739-42. [PubMed Link Image]
  2. Rouleau J: Improved outcome after acute coronary syndromes with an intensive versus standard lipid-lowering regimen: results from the Pravastatin or Atorvastatin Evaluation and Infection Therapy-Thrombolysis in Myocardial Infarction 22 (PROVE IT-TIMI 22) trial. Am J Med. 2005 Dec;118 Suppl 12A:28-35. [PubMed Link Image]
  3. Drugs.com Link Image
  4. Wikipedia Link Image
  5. RxList Link Image
  6. PDRhealth Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 3A4 (CYP3A4)
Targets
  1. Peroxisome proliferator-activated receptor alpha
  2. Vascular endothelial growth factor A
  3. Peroxisome proliferator-activated receptor gamma
  4. Plasminogen activator inhibitor 1
  5. 3-hydroxy-3-methylglutaryl-coenzyme A reductase
  6. Tumor necrosis factor
  7. C-reactive protein
  8. Serum paraoxonase/arylesterase 1
  9. Cytochrome P450 3A3
  10. Apolipoprotein B-100
  11. CD40 ligand
  12. Small inducible cytokine A2
  13. Angiotensinogen
  14. Collagen alpha-1(XIII) chain
  15. Transforming protein RhoA
  16. DNA replication licensing factor MCM7
  17. DNA replication licensing factor MCM6
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 3A4 (CYP3A4)
Enzyme 1 Gene Name CYP3A4
Enzyme 1 SwissProt ID P08684 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P08684|CP3A4_HUMAN Cytochrome P450 3A4 (EC 1.14.13.67)
ALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFD
MECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIA
EDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVF
PREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSII
FIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVN
ETLRLFPIAMRLERVCKKDVEINGMFIPKGWVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGG
LLQPEKPVVLKVESRDGTVSGA
Drug Target 1 [top]
Target 1 ID 80
Target 1 Name Peroxisome proliferator-activated receptor alpha
Target 1 Synonyms
  1. PPAR-alpha
Target 1 Gene Name PPARA
Target 1 Protein Sequence >Peroxisome proliferator-activated receptor alpha
MVDTESPLCPLSPLEAGDLESPLSEEFLQEMGNIQEISQSIGEDSSGSFGFTEYQYLGSC
PGSDGSVITDTLSPASSPSSVTYPVVPGSVDESPSGALNIECRICGDKASGYHYGVHACE
GCKGFFRRTIRLKLVYDKCDRSCKIQKKNRNKCQYCRFHKCLSVGMSHNAIRFGRMPRSE
KAKLKAEILTCEHDIEDSETADLKSLAKRIYEAYLKNFNMNKVKARVILSGKASNNPPFV
IHDMETLCMAEKTLVAKLVANGIQNKEAEVRIFHCCQCTSVETVTELTEFAKAIPGFANL
DLNDQVTLLKYGVYEAIFAMLSSVMNKDGMLVAYGNGFITREFLKSLRKPFCDIMEPKFD
FAMKFNALELDDSDISLFVAAIICCGDRPGLLNVGHIEKMQEGIVHVLRLHLQSNHPDDI
FLFPKLLQKMADLRQLVTEHAQLVQIIKKTESDAALHPLLQEIYRDMY
Target 1 Number of Residues 475
Target 1 Molecular Weight 52226
Target 1 Theoretical pI 6.20
Target 1 GO Classification
Function
steroid hormone receptor activity
transcription factor activity
signal transducer activity
receptor activity
ligand-dependent nuclear receptor activity
binding
nucleic acid binding
DNA binding
Process
regulation of biological process
regulation of physiological process
regulation of metabolism
regulation of cellular metabolism
regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
regulation of transcription
regulation of transcription, DNA-dependent
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
Target 1 General Function Involved in DNA binding
Target 1 Specific Function Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to a promoter element in the gene for acyl-CoA oxidase and activates its transcription. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 307341 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q07869 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name PPARA_HUMAN Link Image
Target 1 PDB ID 1K7L Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Nucleus
Target 1 Gene Sequence >1407 bp
ATGGTGGACACGGAAAGCCCACTCTGCCCCCTCTCCCCACTCGAGGCCGGCGATCTAGAG
AGCCCGTTATCTGAAGAGTTCCTGCAAGAAATGGGAAACATCCAAGAGATTTCGCAATCC
ATCGGCGAGGATAGTTCTGGAAGCTTTGGCTTTACGGAATACCAGTATTTAGGAAGCTGT
CCTGGCTCAGATGGCTCGGTCATCACGGACACGCTTTCACCAGCTTCGAGCCCCTCCTCG
GTGACTTATCCTGTGGTCCCCGGCAGCGTGGACGAGTCTCCCAGTGGAGCATTGAACATC
GAATGTAGAATCTGCGGGGACAAGGCCTCAGGCTATCATTACGGAGTCCACGCGTGTGAA
GGCTGCAAGGGCTTCTTTCGGCGAACGATTCGACTCAAGCTGGTGTATGACAAGTGCGAC
CGCAGCTGCAAGATCCAGAAAAAGAACAGAAACAAATGCCAGTATTGTCGATTTCACAAG
TGCCTTTCTGTCGGGATGTCACACAACGCGATTCGTTTTGGACGAATGCCAAGATCTGAG
AAAGCAAAACTGAAAGCAGAAATTCTTACCTGTGAACATGACATAGAAGATTCTGAAACT
GCAGATCTCAAATCTCTGGCCAAGAGAATCTACGAGGCCTACTTGAAGAACTTCAACATG
AACAAGGTCAAAGCCCGGGTCATCCTCTCAGGAAAGGCCAGTAACAATCCACCTTTTGTC
ATACATGATATGGAGACACTGTGTATGGCTGAGAAGACGCTGGTGGCCAAGCTGGTGGCC
AATGGCATCCAGAACAAGGAGGTGGAGGTCCGCATCTTTCACTGCTGCCAGTGCACGTCA
GTGGAGACCGTCACGGAGCTCACGGAATTCGCCAAGGCCATCCCAGCGTTCGCAAACTTG
GACCTGAACGATCAAGTGACATTGCTAAAATACGGAGTTTATGAGGCCATATTCGCCATG
CTGTCTTCTGTGATGAACAAAGACGGGATGCTGGTAGCGTATGGAAATGGGTTTATAACT
CGTGAATTCCTAAAAAGCCTAAGGAAACCGTTCTGTGATATCATGGAACCCAAGTTTGAT
TTTGCCATGAAGTTCAATGCACTGGAACTGGATGACAGTGATATCTCCCTTTTTGTGGCT
GCTATCATTTGCTGTGGAGATCGTCCTGGCCTTCTAAACGTAGGACACATTGAAAAAATG
CAGGAGGGTATTGTACATGTGCTCAGACTCCACCTGCAGAGCAACCACCCGGACGATATC
TTTCTCTTCCCAAAACTTCTTCAAAAAATGGCAGACCTCCGGCAGCTGGTGACGGAGCAT
GCGCAGCTGGTGCAGATCATCAAGAAGACGGAGTCGGATGCTGCGCTGCACCCGCTACTG
CAGGAGATCTACAGGGACATGTACTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID PPARA Link Image
Target 1 GenAtlas ID PPARA Link Image
Target 1 HGNC ID HGNC:9232 Link Image
Target 1 Chromosome Location 22
Target 1 Locus 22q12-q13.1|22q13.31
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. 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]
  2. Caira F, Antonson P, Pelto-Huikko M, Treuter E, Gustafsson JA: Cloning and characterization of RAP250, a novel nuclear receptor coactivator. J Biol Chem. 2000 Feb 25;275(8):5308-17. [PubMed Link Image]
  3. Sher T, Yi HF, McBride OW, Gonzalez FJ: cDNA cloning, chromosomal mapping, and functional characterization of the human peroxisome proliferator activated receptor. Biochemistry. 1993 Jun 1;32(21):5598-604. [PubMed Link Image]
  4. Mukherjee R, Jow L, Noonan D, McDonnell DP: Human and rat peroxisome proliferator activated receptors (PPARs) demonstrate similar tissue distribution but different responsiveness to PPAR activators. J Steroid Biochem Mol Biol. 1994 Nov;51(3-4):157-66. [PubMed Link Image]
  5. Tugwood JD, Aldridge TC, Lambe KG, Macdonald N, Woodyatt NJ: Peroxisome proliferator-activated receptors: structures and function. Ann N Y Acad Sci. 1996 Dec 27;804:252-65. [PubMed Link Image]
  6. Li H, Gomes PJ, Chen JD: RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8479-84. [PubMed Link Image]
Target 1 Drug References
  1. Bays H, Stein EA: Pharmacotherapy for dyslipidaemia--current therapies and future agents. Expert Opin Pharmacother. 2003 Nov;4(11):1901-38. [PubMed Link Image]
  2. Kleemann R, Verschuren L, de Rooij BJ, Lindeman J, de Maat MM, Szalai AJ, Princen HM, Kooistra T: Evidence for anti-inflammatory activity of statins and PPARalpha activators in human C-reactive protein transgenic mice in vivo and in cultured human hepatocytes in vitro. Blood. 2004 Jun 1;103(11):4188-94. Epub 2004 Feb 19. [PubMed Link Image]
  3. Planavila A, Laguna JC, Vazquez-Carrera M: Atorvastatin improves peroxisome proliferator-activated receptor signaling in cardiac hypertrophy by preventing nuclear factor-kappa B activation. Biochim Biophys Acta. 2005 Feb 21;1687(1-3):76-83. [PubMed Link Image]
  4. Sanguino E, Roglans N, Alegret M, Sanchez RM, Vazquez-Carrera M, Laguna JC: Atorvastatin reverses age-related reduction in rat hepatic PPARalpha and HNF-4. Br J Pharmacol. 2005 Aug;145(7):853-61. [PubMed Link Image]
  5. Sheng L, Ye P, Liu YX: [Atorvastatin upregulates the expression of PPAR alpha/gamma and inhibits the hypertrophy of cardiac myocytes in vitro] Zhonghua Xin Xue Guan Bing Za Zhi. 2005 Dec;33(12):1080-4. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 183
Target 2 Name Vascular endothelial growth factor A
Target 2 Synonyms
  1. VEGF-A
  2. VPF
  3. Vascular endothelial growth factor A precursor
  4. Vascular permeability factor
Target 2 Gene Name VEGF
Target 2 Protein Sequence >Vascular endothelial growth factor A precursor
MNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVD
IFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEM
SFLQHNKCECRPKKDRARQEKKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPG
PHPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR
Target 2 Number of Residues 235
Target 2 Molecular Weight 27043
Target 2 Theoretical pI 9.08
Target 2 GO Classification
Function
signal transducer activity
receptor binding
growth factor activity
Process
Not Available
Component
cell
membrane
Target 2 General Function Involved in growth factor activity
Target 2 Specific Function Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis, and induces permeabilization of blood vessels. Binds to the VEGFR1/Flt-1 and VEGFR2/Kdr receptors, heparan sulfate and heparin. Neuropilin-1 binds isoforms VEGF-165 and VEGF-145
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-26
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 181971 Link Image
Target 2 UniProtKB/Swiss-Prot ID P15692 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name VEGFA_HUMAN Link Image
Target 2 PDB ID 1TZI Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Secreted protein. VEGF121 is acidic and freely secreted. VEGF165 is more basic, has heparin-binding
Target 2 Gene Sequence >699 bp
ATGAACTTTCTGCTGTCTTGGGTGCATTGGAGCCTTGCCTTGCTGCTCTACCTCCACCAT
GCCAAGTGGTCCCAGGCTGCACCCATGGCAGAAGGAGGAGGGCAGAATCATCACGAAGTG
GTGAAGTTCATGGATGTCTATCAGCGCAGCTACTGCCATCCAATCGAGACCCTGGTGGAC
ATCTTCCAGGAGTACCCTGATGAGATCGAGTACATCTTCAAGCCATCCTGTGTGCCCCTG
ATGCGATGCGGGGGCTGCTGCAATGACGAGGGCCTGGAGTGTGTGCCCACTGAGGAGTCC
AACATCACCATGCAGATTATGCGGATCAAACCTCACCAAGGCCAGCACATAGGAGAGATG
AGCTTCCTACAGCACAACAAATGTGAATGCAGACCAAAGAAAGATAGAGCAAGACAAGAA
AAAAAATCAGTTCGAGGAAAGGGAAAGGGGCAAAAACGAAAGCGCAAGAAATCCCGGTAT
AAGTCCTGGAGCGTGTACGTTGGTGCCCGCTGCTGTCTAATGCCCTGGAGCCTCCCTGGC
CCCCATCCCTGTGGGCCTTGCTCAGAGCGGAGAAAGCATTTGTTTGTACAAGATCCGCAG
ACGTGTAAATGTTCCTGCAAAAACACAGACTCGCGTTGCAAGGCGAGGCAGCTTGAGTTA
AACGAACGTACTTGCAGATGTGACAAGCCGAGGCGGTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID VEGF Link Image
Target 2 GenAtlas ID VEGF Link Image
Target 2 HGNC ID HGNC:12680 Link Image
Target 2 Chromosome Location 6
Target 2 Locus 6p12
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Jingjing L, Xue Y, Agarwal N, Roque RS: Human Muller cells express VEGF183, a novel spliced variant of vascular endothelial growth factor. Invest Ophthalmol Vis Sci. 1999 Mar;40(3):752-9. [PubMed Link Image]
  2. Whittle C, Gillespie K, Harrison R, Mathieson PW, Harper SJ: Heterogeneous vascular endothelial growth factor (VEGF) isoform mRNA and receptor mRNA expression in human glomeruli, and the identification of VEGF148 mRNA, a novel truncated splice variant. Clin Sci (Lond). 1999 Sep;97(3):303-12. [PubMed Link Image]
  3. Murphy JF, Fitzgerald DJ: Vascular endothelial growth factor induces cyclooxygenase-dependent proliferation of endothelial cells via the VEGF-2 receptor. FASEB J. 2001 Jul;15(9):1667-9. [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. Weindel K, Marme D, Weich HA: AIDS-associated Kaposi's sarcoma cells in culture express vascular endothelial growth factor. Biochem Biophys Res Commun. 1992 Mar 31;183(3):1167-74. [PubMed Link Image]
  6. Tischer E, Mitchell R, Hartman T, Silva M, Gospodarowicz D, Fiddes JC, Abraham JA: The human gene for vascular endothelial growth factor. Multiple protein forms are encoded through alternative exon splicing. J Biol Chem. 1991 Jun 25;266(18):11947-54. [PubMed Link Image]
  7. Houck KA, Ferrara N, Winer J, Cachianes G, Li B, Leung DW: The vascular endothelial growth factor family: identification of a fourth molecular species and characterization of alternative splicing of RNA. Mol Endocrinol. 1991 Dec;5(12):1806-14. [PubMed Link Image]
  8. Leung DW, Cachianes G, Kuang WJ, Goeddel DV, Ferrara N: Vascular endothelial growth factor is a secreted angiogenic mitogen. Science. 1989 Dec 8;246(4935):1306-9. [PubMed Link Image]
  9. Keck PJ, Hauser SD, Krivi G, Sanzo K, Warren T, Feder J, Connolly DT: Vascular permeability factor, an endothelial cell mitogen related to PDGF. Science. 1989 Dec 8;246(4935):1309-12. [PubMed Link Image]
  10. Connolly DT, Olander JV, Heuvelman D, Nelson R, Monsell R, Siegel N, Haymore BL, Leimgruber R, Feder J: Human vascular permeability factor. Isolation from U937 cells. J Biol Chem. 1989 Nov 25;264(33):20017-24. [PubMed Link Image]
  11. 7678805 Fiebich BL, Jager B, Schollmann C, Weindel K, Wilting J, Kochs G, Marme D, Hug H, Weich HA: Synthesis and assembly of functionally active human vascular endothelial growth factor homodimers in insect cells. Eur J Biochem. 1993 Jan 15;211(1-2):19-26.
  12. 9054410 Poltorak Z, Cohen T, Sivan R, Kandelis Y, Spira G, Vlodavsky I, Keshet E, Neufeld G: VEGF145, a secreted vascular endothelial growth factor isoform that binds to extracellular matrix. J Biol Chem. 1997 Mar 14;272(11):7151-8.
  13. 9207067 Muller YA, Li B, Christinger HW, Wells JA, Cunningham BC, de Vos AM: Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site. Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7192-7.
  14. 9336848 Fairbrother WJ, Champe MA, Christinger HW, Keyt BA, Starovasnik MA: 1H, 13C, and 15N backbone assignment and secondary structure of the receptor-binding domain of vascular endothelial growth factor. Protein Sci. 1997 Oct;6(10):2250-60.
  15. 9351807 Muller YA, Christinger HW, Keyt BA, de Vos AM: The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 A resolution: multiple copy flexibility and receptor binding. Structure. 1997 Oct 15;5(10):1325-38.
  16. 9450968 Claffey KP, Shih SC, Mullen A, Dziennis S, Cusick JL, Abrams KR, Lee SW, Detmar M: Identification of a human VPF/VEGF 3' untranslated region mediating hypoxia-induced mRNA stability. Mol Biol Cell. 1998 Feb;9(2):469-81.
  17. 9634701 Fairbrother WJ, Champe MA, Christinger HW, Keyt BA, Starovasnik MA: Solution structure of the heparin-binding domain of vascular endothelial growth factor. Structure. 1998 May 15;6(5):637-48.
  18. 9878851 Lei J, Jiang A, Pei D: Identification and characterization of a new splicing variant of vascular endothelial growth factor: VEGF183. Biochim Biophys Acta. 1998 Dec 22;1443(3):400-6.
  19. 9922142 Wiesmann C, Christinger HW, Cochran AG, Cunningham BC, Fairbrother WJ, Keenan CJ, Meng G, de Vos AM: Crystal structure of the complex between VEGF and a receptor-blocking peptide. Biochemistry. 1998 Dec 22;37(51):17765-72.
Target 2 Drug References
  1. Chen J, Zhang ZG, Li Y, Wang Y, Wang L, Jiang H, Zhang C, Lu M, Katakowski M, Feldkamp CS, Chopp M: Statins induce angiogenesis, neurogenesis, and synaptogenesis after stroke. Ann Neurol. 2003 Jun;53(6):743-51. [PubMed Link Image]
  2. Saijonmaa O, Nyman T, Stewen P, Fyhrquist F: Atorvastatin completely inhibits VEGF-induced ACE upregulation in human endothelial cells. Am J Physiol Heart Circ Physiol. 2004 Jun;286(6):H2096-102. Epub 2004 Jan 2. [PubMed Link Image]
  3. Chen J, Zhang C, Jiang H, Li Y, Zhang L, Robin A, Katakowski M, Lu M, Chopp M: Atorvastatin induction of VEGF and BDNF promotes brain plasticity after stroke in mice. J Cereb Blood Flow Metab. 2005 Feb;25(2):281-90. [PubMed Link Image]
  4. Motoyama K, Fukumoto S, Koyama H, Emoto M, Shimano H, Maemura K, Nishizawa Y: SREBP inhibits VEGF expression in human smooth muscle cells. Biochem Biophys Res Commun. 2006 Mar 31;342(1):354-60. Epub 2006 Feb 3. [PubMed Link Image]
  5. Loboda A, Jazwa A, Jozkowicz A, Molema G, Dulak J: Angiogenic transcriptome of human microvascular endothelial cells: Effect of hypoxia, modulation by atorvastatin. Vascul Pharmacol. 2006 Apr;44(4):206-14. Epub 2006 Feb 14. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 238
Target 3 Name Peroxisome proliferator-activated receptor gamma
Target 3 Synonyms
  1. PPAR-gamma
Target 3 Gene Name PPARG
Target 3 Protein Sequence >Peroxisome proliferator-activated receptor gamma
MGETLGDSPIDPESDSFTDTLSANISQEMTMVDTEMPFWPTNFGISSVDLSVMEDHSHSF
DIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKT
QLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNC
RIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLR
ALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQE
QSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLAS
LMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVII
LSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQL
LQVIKKTETDMSLHPLLQEIYKDLY
Target 3 Number of Residues 513
Target 3 Molecular Weight 57621
Target 3 Theoretical pI 5.77
Target 3 GO Classification
Function
steroid hormone receptor activity
transcription factor activity
signal transducer activity
receptor activity
ligand-dependent nuclear receptor activity
binding
nucleic acid binding
DNA binding
Process
regulation of biological process
regulation of physiological process
regulation of metabolism
regulation of cellular metabolism
regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
regulation of transcription
regulation of transcription, DNA-dependent
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
Target 3 General Function Involved in DNA binding
Target 3 Specific Function Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to a promoter element in the gene for acyl-CoA oxidase and activates its transcription. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 1711117 Link Image
Target 3 UniProtKB/Swiss-Prot ID P37231 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name PPARG_HUMAN Link Image
Target 3 PDB ID 1I7I Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location
  • Nucleus
Target 3 Gene Sequence >1518 bp
ATGGGTGAAACTCTGGGAGATTCTCCTATTGACCCAGAAAGCGATTCCTTCACTGATACA
CTGTCTGCAAACATATCACAAGAAATGACCATGGTTGACACAGAGATGCCATTCTGGCCC
ACCAACTTTGGGATCAGCTCCGTGGATCTCTCCGTAATGGAAGACCACTCCCACTCCTTT
GATATCAAGCCCTTCACTACTGTTGACTTCTCCAGCATTTCTACTCCACATTACGAAGAC
ATTCCATTCACAAGAACAGATCCAGTGGTTGCAGATTACAAGTATGACCTGAAACTTCAA
GAGTACCAAAGTGCAATCAAAGTGGAGCCTGCATCTCCACCTTATTATTCTGAGAAGACT
CAGCTCTACAATAAGCCTCATGAAGAGCCTTCCAACTCCCTCATGGCAATTGAATGTCGT
GTCTGTGGAGATAAAGCTTCTGGATTTCACTATGGAGTTCATGCTTGTGAAGGATGCAAG
GGTTTCTTCCGGAGAACAATCAGATTGAAGCTTATCTATGACAGATGTGATCTTAACTGT
CGGATCCACAAAAAAAGTAGAAATAAATGTCAGTACTGTCGGTTTCAGAAATGCCTTGCA
GTGGGGATGTCTCATAATGCCATCAGGTTTGGGCGGATGCCACAGGCCGAGAAGGAGAAG
CTGTTGGCGGAGATCTCCAGTGATATCGACCAGCTGAATCCAGAGTCCGCTGACCTCCGG
GCCCTGGCAAAACATTTGTATGACTCATACATAAAGTCCTTCCCGCTGACCAAAGCAAAG
GCGAGGGCGATCTTGACAGGAAAGACAACAGACAAATCACCATTCGTTATCTATGACATG
AATTCCTTAATGATGGGAGAAGATAAAATCAAGTTCAAACACATCACCCCCCTGCAGGAG
CAGAGCAAAGAGGTGGCCATCCGCATCTTTCAGGGCTGCCAGTTTCGCTCCGTGGAGGCT
GTGCAGGAGATCACAGAGTATGCCAAAAGCATTCCTGGTTTTGTAAATCTTGACTTGAAC
GACCAAGTAACTCTCCTCAAATATGGAGTCCACGAGATCATTTACACAATGCTGGCCTCC
TTGATGAATAAAGATGGGGTTCTCATATCCGAGGGCCAAGGCTTCATGACAAGGGAGTTT
CTAAAGAGCCTGCGAAAGCCTTTTGGTGACTTTATGGAGCCCAAGTTTGAGTTTGCTGTG
AAGTTCAATGCACTGGAATTAGATGACAGCGACTTGGCAATATTTATTGCTGTCATTATT
CTCAGTGGAGACCGCCCAGGTTTGCTGAATGTGAAGCCCATTGAAGACATTCAAGACAAC
CTGCTACAAGCCCTGGAGCTCCAGCTGAAGCTGAACCACCCTGAGTCCTCACAGCTGTTT
GCCAAGCTGCTCCAGAAAATGACAGACCTCAGACAGATTGTCACGGAACACGTGCAGCTA
CTGCAGGTGATCAAGAAGACGGAGACAGACATGAGTCTTCACCCGCTCCTGCAGGAGATC
TACAAGGACTTGTACTAG
Target 3 GenBank Gene ID
Target 3 GeneCard ID PPARG Link Image
Target 3 GenAtlas ID PPARG Link Image
Target 3 HGNC ID HGNC:9236 Link Image
Target 3 Chromosome Location 3
Target 3 Locus 3p25
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Sarraf P, Mueller E, Smith WM, Wright HM, Kum JB, Aaltonen LA, de la Chapelle A, Spiegelman BM, Eng C: Loss-of-function mutations in PPAR gamma associated with human colon cancer. Mol Cell. 1999 Jun;3(6):799-804. [PubMed Link Image]
  2. Hamann A, Munzberg H, Buttron P, Busing B, Hinney A, Mayer H, Siegfried W, Hebebrand J, Greten H: Missense variants in the human peroxisome proliferator-activated receptor-gamma2 gene in lean and obese subjects. Eur J Endocrinol. 1999 Jul;141(1):90-2. [PubMed Link Image]
  3. Barroso I, Gurnell M, Crowley VE, Agostini M, Schwabe JW, Soos MA, Maslen GL, Williams TD, Lewis H, Schafer AJ, Chatterjee VK, O'Rahilly S: Dominant negative mutations in human PPARgamma associated with severe insulin resistance, diabetes mellitus and hypertension. Nature. 1999 Dec 23-30;402(6764):880-3. [PubMed Link Image]
  4. Caira F, Antonson P, Pelto-Huikko M, Treuter E, Gustafsson JA: Cloning and characterization of RAP250, a novel nuclear receptor coactivator. J Biol Chem. 2000 Feb 25;275(8):5308-17. [PubMed Link Image]
  5. Gampe RT Jr, Montana VG, Lambert MH, Miller AB, Bledsoe RK, Milburn MV, Kliewer SA, Willson TM, Xu HE: Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors. Mol Cell. 2000 Mar;5(3):545-55. [PubMed Link Image]
  6. Agarwal AK, Garg A: A novel heterozygous mutation in peroxisome proliferator-activated receptor-gamma gene in a patient with familial partial lipodystrophy. J Clin Endocrinol Metab. 2002 Jan;87(1):408-11. [PubMed Link Image]
  7. Shao W, Halachmi S, Brown M: ERAP140, a conserved tissue-specific nuclear receptor coactivator. Mol Cell Biol. 2002 May;22(10):3358-72. [PubMed Link Image]
  8. Greene ME, Blumberg B, McBride OW, Yi HF, Kronquist K, Kwan K, Hsieh L, Greene G, Nimer SD: Isolation of the human peroxisome proliferator activated receptor gamma cDNA: expression in hematopoietic cells and chromosomal mapping. Gene Expr. 1995;4(4-5):281-99. [PubMed Link Image]
  9. Elbrecht A, Chen Y, Cullinan CA, Hayes N, Leibowitz M, Moller DE, Berger J: Molecular cloning, expression and characterization of human peroxisome proliferator activated receptors gamma 1 and gamma 2. Biochem Biophys Res Commun. 1996 Jul 16;224(2):431-7. [PubMed Link Image]
  10. Lambe KG, Tugwood JD: A human peroxisome-proliferator-activated receptor-gamma is activated by inducers of adipogenesis, including thiazolidinedione drugs. Eur J Biochem. 1996 Jul 1;239(1):1-7. [PubMed Link Image]
  11. 9065481 Mukherjee R, Jow L, Croston GE, Paterniti JR Jr: Identification, characterization, and tissue distribution of human peroxisome proliferator-activated receptor (PPAR) isoforms PPARgamma2 versus PPARgamma1 and activation with retinoid X receptor agonists and antagonists. J Biol Chem. 1997 Mar 21;272(12):8071-6.
  12. 9144532 Yanase T, Yashiro T, Takitani K, Kato S, Taniguchi S, Takayanagi R, Nawata H: Differential expression of PPAR gamma1 and gamma2 isoforms in human adipose tissue. Biochem Biophys Res Commun. 1997 Apr 17;233(2):320-4.
  13. 9356045 Okazawa H, Mori H, Tamori Y, Araki S, Niki T, Masugi J, Kawanishi M, Kubota T, Shinoda H, Kasuga M: No coding mutations are detected in the peroxisome proliferator-activated receptor-gamma gene in Japanese patients with lipoatrophic diabetes. Diabetes. 1997 Nov;46(11):1904-6.
  14. 9425261 Yen CJ, Beamer BA, Negri C, Silver K, Brown KA, Yarnall DP, Burns DK, Roth J, Shuldiner AR: Molecular scanning of the human peroxisome proliferator activated receptor gamma (hPPAR gamma) gene in diabetic Caucasians: identification of a Pro12Ala PPAR gamma 2 missense mutation. Biochem Biophys Res Commun. 1997 Dec 18;241(2):270-4.
  15. 9753710 Ristow M, Muller-Wieland D, Pfeiffer A, Krone W, Kahn CR: Obesity associated with a mutation in a genetic regulator of adipocyte differentiation. N Engl J Med. 1998 Oct 1;339(14):953-9.
Target 3 Drug References
  1. Zhao SP, Zhang DQ: Atorvastatin enhances cellular uptake of oxidized LDL in adipocytes from hypercholesterolemic rabbits. Clin Chim Acta. 2004 Jan;339(1-2):189-94. [PubMed Link Image]
  2. Argmann CA, Edwards JY, Sawyez CG, O'Neil CH, Hegele RA, Pickering JG, Huff MW: Regulation of macrophage cholesterol efflux through hydroxymethylglutaryl-CoA reductase inhibition: a role for RhoA in ABCA1-mediated cholesterol efflux. J Biol Chem. 2005 Jun 10;280(23):22212-21. Epub 2005 Apr 6. [PubMed Link Image]
  3. Planavila A, Sanchez RM, Merlos M, Laguna JC, Vazquez-Carrera M: Atorvastatin prevents peroxisome proliferator-activated receptor gamma coactivator-1 (PGC-1) downregulation in lipopolysaccharide-stimulated H9c2 cells. Biochim Biophys Acta. 2005 Sep 15;1736(2):120-7. [PubMed Link Image]
  4. Ye P, Sheng L, Zhang C, Liu Y: Atorvastatin attenuating down-regulation of peroxisome proliferator-activated receptor gamma in preventing cardiac hypertrophy of rats in vitro and in vivo. J Pharm Pharm Sci. 2006;9(3):365-75. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 267
Target 4 Name Plasminogen activator inhibitor 1
Target 4 Synonyms
  1. Endothelial plasminogen activator inhibitor
  2. PAI
  3. PAI-1
  4. Plasminogen activator inhibitor 1 precursor
Target 4 Gene Name SERPINE1
Target 4 Protein Sequence >Plasminogen activator inhibitor 1 precursor
MQMSPALTCLVLGLALVFGEGSAVHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPY
GVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAI
FVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAV
DQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPD
GHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPK
FSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASS
STAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP
Target 4 Number of Residues 408
Target 4 Molecular Weight 45061
Target 4 Theoretical pI 7.22
Target 4 GO Classification
Function
enzyme regulator activity
enzyme inhibitor activity
protease inhibitor activity
endopeptidase inhibitor activity
serine-type endopeptidase inhibitor activity
Process
Not Available
Component
Not Available
Target 4 General Function Involved in serine-type endopeptidase inhibitor activity
Target 4 Specific Function This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, and protein C. Its rapid interaction with TPA may function as a major control point in the regulation of fibrinolysis
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • 1-23
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 35272 Link Image
Target 4 UniProtKB/Swiss-Prot ID P05121 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name PAI1_HUMAN Link Image
Target 4 PDB ID 1C5G Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location
  • Secreted protein
Target 4 Gene Sequence >1209 bp
ATGCAGATGTCTCCAGCCCTCACCTGCCTAGTCCTGGGCCTGGCCCTTGTCTTTGGTGAA
GGGTCTGCTGTGCACCATCCCCCATCCTACGTGGCCCACCTGGCCTCAGACTTCGGGGTG
AGGGTGTTTCAGCAGGTGGCGCAGGCCTCCAAGGACCGCAACGTGGTTTTCTCACCCTAT
GGGGTGGCCTCGGTGTTGGCCATGCTCCAGCTGACAACAGGAGGAGAAACCCAGCAGCAG
ATTCAAGCAGCTATGGGATTCAAGATTGATGACAAGGGCATGGCCCCCGCCCTCCGGCAT
CTGTACAAGGAGCTCATGGGGCCATGGAACAAGGACGAGATCAGCACCACAGACGCGATC
TTCGTCCAGCGGGATCTGAAGCTGGTCCAGGGCTTCATGCCCCACTTCTTCAGGCTGTTC
CGGAGCACGGTCAAGCAAGTGGACTTTTCAGAGGTGGAGAGAGCCAGATTCATCATCAAT
GACTGGGTGAAGACACACACAAAAGGTATGATCAGCAACTTGCTTGGGAAAGGAGCCGTG
GACCAGCTGACACGGCTGGTGCTGGTGAATGCCCTCTACTTCAACGGCCAGTGGAAGACT
CCCTTCCCCGACTCCAGCACCCACCGCCGCCTCTTCCACAAATCAGACGGCAGCACTGTC
TCTGTGCCCATGATGGCTCAGACCAACAAGTTCAACTATACTGAGTTCACCACGCCCGAT
GGCCATTACTACGACATCCTGGAACTGCCCTACCACGGGGACACCCTCAGCATGTTCATT
GCTGCCCCTTATGAAAAAGAGGTGCCTCTCTCTGCCCTCACCAACATTCTGAGTGCCCAG
CTCATCAGCCACTGGAAAGGCAACATGACCAGGCTGCCCCGCCTCCTGGTTCTGCCCAAG
TTCTCCCTGGAGACTGAAGTCGACCTCAGGAAGCCCCTAGAGAACCTGGGAATGACCGAC
ATGTTCAGACAGTTTCAGGCTGACTTCACGAGTCTTTCAGACCAAGAGCCTCTCCACGTC
GCGCAGGCGCTGCAGAAAGTGAAGATCGAGGTGAACGAGAGTGGCACGGTGGCCTCCTCA
TCCACAGCTGTCATAGTCTCAGCCCGCATGGCCCCCGAGGAGATCATCATGGACAGACCC
TTCCTCTTTGTGGTCCGGCACAACCCCACAGGAACAGTCCTTTTCATGGGCCAAGTGATG
GAACCCTGA
Target 4 GenBank Gene ID
Target 4 GeneCard ID SERPINE1 Link Image
Target 4 GenAtlas ID SERPINE1 Link Image
Target 4 HGNC ID HGNC:8583 Link Image
Target 4 Chromosome Location 7
Target 4 Locus 7q21.3-q22
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Sharp AM, Stein PE, Pannu NS, Carrell RW, Berkenpas MB, Ginsburg D, Lawrence DA, Read RJ: The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion. Structure. 1999 Feb 15;7(2):111-8. [PubMed Link Image]
  2. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  3. Nar H, Bauer M, Stassen JM, Lang D, Gils A, Declerck PJ: Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation. J Mol Biol. 2000 Mar 31;297(3):683-95. [PubMed Link Image]
  4. Liu CX, Li Y, Obermoeller-McCormick LM, Schwartz AL, Bu G: The putative tumor suppressor LRP1B, a novel member of the low density lipoprotein (LDL) receptor family, exhibits both overlapping and distinct properties with the LDL receptor-related protein. J Biol Chem. 2001 Aug 3;276(31):28889-96. Epub 2001 May 30. [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. Mottonen J, Strand A, Symersky J, Sweet RM, Danley DE, Geoghegan KF, Gerard RD, Goldsmith EJ: Structural basis of latency in plasminogen activator inhibitor-1. Nature. 1992 Jan 16;355(6357):270-3. [PubMed Link Image]
  7. Pannekoek H, Veerman H, Lambers H, Diergaarde P, Verweij CL, van Zonneveld AJ, van Mourik JA: Endothelial plasminogen activator inhibitor (PAI): a new member of the Serpin gene family. EMBO J. 1986 Oct;5(10):2539-44. [PubMed Link Image]
  8. Follo M, Ginsburg D: Structure and expression of the human gene encoding plasminogen activator inhibitor, PAI-1. Gene. 1989 Dec 14;84(2):447-53. [PubMed Link Image]
  9. Loskutoff DJ, Linders M, Keijer J, Veerman H, van Heerikhuizen H, Pannekoek H: Structure of the human plasminogen activator inhibitor 1 gene: nonrandom distribution of introns. Biochemistry. 1987 Jun 30;26(13):3763-8. [PubMed Link Image]
  10. Andreasen PA, Riccio A, Welinder KG, Douglas R, Sartorio R, Nielsen LS, Oppenheimer C, Blasi F, Dano K: Plasminogen activator inhibitor type-1: reactive center and amino-terminal heterogeneity determined by protein and cDNA sequencing. FEBS Lett. 1986 Dec 15;209(2):213-8. [PubMed Link Image]
  11. 3026837 Wun TC, Kretzmer KK: cDNA cloning and expression in E. coli of a plasminogen activator inhibitor (PAI) related to a PAI produced by Hep G2 hepatoma cell. FEBS Lett. 1987 Jan 1;210(1):11-6.
  12. 3092219 Ny T, Sawdey M, Lawrence D, Millan JL, Loskutoff DJ: Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6776-80.
  13. 3097076 Ginsburg D, Zeheb R, Yang AY, Rafferty UM, Andreasen PA, Nielsen L, Dano K, Lebo RV, Gelehrter TD: cDNA cloning of human plasminogen activator-inhibitor from endothelial cells. J Clin Invest. 1986 Dec;78(6):1673-80.
  14. 3132455 Bosma PJ, van den Berg EA, Kooistra T, Siemieniak DR, Slightom JL: Human plasminogen activator inhibitor-1 gene. Promoter and structural gene nucleotide sequences. J Biol Chem. 1988 Jul 5;263(19):9129-41.
  15. 3262512 Strandberg L, Lawrence D, Ny T: The organization of the human-plasminogen-activator-inhibitor-1 gene. Implications on the evolution of the serine-protease inhibitor family. Eur J Biochem. 1988 Oct 1;176(3):609-16.
  16. 7522053 Sigurdardottir O, Wiman B: Identification of a PAI-1 binding site in vitronectin. Biochim Biophys Acta. 1994 Sep 21;1208(1):104-10.
  17. 7552714 Aertgeerts K, De Bondt HL, De Ranter CJ, Declerck PJ: Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1. Nat Struct Biol. 1995 Oct;2(10):891-7.
  18. 9194591 Turkmen B, Schmitt M, Schmalfeldt B, Trommler P, Hell W, Creutzburg S, Graeff H, Magdolen V: Mutational analysis of the genes encoding urokinase-type plasminogen activator (uPA) and its inhibitor PAI-1 in advanced ovarian cancer. Electrophoresis. 1997 May;18(5):686-9.
  19. 9634700 Xue Y, Bjorquist P, Inghardt T, Linschoten M, Musil D, Sjolin L, Deinum J: Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide. Structure. 1998 May 15;6(5):627-36.
Target 4 Drug References
  1. Van De Ree MA, De Maat MP, Kluft C, Meinders AE, Princen HM, Huisman MV: Decrease of hemostatic cardiovascular risk factors by aggressive vs. conventional atorvastatin treatment in patients with Type 2 diabetes mellitus. J Thromb Haemost. 2003 Aug;1(8):1753-7. [PubMed Link Image]
  2. Sakabe K, Fukuda N, Wakayama K, Nada T, Shinohara H, Tamura Y: Time course differences for statin-induced pleiotropic effects in hypercholesterolemic patients. Int J Cardiol. 2004 Mar;94(1):111-7. [PubMed Link Image]
  3. Sakabe K, Fukuda N, Wakayama K, Nada T, Shinohara H, Tamura Y: Lipid-altering changes and pleiotropic effects of atorvastatin in patients with hypercholesterolemia. Am J Cardiol. 2004 Aug 15;94(4):497-500. [PubMed Link Image]
  4. Fogari R, Derosa G, Lazzari P, Zoppi A, Fogari E, Rinaldi A, Mugellini A: Effect of amlodipine-atorvastatin combination on fibrinolysis in hypertensive hypercholesterolemic patients with insulin resistance. Am J Hypertens. 2004 Sep;17(9):823-7. [PubMed Link Image]
  5. Okopien B, Krysiak R, Herman ZS: Effect of monthly atorvastatin treatment on hemostasis. Int J Clin Pharmacol Ther. 2004 Nov;42(11):589-93. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 631
Target 5 Name 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Target 5 Synonyms
  1. EC 1.1.1.34
  2. HMG-CoA reductase
Target 5 Gene Name HMGCR
Target 5 Protein Sequence >3-hydroxy-3-methylglutaryl-coenzyme A reductase
MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSS
DIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTG
LNEALPFFLLLIDLSRASTLAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIG
VGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFAR
VLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADTSKVSLGLDENVSKR
IEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQTETESTLSLKNPITSPVVT
QKKVPDNCCRREPMLVRNNQKCDSVEEETGINRERKVEVIKPLVAETDTPNRATFVVGNS
SLLDTSSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYK
LETLMETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGV
AGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRAC
DSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMI
SKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREV
LKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITL
MEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLAR
IVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA
Target 5 Number of Residues 902
Target 5 Molecular Weight 97477
Target 5 Theoretical pI 6.72
Target 5 GO Classification
Function
hydroxymethylglutaryl-CoA reductase (NADPH) activity
hydroxymethylglutaryl-CoA reductase (NADPH) activity
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
hydroxymethylglutaryl-CoA reductase (NADPH) activity
Process
primary metabolism
lipid metabolism
physiological process
metabolism
biosynthesis
Component
organelle membrane
endoplasmic reticulum membrane
cell
membrane
intrinsic to membrane
integral to membrane
Target 5 General Function Lipid transport and metabolism
Target 5 Specific Function This transmembrane glycoprotein is involved in the control of cholesterol biosynthesis. It is the rate-limiting enzyme of sterol biosynthesis
Target 5 Pathways
Name SMPDB Link KEGG Link
Biosynthesis of steroids map00100 Link Image
Target 5 Reactions
  • (R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • 10-39
  • 57-78
  • 90-114
  • 124-149
  • 160-187
  • 192-220
  • 315-339
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 306865 Link Image
Target 5 UniProtKB/Swiss-Prot ID P04035 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name HMDH_HUMAN Link Image
Target 5 PDB ID 1HWL Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location
  • Endoplasmic reticulum
  • endoplasmic reticulum membrane
  • multi-pass membrane protein. Peroxisome
  • pero
Target 5 Gene Sequence >2667 bp
ATGTTGTCAAGACTTTTTCGAATGCATGGCCTCTTTGTGGCCTCCCATCCCTGGGAAGTC
ATAGTGGGGACAGTGACACTGACCATCTGCATGATGTCCATGAACATGTTTACTGGTAAC
AATAAGATCTGTGGTTGGAATTATGAATGTCCAAAGTTTGAAGAGGATGTTTTGAGCAGT
GACATTATAATTCTGACAATAACACGATGCATAGCCATCCTGTATATTTACTTCCAGTTC
CAGAATTTACGTCAACTTGGATCAAAATATATTTTGGGTATTGCTGGCCTTTTCACAATT
TTCTCAAGTTTTGTATTCAGTACAGTTGTCATTCACTTCTTAGACAAAGAATTGACAGGC
TTGAATGAAGCTTTGCCCTTTTTCCTACTTTTGATTGACCTTTCCAGAGCAAGCACATTA
GCAAAGTTTGCCCTCAGTTCCAACTCACAGGATGAAGTAAGGGAAAATATTGCTCGTGGA
ATGGCAATTTTAGGTCCTACGTTTACCCTCGATGCTCTTGTTGAATGTCTTGTGATTGGA
GTTGGTACCATGTCAGGGGTACGTCAGCTTGAAATTATGTGCTGCTTTGGCTGCATGTCA
GTTCTTGCCAACTACTTCGTGTTCATGACTTTCTTCCCAGCTTGTGTGTCCTTGGTATTA
GAGCTTTCTCGGGAAAGCCGCGAGGGTCGTCCAATTTGGCAGCTCAGCCATTTTGCCCGA
GTTTTAGAAGAAGAAGAAAATAAGCCGAATCCTGTAACTCAGAGGGTCAAGATGATTATG
TCTCTAGGCTTGGTTCTTGTTCATGCTCACAGTCGCTGGATAGCTGATCCTTCTCCTCAA
AACAGTACAGCAGATACTTCTAAGGTTTCATTAGGACTGGATGAAAATGTGTCCAAGAGA
ATTGAACCAAGTGTTTCCCTCTGGCAGTTTTATCTCTCTAAAATGATCAGCATGGATATT
GAACAAGTTATTACCCTAAGTTTAGCTCTCCTTCTGGCTGTCAAGTACATCTTCTTTGAA
CAAACAGAGACAGAATCTACACTCTCATTAAAAAACCCTATCACATCTCCTGTAGTGACA
CAAAAGAAAGTCCCAGACAATTGTTGTAGACGTGAACCTATGCTGGTCAGAAATAACCAG
AAATGTGATTCAGTAGAGGAAGAGACAGGGATAAACCGAGAAAGAAAAGTTGAGGTTATA
AAACCCTTAGTGGCTGAAACAGATACCCCAAACAGAGCTACATTTGTGGTTGGTAACTCC
TCCTTACTCGATACTTCATCAGTACTGGTGACACAGGAACCTGAAATTGAACTTCCCAGG
GAACCTCGGCCTAATGAAGAATGTCTACAGATACTTGGGAATGCAGAGAAAGGTGCAAAA
TTCCTTAGTGATGCTGAGATCATCCAGTTAGTCAATGCTAAGCATATCCCAGCCTACAAG
TTGGAAACTCTGATGGAAACTCATGAGCGTGGTGTATCTATTCGCCGACAGTTACTTTCC
AAGAAGCTTTCAGAACCTTCTTCTCTCCAGTACCTACCTTACAGGGATTATAATTACTCC
TTGGTGATGGGAGCTTGTTGTGAGAATGTTATTGGATATATGCCCATCCCTGTTGGAGTG
GCAGGACCCCTTTGCTTAGATGAAAAAGAATTTCAGGTTCCAATGGCAACAACAGAAGGT
TGTCTTGTGGCCAGCACCAATAGAGGCTGCAGAGCAATAGGTCTTGGTGGAGGTGCCAGC
AGCCGAGTCCTTGCAGATGGGATGACTCGTGGCCCAGTTGTGCGTCTTCCACGTGCTTGT
GACTCTGCAGAAGTGAAAGCCTGGCTCGAAACATCTGAAGGGTTCGCAGTGATAAAGGAG
GCATTTGACAGCACTAGCAGATTTGCACGTCTACAGAAACTTCATACAAGTATAGCTGGA
CGCAACCTTTATATCCGTTTCCAGTCCAGGTCAGGGGATGCCATGGGGATGAACATGATT
TCAAAGGGTACAGAGAAAGCACTTTCAAAACTTCACGAGTATTTCCCTGAAATGCAGATT
CTAGCCGTTAGTGGTAACTATTGTACTGACAAGAAACCTGCTGCTATAAATTGGATAGAG
GGAAGAGGAAAATCTGTTGTTTGTGAAGCTGTCATTCCAGCCAAGGTTGTCAGAGAAGTA
TTAAAGACTACCACAGAGGCTATGATTGAGGTCAACATTAACAAGAATTTAGTGGGCTCT
GCCATGGCTGGGAGCATAGGAGGCTACAACGCCCATGCAGCAAACATTGTCACCGCCATC
TACATTGCCTGTGGACAGGATGCAGCACAGAATGTTGGTAGTTCAAACTGTATTACTTTA
ATGGAAGCAAGTGGTCCCACAAATGAAGATTTATATATCAGCTGCACCATGCCATCTATA
GAGATAGGAACGGTGGGTGGTGGGACCAACCTACTACCTCAGCAAGCCTGTTTGCAGATG
CTAGGTGTTCAAGGAGCATGCAAAGATAATCCTGGGGAAAATGCCCGGCAGCTTGCCCGA
ATTGTGTGTGGGACCGTAATGGCTGGGGAATTGTCACTTATGGCAGCATTGGCAGCAGGA
CATCTTGTCAAAAGTCACATGATTCACAACAGGTCGAAGATCAATTTACAAGACCTCCAA
GGAGCTTGCACCAAGAAGACAGCCTGA
Target 5 GenBank Gene ID
Target 5 GeneCard ID HMGCR Link Image
Target 5 GenAtlas ID HMGCR Link Image
Target 5 HGNC ID HGNC:5006 Link Image
Target 5 Chromosome Location 5
Target 5 Locus 5q13.3-q14
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  2. Istvan ES, Palnitkar M, Buchanan SK, Deisenhofer J: Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis. EMBO J. 2000 Mar 1;19(5):819-30. [PubMed Link Image]
  3. Luskey KL, Stevens B: Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. Conserved domains responsible for catalytic activity and sterol-regulated degradation. J Biol Chem. 1985 Aug 25;260(18):10271-7. [PubMed Link Image]
Target 5 Drug References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed Link Image]
  2. Davidson MH: Rosuvastatin: a highly efficacious statin for the treatment of dyslipidaemia. Expert Opin Investig Drugs. 2002 Mar;11(3):125-41. [PubMed Link Image]
  3. Jafari M, Ebrahimi R, Ahmadi-Kashani M, Balian H, Bashir M: Efficacy of alternate-day dosing versus daily dosing of atorvastatin. J Cardiovasc Pharmacol Ther. 2003 Jun;8(2):123-6. [PubMed Link Image]
  4. Baxter JD, Webb P, Grover G, Scanlan TS: Selective activation of thyroid hormone signaling pathways by GC-1: a new approach to controlling cholesterol and body weight. Trends Endocrinol Metab. 2004 May-Jun;15(4):154-7. [PubMed Link Image]
  5. Maejima T, Yamazaki H, Aoki T, Tamaki T, Sato F, Kitahara M, Saito Y: Effect of pitavastatin on apolipoprotein A-I production in HepG2 cell. Biochem Biophys Res Commun. 2004 Nov 12;324(2):835-9. [PubMed Link Image]
  6. Bosel J, Gandor F, Harms C, Synowitz M, Harms U, Djoufack PC, Megow D, Dirnagl U, Hortnagl H, Fink KB, Endres M: Neuroprotective effects of atorvastatin against glutamate-induced excitotoxicity in primary cortical neurones. J Neurochem. 2005 Mar;92(6):1386-98. [PubMed Link Image]
Drug Target 6 [top]
Target 6 ID 777
Target 6 Name Tumor necrosis factor
Target 6 Synonyms
  1. Cachectin
  2. TNF-a
  3. TNF-alpha
  4. Tumor necrosis factor ligand superfamily member 2
  5. Tumor necrosis factor precursor
Target 6 Gene Name TNF
Target 6 Protein Sequence >Tumor necrosis factor precursor
MSTESMIRDVELAEEALPKKTGGPQGSRRCLFLSLFSFLIVAGATTLFCLLHFGVIGPQR
EEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELR
DNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRE
TPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL
Target 6 Number of Residues 236
Target 6 Molecular Weight 25645
Target 6 Theoretical pI 6.92
Target 6 GO Classification
Function
signal transducer activity
receptor binding
cytokine activity
tumor necrosis factor receptor binding
Process
response to stimulus
response to biotic stimulus
defense response
immune response
Component
cell
membrane
Target 6 General Function Involved in tumor necrosis factor receptor binding
Target 6 Specific Function Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin 1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation
Target 6 Pathways Not Available
Target 6 Reactions Not Available
Target 6 Pfam Domain Function
Target 6 Signals
  • None
Target 6 Transmembrane Regions
  • 36-56
Target 6 Essentiality Non-Essential
Target 6 GenBank ID Protein 339741 Link Image
Target 6 UniProtKB/Swiss-Prot ID P01375 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name TNFA_HUMAN Link Image
Target 6 PDB ID 1A8M Link Image
Target 6 PDB File Show
Target 6 3D Structure
Target 6 Cellular Location
  • Cell membrane
  • single-pass type II membrane protein. Processed form:Secreted protein. Also exists as
Target 6 Gene Sequence >702 bp
ATGAGCACTGAAAGCATGATCCGGGACGTGGAGCTGGCCGAGGAGGCGCTCCCCAAGAAG
ACAGGGGGGCCCCAGGGCTCCAGGCGGTGCTTGTTCCTCAGCCTCTTCTCCTTCCTGATC
GTGGCAGGCGCCACCACGCTCTTCTGCCTGCTGCACTTTGGAGTGATCGGCCCCCAGAGG
GAAGAGTTCCCCAGGGACCTCTCTCTAATCAGCCCTCTGGCCCAGGCAGTCAGATCATCT
TCTCGAACCCCGAGTGACAAGCCTGTAGCCCATGTTGTAGCAAACCCTCAAGCTGAGGGG
CAGCTCCAGTGGCTGAACCGCCGGGCCAATGCCCTCCTGGCCAATGGCGTGGAGCTGAGA
GATAACCAGCTGGTGGTGCCATCAGAGGGCCTGTACCTCATCTACTCCCAGGTCCTCTTC
AAGGGCCAAGGCTGCCCCTCCACCCATGTGCTCCTCACCCACACCATCAGCCGCATCGCC
GTCTCCTACCAGACCAAGGTCAACCTCCTCTCTGCCATCAAGAGCCCCTGCCAGAGGGAG
ACCCCAGAGGGGGCTGAGGCCAAGCCCTGGTATGAGCCCATCTATCTGGGAGGGGTCTTC
CAGCTGGAGAAGGGTGACCGACTCAGCGCTGAGATCAATCGGCCCGACTATCTCGACTTT
GCCGAGTCTGGGCAGGTCTACTTTGGGATCATTGCCCTGTGA
Target 6 GenBank Gene ID
Target 6 GeneCard ID TNF Link Image
Target 6 GenAtlas ID TNF Link Image
Target 6 HGNC ID HGNC:11892 Link Image
Target 6 Chromosome Location 6
Target 6 Locus 6p21.3
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Neville MJ, Campbell RD: A new member of the Ig superfamily and a V-ATPase G subunit are among the predicted products of novel genes close to the TNF locus in the human MHC. J Immunol. 1999 Apr 15;162(8):4745-54. [PubMed Link Image]
  2. Watts AD, Hunt NH, Wanigasekara Y, Bloomfield G, Wallach D, Roufogalis BD, Chaudhri G: A casein kinase I motif present in the cytoplasmic domain of members of the tumour necrosis factor ligand family is implicated in 'reverse signalling'. EMBO J. 1999 Apr 15;18(8):2119-26. [PubMed Link Image]
  3. Stevenson FT, Bursten SL, Locksley RM, Lovett DH: Myristyl acylation of the tumor necrosis factor alpha precursor on specific lysine residues. J Exp Med. 1992 Oct 1;176(4):1053-62. [PubMed Link Image]
  4. Jones EY, Stuart DI, Walker NP: The structure of tumour necrosis factor--implications for biological function. J Cell Sci Suppl. 1990;13:11-8. [PubMed Link Image]
  5. Van Ostade X, Tavernier J, Prange T, Fiers W: Localization of the active site of human tumour necrosis factor (hTNF) by mutational analysis. EMBO J. 1991 Apr;10(4):827-36. [PubMed Link Image]
  6. Eck MJ, Sprang SR: The structure of tumor necrosis factor-alpha at 2.6 A resolution. Implications for receptor binding. J Biol Chem. 1989 Oct 15;264(29):17595-605. [PubMed Link Image]
  7. Jones EY, Stuart DI, Walker NP: Structure of tumour necrosis factor. Nature. 1989 Mar 16;338(6212):225-8. [PubMed Link Image]
  8. Nedwin GE, Naylor SL, Sakaguchi AY, Smith D, Jarrett-Nedwin J, Pennica D, Goeddel DV, Gray PW: Human lymphotoxin and tumor necrosis factor genes: structure, homology and chromosomal localization. Nucleic Acids Res. 1985 Sep 11;13(17):6361-73. [PubMed Link Image]
  9. Nedospasov SA, Shakhov AN, Turetskaya RL, Mett VA, Azizov MM, Georgiev GP, Korobko VG, Dobrynin VN, Filippov SA, Bystrov NS, et al.: Tandem arrangement of genes coding for tumor necrosis factor (TNF-alpha) and lymphotoxin (TNF-beta) in the human genome. Cold Spring Harb Symp Quant Biol. 1986;51 Pt 1:611-24. [PubMed Link Image]
  10. Wang AM, Creasey AA, Ladner MB, Lin LS, Strickler J, Van Arsdell JN, Yamamoto R, Mark DF: Molecular cloning of the complementary DNA for human tumor necrosis factor. Science. 1985 Apr 12;228(4696):149-54. [PubMed Link Image]
  11. 3883195 Shirai T, Yamaguchi H, Ito H, Todd CW, Wallace RB: Cloning and expression in Escherichia coli of the gene for human tumour necrosis factor. Nature. 1985 Feb 28-Mar 6;313(6005):803-6.
  12. 3932069 Marmenout A, Fransen L, Tavernier J, Van der Heyden J, Tizard R, Kawashima E, Shaw A, Johnson MJ, Semon D, Muller R, et al.: Molecular cloning and expression of human tumor necrosis factor and comparison with mouse tumor necrosis factor. Eur J Biochem. 1985 Nov 4;152(3):515-22.
  13. 6392892 Pennica D, Nedwin GE, Hayflick JS, Seeburg PH, Derynck R, Palladino MA, Kohr WJ, Aggarwal BB, Goeddel DV: Human tumour necrosis factor: precursor structure, expression and homology to lymphotoxin. Nature. 1984 Dec 20-1985 Jan 2;312(5996):724-9.
  14. 8499947 Iris FJ, Bougueleret L, Prieur S, Caterina D, Primas G, Perrot V, Jurka J, Rodriguez-Tome P, Claverie JM, Dausset J, et al.: Dense Alu clustering and a potential new member of the NF kappa B family within a 90 kilobase HLA class III segment. Nat Genet. 1993 Feb;3(2):137-45.
  15. 8597870 Pocsik E, Duda E, Wallach D: Phosphorylation of the 26 kDa TNF precursor in monocytic cells and in transfected HeLa cells. J Inflamm. 1995;45(3):152-60.
  16. 9034191 Moss ML, Jin SL, Milla ME, Bickett DM, Burkhart W, Carter HL, Chen WJ, Clay WC, Didsbury JR, Hassler D, Hoffman CR, Kost TA, Lambert MH, Leesnitzer MA, McCauley P, McGeehan G, Mitchell J, Moyer M, Pahel G, Rocque W, Overton LK, Schoenen F, Seaton T, Su JL, Becherer JD, et al.: Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature. 1997 Feb 20;385(6618):733-6.
  17. 9442056 Cha SS, Kim JS, Cho HS, Shin NK, Jeong W, Shin HC, Kim YJ, Hahn JH, Oh BH: High resolution crystal structure of a human tumor necrosis factor-alpha mutant with low systemic toxicity. J Biol Chem. 1998 Jan 23;273(4):2153-60.
  18. 9488135 Reed C, Fu ZQ, Wu J, Xue YN, Harrison RW, Chen MJ, Weber IT: Crystal structure of TNF-alpha mutant R31D with greater affinity for receptor R1 compared with R2. Protein Eng. 1997 Oct;10(10):1101-7.
Target 6 Drug References
  1. Yilmaz A, Reiss C, Tantawi O, Weng A, Stumpf C, Raaz D, Ludwig J, Berger T, Steinkasserer A, Daniel WG, Garlichs CD: HMG-CoA reductase inhibitors suppress maturation of human dendritic cells: new implications for atherosclerosis. Atherosclerosis. 2004 Jan;172(1):85-93. [PubMed Link Image]
  2. Grip O, Janciauskiene S, Lindgren S: Circulating monocytes and plasma inflammatory biomarkers in active Crohn's disease: elevated oxidized low-density lipoprotein and the anti-inflammatory effect of atorvastatin. Inflamm Bowel Dis. 2004 May;10(3):193-200. [PubMed Link Image]
  3. Tousoulis D, Antoniades C, Bosinakou E, Kotsopoulou M, Pitsavos C, Vlachopoulos C, Panagiotakos D, Stefanadis C: Effects of atorvastatin on reactive hyperemia and inflammatory process in patients with congestive heart failure. Atherosclerosis. 2005 Feb;178(2):359-63. [PubMed Link Image]
  4. Thomas PB, Albini T, Giri RK, See RF, Evans M, Rao NA: The effects of atorvastatin in experimental autoimmune uveitis. Br J Ophthalmol. 2005 Mar;89(3):275-9. [PubMed Link Image]
  5. Tousoulis D, Antoniades C, Katsi V, Bosinakou E, Kotsopoulou M, Tsioufis C, Stefanadis C: The impact of early administration of low-dose atorvastatin treatment on inflammatory process, in patients with unstable angina and low cholesterol level. Int J Cardiol. 2006 Apr 28;109(1):48-52. Epub 2005 Jul 6. [PubMed Link Image]
Drug Target 7 [top]
Target 7 ID 1017
Target 7 Name C-reactive protein
Target 7 Synonyms
  1. C-reactive protein precursor
Target 7 Gene Name CRP
Target 7 Protein Sequence >C-reactive protein precursor [Contains: C-reactive protein(1-205)]
MEKLLCFLVLTSLSHAFGQTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFYTE
LSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGSEILFEVPEVTVAPVHICTSWES
ASGIVEFWVDGKPRVRKSLKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVNMW
DFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFTKPQLWP
Target 7 Number of Residues 227
Target 7 Molecular Weight 25039
Target 7 Theoretical pI 5.32
Target 7 GO Classification Not Available
Target 7 General Function Involved in host defense response
Target 7 Specific Function Displays several functions associated with host defense:it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells
Target 7 Pathways Not Available
Target 7 Reactions Not Available
Target 7 Pfam Domain Function
Target 7 Signals
  • 1-18
Target 7 Transmembrane Regions
  • None
Target 7 Essentiality Non-Essential
Target 7 GenBank ID Protein 181066 Link Image
Target 7 UniProtKB/Swiss-Prot ID P02741 Link Image
Target 7 UniProtKB/Swiss-Prot Entry Name CRP_HUMAN Link Image
Target 7 PDB ID 1LJ7 Link Image
Target 7 PDB File Show
Target 7 3D Structure
Target 7 Cellular Location
  • Secreted protein
Target 7 Gene Sequence >675 bp
ATGGAGAAGCTGTTGTGTTTCTTGGTCTTGACCAGCCTCTCTCATGCTTTTGGCCAGACA
GACATGTCGAGGAAGGCTTTTGTGTTTCCCAAAGAGTCGGATACTTCCTATGTATCCCTC
AAAGCACCGTTAACGAAGCCTCTCAAAGCCTTCACTGTGTGCCTCCACTTCTACACGGAA
CTGTCCTCGACCCGTGGGTACAGTATTTTCTCGTATGCCACCAAGAGACAAGACAATGAG
ATTCTCATATTTTGGTCTAAGGATATAGGATACAGTTTTACAGTGGGTGGGTCTGAAATA
TTATTCGAGGTTCCTGAAGTCACAGTAGCTCCAGTACACATTTGTACAAGCTGGGAGTCC
GCCTCAGGGATCGTGGAGTTCTGGGTAGATGGGAAGCCCAGGGTGAGGAAGAGTCTGAAG
AAGGGATACACTGTGGGGGCAGAAGCAAGCATCATCTTGGGGCAGGAGCAGGATTCCTTC
GGTGGGAACTTTGAAGGAAGCCAGTCCCTAGTGGGAGACATTGGAAATGTGAACATGTGG
GACTTTGTGCTGTCACCAGATGAGATTAACACCATCTATCTTGGCGGGCCCTTCAGTCCT
AATGTCCTGAACTGGCGGGCACTGAAGTATGAAGTGCAAGGCGAAGTGTTCACCAAACCC
CAGCTGTGGCCCTGA
Target 7 GenBank Gene ID
Target 7 GeneCard ID CRP Link Image
Target 7 GenAtlas ID CRP Link Image
Target 7 HGNC ID HGNC:2367 Link Image
Target 7 Chromosome Location 1
Target 7 Locus 1q21-q23
Target 7 SNPs SNPJam Report Link Image
Target 7 General References
  1. Thompson D, Pepys MB, Wood SP: The physiological structure of human C-reactive protein and its complex with phosphocholine. Structure. 1999 Feb 15;7(2):169-77. [PubMed Link Image]
  2. Lei KJ, Liu T, Zon G, Soravia E, Liu TY, Goldman ND: Genomic DNA sequence for human C-reactive protein. J Biol Chem. 1985 Oct 25;260(24):13377-83. [PubMed Link Image]
  3. Woo P, Korenberg JR, Whitehead AS: Characterization of genomic and complementary DNA sequence of human C-reactive protein, and comparison with the complementary DNA sequence of serum amyloid P component. J Biol Chem. 1985 Oct 25;260(24):13384-8. [PubMed Link Image]
  4. Osmand AP, Gerwurz H, Friedenson B: Partial amino-acid sequences of human and rabbit C-reactive proteins: homology with immunoglobulins and histocompatibility antigens. Proc Natl Acad Sci U S A. 1977 Mar;74(3):1214-8. [PubMed Link Image]
  5. Tucci A, Goldberger G, Whitehead AS, Kay RM, Woods DE, Colten HR: Biosynthesis and postsynthetic processing of human C-reactive protein. J Immunol. 1983 Nov;131(5):2416-9. [PubMed Link Image]
  6. Whitehead AS, Bruns GA, Markham AF, Colten HR, Woods DE: Isolation of human C-reactive protein complementary DNA and localization of the gene to chromosome 1. Science. 1983 Jul 1;221(4605):69-71. [PubMed Link Image]
  7. Oliveira EB, Gotschlich C, Liu TY: Primary structure of human C-reactive protein. J Biol Chem. 1979 Jan 25;254(2):489-502. [PubMed Link Image]
  8. Srinivasan N, White HE, Emsley J, Wood SP, Pepys MB, Blundell TL: Comparative analyses of pentraxins: implications for protomer assembly and ligand binding. Structure. 1994 Nov 15;2(11):1017-27. [PubMed Link Image]
  9. Shrive AK, Cheetham GM, Holden D, Myles DA, Turnell WG, Volanakis JE, Pepys MB, Bloomer AC, Greenhough TJ: Three dimensional structure of human C-reactive protein. Nat Struct Biol. 1996 Apr;3(4):346-54. [PubMed Link Image]
Target 7 Drug References
  1. van den Akker JM, Bredie SJ, Diepenveen SH, van Tits LJ, Stalenhoef AF, van Leusen R: Atorvastatin and simvastatin in patients on hemodialysis: effects on lipoproteins, C-reactive protein and in vivo oxidized LDL. J Nephrol. 2003 Mar-Apr;16(2):238-44. [PubMed Link Image]
  2. Karaca I, Ilkay E, Akbulut M, Yavuzkir M, Pekdemir M, Akbulut H, Arslan N: Atorvastatin affects C-reactive protein levels in patients with coronary artery disease. Curr Med Res Opin. 2003;19(3):187-91. [PubMed Link Image]
  3. Abud-Mendoza C, de la Fuente H, Cuevas-Orta E, Baranda L, Cruz-Rizo J, Gonzalez-Amaro R: Therapy with statins in patients with refractory rheumatic diseases: a preliminary study. Lupus. 2003;12(8):607-11. [PubMed Link Image]
  4. Nissen SE, Tuzcu EM, Schoenhagen P, Brown BG, Ganz P, Vogel RA, Crowe T, Howard G, Cooper CJ, Brodie B, Grines CL, DeMaria AN: Effect of intensive compared with moderate lipid-lowering therapy on progression of coronary atherosclerosis: a randomized controlled trial. JAMA. 2004 Mar 3;291(9):1071-80. [PubMed Link Image]
  5. Macin SM, Perna ER, Farias EF, Franciosi V, Cialzeta JR, Brizuela M, Medina F, Tajer C, Doval H, Badaracco R: Atorvastatin has an important acute anti-inflammatory effect in patients with acute coronary syndrome: results of a randomized, double-blind, placebo-controlled study. Am Heart J. 2005 Mar;149(3):451-7. [PubMed Link Image]
Drug Target 8 [top]
Target 8 ID 1198
Target 8 Name Serum paraoxonase/arylesterase 1
Target 8 Synonyms
  1. A-esterase 1
  2. Aromatic esterase 1
  3. EC 3.1.1.2
  4. EC 3.1.8.1
  5. K-45
  6. PON 1
  7. Serum aryldialkylphosphatase 1
Target 8 Gene Name PON1
Target 8 Protein Sequence >Serum paraoxonase/arylesterase 1
MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDMEILPN
GLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTF
TDEDNAMYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYG
TNDHYFLDPYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAEL
LAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPP
ASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCEL
Target 8 Number of Residues 360
Target 8 Molecular Weight 39750
Target 8 Theoretical pI 4.89
Target 8 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
carboxylic ester hydrolase activity
arylesterase activity
Process
Not Available
Component
extracellular region
Target 8 General Function Involved in arylesterase activity
Target 8 Specific Function Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and a number of aromatic carboxylic acid esters. May mediate an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation
Target 8 Pathways
Name SMPDB Link KEGG Link
gamma-Hexachlorocyclohexane degradation map00361 Link Image
Target 8 Reactions
  • a phenyl acetate + H2O = a phenol + acetate
Target 8 Pfam Domain Function
Target 8 Signals
  • 1-
Target 8 Transmembrane Regions
  • None
Target 8 Essentiality Non-Essential
Target 8 GenBank ID Protein 190192 Link Image
Target 8 UniProtKB/Swiss-Prot ID P27169 Link Image
Target 8 UniProtKB/Swiss-Prot Entry Name PON1_HUMAN Link Image
Target 8 PDB ID Not Available
Target 8 Cellular Location
  • Secreted protein
  • extracellular space
Target 8 Gene Sequence >1068 bp
ATGGCGAAGCTGATTGCGCTCACCCTCTTGGGGATGGGACTGGCACTCTTCAGGAACCAC
CAGTCTTCTTACCAAACACGACTTAATGCTCTCCGAGAGGTACAACCCGTAGAACTTCCT
AACTGTAATTTAGTTAAAGGAATCGAAACTGGCTCTGAAGACATGGAGATACTGCCTAAT
GGACTGGCTTTCATTAGCTCTGGATTAAAGTATCCTGGAATAAAGAGCTTCAACCCCAAC
AGTCCTGGAAAAATACTTCTGATGGACCTGAATGAAGAAGATCCAACAGTGTTGGAATTG
GGGATCACTGGAAGTAAATTTGATGTATCTTCATTTAACCCTCATGGGATTAGCACATTC
ACAGATGAAGATAATGCCATGTACCTCCTGGTGGTGAACCATCCAGATGCCAAGTCCACA
GTGGAGTTGTTTAAATTTCAAGAAGAAGAAAAATCGCTTTTGCATCTAAAAACCATCAGA
CATAAACTTCTGCCTAATTTGAATGATATTGTTGCTGTGGGACCTGAGCACTTTTATGGC
ACAAATGATCACTATTTTCTTGACCCCTACTTACAATCCTGGGAGATGTATTTGGGTTTA
GCGTGGTCGTATGTTGTCTACTATAGTCCAAGTGAAGTTCGAGTGGTGGCAGAAGGATTT
GATTTTGCTAATGGAATCAACATTTCACCCGATGGCAAGTATGTCTATATAGCTGAGTTG
CTGGCTCATAAGATTCATGTGTATGAAAAGCATGCTAATTGGACTTTAACTCCATTGAAG
TCCCTTGACTTTAATACCCTCGTGGATAACATATCTGTGGATCCTGAGACAGGAGACCTT
TGGGTTGGATGCCATCCCAATGGCATGAAAATCTTCTTCTATGACTCAGAGAATCCTCCT
GCATCAGAGGTGCTTCGAATCCAGAACATTCTAACAGAAGAACCTAAAGTGACACAGGTT
TATGCAGAAAATGGCACAGTGTTGCAAGGCAGTACAGTTGCCTCTGTGTACAAAGGGAAA
CTGCTGATTGGCACAGTGTTTCACAAAGCTCTTTACTGTGAGCTCTAA
Target 8 GenBank Gene ID
Target 8 GeneCard ID PON1 Link Image
Target 8 GenAtlas ID PON1 Link Image
Target 8 HGNC ID HGNC:9204 Link Image
Target 8 Chromosome Location 7
Target 8 Locus 7q21.3
Target 8 SNPs SNPJam Report Link Image
Target 8 General References
  1. Marchesani M, Hakkarainen A, Tuomainen TP, Kaikkonen J, Pukkala E, Uimari P, Seppala E, Matikainen M, Kallioniemi OP, Schleutker J, Lehtimaki T, Salonen JT: New paraoxonase 1 polymorphism I102V and the risk of prostate cancer in Finnish men. J Natl Cancer Inst. 2003 Jun 4;95(11):812-8. [PubMed Link Image]
  2. 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]
  3. Hassett C, Richter RJ, Humbert R, Chapline C, Crabb JW, Omiecinski CJ, Furlong CE: Characterization of cDNA clones encoding rabbit and human serum paraoxonase: the mature protein retains its signal sequence. Biochemistry. 1991 Oct 22;30(42):10141-9. [PubMed Link Image]
  4. Gan KN, Smolen A, Eckerson HW, La Du BN: Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities. Drug Metab Dispos. 1991 Jan-Feb;19(1):100-6. [PubMed Link Image]
  5. Furlong CE, Richter RJ, Chapline C, Crabb JW: Purification of rabbit and human serum paraoxonase. Biochemistry. 1991 Oct 22;30(42):10133-40. [PubMed Link Image]
  6. Sorenson RC, Primo-Parmo SL, Kuo CL, Adkins S, Lockridge O, La Du BN: Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesterase. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7187-91. [PubMed Link Image]
  7. Adkins S, Gan KN, Mody M, La Du BN: Molecular basis for the polymorphic forms of human serum paraoxonase/arylesterase: glutamine or arginine at position 191, for the respective A or B allozymes. Am J Hum Genet. 1993 Mar;52(3):598-608. [PubMed Link Image]
  8. Humbert R, Adler DA, Disteche CM, Hassett C, Omiecinski CJ, Furlong CE: The molecular basis of the human serum paraoxonase activity polymorphism. Nat Genet. 1993 Jan;3(1):73-6. [PubMed Link Image]
  9. Blatter MC, James RW, Messmer S, Barja F, Pometta D: Identification of a distinct human high-density lipoprotein subspecies defined by a lipoprotein-associated protein, K-45. Identity of K-45 with paraoxonase. Eur J Biochem. 1993 Feb 1;211(3):871-9. [PubMed Link Image]
  10. La Du BN, Adkins S, Kuo CL, Lipsig D: Studies on human serum paraoxonase/arylesterase. Chem Biol Interact. 1993 Jun;87(1-3):25-34. [PubMed Link Image]
  11. 8393745 Furlong CE, Costa LG, Hassett C, Richter RJ, Sundstrom JA, Adler DA, Disteche CM, Omiecinski CJ, Chapline C, Crabb JW, et al.: Human and rabbit paraoxonases: purification, cloning, sequencing, mapping and role of polymorphism in organophosphate detoxification. Chem Biol Interact. 1993 Jun;87(1-3):35-48.
  12. 8812495 Clendenning JB, Humbert R, Green ED, Wood C, Traver D, Furlong CE: Structural organization of the human PON1 gene. Genomics. 1996 Aug 1;35(3):586-9.
Target 8 Drug References
  1. Kural BV, Orem C, Uydu HA, Alver A, Orem A: The effects of lipid-lowering therapy on paraoxonase activities and their relationships with the oxidant-antioxidant system in patients with dyslipidemia. Coron Artery Dis. 2004 Aug;15(5):277-83. [PubMed Link Image]
  2. Harangi M, Seres I, Varga Z, Emri G, Szilvassy Z, Paragh G, Remenyik E: Atorvastatin effect on high-density lipoprotein-associated paraoxonase activity and oxidative DNA damage. Eur J Clin Pharmacol. 2004 Dec;60(10):685-91. Epub 2004 Oct 14. [PubMed Link Image]
  3. Ota K, Suehiro T, Arii K, Ikeda Y, Kumon Y, Osaki F, Hashimoto K: Effect of pitavastatin on transactivation of human serum paraoxonase 1 gene. Metabolism. 2005 Feb;54(2):142-50. [PubMed Link Image]
  4. Sardo MA, Campo S, Bonaiuto M, Bonaiuto A, Saitta C, Trimarchi G, Castaldo M, Bitto A, Cinquegrani M, Saitta A: Antioxidant effect of atorvastatin is independent of PON1 gene T(-107)C, Q192R and L55M polymorphisms in hypercholesterolaemic patients. Curr Med Res Opin. 2005 May;21(5):777-84. [PubMed Link Image]
  5. Bolayirli IM, Aslan M, Balci H, Altug T, Hacibekiroglu M, Seven A: Effects of atorvastatin therapy on hypercholesterolemic rabbits with respect to oxidative stress, nitric oxide pathway and homocysteine. Life Sci. 2007 Jun 20;81(2):121-7. Epub 2007 May 6. [PubMed Link Image]
Drug Target 9 [top]
Target 9 ID 1337
Target 9 Name Cytochrome P450 3A3
Target 9 Synonyms
  1. CYPIIIA3
  2. EC 1.14.14.1
  3. HLp
Target 9 Gene Name CYP3A3
Target 9 Protein Sequence >Cytochrome P450 3A3
MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMF
DMECHKKYGKVWGFYDGQQPVLAITDPDMIKLVLVKECYSVFTNREPFGPVGFMKSAISI
AEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRRERETGKPVTLKDVFGAYS
MDVITSSSFGVNVDSLNNPQDPLVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICV
FPREVTNFLRKAVKRMKESRLEDTQKHRVDFLQLMIDSHKNSKETESHKALSDLELVAQS
IIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMV
VNETLRLFPIAMRLERVCKKDVEINGMFIPKGWVVMIPSYALHRDPKYWTEPEKFLPERF
SKKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSL
GGLLQPEKPVVLKVESRDGTVSGA
Target 9 Number of Residues 512
Target 9 Molecular Weight 57560
Target 9 Theoretical pI 8.25
Target 9 GO Classification
Function
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
tetrapyrrole binding
heme binding
binding
ion binding
cation binding
transition metal ion binding
iron ion binding
catalytic activity
oxidoreductase activity
monooxygenase activity
Process
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
Component
Not Available
Target 9 General Function Secondary metabolites biosynthesis, transport and catabolism
Target 9 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Target 9 Pathways
Name SMPDB Link KEGG Link
Fatty acid metabolism SMP00051 Link Image map00071 Link Image
Target 9 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Target 9 Pfam Domain Function
Target 9 Signals
  • None
Target 9 Transmembrane Regions
  • None
Target 9 Essentiality Non-Essential
Target 9 GenBank ID Protein 219963 Link Image
Target 9 UniProtKB/Swiss-Prot ID P05184 Link Image
Target 9 UniProtKB/Swiss-Prot Entry Name CP3A3_HUMAN Link Image
Target 9 PDB ID 1TQN Link Image
Target 9 PDB File Show
Target 9 3D Structure
Target 9 Cellular Location
  • Endoplasmic reticulum
  • endoplasmic reticulum membrane
  • peripheral membrane protein
Target 9 Gene Sequence >1515 bp
ATGGCTCTCATCCCAGACTTGGCCATGGAAACCTGGCTTCTCCTGGCTGTCAGCCTGGTG
CTCCTCTATCTATATGGAACCCATTCACATGGACTTTTTAAGAAGCTTGGAATTCCAGGG
CCCACACCTCTGCCTTTTTTGGGAAATATTTTGTCCTACCATAAGGGCTTTTGTATGTTT
GACATGGAATGTCATAAAAAGTATGGAAAAGTGTGGGGCTTTTATGATGGTCAACAGCCT
GTGCTGGCTATCACAGATCCTGACATGATCAAACTAGTGCTAGTGAAAGAATGTTATTCT
GTCTTCACAAACCGCGAGCCTTTTGGTCCAGTGGGATTTATGAAAAGTGCCATCTCTATA
GCTGAGGATGAAGAATGGAAGAGATTACGATCATTGCTGTCTCCAACCTTCACCAGTGGA
AAACTCAAGGAGATGGTCCCTATCATTGCCCAGTATGGAGATGTGTTGGTGAGAAATCTG
AGGCGGGAACGAGAGACAGGCAAGCCTGTCACCTTGAAAGACGTCTTTGGGGCCTACAGC
ATGGATGTGATCACTAGCTCATCATTTGGAGTGAACGTCGACTCTCTCAACAATCCACAG
GACCCCCTTGTGGAAAACACCAAGAAGCTTTTAAGATTTGATTTTTTGGATCCATTCTTT
CTCTCAATAACAGTCTTTCCATTCCTCATCCCAATTCTTGAAGTATTAAATATCTGTGTG
TTTCCAAGAGAAGTTACAAATTTTTTAAGAAAAGCTGTAAAAAGGATGAAAGAAAGTCGC
CTCGAAGATACACAAAAGCACCGAGTGGATTTCCTTCAGCTGATGATTGACTCTCATAAG
AATTCAAAAGAAACTGAGTCCCACAAAGCTCTGTCCGATCTGGAGCTCGTGGCCCAATCA
ATTATCTTTATTTTTGCTGGCTATGAAACCACGAGCAGTGTTCTCTCCTTCATTATGTAT
GAACTGGCCACTCACCCTGATGTCCAGCAGAAACTGCAGGAGGAAATTGATGCAGTTTTA
CCCAATAAGGCACCACCCACCTATGATACTGTGCTACAGATGGAGTATCTTGACATGGTG
GTGAATGAAACGCTCAGATTATTCCCAATTGCTATGAGACTTGAGAGGGTCTGCAAAAAA
GATGTTGAGATCAATGGGATGTTCATTCCCAAAGGGTGGGTGGTGATGATTCCAAGCTAT
GCTCTTCACCGTGACCCAAAGTACTGGACAGAGCCTGAGAAGTTCCTCCCTGAAAGATTC
AGCAAGAAGAACAAGGACAACATAGATCCTTACATATACACACCCTTTGGAAGTGGACCC
AGAAACTGCATTGGCATGAGGTTTGCTCTCATGAACATGAAACTTGCTCTAATCAGAGTC
CTTCAGAACTTCTCCTTCAAACCTTGTAAAGAAACACAGATCCCCCTGAAATTAAGCTTA
GGAGGACTTCTTCAACCAGAAAAACCCGTTGTTCTAAAGGTTGAGTCAAGGGATGGCACC
GTAAGTGGAGCCTGA
Target 9 GenBank Gene ID
Target 9 GeneCard ID CYP3A3 Link Image
Target 9 GenAtlas ID CYP3A3 Link Image
Target 9 HGNC ID HGNC:2636 Link Image
Target 9 Chromosome Location 7
Target 9 Locus 7q21.1
Target 9 SNPs SNPJam Report Link Image
Target 9 General References
  1. Molowa DT, Schuetz EG, Wrighton SA, Watkins PB, Kremers P, Mendez-Picon G, Parker GA, Guzelian PS: Complete cDNA sequence of a cytochrome P-450 inducible by glucocorticoids in human liver. Proc Natl Acad Sci U S A. 1986 Jul;83(14):5311-5. [PubMed Link Image]
  2. Watkins PB, Wrighton SA, Maurel P, Schuetz EG, Mendez-Picon G, Parker GA, Guzelian PS: Identification of an inducible form of cytochrome P-450 in human liver. Proc Natl Acad Sci U S A. 1985 Sep;82(18):6310-4. [PubMed Link Image]
Target 9 Drug References
  1. Becquemont L: [Drug interactions with antilipemics] Therapie. 2003 Jan-Feb;58(1):85-90. [PubMed Link Image]
  2. Mc Donnell CG, Harte S, O'Driscoll J, O'Loughlin C, Van Pelt FN, Shorten GD: The effects of concurrent atorvastatin therapy on the pharmacokinetics of intravenous midazolam. Anaesthesia. 2003 Sep;58(9):899-904. [PubMed Link Image]
  3. Saw J, Steinhubl SR, Berger PB, Kereiakes DJ, Serebruany VL, Brennan D, Topol EJ: Lack of adverse clopidogrel-atorvastatin clinical interaction from secondary analysis of a randomized, placebo-controlled clopidogrel trial. Circulation. 2003 Aug 26;108(8):921-4. Epub 2003 Aug 18. [PubMed Link Image]
  4. Neubauer H, Gunesdogan B, Hanefeld C, Spiecker M, Mugge A: Lipophilic statins interfere with the inhibitory effects of clopidogrel on platelet function--a flow cytometry study. Eur Heart J. 2003 Oct;24(19):1744-9. [PubMed Link Image]
  5. Lennernas H: Clinical pharmacokinetics of atorvastatin. Clin Pharmacokinet. 2003;42(13):1141-60. [PubMed Link Image]
Drug Target 10 [top]
Target 10 ID 1419
Target 10 Name Apolipoprotein B-100
Target 10 Synonyms
  1. Apo B-100
  2. Apolipoprotein B-100 precursor
Target 10 Gene Name APOB
Target 10 Protein Sequence >Apolipoprotein B-100 precursor
MDPPRPALLALLALPALLLLLLAGARAEEEMLENVSLVCPKDATRFKHLRKYTYNYEAES
SSGVPGTADSRSATRINCKVELEVPQLCSFILKTSQCTLKEVYGFNPEGKALLKKTKNSE
EFAAAMSRYELKLAIPEGKQVFLYPEKDEPTYILNIKRGIISALLVPPETEEAKQVLFLD
TVYGNCSTHFTVKTRKGNVATEISTERDLGQCDRFKPIRTGISPLALIKGMTRPLSTLIS
SSQSCQYTLDAKRKHVAEAICKEQHLFLPFSYNNKYGMVAQVTQTLKLEDTPKINSRFFG
EGTKKMGLAFESTKSTSPPKQAEAVLKTLQELKKLTISEQNIQRANLFNKLVTELRGLSD
EAVTSLLPQLIEVSSPITLQALVQCGQPQCSTHILQWLKRVHANPLLIDVVTYLVALIPE
PSAQQLREIFNMARDQRSRATLYALSHAVNNYHKTNPTGTQELLDIANYLMEQIQDDCTG
DEDYTYLILRVIGNMGQTMEQLTPELKSSILKCVQSTKPSLMIQKAAIQALRKMEPKDKD
QEVLLQTFLDDASPGDKRLAAYLMLMRSPSQADINKIVQILPWEQNEQVKNFVASHIANI
LNSEELDIQDLKKLVKEALKESQLPTVMDFRKFSRNYQLYKSVSLPSLDPASAKIEGNLI
FDPNNYLPKESMLKTTLTAFGFASADLIEIGLEGKGFEPTLEALFGKQGFFPDSVNKALY
WVNGQVPDGVSKVLVDHFGYTKDDKHEQDMVNGIMLSVEKLIKDLKSKEVPEARAYLRIL
GEELGFASLHDLQLLGKLLLMGARTLQGIPQMIGEVIRKGSKNDFFLHYIFMENAFELPT
GAGLQLQISSSGVIAPGAKAGVKLEVANMQAELVAKPSVSVEFVTNMGIIIPDFARSGVQ
MNTNFFHESGLEAHVALKAGKLKFIIPSPKRPVKLLSGGNTLHLVSTTKTEVIPPLIENR
QSWSVCKQVFPGLNYCTSGAYSNASSTDSASYYPLTGDTRLELELRPTGEIEQYSVSATY
ELQREDRALVDTLKFVTQAEGAKQTEATMTFKYNRQSMTLSSEVQIPDFDVDLGTILRVN
DESTEGKTSYRLTLDIQNKKITEVALMGHLSCDTKEERKIKGVISIPRLQAEARSEILAH
WSPAKLLLQMDSSATAYGSTVSKRVAWHYDEEKIEFEWNTGTNVDTKKMTSNFPVDLSDY
PKSLHMYANRLLDHRVPETDMTFRHVGSKLIVAMSSWLQKASGSLPYTQTLQDHLNSLKE
FNLQNMGLPDFHIPENLFLKSDGRVKYTLNKNSLKIEIPLPFGGKSSRDLKMLETVRTPA
LHFKSVGFHLPSREFQVPTFTIPKLYQLQVPLLGVLDLSTNVYSNLYNWSASYSGGNTST
DHFSLRARYHMKADSVVDLLSYNVQGSGETTYDHKNTFTLSCDGSLRHKFLDSNIKFSHV
EKLGNNPVSKGLLIFDASSSWGPQMSASVHLDSKKKQHLFVKEVKIDGQFRVSSFYAKGT
YGLSCQRDPNTGRLNGESNLRFNSSYLQGTNQITGRYEDGTLSLTSTSDLQSGIIKNTAS
LKYENYELTLKSDTNGKYKNFATSNKMDMTFSKQNALLRSEYQADYESLRFFSLLSGSLN
SHGLELNADILGTDKINSGAHKATLRIGQDGISTSATTNLKCSLLVLENELNAELGLSGA
SMKLTTNGRFREHNAKFSLDGKAALTELSLGSAYQAMILGVDSKNIFNFKVSQEGLKLSN
DMMGSYAEMKFDHTNSLNIAGLSLDFSSKLDNIYSSDKFYKQTVNLQLQPYSLVTTLNSD
LKYNALDLTNNGKLRLEPLKLHVAGNLKGAYQNNEIKHIYAISSAALSASYKADTVAKVQ
GVEFSHRLNTDIAGLASAIDMSTNYNSDSLHFSNVFRSVMAPFTMTIDAHTNGNGKLALW
GEHTGQLYSKFLLKAEPLAFTFSHDYKGSTSHHLVSRKSISAALEHKVSALLTPAEQTGT
WKLKTQFNNNEYSQDLDAYNTKDKIGVELTGRTLADLTLLDSPIKVPLLLSEPINIIDAL
EMRDAVEKPQEFTIVAFVKYDKNQDVHSINLPFFETLQEYFERNRQTIIVVVENVQRNLK
HINIDQFVRKYRAALGKLPQQANDYLNSFNWERQVSHAKEKLTALTKKYRITENDIQIAL
DDAKINFNEKLSQLQTYMIQFDQYIKDSYDLHDLKIAIANIIDEIIEKLKSLDEHYHIRV
NLVKTIHDLHLFIENIDFNKSGSSTASWIQNVDTKYQIRIQIQEKLQQLKRHIQNIDIQH
LAGKLKQHIEAIDVRVLLDQLGTTISFERINDVLEHVKHFVINLIGDFEVAEKINAFRAK
VHELIERYEVDQQIQVLMDKLVELTHQYKLKETIQKLSNVLQQVKIKDYFEKLVGFIDDA
VKKLNELSFKTFIEDVNKFLDMLIKKLKSFDYHQFVDETNDKIREVTQRLNGEIQALELP
QKAEALKLFLEETKATVAVYLESLQDTKITLIINWLQEALSSASLAHMKAKFRETLEDTR
DRMYQMDIQQELQRYLSLVGQVYSTLVTYISDWWTLAAKNLTDFAEQYSIQDWAKRMKAL
VEQGFTVPEIKTILGTMPAFEVSLQALQKATFQTPDFIVPLTDLRIPSVQINFKDLKNIK
IPSRFSTPEFTILNTFHIPSFTIDFVEMKVKIIRTIDQMQNSELQWPVPDIYLRDLKVED
IPLARITLPDFRLPEIAIPEFIIPTLNLNDFQVPDLHIPEFQLPHISHTIEVPTFGKLYS
ILKIQSPLFTLDANADIGNGTTSANEAGIAASITAKGESKLEVLNFDFQANAQLSNPKIN
PLALKESVKFSSKYLRTEHGSEMLFFGNAIEGKSNTVASLHTEKNTLELSNGVIVKINNQ
LTLDSNTKYFHKLNIPKLDFSSQADLRNEIKTLLKAGHIAWTSSGKGSWKWACPRFSDEG
THESQISFTIEGPLTSFGLSNKINSKHLRVNQNLVYESGSLNFSKLEIQSQVDSQHVGHS
VLTAKGMALFGEGKAEFTGRHDAHLNGKVIGTLKNSLFFSAQPFEITASTNNEGNLKVRF
PLRLTGKIDFLNNYALFLSPSAQQASWQVSARFNQYKYNQNFSAGNNENIMEAHVGINGE
ANLDFLNIPLTIPEMRLPYTIITTPPLKDFSLWEKTGLKEFLKTTKQSFDLSVKAQYKKN
KHRHSITNPLAVLCEFISQSIKSFDRHFEKNRNNALDFVTKSYNETKIKFDKYKAEKSHD
ELPRTFQIPGYTVPVVNVEVSPFTIEMSAFGYVFPKAVSMPSFSILGSDVRVPSYTLILP
SLELPVLHVPRNLKLSLPHFKELCTISHIFIPAMGNITYDFSFKSSVITLNTNAELFNQS
DIVAHLLSSSSSVIDALQYKLEGTTRLTRKRGLKLATALSLSNKFVEGSHNSTVSLTTKN
MEVSVAKTTKAEIPILRMNFKQELNGNTKSKPTVSSSMEFKYDFNSSMLYSTAKGAVDHK
LSLESLTSYFSIESSTKGDVKGSVLSREYSGTIASEANTYLNSKSTRSSVKLQGTSKIDD
IWNLEVKENFAGEATLQRIYSLWEHSTKNHLQLEGLFFTNGEHTSKATLELSPWQMSALV
QVHASQPSSFHDFPDLGQEVALNANTKNQKIRWKNEVRIHSGSFQSQVELSNDQEKAHLD
IAGSLEGHLRFLKNIILPVYDKSLWDFLKLDVTTSIGRRQHLRVSTAFVYTKNPNGYSFS
IPVKVLADKFITPGLKLNDLNSVLVMPTFHVPFTDLQVPSCKLDFREIQIYKKLRTSSFA
LNLPTLPEVKFPEVDVLTKYSQPEDSLIPFFEITVPESQLTVSQFTLPKSVSDGIAALDL
NAVANKIADFELPTIIVPEQTIEIPSIKFSVPAGIVIPSFQALTARFEVDSPVYNATWSA
SLKNKADYVETVLDSTCSSTVQFLEYELNVLGTHKIEDGTLASKTKGTLAHRDFSAEYEE
DGKFEGLQEWEGKAHLNIKSPAFTDLHLRYQKDKKGISTSAASPAVGTVGMDMDEDDDFS
KWNFYYSPQSSPDKKLTIFKTELRVRESDEETQIKVNWEEEAASGLLTSLKDNVPKATGV
LYDYVNKYHWEHTGLTLREVSSKLRRNLQNNAEWVYQGAIRQIDDIDVRFQKAASGTTGT
YQEWKDKAQNLYQELLTQEGQASFQGLKDNVFDGLVRVTQKFHMKVKHLIDSLIDFLNFP
RFQFPGKPGIYTREELCTMFIREVGTVLSQVYSKVHNGSEILFSYFQDLVITLPFELRKH
KLIDVISMYRELLKDLSKEAQEVFKAIQSLKTTEVLRNLQDLLQFIFQLIEDNIKQLKEM
KFTYLINYIQDEINTIFNDYIPYVFKLLKENLCLNLHKFNEFIQNELQEASQELQQIHQY
IMALREEYFDPSIVGWTVKYYELEEKIVSLIKNLLVALKDFHSEYIVSASNFTSQLSSQV
EQFLHRNIQEYLSILTDPDGKGKEKIAELSATAQEIIKSQAIATKKIISDYHQQFRYKLQ
DFSDQLSDYYEKFIAESKRLIDLSIQNYHTFLIYITELLKKLQSTTVMNPYMKLAPGELT
IIL
Target 10 Number of Residues 4639
Target 10 Molecular Weight 515568
Target 10 Theoretical pI 7.06
Target 10 GO Classification
Function
transporter activity
lipid transporter activity
Process
physiological process
cellular physiological process
transport
lipid transport
Component
Not Available
Target 10 General Function Replication, recombination and repair
Target 10 Specific Function Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor
Target 10 Pathways Not Available
Target 10 Reactions Not Available
Target 10 Pfam Domain Function
Target 10 Signals
  • 1-27
Target 10 Transmembrane Regions
  • None
Target 10 Essentiality Non-Essential
Target 10 GenBank ID Protein 34331 Link Image
Target 10 UniProtKB/Swiss-Prot ID P04114 Link Image
Target 10 UniProtKB/Swiss-Prot Entry Name APOB_HUMAN Link Image
Target 10 PDB ID Not Available
Target 10 Cellular Location
  • Secreted protein
Target 10 Gene Sequence >13692 bp
ATGGACCCGCCGAGGCCCGCGCTGCTGGCGCTGCTGGCGCTGCCTGCGCTGCTGCTGCTG
CTGCTGGCGGGCGCCAGGGCCGAAGAGGAAATGCTGGAAAATGTCAGCCTGGTCTGTCCA
AAAGATGCGACCCGATTCAAGCACCTCCGGAAGTACACATACAACTATGAGGCTGAGAGT
TCCAGTGGAGTCCCTGGGACTGCTGATTCAAGAAGTGCCACCAGGATCAACTGCAAGGTT
GAGCTGGAGGTTCCCCAGCTCTGCAGCTTCATCCTGAAGACCAGCCAGTGCACCCTGAAA
GAGGTGTATGGCTTCAACCCTGAGGGCAAAGCCTTGCTGAAGAAAACCAAGAACTCTGAG
GAGTTTGCTGCAGCCATGTCCAGGTATGAGCTCAAGCTGGCCATTCCAGAAGGGAAGCAG
GTTTTCCTTTACCCGGAGAAAGATGAACCTACTTACATCCTGAACATCAAGAGGGGCATC
ATTTCTGCCCTCCTGGTTCCCCCAGAGACAGAAGAAGCCAAGCAAGTGTTGTTTCTGGAT
ACCGTGTATGGAAACTGCTCCACTCACTTTACCGTCAAGACGAGGAAGGGCAATGTGGCA
ACAGAAATATCCACTGAAAGAGACCTGGGGCAGTGTGATCGCTTCAAGCCCATCCGCACA
GGCATCAGCCCACTTGCTCTCATCAAAGGCATGACCCGCCCCTTGTCAACTCTGATCAGC
AGCAGCCAGTCCTGTCAGTACACACTGGACGCTAAGAGGAAGCATGTGGCAGAAGCCATC
TGCAAGGAGCAACACCTCTTCCTGCCTTTCTCCTACAACAATAAGTATGGGATGGTAGCA
CAAGTGACACAGACTTTGAAACTTGAAGACACACCAAAGATCAACAGCCGCTTCTTTGGT
GAAGGTACTAAGAAGATGGGCCTCGCATTTGAGAGCACCAAATCCACATCACCTCCAAAG
CAGGCCGAAGCTGTTTTGAAGACTCTCCAGGAACTGAAAAAACTAACCATCTCTGAGCAA
AATATCCAGAGAGCTAATCTCTTCAATAAGCTGGTTACTGAGCTGAGAGGCCTCAGTGAT
GAAGCAGTCACATCTCTCTTGCCACAGCTGATTGAGGTGTCCAGCCCCATCACTTTACAA
GCCTTGGTTCAGTGTGGACAGCCTCAGTGCTCCACTCACATCCTCCAGTGGCTGAAACGT
GTGCATGCCAACCCCCTTCTGATAGATGTGGTCACCTACCTGGTGGCCCTGATCCCCGAG
CCCTCAGCACAGCAGCTGCGAGAGATCTTCAACATGGCGAGGGATCAGCGCAGCCGAGCC
ACCTTGTATGCGCTGAGCCACGCGGTCAACAACTATCATAAGACAAACCCTACAGGGACC
CAGGAGCTGCTGGACATTGCTAATTACCTGATGGAACAGATTCAAGATGACTGCACTGGG
GATGAAGATTACACCTATTTGATTCTGCGGGTCATTGGAAATATGGGCCAAACCATGGAG
CAGTTAACTCCAGAACTCAAGTCTTCAATCCTCAAATGTGTCCAAAGTACAAAGCCATCA
CTGATGATCCAGAAAGCTGCCATCCAGGCTCTGCGGAAAATGGAGCCTAAAGACAAGGAC
CAGGAGGTTCTTCTTCAGACTTTCCTTGATGATGCTTCTCCGGGAGATAAGCGACTGGCT
GCCTATCTTATGTTGATGAGGAGTCCTTCACAGGCAGATATTAACAAAATTGTCCAAATT
CTACCATGGGAACAGAATGAGCAAGTGAAGAACTTTGTGGCTTCCCATATTGCCAATATC
TTGAACTCAGAAGAATTGGATATCCAAGATCTGAAAAAGTTAGTGAAAGAAGCTCTGAAA
GAATCTCAACTTCCAACTGTCATGGACTTCAGAAAATTCTCTCGGAACTATCAACTCTAC
AAATCTGTTTCTCTTCCATCACTTGACCCAGCCTCAGCCAAAATAGAAGGGAATCTTATA
TTTGATCCAAATAACTACCTTCCTAAAGAAAGCATGCTGAAAACTACCCTCACTGCCTTT
GGATTTGCTTCAGCTGACCTCATCGAGATTGGCTTGGAAGGAAAAGGCTTTGAGCCAACA
TTGGAAGCTCTTTTTGGGAAGCAAGGATTTTTCCCAGACAGTGTCAACAAAGCTTTGTAC
TGGGTTAATGGTCAAGTTCCTGATGGTGTCTCTAAGGTCTTAGTGGACCACTTTGGCTAT
ACCAAAGATGATAAACATGAGCAGGATATGGTAAATGGAATAATGCTCAGTGTTGAGAAG
CTGATTAAAGATTTGAAATCCAAAGAAGTCCCGGAAGCCAGAGCCTACCTCCGCATCTTG
GGAGAGGAGCTTGGTTTTGCCAGTCTCCATGACCTCCAGCTCCTGGGAAAGCTGCTTCTG
ATGGGTGCCCGCACTCTGCAGGGGATCCCCCAGATGATTGGAGAGGTCATCAGGAAGGGC
TCAAAGAATGACTTTTTTCTTCACTACATCTTCATGGAGAATGCCTTTGAACTCCCCACT
GGAGCTGGATTACAGTTGCAAATATCTTCATCTGGAGTCATTGCTCCCGGAGCCAAGGCT
GGAGTAAAACTGGAAGTAGCCAACATGCAGGCTGAACTGGTGGCAAAACCCTCCGTGTCT
GTGGAGTTTGTGACAAATATGGGCATCATCATTCCGGACTTCGCTAGGAGTGGGGTCCAG
ATGAACACCAACTTCTTCCACGAGTCGGGTCTGGAGGCTCATGTTGCCCTAAAAGCTGGG
AAGCTGAAGTTTATCATTCCTTCCCCAAAGAGACCAGTCAAGCTGCTCAGTGGAGGCAAC
ACATTACATTTGGTCTCTACCACCAAAACGGAGGTGATCCCACCTCTCATTGAGAACAGG
CAGTCCTGGTCAGTTTGCAAGCAAGTCTTTCCTGGCCTGAATTACTGCACCTCAGGCGCT
TACTCCAACGCCAGCTCCACAGACTCCGCCTCCTACTATCCGCTGACCGGGGACACCAGA
TTAGAGCTGGAACTGAGGCCTACAGGAGAGATTGAGCAGTATTCTGTCAGCGCAACCTAT
GAGCTCCAGAGAGAGGACAGAGCCTTGGTGGATACCCTGAAGTTTGTAACTCAAGCAGAA
GGTGCGAAGCAGACTGAGGCTACCATGACATTCAAATATAATCGGCAGAGTATGACCTTG
TCCAGTGAAGTCCAAATTCCGGATTTTGATGTTGACCTCGGAACAATCCTCAGAGTTAAT
GATGAATCTACTGAGGGCAAAACGTCTTACAGACTCACCCTGGACATTCAGAACAAGAAA
ATTACTGAGGTCGCCCTCATGGGCCACCTAAGTTGTGACACAAAGGAAGAAAGAAAAATC
AAGGGTGTTATTTCCATACCCCGTTTGCAAGCAGAAGCCAGAAGTGAGATCCTCGCCCAC
TGGTCGCCTGCCAAACTGCTTCTCCAAATGGACTCATCTGCTACAGCTTATGGCTCCACA
GTTTCCAAGAGGGTGGCATGGCATTATGATGAAGAGAAGATTGAATTTGAATGGAACACA
GGCACCAATGTAGATACCAAAAAAATGACTTCCAATTTCCCTGTGGATCTCTCCGATTAT
CCTAAGAGCTTGCATATGTATGCTAATAGACTCCTGGATCACAGAGTCCCTGAAACAGAC
ATGACTTTCCGGCACGTGGGTTCCAAATTAATAGTTGCAATGAGCTCATGGCTTCAGAAG
GCATCTGGGAGTCTTCCTTATACCCAGACTTTGCAAGACCACCTCAATAGCCTGAAGGAG
TTCAACCTCCAGAACATGGGATTGCCAGACTTCCACATCCCAGAAAACCTCTTCTTAAAA
AGCGATGGCCGGGTCAAATATACCTTGAACAAGAACAGTTTGAAAATTGAGATTCCTTTG
CCTTTTGGTGGCAAATCCTCCAGAGATCTAAAGATGTTAGAGACTGTTAGGACACCAGCC
CTCCACTTCAAGTCTGTGGGATTCCATCTGCCATCTCGAGAGTTCCAAGTCCCTACTTTT
ACCATTCCCAAGTTGTATCAACTGCAAGTGCCTCTCCTGGGTGTTCTAGACCTCTCCACG
AATGTCTACAGCAACTTGTACAACTGGTCCGCCTCCTACAGTGGTGGCAACACCAGCACA
GACCATTTCAGCCTTCGGGCTCGTTACCACATGAAGGCTGACTCTGTGGTTGACCTGCTT
TCCTACAATGTGCAAGGATCTGGAGAAACAACATATGACCACAAGAATACGTTCACACTA
TCATGTGATGGGTCTCTACGCCACAAATTTCTAGATTCGAATATCAAATTCAGTCATGTA
GAAAAACTTGGAAACAACCCAGTCTCAAAAGGTTTACTAATATTCGATGCATCTAGTTCC
TGGGGACCACAGATGTCTGCTTCAGTTCATTTGGACTCCAAAAAGAAACAGCATTTGTTT
GTCAAAGAAGTCAAGATTGATGGGCAGTTCAGAGTCTCTTCGTTCTATGCTAAAGGCACA
TATGGCCTGTCTTGTCAGAGGGATCCTAACACTGGCCGGCTCAATGGAGAGTCCAACCTG
AGGTTTAACTCCTCCTACCTCCAAGGCACCAACCAGATAACAGGAAGATATGAAGATGGA
ACCCTCTCCCTCACCTCCACCTCTGATCTGCAAAGTGGCATCATTAAAAATACTGCTTCC
CTAAAGTATGAGAACTACGAGCTGACTTTAAAATCTGACACCAATGGGAAGTATAAGAAC
TTTGCCACTTCTAACAAGATGGATATGACCTTCTCTAAGCAAAATGCACTGCTGCGTTCT
GAATATCAGGCTGATTACGAGTCATTGAGGTTCTTCAGCCTGCTTTCTGGATCACTAAAT
TCCCATGGTCTTGAGTTAAATGCTGACATCTTAGGCACTGACAAAATTAATAGTGGTGCT
CACAAGGCGACACTAAGGATTGGCCAAGATGGAATATCTACCAGTGCAACGACCAACTTG
AAGTGTAGTCTCCTGGTGCTGGAGAATGAGCTGAATGCAGAGCTTGGCCTCTCTGGGGCA
TCTATGAAATTAACAACAAATGGCCGCTTCAGGGAACACAATGCAAAATTCAGTCTGGAT
GGGAAAGCCGCCCTCACAGAGCTATCACTGGGAAGTGCTTATCAGGCCATGATTCTGGGT
GTCGACAGCAAAAACATTTTCAACTTCAAGGTCAGTCAAGAAGGACTTAAGCTCTCAAAT
GACATGATGGGCTCATATGCTGAAATGAAATTTGACCACACAAACAGTCTGAACATTGCA
GGCTTATCACTGGACTTCTCTTCAAAACTTGACAACATTTACAGCTCTGACAAGTTTTAT
AAGCAAACTGTTAATTTACAGCTACAGCCCTATTCTCTGGTAACTACTTTAAACAGTGAC
CTGAAATACAATGCTCTGGATCTCACCAACAATGGGAAACTACGGCTAGAACCCCTGAAG
CTGCATGTGGCTGGTAACCTAAAAGGAGCCTACCAAAATAATGAAATAAAACACATCTAT
GCCATCTCTTCTGCTGCCTTATCAGCAAGCTATAAAGCAGACACTGTTGCTAAGGTTCAG
GGTGTGGAGTTTAGCCATCGGCTCAACACAGACATCGCTGGGCTGGCTTCAGCCATTGAC
ATGAGCACAAACTATAATTCAGACTCACTGCATTTCAGCAATGTCTTCCGTTCTGTAATG
GCCCCGTTTACCATGACCATCGATGCACATACAAATGGCAATGGGAAACTCGCTCTCTGG
GGAGAACATACTGGGCAGCTGTATAGCAAATTCCTGTTGAAAGCAGAACCTCTGGCATTT
ACTTTCTCTCATGATTACAAAGGCTCCACAAGTCATCATCTCGTGTCTAGGAAAAGCATC
AGTGCAGCTCTTGAACACAAAGTCAGTGCCCTGCTTACTCCAGCTGAGCAGACAGGCACC
TGGAAACTCAAGACCCAATTTAACAACAATGAATACAGCCAGGACTTGGATGCTTACAAC
ACTAAAGATAAAATTGGCGTGGAGCTTACTGGACGAACTCTGGCTGACCTAACTCTACTA
GACTCCCCAATTAAAGTGCCACTTTTACTCAGTGAGCCCATCAATATCATTGATGCTTTA
GAGATGAGAGATGCCGTTGAGAAGCCCCAAGAATTTACAATTGTTGCTTTTGTAAAGTAT
GATAAAAACCAAGATGTTCACTCCATTAACCTCCCATTTTTTGAGACCTTGCAAGAATAT
TTTGAGAGGAATCGACAAACCATTATAGTTGTAGTGGAAAACGTACAGAGAAACCTGAAG
CACATCAATATTGATCAATTTGTAAGAAAATACAGAGCAGCCCTGGGAAAACTCCCACAG
CAAGCTAATGATTATCTGAATTCATTCAATTGGGAGAGACAAGTTTCACATGCCAAGGAG
AAACTGACTGCTCTCACAAAAAAGTATAGAATTACAGAAAATGATATACAAATTGCATTA
GATGATGCCAAAATCAACTTTAATGAAAAACTATCTCAACTGCAGACATATATGATACAA
TTTGATCAGTATATTAAAGATAGTTATGATTTACATGATTTGAAAATAGCTATTGCTAAT
ATTATTGATGAAATCATTGAAAAATTAAAAAGTCTTGATGAGCACTATCATATCCGTGTA
AATTTAGTAAAAACAATCCATGATCTACATTTGTTTATTGAAAATATTGATTTTAACAAA
AGTGGAAGTAGTACTGCATCCTGGATTCAAAATGTGGATACTAAGTACCAAATCAGAATC
CAGATACAAGAAAAACTGCAGCAGCTTAAGAGACACATACAGAATATAGACATCCAGCAC
CTAGCTGGAAAGTTAAAACAACACATTGAGGCTATTGATGTTAGAGTGCTTTTAGATCAA
TTGGGAACTACAATTTCATTTGAAAGAATAAATGATGTTCTTGAGCATGTCAAACACTTT
GTTATAAATCTTATTGGGGATTTTGAAGTAGCTGAGAAAATCAATGCCTTCAGAGCCAAA
GTCCATGAGTTAATCGAGAGGTATGAAGTAGACCAACAAATCCAGGTTTTAATGGATAAA
TTAGTAGAGTTGACCCACCAATACAAGTTGAAGGAGACTATTCAGAAGCTAAGCAATGTC
CTACAACAAGTTAAGATAAAAGATTACTTTGAGAAATTGGTTGGATTTATTGATGATGCT
GTGAAGAAGCTTAATGAATTATCTTTTAAAACATTCATTGAAGATGTTAACAAATTCCTT
GACATGTTGATAAAGAAATTAAAGTCATTTGATTACCACCAGTTTGTAGATGAAACCAAT
GACAAAATCCGTGAGGTGACTCAGAGACTCAATGGTGAAATTCAGGCTCTGGAACTACCA
CAAAAAGCTGAAGCATTAAAACTGTTTTTAGAGGAAACCAAGGCCACAGTTGCAGTGTAT
CTGGAAAGCCTACAGGACACCAAAATAACCTTAATCATCAATTGGTTACAGGAGGCTTTA
AGTTCAGCATCTTTGGCTCACATGAAGGCCAAATTCCGAGAGACTCTAGAAGATACACGA
GACCGAATGTATCAAATGGACATTCAGCAGGAACTTCAACGATACCTGTCTCTGGTAGGC
CAGGTTTATAGCACACTTGTCACCTACATTTCTGATTGGTGGACTCTTGCTGCTAAGAAC
CTTACTGACTTTGCAGAGCAATATTCTATCCAAGATTGGGCTAAACGTATGAAAGCATTG
GTAGAGCAAGGGTTCACTGTTCCTGAAATCAAGACCATCCTTGGGACCATGCCTGCCTTT
GAAGTCAGTCTTCAGGCTCTTCAGAAAGCTACCTTCCAGACACCTGATTTTATAGTCCCC
CTAACAGATTTGAGGATTCCATCAGTTCAGATAAACTTCAAAGACTTAAAAAATATAAAA
ATCCCATCCAGGTTTTCCACACCAGAATTTACCATCCTTAACACCTTCCACATTCCTTCC
TTTACAATTGACTTTGTCGAAATGAAAGTAAAGATCATCAGAACCATTGACCAGATGCAG
AACAGTGAGCTGCAGTGGCCCGTTCCAGATATATATCTCAGGGATCTGAAGGTGGAGGAC
ATTCCTCTAGCGAGAATCACCCTGCCAGACTTCCGTTTACCAGAAATCGCAATTCCAGAA
TTCATAATCCCAACTCTCAACCTTAATGATTTTCAAGTTCCTGACCTTCACATACCAGAA
TTCCAGCTTCCCCACATCTCACACACAATTGAAGTACCTACTTTTGGCAAGCTATACAGT
ATTCTGAAAATCCAATCTCCTCTTTTCACATTAGATGCAAATGCTGACATAGGGAATGGA
ACCACCTCAGCAAACGAAGCAGGTATCGCAGCTTCCATCACTGCCAAAGGAGAGTCCAAA
TTAGAAGTTCTCAATTTTGATTTTCAAGCAAATGCACAACTCTCAAACCCTAAGATTAAT
CCGCTGGCTCTGAAGGAGTCAGTGAAGTTCTCCAGCAAGTACCTGAGAACGGAGCATGGG
AGTGAAATGCTGTTTTTTGGAAATGCTATTGAGGGAAAATCAAACACAGTGGCAAGTTTA
CACACAGAAAAAAATACACTGGAGCTTAGTAATGGAGTGATTGTCAAGATAAACAATCAG
CTTACCCTGGATAGCAACACTAAATACTTCCACAAATTGAACATCCCCAAACTGGACTTC
TCTAGTCAGGCTGACCTGCGCAACGAGATCAAGACACTGTTGAAAGCTGGCCACATAGCA
TGGACTTCTTCTGGAAAAGGGTCATGGAAATGGGCCTGCCCCAGATTCTCAGATGAGGGA
ACACATGAATCACAAATTAGTTTCACCATAGAAGGACCCCTCACTTCCTTTGGACTGTCC
AATAAGATCAATAGCAAACACCTAAGAGTAAACCAAAACTTGGTTTATGAATCTGGCTCC
CTCAACTTTTCTAAACTTGAAATTCAATCACAAGTCGATTCCCAGCATGTGGGCCACAGT
GTTCTAACTGCTAAAGGCATGGCACTGTTTGGAGAAGGGAAGGCAGAGTTTACTGGGAGG
CATGATGCTCATTTAAATGGAAAGGTTATTGGAACTTTGAAAAATTCTCTTTTCTTTTCA
GCCCAGCCATTTGAGATCACGGCATCCACAAACAATGAAGGGAATTTGAAAGTTCGTTTT
CCATTAAGGTTAACAGGGAAGATAGACTTCCTGAATAACTATGCACTGTTTCTGAGTCCC
AGTGCCCAGCAAGCAAGTTGGCAAGTAAGTGCTAGGTTCAATCAGTATAAGTACAACCAA
AATTTCTCTGCTGGAAACAACGAGAACATTATGGAGGCCCATGTAGGAATAAATGGAGAA
GCAAATCTGGATTTCTTAAACATTCCTTTAACAATTCCTGAAATGCGTCTACCTTACACA
ATAATCACAACTCCTCCACTGAAAGATTTCTCTCTATGGGAAAAAACAGGCTTGAAGGAA
TTCTTGAAAACGACAAAGCAATCATTTGATTTAAGTGTAAAAGCTCAGTATAAGAAAAAC
AAACACAGGCATTCCATCACAAATCCTTTGGCTGTGCTTTGTGAGTTTATCAGTCAGAGC
ATCAAATCCTTTGACAGGCATTTTGAAAAAAACAGAAACAATGCATTAGATTTTGTCACC
AAATCCTATAATGAAACAAAAATTAAGTTTGATAAGTACAAAGCTGAAAAATCTCACGAC
GAGCTCCCCAGGACCTTTCAAATTCCTGGATACACTGTTCCAGTTGTCAATGTTGAAGTG
TCTCCATTCACCATAGAGATGTCGGCATTCGGCTATGTGTTCCCAAAAGCAGTCAGCATG
CCTAGTTTCTCCATCCTAGGTTCTGACGTCCGTGTGCCTTCATACACATTAATCCTGCCA
TCATTAGAGCTGCCAGTCCTTCATGTCCCTAGAAATCTCAAGCTTTCTCTTCCACATTTC
AAGGAATTGTGTACCATAAGCCATATTTTTATTCCTGCCATGGGCAATATTACCTATGAT
TTCTCCTTTAAATCAAGTGTCATCACACTGAATACCAATGCTGAACTTTTTAACCAGTCA
GATATTGTTGCTCATCTCCTTTCTTCATCTTCATCTGTCATTGATGCACTGCAGTACAAA
TTAGAGGGCACCACAAGATTGACAAGAAAAAGGGGATTGAAGTTAGCCACAGCTCTGTCT
CTGAGCAACAAATTTGTGGAGGGTAGTCATAACAGTACTGTGAGCTTAACCACGAAAAAT
ATGGAAGTGTCAGTGGCAAAAACCACAAAAGCCGAAATTCCAATTTTGAGAATGAATTTC
AAGCAAGAACTTAATGGAAATACCAAGTCAAAACCTACTGTCTCTTCCTCCATGGAATTT
AAGTATGATTTCAATTCTTCAATGCTGTACTCTACCGCTAAAGGAGCAGTTGACCACAAG
CTTAGCTTGGAAAGCCTCACCTCTTACTTTTCCATTGAGTCATCTACCAAAGGAGATGTC
AAGGGTTCGGTTCTTTCTCGGGAATATTCAGGAACTATTGCTAGTGAGGCCAACACTTAC
TTGAATTCCAAGAGCACACGGTCTTCAGTGAAGCTGCAGGGCACTTCCAAAATTGATGAT
ATCTGGAACCTTGAAGTAAAAGAAAATTTTGCTGGAGAAGCCACACTCCAACGCATATAT
TCCCTCTGGGAGCACAGTACGAAAAACCACTTACAGCTAGAGGGCCTCTTTTTCACCAAC
GGAGAACATACAAGCAAAGCCACCCTGGAACTCTCTCCATGGCAAATGTCAGCTCTTGTT
CAGGTCCATGCAAGTCAGCCCAGTTCCTTCCATGATTTCCCTGACCTTGGCCAGGAAGTG
GCCCTGAATGCTAACACTAAGAACCAGAAGATCAGATGGAAAAATGAAGTCCGGATTCAT
TCTGGGTCTTTCCAGAGCCAGGTCGAGCTTTCCAATGACCAAGAAAAGGCACACCTTGAC
ATTGCAGGATCCTTAGAAGGACACCTAAGGTTCCTCAAAAATATCATCCTACCAGTCTAT
GACAAGAGCTTATGGGATTTCCTAAAGCTGGATGTAACCACCAGCATTGGTAGGAGACAG
CATCTTCGTGTTTCAACTGCCTTTGTGTACACCAAAAACCCCAATGGCTATTCATTCTCC
ATCCCTGTAAAAGTTTTGGCTGATAAATTCATTACTCCTGGGCTGAAACTAAATGATCTA
AATTCAGTTCTTGTCATGCCTACGTTCCATGTCCCATTTACAGATCTTCAGGTTCCATCG
TGCAAACTTGACTTCAGAGAAATACAAATCTATAAGAAGCTGAGAACTTCATCATTTGCC
CTCAACCTACCAACACTCCCCGAGGTAAAATTCCCTGAAGTTGATGTGTTAACAAAATAT
TCTCAACCAGAAGACTCCTTGATTCCCTTTTTTGAGATAACCGTGCCTGAATCTCAGTTA
ACTGTGTCCCAGTTCACGCTTCCAAAAAGTGTTTCAGATGGCATTGCTGCTTTGGATCTA
AATGCAGTAGCCAACAAGATCGCAGACTTTGAGTTGCCCACCATCATCGTGCCTGAGCAG
ACCATTGAGATTCCCTCCATTAAGTTCTCTGTACCTGCTGGAATTGTCATTCCTTCCTTT
CAAGCACTGACTGCACGCTTTGAGGTAGACTCTCCCGTGTATAATGCCACTTGGAGTGCC
AGTTTGAAAAACAAAGCAGATTATGTTGAAACAGTCCTGGATTCCACATGCAGCTCAACC
GTACAGTTCCTAGAATATGAACTAAATGTTTTGGGAACACACAAAATCGAAGATGGTACG
TTAGCCTCTAAGACTAAAGGAACACTTGCACACCGTGACTTCAGTGCAGAATATGAAGAA
GATGGCAAATTTGAAGGACTTCAGGAATGGGAAGGAAAAGCGCACCTCAATATCAAAAGC
CCAGCGTTCACCGATCTCCATCTGCGCTACCAGAAAGACAAGAAAGGCATCTCCACCTCA
GCAGCCTCCCCAGCCGTAGGCACCGTGGGCATGGATATGGATGAAGATGACGACTTTTCT
AAATGGAACTTCTACTACAGCCCTCAGTCCTCTCCAGATAAAAAACTCACCATATTCAAA
ACTGAGTTGAGGGTCCGGGAATCTGATGAGGAAACTCAGATCAAAGTTAATTGGGAAGAA
GAGGCAGCTTCTGGCTTGCTAACCTCTCTGAAAGACAACGTGCCCAAGGCCACAGGGGTC
CTTTATGATTATGTCAACAAGTACCACTGGGAACACACAGGGCTCACCCTGAGAGAAGTG
TCTTCAAAGCTGAGAAGAAATCTGCAGAACAATGCTGAGTGGGTTTATCAAGGGGCCATT
AGGCAAATTGATGATATCGACGTGAGGTTCCAGAAAGCAGCCAGTGGCACCACTGGGACC
TACCAAGAGTGGAAGGACAAGGCCCAGAATCTGTACCAGGAACTGTTGACTCAGGAAGGC
CAAGCCAGTTTCCAGGGACTCAAGGATAACGTGTTTGATGGCTTGGTACGAGTTACTCAA
AAATTCCATATGAAAGTCAAGCATCTGATTGACTCACTCATTGATTTTCTGAACTTCCCC
AGATTCCAGTTTCCGGGGAAACCTGGGATATACACTAGGGAGGAACTTTGCACTATGTTC
ATAAGGGAGGTAGGGACGGTACTGTCCCAGGTATATTCGAAAGTCCATAATGGTTCAGAA
ATACTGTTTTCCTATTTCCAAGACCTAGTGATTACACTTCCTTTCGAGTTAAGGAAACAT
AAACTAATAGATGTAATCTCGATGTATAGGGAACTGTTGAAAGATTTATCAAAAGAAGCC
CAAGAGGTATTTAAAGCCATTCAGTCTCTCAAGACCACAGAGGTGCTACGTAATCTTCAG
GACCTTTTACAATTCATTTTCCAACTAATAGAAGATAACATTAAACAGCTGAAAGAGATG
AAATTTACTTATCTTATTAATTATATCCAAGATGAGATCAACACAATCTTCAATGATTAT
ATCCCATATGTTTTTAAATTGTTGAAAGAAAACCTATGCCTTAATCTTCATAAGTTCAAT
GAATTTATTCAAAACGAGCTTCAGGAAGCTTCTCAAGAGTTACAGCAGATCCATCAATAC
ATTATGGCCCTTCGTGAAGAATATTTTGATCCAAGTATAGTTGGCTGGACAGTGAAATAT
TATGAACTTGAAGAAAAGATAGTCAGTCTGATCAAGAACCTGTTAGTTGCTCTTAAGGAC
TTCCATTCTGAATATATTGTCAGTGCCTCTAACTTTACTTCCCAACTCTCAAGTCAAGTT
GAGCAATTTCTGCACAGAAATATTCAGGAATATCTTAGCATCCTTACCGATCCAGATGGA
AAAGGGAAAGAGAAGATTGCAGAGCTTTCTGCCACTGCTCAGGAAATAATTAAAAGCCAG
GCCATTGCGACGAAGAAAATAATTTCTGATTACCACCAGCAGTTTAGATATAAACTGCAA
GATTTTTCAGACCAACTCTCTGATTACTATGAAAAATTTATTGCTGAATCCAAAAGATTG
ATTGACCTGTCCATTCAAAACTACCACACATTTCTGATATACATCACGGAGTTACTGAAA
AAGCTGCAATCAACCACAGTCATGAACCCCTACATGAAGCTTGCTCCAGGAGAACTTACT
ATCATCCTCTAA
Target 10 GenBank Gene ID
Target 10 GeneCard ID APOB Link Image
Target 10 GenAtlas ID APOB Link Image
Target 10 HGNC ID HGNC:603 Link Image
Target 10 Chromosome Location 2
Target 10 Locus 2p24-p23
Target 10 SNPs SNPJam Report Link Image
Target 10 General References
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  2. Burnett JR, Shan J, Miskie BA, Whitfield AJ, Yuan J, Tran K, McKnight CJ, Hegele RA, Yao Z: A novel nontruncating APOB gene mutation, R463W, causes familial hypobetalipoproteinemia. J Biol Chem. 2003 Apr 11;278(15):13442-52. Epub 2003 Jan 27. [PubMed Link Image]
  3. Navajas M, Laurent AM, Moreel JF, Ragab A, Cambou JP, Cuny G, Cambien F, Roizes G: Detection by denaturing gradient gel electrophoresis of a new polymorphism in the apolipoprotein B gene. Hum Genet. 1990 Nov;86(1):91-3. [PubMed Link Image]
  4. Yang CY, Kim TW, Weng SA, Lee BR, Yang ML, Gotto AM Jr: Isolation and characterization of sulfhydryl and disulfide peptides of human apolipoprotein B-100. Proc Natl Acad Sci U S A. 1990 Jul;87(14):5523-7. [PubMed Link Image]
  5. Huang LS, Gavish D, Breslow JL: Sequence polymorphism in the human apoB gene at position 8344. Nucleic Acids Res. 1990 Oct 11;18(19):5922. [PubMed Link Image]
  6. Hospattankar AV, Higuchi K, Law SW, Meglin N, Brewer HB Jr: Identification of a novel in-frame translational stop codon in human intestine apoB mRNA. Biochem Biophys Res Commun. 1987 Oct 14;148(1):279-85. [PubMed Link Image]
  7. Higuchi K, Hospattankar AV, Law SW, Meglin N, Cortright J, Brewer HB Jr: Human apolipoprotein B (apoB) mRNA: identification of two distinct apoB mRNAs, an mRNA with the apoB-100 sequence and an apoB mRNA containing a premature in-frame translational stop codon, in both liver and intestine. Proc Natl Acad Sci U S A. 1988 Mar;85(6):1772-6. [PubMed Link Image]
  8. Soria LF, Ludwig EH, Clarke HR, Vega GL, Grundy SM, McCarthy BJ: Association between a specific apolipoprotein B mutation and familial defective apolipoprotein B-100. Proc Natl Acad Sci U S A. 1989 Jan;86(2):587-91. [PubMed Link Image]
  9. Huang LS, Ripps ME, Korman SH, Deckelbaum RJ, Breslow JL: Hypobetalipoproteinemia due to an apolipoprotein B gene exon 21 deletion derived by Alu-Alu recombination. J Biol Chem. 1989 Jul 5;264(19):11394-400. [PubMed Link Image]
  10. Carlsson P, Darnfors C, Olofsson SO, Bjursell G: Analysis of the human apolipoprotein B gene; complete structure of the B-74 region. Gene. 1986;49(1):29-51. [PubMed Link Image]
  11. 2932736 Wei CF, Chen SH, Yang CY, Marcel YL, Milne RW, Li WH, Sparrow JT, Gotto AM Jr, Chan L: Molecular cloning and expression of partial cDNAs and deduced amino acid sequence of a carboxyl-terminal fragment of human apolipoprotein B-100. Proc Natl Acad Sci U S A. 1985 Nov;82(21):7265-9.
  12. 2994225 Knott TJ, Rall SC Jr, Innerarity TL, Jacobson SF, Urdea MS, Levy-Wilson B, Powell LM, Pease RJ, Eddy R, Nakai H, et al.: Human apolipoprotein B: structure of carboxyl-terminal domains, sites of gene expression, and chromosomal localization. Science. 1985 Oct 4;230(4721):37-43.
  13. 3001697 Law SW, Lackner KJ, Hospattankar AV, Anchors JM, Sakaguchi AY, Naylor SL, Brewer HB Jr: Human apolipoprotein B-100: cloning, analysis of liver mRNA, and assignment of the gene to chromosome 2. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8340-4.
  14. 3024665 Pfitzner R, Wagener R, Stoffel W: Isolation, expression and characterization of a human apolipoprotein B 100-specific cDNA clone. Biol Chem Hoppe Seyler. 1986 Oct;367(10):1077-83.
  15. 3030729 Cladaras C, Hadzopoulou-Cladaras M, Nolte RT, Atkinson D, Zannis VI: The complete sequence and structural analysis of human apolipoprotein B-100: relationship between apoB-100 and apoB-48 forms. EMBO J. 1986 Dec 20;5(13):3495-507.
  16. 3087360 Dashti N, Lee DM, Mok T: Apolipoprotein B is a calcium binding protein. Biochem Biophys Res Commun. 1986 May 29;137(1):493-9.
  17. 3426612 Hardman DA, Protter AA, Schilling JW, Kane JP: Carboxyl terminal analysis of human B-48 protein confirms the novel mechanism proposed for chain termination. Biochem Biophys Res Commun. 1987 Dec 31;149(3):1214-9.
  18. 3461454 Protter AA, Hardman DA, Sato KY, Schilling JW, Yamanaka M, Hort YJ, Hjerrild KA, Chen GC, Kane JP: Analysis of cDNA clones encoding the entire B-26 region of human apolipoprotein B. Proc Natl Acad Sci U S A. 1986 Aug;83(15):5678-82.
  19. 3464946 Law SW, Grant SM, Higuchi K, Hospattankar A, Lackner K, Lee N, Brewer HB Jr: Human liver apolipoprotein B-100 cDNA: complete nucleic acid and derived amino acid sequence. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8142-6.
  20. 3513177 Protter AA, Hardman DA, Schilling JW, Miller J, Appleby V, Chen GC, Kirsher SW, McEnroe G, Kane JP: Isolation of a cDNA clone encoding the amino-terminal region of human apolipoprotein B. Proc Natl Acad Sci U S A. 1986 Mar;83(5):1467-71.
  21. 3621347 Powell LM, Wallis SC, Pease RJ, Edwards YH, Knott TJ, Scott J: A novel form of tissue-specific RNA processing produces apolipoprotein-B48 in intestine. Cell. 1987 Sep 11;50(6):831-40.
  22. 3652907 Ludwig EH, Blackhart BD, Pierotti VR, Caiati L, Fortier C, Knott T, Scott J, Mahley RW, Levy-Wilson B, McCarthy BJ: DNA sequence of the human apolipoprotein B gene. DNA. 1987 Aug;6(4):363-72.
  23. 3659919 Chen SH, Habib G, Yang CY, Gu ZW, Lee BR, Weng SA, Silberman SR, Cai SJ, Deslypere JP, Rosseneu M, et al.: Apolipoprotein B-48 is the product of a messenger RNA with an organ-specific in-frame stop codon. Science. 1987 Oct 16;238(4825):363-6.
  24. 3676265 Hardman DA, Protter AA, Chen GC, Schilling JW, Sato KY, Lau K, Yamanaka M, Mikita T, Miller J, Crisp T, et al.: Structural comparison of human apolipoproteins B-48 and B-100. Biochemistry. 1987 Aug 25;26(17):5478-86.
  25. 3759943 Chen SH, Yang CY, Chen PF, Setzer D, Tanimura M, Li WH, Gotto AM Jr, Chan L: The complete cDNA and amino acid sequence of human apolipoprotein B-100. J Biol Chem. 1986 Oct 5;261(28):12918-21.
  26. 3763409 Knott TJ, Wallis SC, Powell LM, Pease RJ, Lusis AJ, Blackhart B, McCarthy BJ, Mahley RW, Levy-Wilson B, Scott J: Complete cDNA and derived protein sequence of human apolipoprotein B-100. Nucleic Acids Res. 1986 Sep 25;14(18):7501-3.
  27. 3773997 Knott TJ, Pease RJ, Powell LM, Wallis SC, Rall SC Jr, Innerarity TL, Blackhart B, Taylor WH, Marcel Y, Milne R, et al.: Complete protein sequence and identification of structural domains of human apolipoprotein B. Nature. 1986 Oct 23-29;323(6090):734-8.
  28. 3841204 Carlsson P, Olofsson SO, Bondjers G, Darnfors C, Wiklund O, Bjursell G: Molecular cloning of human apolipoprotein B cDNA. Nucleic Acids Res. 1985 Dec 20;13(24):8813-26.
  29. 3841481 Shoulders CC, Myant NB, Sidoli A, Rodriguez JC, Cortese C, Baralle FE, Cortese R: Molecular cloning of human LDL apolipoprotein B cDNA. Evidence for more than one gene per haploid genome. Atherosclerosis. 1985 Dec;58(1-3):277-89.
  30. 3860836 Deeb SS, Motulsky AG, Albers JJ: A partial cDNA clone for human apolipoprotein B. Proc Natl Acad Sci U S A. 1985 Aug;82(15):4983-6.
  31. 3903660 Mehrabian M, Schumaker VN, Fareed GC, West R, Johnson DF, Kirchgessner T, Lin HC, Wang XB, Ma YH, Mendiaz E, et al.: Human apolipoprotein B: identification of cDNA clones and characterization of mRNA. Nucleic Acids Res. 1985 Oct 11;13(19):6937-53.
  32. 6373369 LeBoeuf RC, Miller C, Shively JE, Schumaker VN, Balla MA, Lusis AJ: Human apolipoprotein B: partial amino acid sequence. FEBS Lett. 1984 May 7;170(1):105-8.
  33. 7883971 Pullinger CR, Hennessy LK, Chatterton JE, Liu W, Love JA, Mendel CM, Frost PH, Malloy MJ, Schumaker VN, Kane JP: Familial ligand-defective apolipoprotein B. Identification of a new mutation that decreases LDL receptor binding affinity. J Clin Invest. 1995 Mar;95(3):1225-34.
  34. 8889592 Poirier O, Ricard S, Behague I, Souriau C, Evans AE, Arveiler D, Marques-Vidal P, Luc G, Roizes G, Cambien F: Detection of new variants in the apolipoprotein B (Apo B) gene by PCR-SSCP. Hum Mutat. 1996;8(3):282-5.
  35. 9259199 Rabes JP, Varret M, Saint-Jore B, Erlich D, Jondeau G, Krempf M, Giraudet P, Junien C, Boileau C: Familial ligand-defective apolipoprotein B-100: simultaneous detection of the ARG3500-->GLN and ARG3531-->CYS mutations in a French population. Hum Mutat. 1997;10(2):160-3.
  36. 9490296 Leren TP, Bakken KS, Hoel V, Hjermann I, Berg K: Screening for mutations of the apolipoprotein B gene causing hypocholesterolemia. Hum Genet. 1998 Jan;102(1):44-9.
Target 10 Drug References
  1. Ishigami M, Yamashita S, Sakai N, Hirano K, Hiraoka H, Nakamura T, Matsuzawa Y: Atorvastatin markedly improves type III hyperlipoproteinemia in association with reduction of both exogenous and endogenous apolipoprotein B-containing lipoproteins. Atherosclerosis. 2003 Jun;168(2):359-66. [PubMed Link Image]
  2. Dallinga-Thie GM, Berk-Planken II, Bootsma AH, Jansen H: Atorvastatin decreases apolipoprotein C-III in apolipoprotein B-containing lipoprotein and HDL in type 2 diabetes: a potential mechanism to lower plasma triglycerides. Diabetes Care. 2004 Jun;27(6):1358-64. [PubMed Link Image]
  3. Tsimikas S, Witztum JL, Miller ER, Sasiela WJ, Szarek M, Olsson AG, Schwartz GG: High-dose atorvastatin reduces total plasma levels of oxidized phospholipids and immune complexes present on apolipoprotein B-100 in patients with acute coronary syndromes in the MIRACL trial. Circulation. 2004 Sep 14;110(11):1406-12. Epub 2004 Sep 7. [PubMed Link Image]
  4. Castro Cabezas M, Verseyden C, Meijssen S, Jansen H, Erkelens DW: Effects of atorvastatin on the clearance of triglyceride-rich lipoproteins in familial combined hyperlipidemia. J Clin Endocrinol Metab. 2004 Dec;89(12):5972-80. [PubMed Link Image]
  5. Dogra GK, Watts GF, Chan DC, Stanton K: Statin therapy improves brachial artery vasodilator function in patients with Type 1 diabetes and microalbuminuria. Diabet Med. 2005 Mar;22(3):239-42. [PubMed Link Image]
Drug Target 11 [top]
Target 11 ID 1498
Target 11 Name CD40 ligand
Target 11 Synonyms
  1. CD154 antigen
  2. CD40-L
  3. T cell antigen Gp39
  4. TNF-related activation protein
  5. TRAP
  6. Tumor necrosis factor ligand superfamily member 5
Target 11 Gene Name CD40LG
Target 11 Protein Sequence >CD40 ligand
MIETYNQTSPRSAATGLPISMKIFMYLLTVFLITQMIGSALFAVYLHRRLDKIEDERNLH
EDFVFMKTIQRCNTGERSLSLLNCEEIKSQFEGFVKDIMLNKEETKKENSFEMQKGDQNP
QIAAHVISEASSKTTSVLQWAEKGYYTMSNNLVTLENGKQLTVKRQGLYYIYAQVTFCSN
REASSQAPFIASLCLKSPGRFERILLRAANTHSSAKPCGQQSIHLGGVFELQPGASVFVN
VTDPSQVSHGTGFTSFGLLKL
Target 11 Number of Residues 265
Target 11 Molecular Weight 29274
Target 11 Theoretical pI 8.46
Target 11 GO Classification
Function
signal transducer activity
receptor binding
cytokine activity
tumor necrosis factor receptor binding
Process
response to stimulus
response to biotic stimulus
defense response
immune response
Component
cell
membrane
Target 11 General Function Involved in tumor necrosis factor receptor binding
Target 11 Specific Function Mediates B-cell proliferation in the absence of co- stimulus as well as IgE production in the presence of IL-4. Involved in immunoglobulin class switching
Target 11 Pathways Not Available
Target 11 Reactions Not Available
Target 11 Pfam Domain Function
Target 11 Signals
  • None
Target 11 Transmembrane Regions
  • 23-46
Target 11 Essentiality Non-Essential
Target 11 GenBank ID Protein 37270 Link Image
Target 11 UniProtKB/Swiss-Prot ID P29965 Link Image
Target 11 UniProtKB/Swiss-Prot Entry Name CD40L_HUMAN Link Image
Target 11 PDB ID 1I9R Link Image
Target 11 PDB File Show
Target 11 3D Structure
Target 11 Cellular Location
  • Cell membrane
  • single-pass type II membrane protein. Processed form:Secreted protein. Note=Also exis
Target 11 Gene Sequence >786 bp
ATGATCGAAACATACAACCAAACTTCTCCCCGATCTGCGGCCACTGGACTGCCCATCAGC
ATGAAAATTTTTATGTATTTACTTACTGTTTTTCTTATCACCCAGATGATTGGGTCAGCA
CTTTTTGCTGTGTATCTTCATAGAAGGCTGGACAAGATAGAAGATGAAAGGAATCTTCAT
GAAGATTTTGTATTCATGAAAACGATACAGAGATGCAACACAGGAGAAAGATCCTTATCC
TTACTGAACTGTGAGGAGATTAAAAGCCAGTTTGAAGGCTTTGTGAAGGATATAATGTTA
AACAAAGAGGAGACGAAGAAAGAAAACAGCTTTGAAATGCAAAAAGGTGATCAGAATCCT
CAAATTGCGGCACATGTCATAAGTGAGGCCAGCAGTAAAACAACATCTGTGTTACAGTGG
GCTGAAAAAGGATACTACACCATGAGCAACAACTTGGTAACCCTGGAAAATGGGAAACAG
CTGACCGTTAAAAGACAAGGACTCTATTATATCTATGCCCAAGTCACCTTCTGTTCCAAT
CGGGAAGCTTCGAGTCAAGCTCCATTTATAGCCAGCCTCTGCCTAAAGTCCCCCGGTAGA
TTCGAGAGAATCTTACTCAGAGCTGCAAATACCCACAGTTCCGCCAAACCTTGCGGGCAA
CAATCCATTCACTTGGGAGGAGTATTTGAATTGCAACCAGGTGCTTCGGTGTTTGTCAAT
GTGACTGATCCAAGCCAAGTGAGCCATGGCACTGGCTTCACGTCCTTTGGCTTACTCAAA
CTCTGA
Target 11 GenBank Gene ID
Target 11 GeneCard ID CD40LG Link Image
Target 11 GenAtlas ID CD40LG Link Image
Target 11 HGNC ID HGNC:11935 Link Image
Target 11 Chromosome Location X
Target 11 Locus Xq26
Target 11 SNPs SNPJam Report Link Image
Target 11 General References
  1. Graf D, Korthauer U, Mages HW, Senger G, Kroczek RA: Cloning of TRAP, a ligand for CD40 on human T cells. Eur J Immunol. 1992 Dec;22(12):3191-4. [PubMed Link Image]
  2. Spriggs MK, Armitage RJ, Strockbine L, Clifford KN, Macduff BM, Sato TA, Maliszewski CR, Fanslow WC: Recombinant human CD40 ligand stimulates B cell proliferation and immunoglobulin E secretion. J Exp Med. 1992 Dec 1;176(6):1543-50. [PubMed Link Image]
  3. Hollenbaugh D, Grosmaire LS, Kullas CD, Chalupny NJ, Braesch-Andersen S, Noelle RJ, Stamenkovic I, Ledbetter JA, Aruffo A: The human T cell antigen gp39, a member of the TNF gene family, is a ligand for the CD40 receptor: expression of a soluble form of gp39 with B cell co-stimulatory activity. EMBO J. 1992 Dec;11(12):4313-21. [PubMed Link Image]
  4. Gauchat JF, Aubry JP, Mazzei G, Life P, Jomotte T, Elson G, Bonnefoy JY: Human CD40-ligand: molecular cloning, cellular distribution and regulation of expression by factors controlling IgE production. FEBS Lett. 1993 Jan 11;315(3):259-66. [PubMed Link Image]
  5. Aruffo A, Farrington M, Hollenbaugh D, Li X, Milatovich A, Nonoyama S, Bajorath J, Grosmaire LS, Stenkamp R, Neubauer M, et al.: The CD40 ligand, gp39, is defective in activated T cells from patients with X-linked hyper-IgM syndrome. Cell. 1993 Jan 29;72(2):291-300. [PubMed Link Image]
  6. Korthauer U, Graf D, Mages HW, Briere F, Padayachee M, Malcolm S, Ugazio AG, Notarangelo LD, Levinsky RJ, Kroczek RA: Defective expression of T-cell CD40 ligand causes X-linked immunodeficiency with hyper-IgM. Nature. 1993 Feb 11;361(6412):539-41. [PubMed Link Image]
  7. Allen RC, Armitage RJ, Conley ME, Rosenblatt H, Jenkins NA, Copeland NG, Bedell MA, Edelhoff S, Disteche CM, Simoneaux DK, et al.: CD40 ligand gene defects responsible for X-linked hyper-IgM syndrome. Science. 1993 Feb 12;259(5097):990-3. [PubMed Link Image]
  8. Macchi P, Villa A, Strina D, Sacco MG, Morali F, Brugnoni D, Giliani S, Mantuano E, Fasth A, Andersson B, et al.: Characterization of nine novel mutations in the CD40 ligand gene in patients with X-linked hyper IgM syndrome of various ancestry. Am J Hum Genet. 1995 Apr;56(4):898-906. [PubMed Link Image]
  9. DiSanto JP, Bonnefoy JY, Gauchat JF, Fischer A, de Saint Basile G: CD40 ligand mutations in x-linked immunodeficiency with hyper-IgM. Nature. 1993 Feb 11;361(6412):541-3. [PubMed Link Image]
  10. Lin Q, Rohrer J, Allen RC, Larche M, Greene JM, Shigeoka AO, Gatti RA, Derauf DC, Belmont JW, Conley ME: A single strand conformation polymorphism study of CD40 ligand. Efficient mutation analysis and carrier detection for X-linked hyper IgM syndrome. J Clin Invest. 1996 Jan 1;97(1):196-201. [PubMed Link Image]
  11. 8589998 Karpusas M, Hsu YM, Wang JH, Thompson J, Lederman S, Chess L, Thomas D: 2 A crystal structure of an extracellular fragment of human CD40 ligand. Structure. 1995 Oct 15;3(10):1031-9.
  12. 8626375 Pietravalle F, Lecoanet-Henchoz S, Blasey H, Aubry JP, Elson G, Edgerton MD, Bonnefoy JY, Gauchat JF: Human native soluble CD40L is a biologically active trimer, processed inside microsomes. J Biol Chem. 1996 Mar 15;271(11):5965-7.
  13. 9150729 Nonoyama S, Shimadzu M, Toru H, Seyama K, Nunoi H, Neubauer M, Yata J, Och HD: Mutations of the CD40 ligand gene in 13 Japanese patients with X-linked hyper-IgM syndrome. Hum Genet. 1997 May;99(5):624-7.
  14. 9605317 Singh J, Garber E, Van Vlijmen H, Karpusas M, Hsu YM, Zheng Z, Naismith JH, Thomas D: The role of polar interactions in the molecular recognition of CD40L with its receptor CD40. Protein Sci. 1998 May;7(5):1124-35.
Target 11 Drug References
  1. Kinlay S, Schwartz GG, Olsson AG, Rifai N, Sasiela WJ, Szarek M, Ganz P, Libby P: Effect of atorvastatin on risk of recurrent cardiovascular events after an acute coronary syndrome associated with high soluble CD40 ligand in the Myocardial Ischemia Reduction with Aggressive Cholesterol Lowering (MIRACL) Study. Circulation. 2004 Jul 27;110(4):386-91. Epub 2004 Jul 19. [PubMed Link Image]
  2. Hwang YS, Tsai WC, Lu YH, Lin CC, Chen YF: Effect of atorvastatin on the expression of CD40 ligand and P-selectin on platelets in patients with hypercholesterolemia. Am J Cardiol. 2004 Aug 1;94(3):364-6. [PubMed Link Image]
  3. Sanguigni V, Pignatelli P, Lenti L, Ferro D, Bellia A, Carnevale R, Tesauro M, Sorge R, Lauro R, Violi F: Short-term treatment with atorvastatin reduces platelet CD40 ligand and thrombin generation in hypercholesterolemic patients. Circulation. 2005 Feb 1;111(4):412-9. [PubMed Link Image]
  4. Mosheimer BA, Kaneider NC, Feistritzer C, Djanani A, Sturn DH, Patsch JR, Wiedermann CJ: CD40-ligand-dependent induction of COX-2 gene expression in endothelial cells by activated platelets: inhibitory effects of atorvastatin. Blood Coagul Fibrinolysis. 2005 Mar;16(2):105-10. [PubMed Link Image]
  5. Zineh I, Welder GJ, DeBella AE, Arant CB, Wessel TR, Schofield RS: Atorvastatin effect on circulating and leukocyte-produced CD40 ligand concentrations in people with normal cholesterol levels: a pilot study. Pharmacotherapy. 2006 Nov;26(11):1572-7. [PubMed Link Image]
Drug Target 12 [top]
Target 12 ID 1649
Target 12 Name Small inducible cytokine A2
Target 12 Synonyms
  1. CCL2
  2. HC11
  3. MCAF
  4. MCP-1
  5. Monocyte chemoattractant protein 1
  6. Monocyte chemotactic and activating factor
  7. Monocyte chemotactic protein 1
  8. Monocyte secretory protein JE
  9. Small inducible cytokine A2 precursor
Target 12 Gene Name CCL2
Target 12 Protein Sequence >Small inducible cytokine A2 precursor
MKVSAALLCLLLIAATFIPQGLAQPDAINAPVTCCYNFTNRKISVQRLASYRRITSSKCP
KEAVIFKTIVAKEICADPKQKWVQDSMDHLDKQTQTPKT
Target 12 Number of Residues 100
Target 12 Molecular Weight 11025
Target 12 Theoretical pI 9.72
Target 12 GO Classification
Function
signal transducer activity
receptor binding
cytokine activity
chemokine activity
Process
response to stimulus
response to biotic stimulus
defense response
immune response
Component
cell
membrane
extracellular region
Target 12 General Function Involved in chemokine activity
Target 12 Specific Function Chemotactic factor that attracts monocytes and basophils but not neutrophils or eosinophils. Augments monocyte anti-tumor activity. Has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis or atherosclerosis. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis
Target 12 Pathways Not Available
Target 12 Reactions Not Available
Target 12 Pfam Domain Function
Target 12 Signals
  • 1-23
Target 12 Transmembrane Regions
  • None
Target 12 Essentiality Non-Essential
Target 12 GenBank ID Protein 307163 Link Image
Target 12 UniProtKB/Swiss-Prot ID P13500 Link Image
Target 12 UniProtKB/Swiss-Prot Entry Name CCL2_HUMAN Link Image
Target 12 PDB ID 1DON Link Image
Target 12 PDB File Show
Target 12 3D Structure
Target 12 Cellular Location
  • Secreted protein
Target 12 Gene Sequence >300 bp
ATGAAAGTCTCTGCCGCCCTTCTGTGCCTGCTGCTCATAGCAGCCACCTTCATTCCCCAA
GGGCTCGCTCAGCCAGATGCAATCAATGCCCCAGTCACCTGCTGTTATAACTTCACCAAT
AGGAAGATCTCAGTGCAGAGGCTCGCGAGCTATAGAAGAATCACCAGCAGCAAGTGTCCC
AAAGAAGCTGTGATCTTCAAGACCATTGTGGCCAAGGAGATCTGTGCTGACCCCAAGCAG
AAGTGGGTTCAGGATTCCATGGACCACCTGGACAAGCAAACCCAAACTCCGAAGACTTGA
Target 12 GenBank Gene ID
Target 12 GeneCard ID CCL2 Link Image
Target 12 GenAtlas ID CCL2 Link Image
Target 12 HGNC ID HGNC:10618 Link Image
Target 12 Chromosome Location 17
Target 12 Locus 17q11.2-q12
Target 12 SNPs SNPJam Report Link Image
Target 12 General References
  1. Finzer P, Soto U, Delius H, Patzelt A, Coy JF, Poustka A, zur Hausen H, Rosl F: Differential transcriptional regulation of the monocyte-chemoattractant protein-1 (MCP-1) gene in tumorigenic and non-tumorigenic HPV 18 positive cells: the role of the chromatin structure and AP-1 composition. Oncogene. 2000 Jul 6;19(29):3235-44. [PubMed Link Image]
  2. Yoshimura T, Leonard EJ: Human monocyte chemoattractant protein-1 (MCP-1). Adv Exp Med Biol. 1991;305:47-56. [PubMed Link Image]
  3. Gronenborn AM, Clore GM: Modeling the three-dimensional structure of the monocyte chemo-attractant and activating protein MCAF/MCP-1 on the basis of the solution structure of interleukin-8. Protein Eng. 1991 Feb;4(3):263-9. [PubMed Link Image]
  4. Rollins BJ, Morton CC, Ledbetter DH, Eddy RL Jr, Shows TB: Assignment of the human small inducible cytokine A2 gene, SCYA2 (encoding JE or MCP-1), to 17q11.2-12: evolutionary relatedness of cytokines clustered at the same locus. Genomics. 1991 Jun;10(2):489-92. [PubMed Link Image]
  5. Decock B, Conings R, Lenaerts JP, Billiau A, Van Damme J: Identification of the monocyte chemotactic protein from human osteosarcoma cells and monocytes: detection of a novel N-terminally processed form. Biochem Biophys Res Commun. 1990 Mar 30;167(3):904-9. [PubMed Link Image]
  6. Shyy YJ, Li YS, Kolattukudy PE: Structure of human monocyte chemotactic protein gene and its regulation by TPA. Biochem Biophys Res Commun. 1990 Jun 15;169(2):346-51. [PubMed Link Image]
  7. Yoshimura T, Yuhki N, Moore SK, Appella E, Lerman MI, Leonard EJ: Human monocyte chemoattractant protein-1 (MCP-1). Full-length cDNA cloning, expression in mitogen-stimulated blood mononuclear leukocytes, and sequence similarity to mouse competence gene JE. FEBS Lett. 1989 Feb 27;244(2):487-93. [PubMed Link Image]
  8. Rollins BJ, Stier P, Ernst T, Wong GG: The human homolog of the JE gene encodes a monocyte secretory protein. Mol Cell Biol. 1989 Nov;9(11):4687-95. [PubMed Link Image]
  9. Chang HC, Hsu F, Freeman GJ, Griffin JD, Reinherz EL: Cloning and expression of a gamma-interferon-inducible gene in monocytes: a new member of a cytokine gene family. Int Immunol. 1989;1(4):388-97. [PubMed Link Image]
  10. Robinson EA, Yoshimura T, Leonard EJ, Tanaka S, Griffin PR, Shabanowitz J, Hunt DF, Appella E: Complete amino acid sequence of a human monocyte chemoattractant, a putative mediator of cellular immune reactions. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1850-4. [PubMed Link Image]
  11. 2923622 Furutani Y, Nomura H, Notake M, Oyamada Y, Fukui T, Yamada M, Larsen CG, Oppenheim JJ, Matsushima K: Cloning and sequencing of the cDNA for human monocyte chemotactic and activating factor (MCAF). Biochem Biophys Res Commun. 1989 Feb 28;159(1):249-55.
  12. 8107690 Li YS, Shyy YJ, Wright JG, Valente AJ, Cornhill JF, Kolattukudy PE: The expression of monocyte chemotactic protein (MCP-1) in human vascular endothelium in vitro and in vivo. Mol Cell Biochem. 1993 Sep 8;126(1):61-8.
  13. 8195247 Zhang YJ, Rutledge BJ, Rollins BJ: Structure/activity analysis of human monocyte chemoattractant protein-1 (MCP-1) by mutagenesis. Identification of a mutated protein that inhibits MCP-1-mediated monocyte chemotaxis. J Biol Chem. 1994 Jun 3;269(22):15918-24.
  14. 8627182 Weber M, Uguccioni M, Baggiolini M, Clark-Lewis I, Dahinden CA: Deletion of the NH2-terminal residue converts monocyte chemotactic protein 1 from an activator of basophil mediator release to an eosinophil chemoattractant. J Exp Med. 1996 Feb 1;183(2):681-5.
  15. 8639605 Handel TM, Domaille PJ: Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure of the monocyte chemoattractant protein-1 (MCP-1) dimer. Biochemistry. 1996 May 28;35(21):6569-84.
  16. 8898111 Kim KS, Rajarathnam K, Clark-Lewis I, Sykes BD: Structural characterization of a monomeric chemokine: monocyte chemoattractant protein-3. FEBS Lett. 1996 Oct 21;395(2-3):277-82.
  17. 8989326 Lubkowski J, Bujacz G, Boque L, Domaille PJ, Handel TM, Wlodawer A: The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions. Nat Struct Biol. 1997 Jan;4(1):64-9.
Target 12 Drug References
  1. Kowalski J, Okopien B, Madej A, Zielinski M, Belowski D, Kalina Z, Herman ZS: Effects of atorvastatin, simvastatin, and fenofibrate therapy on monocyte chemoattractant protein-1 secretion in patients with hyperlipidemia. Eur J Clin Pharmacol. 2003 Jul;59(3):189-93. Epub 2003 May 17. [PubMed Link Image]
  2. Xu ZM, Zhao SP, Li QZ, Nie S, Zhou HN: Atorvastatin reduces plasma MCP-1 in patients with acute coronary syndrome. Clin Chim Acta. 2003 Dec;338(1-2):17-24. [PubMed Link Image]
  3. Grip O, Janciauskiene S, Lindgren S: Circulating monocytes and plasma inflammatory biomarkers in active Crohn's disease: elevated oxidized low-density lipoprotein and the anti-inflammatory effect of atorvastatin. Inflamm Bowel Dis. 2004 May;10(3):193-200. [PubMed Link Image]
  4. Okopien B, Krysiak R, Haberka M, Herman ZS: Effect of monthly atorvastatin and fenofibrate treatment on monocyte chemoattractant protein-1 release in patients with primary mixed dyslipidemia. J Cardiovasc Pharmacol. 2005 Apr;45(4):314-20. [PubMed Link Image]
  5. Barsante MM, Roffe E, Yokoro CM, Tafuri WL, Souza DG, Pinho V, Castro MS, Teixeira MM: Anti-inflammatory and analgesic effects of atorvastatin in a rat model of adjuvant-induced arthritis. Eur J Pharmacol. 2005 Jun 15;516(3):282-9. [PubMed Link Image]
Drug Target 13 [top]
Target 13 ID 1694
Target 13 Name Angiotensinogen
Target 13 Synonyms
  1. Angiotensinogen precursor
  2. Serpin A8
Target 13 Gene Name AGT
Target 13 Protein Sequence >Angiotensinogen precursor
MRKRAPQSEMAPAGVSLRATILCLLAWAGLAAGDRVYIHPFHLVIHNESTCEQLAKANAG
KPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGM
HSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKV
LSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLD
FTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEF
WVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVTQVPFTESACLLLIQPHYASDLDKVEGLT
FQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPAILHTELNLQKLSNDRIR
VGEVLNSIFFELEADEREPTESTQQLNKPEVLEVTLNRPFLFAVYDQSATALHFLGRVAN
PLSTA
Target 13 Number of Residues 493
Target 13 Molecular Weight 53155
Target 13 Theoretical pI 6.27
Target 13 GO Classification
Function
enzyme regulator activity
enzyme inhibitor activity
protease inhibitor activity
endopeptidase inhibitor activity
serine-type endopeptidase inhibitor activity
Process
Not Available
Component
Not Available
Target 13 General Function Involved in serine-type endopeptidase inhibitor activity
Target 13 Specific Function Angiotensin-3 stimulates aldosterone release
Target 13 Pathways Not Available
Target 13 Reactions Not Available
Target 13 Pfam Domain Function
Target 13 Signals
  • 1-33
Target 13 Transmembrane Regions
  • None
Target 13 Essentiality Non-Essential
Target 13 GenBank ID Protein 178640 Link Image
Target 13 UniProtKB/Swiss-Prot ID P01019 Link Image
Target 13 UniProtKB/Swiss-Prot Entry Name ANGT_HUMAN Link Image
Target 13 PDB ID Not Available
Target 13 Cellular Location
  • Secreted protein
Target 13 Gene Sequence >1458 bp
ATGCGGAAGCGAGCACCCCAGTCTGAGATGGCTCCTGCCGGTGTGAGCCTGAGGGCCACC
ATCCTCTGCCTCCTGGCCTGGGCTGGCCTGGCTGCAGGTGACCGGGTGTACATACACCCC
TTCCACCTCGTCATCCACAATGAGAGTACCTGTGAGCAGCTGGCAAAGGCCAATGCCGGG
AAGCCCAAAGACCCCACCTTCATACCTGCTCCAATTCAGGCCAAGACATCCCCTGTGGAT
GAAAAGGCCCTACAGGACCAGCTGGTGCTAGTCGCTGCAAAACTTGACACCGAAGACAAG
TTGAGGGCCGCAATGGTCGGGATGCTGGCCAACTTCTTGGGCTTCCGTATATATGGCATG
CACAGTGAGCTATGGGGCGTGGTCCATGGGGCCACCGTCCTCTCCCCAACGGCTGTCTTT
GGCACCCTGGCCTCTCTCTATCTGGGAGCCTTGGACCACACAGCTGACAGGCTACAGGCA
ATCCTGGGTGTTCCTTGGAAGGACAAGAACTGCACCTCCCGGCTGGATGCGCACAAGGTC
CTGTCTGCCCTGCAGGCTGTACAGGGCCTGCTAGTGGCCCAGGGCAGGGCTGATAGCCAG
GCCCAGCTGCTGCTGTCCACGGTGGTGGGCGTGTTCACAGCCCCAGGCCTGCACCTGAAG
CAGCCGTTTGTGCAGGGCCTGGCTCTCTATACCCCTGTGGTCCTCCCACGCTCTCTGGAC
TTCACAGAACTGGATGTTGCTGCTGAGAAGATTGACAGGTTCATGCAGGCTGTGACAGGA
TGGAAGACTGGCTGCTCCCTGATGGGAGCCAGTGTGGACAGCACCCTGGCTTTCAACACC
TACGTCCACTTCCAAGGGAAGATGAAGGGCTTCTCCCTGCTGGCCGAGCCCCAGGAGTTC
TGGGTGGACAACAGCACCTCAGTGTCTGTTCCCATGCTCTCTGGCATGGGCACCTTCCAG
CACTGGAGTGACATCCAGGACAACTTCTCGGTGACTCAAGTGCCCTTCACTGAGAGCGCC
TGCCTGCTGCTGATCCAGCCTCACTATGCCTCTGACCTGGACAAGGTGGAGGGTCTCACT
TTCCAGCAAAACTCCCTCAACTGGATGAAGAAACTGTCTCCCCGGACCATCCACCTGACC
ATGCCCCAACTGGTGCTGCAAGGATCTTATGACCTGCAGGACCTGCTCGCCCAGGCTGAG
CTGCCCGCCATTCTGCACACCGAGCTGAACCTGCAAAAATTGAGCAATGACCGCATCAGG
GTGGGGGAGGTGCTGAACAGCATTTTTTTTGAGCTTGAAGCGGATGAGAGAGAGCCCACA
GAGTCTACCCAACAGCTTAACAAGCCTGAGGTCTTGGAGGTGACCCTGAACCGCCCATTC
CTGTTTGCTGTGTATGATCAAAGCGCCACTGCCCTGCACTTCCTGGGCCGCGTGGCCAAC
CCGCTGAGCACAGCATGA
Target 13 GenBank Gene ID
Target 13 GeneCard ID AGT Link Image
Target 13 GenAtlas ID AGT Link Image
Target 13 HGNC ID HGNC:333 Link Image
Target 13 Chromosome Location 1
Target 13 Locus 1q42-q43
Target 13 SNPs SNPJam Report Link Image
Target 13 General References
  1. Goodfriend TL, Peach MJ: Angiotensin III: (DES-Aspartic Acid-1)-Angiotensin II. Evidence and speculation for its role as an important agonist in the renin - angiotensin system. Circ Res. 1975 Jun;36(6 Suppl 1):38-48. [PubMed Link Image]
  2. Jeunemaitre X, Soubrier F, Kotelevtsev YV, Lifton RP, Williams CS, Charru A, Hunt SC, Hopkins PN, Williams RR, Lalouel JM, et al.: Molecular basis of human hypertension: role of angiotensinogen. Cell. 1992 Oct 2;71(1):169-80. [PubMed Link Image]
  3. Fukamizu A, Takahashi S, Seo MS, Tada M, Tanimoto K, Uehara S, Murakami K: Structure and expression of the human angiotensinogen gene. Identification of a unique and highly active promoter. J Biol Chem. 1990 May 5;265(13):7576-82. [PubMed Link Image]
  4. Kunapuli SP, Kumar A: Molecular cloning of human angiotensinogen cDNA and evidence for the presence of its mRNA in rat heart. Circ Res. 1987 May;60(5):786-90. [PubMed Link Image]
  5. Gaillard I, Clauser E, Corvol P: Structure of human angiotensinogen gene. DNA. 1989 Mar;8(2):87-99. [PubMed Link Image]
  6. Kunapuli SP, Benedict CR, Kumar A: Tissue specific hormonal regulation of the rat angiotensinogen gene expression. Arch Biochem Biophys. 1987 May 1;254(2):642-6. [PubMed Link Image]
  7. Campbell DJ, Bouhnik J, Coezy E, Menard J, Corvol P: Processing of rat and human angiotensinogen precursors by microsomal membranes. Mol Cell Endocrinol. 1985 Nov;43(1):31-40. [PubMed Link Image]
  8. Arakawa K, Minohara A, Yamada J, Nakamura M: Enzymatic degradation and electrophoresis of human angiotensin I. Biochim Biophys Acta. 1968 Sep 10;168(1):106-12. [PubMed Link Image]
  9. Kageyama R, Ohkubo H, Nakanishi S: Primary structure of human preangiotensinogen deduced from the cloned cDNA sequence. Biochemistry. 1984 Jul 31;23(16):3603-9. [PubMed Link Image]
  10. Tewksbury DA, Dart RA, Travis J: The amino terminal amino acid sequence of human angiotensinogen. Biochem Biophys Res Commun. 1981 Apr 30;99(4):1311-5. [PubMed Link Image]
  11. 7539791 Oxvig C, Haaning J, Kristensen L, Wagner JM, Rubin I, Stigbrand T, Gleich GJ, Sottrup-Jensen L: Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma. J Biol Chem. 1995 Jun 9;270(23):13645-51.
  12. 7607642 Hixson JE, Powers PK: Detection and characterization of new mutations in the human angiotensinogen gene (AGT). Hum Genet. 1995 Jul;96(1):110-2.
  13. 7744780 Inoue I, Rohrwasser A, Helin C, Jeunemaitre X, Crain P, Bohlender J, Lifton RP, Corvol P, Ward K, Lalouel JM: A mutation of angiotensinogen in a patient with preeclampsia leads to altered kinetics of the renin-angiotensin system. J Biol Chem. 1995 May 12;270(19):11430-6.
  14. 8513325 Ward K, Hata A, Jeunemaitre X, Helin C, Nelson L, Namikawa C, Farrington PF, Ogasawara M, Suzumori K, Tomoda S, et al.: A molecular variant of angiotensinogen associated with preeclampsia. Nat Genet. 1993 May;4(1):59-61.
  15. 8621667 Gimenez-Roqueplo AP, Leconte I, Cohen P, Simon D, Guyene TT, Celerier J, Pau B, Corvol P, Clauser E, Jeunemaitre X: The natural mutation Y248C of human angiotensinogen leads to abnormal glycosylation and altered immunological recognition of the protein. J Biol Chem. 1996 Apr 19;271(16):9838-44.
  16. 9492317 Carpenter KA, Wilkes BC, Schiller PW: The octapeptide angiotensin II adopts a well-defined structure in a phospholipid environment. Eur J Biochem. 1998 Jan 15;251(1-2):448-53.
Target 13 Drug References
  1. Maack C, Kartes T, Kilter H, Schafers HJ, Nickenig G, Bohm M, Laufs U: Oxygen free radical release in human failing myocardium is associated with increased activity of rac1-GTPase and represents a target for statin treatment. Circulation. 2003 Sep 30;108(13):1567-74. Epub 2003 Sep 8. [PubMed Link Image]
  2. Kalayci R, Kaya M, Elmas I, Arican N, Ahishali B, Uzun H, Bilgic B, Kucuk M, Kudat H: Effects of atorvastatin on blood-brain barrier permeability during L-NAME hypertension followed by angiotensin-II in rats. Brain Res. 2005 May 3;1042(2):184-93. [PubMed Link Image]
  3. Martin J, Denver R, Bailey M, Krum H: In vitro inhibitory effects of atorvastatin on cardiac fibroblasts: implications for ventricular remodelling. Clin Exp Pharmacol Physiol. 2005 Sep;32(9):697-701. [PubMed Link Image]
  4. Wang D, Hirase T, Inoue T, Node K: Atorvastatin inhibits angiotensin II-induced T-type Ca2+ channel expression in endothelial cells. Biochem Biophys Res Commun. 2006 Aug 25;347(2):394-400. Epub 2006 Jun 22. [PubMed Link Image]
  5. Schindler C, Brosnihan KB, Ferrario CM, Bramlage P, Maywald U, Koch R, Oertel R, Kirch W: Comparison of inhibitory effects of irbesartan and atorvastatin treatment on the renin angiotensin system (RAS) in veins: a randomized double-blind crossover trial in healthy subjects. J Clin Pharmacol. 2007 Jan;47(1):112-20. [PubMed Link Image]
Drug Target 14 [top]
Target 14 ID 1885
Target 14 Name Collagen alpha-1(XIII) chain
Target 14 Synonyms
  1. COLXIIIA1
  2. XIII
Target 14 Gene Name COL13A1
Target 14 Protein Sequence >Collagen alpha-1(XIII) chain
MVAERTHKAAATGARGPGELGAPGTVALVAARAERGARLPSPGSCGLLTLALCSLALSLL
AHFRTAELQARVLRLEAERGEQQMETAILGRVNQLLDEKWKLHSRRRREAPKTSPGCNCP
PGPPGPTGRPGLPGDKGAIGMPGRVGSPGDAGLSIIGPRGPPGQPGTRGFPGFPGPIGLD
GKPGHPGPKGDMGLTGPPGQPGPQGQKGEKGQCGEYPHRECLSSMPAALRSSQIIALKLL
PLLNSVRLAPPPVIKRRTFQGEQSQASIQGPPGPPGPPGPSGPLGHPGLPGPMGPPGLPG
PPGPKGDPGIQGYHGRKGERGMPGMPGKHGAKGAPGIAVAGMKGEPGIPGTKGEKGAEGS
PGLPGLLGQKGEKGDAGNSIGGGRGEPGPPGLPGPPGPKGEAGVDGQVGPPGQPGDKGER
GAAGEQGPDGPKGSKGEPGKGEMVDYNGNINEALQEIRTLALMGPPGLPGQIGPPGAPGI
PGQKGEIGLPGPPGHDGEKGPRGKPGDMGPPGPQGPPGKDGPPGVKGENGHPGSPGEKGE
KGETGQAGSPGEKGEAGEKGNPGAEVPGLPGPEGPPGPPGLQGVPGPKGEAGLDGAKGEK
GFQGEKGDRGPLGLPGASGLDGRPGPPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAA
GLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLDAPCPLGEDGLPVQGCWNK
Target 14 Number of Residues 728
Target 14 Molecular Weight 69951
Target 14 Theoretical pI 9.82
Target 14 GO Classification
Function
Not Available
Process
physiological process
cellular physiological process
transport
ion transport
anion transport
inorganic anion transport
phosphate transport
Component
cell
intracellular
cytoplasm
Target 14 General Function Translation, ribosomal structure and biogenesis
Target 14 Specific Function Involved in cell-matrix and cell-cell adhesion interactions that are required for normal development. May participate in the linkage between muscle fiber and basement membrane. May play a role in endochondral ossification of bone and branching morphogenesis of lung. Binds heparin
Target 14 Pathways Not Available
Target 14 Reactions Not Available
Target 14 Pfam Domain Function
Target 14 Signals
  • None
Target 14 Transmembrane Regions
  • 45-61
Target 14 Essentiality Non-Essential
Target 14 GenBank ID Protein 9650749 Link Image
Target 14 UniProtKB/Swiss-Prot ID Q5TAT6 Link Image
Target 14 UniProtKB/Swiss-Prot Entry Name CODA1_HUMAN Link Image
Target 14 PDB ID Not Available
Target 14 Cellular Location
  • Cell membrane
  • single-pass type II membrane protein
Target 14 Gene Sequence >2154 bp
ATGGTAGCGGAGCGCACCCACAAAGCGGCAGCCACCGGTGCCCGCGGCCCTGGGGAGTTG
GGCGCGCCCGGGACGGTGGCTCTGGTGGCGGCGCGGGCGGAGCGCGGCGCACGGCTGCCG
AGTCCAGGGTCGTGCGGGCTGCTGACGCTGGCCCTCTGCTCGCTGGCACTCAGCCTGCTC
GCCCACTTTCGGACGGCCGAGCTGCAGGCCCGGGTGCTGCGCCTGGAAGCGGAGCGCGGG
GAGCAGCAAATGGAGACAGCTATTTTGGGACGAGTCAATCAACTGCTGGACGAGAAATGG
AAGCTCCACTCAAGGAGGCGCCGGGAGGCCCCAAAGACATCTCCAGGATGTAACTGCCCA
CCAGGACCTCCTGGTCCCACTGGAAGACCCGGACTCCCAGGGGACAAAGGTGCCATTGGG
ATGCCTGGACGTGTGGGGTCCCCCGGAGACGCTGGGCTGTCCATCATTGGTCCCCGCGGC
CCCCCTGGTCAACCAGGCACTAGAGGTTTCCCTGGATTTCCGGGTCCCATTGGGCTGGAC
GGCAAACCGGGCCACCCAGGACCAAAGGGCGACATGGGTCTGACGGGTCCCCCAGGACAG
CCGGGACCCCAGGGACAAAAAGGAGAAAAGGGTCAGTGTGGAGAGTACCCACACCGGGAG
TGCCTAAGCAGCATGCCAGCAGCTCTGCGCTCCAGCCAGATAATTGCCCTGAAGCTGCTG
CCTCTCCTCAATTCAGTGCGACTGGCTCCACCCCCGGTCATAAAAAGGCGGACATTCCAG
GGCGAACAGAGCCAGGCCAGCATCCAAGGTCCACCAGGGCCCCCAGGCCCCCCTGGACCA
AGTGGACCTCTGGGGCACCCAGGACTGCCAGGGCCTATGGGGCCACCTGGCTTACCTGGG
CCTCCTGGACCAAAGGGAGACCCAGGGATCCAGGGCTACCACGGCCGGAAGGGAGAACGG
GGCATGCCAGGGATGCCAGGCAAGCATGGAGCCAAGGGGGCGCCCGGAATTGCCGTGGCT
GGGATGAAGGGTGAGCCAGGGATCCCAGGAACCAAGGGTGAGAAGGGGGCTGAAGGCTCC
CCTGGGCTTCCTGGCCTCCTGGGGCAGAAGGGAGAGAAAGGCGATGCTGGCAACTCCATT
GGAGGAGGCAGAGGGGAACCTGGCCCTCCAGGGCTCCCTGCGCCCCCAGGGCCAAAGGGA
GAAGCAGGTGTCGATGGCCAGGTTGGCCCCCCAGGGCAGCCAGGAGACAAGGGGGAGCGT
GGAGCAGCTGGAGAACAGGGACCAGATGGCCCCAAGGGCTCCAAGGGAGAACCAGGGAAA
GGAGAGATGGTGGATTACAATGGAAACATCAATGAGGCTCTCCAGGAGATCCGGACGCTG
GCCTTGATGGGGCCTCCTGGTCTTCCTGGGCAAATTGGCCCACCTGGAGCTCCAGGGATT
CCAGGCCAGAAGGGGGAGATTGGACTGCCAGGCCCTCCAGGACACGATGGGGAAAAGGGA
CCTCGCGGTAAACCAGGAGACATGGGCCCTCCTGGTCCCCAAGGCCCCCCAGGAAAGGAT
GGACCTCCAGGAGTGAAGGGAGAAAACGGGCACCCAGGGAGCCCAGGAGAGAAGGGGGAA
AAAGGGGAGACAGGACAAGCAGGCTCACCGGGAGAGAAAGGAGAAGCCGGGGAGAAGGGC
AATCCAGGAGCAGAGGTTCCTGGGCTGCCAGGGCCAGAGGGGCCTCCCGGACCTCCGGGG
CTCCAAGGTGTTCCTGGACCAAAGGGGGAAGCAGGACTAGATGGAGCAAAAGGAGAGAAA
GGCTTCCAGGGAGAAAAAGGAGACCGTGGTCCCCTGGGACTACCCGGAGCTTCAGGTTTG
GACGGCAGGCCTGGGCCACCGGGTACTCCAGGACCAATTGGAGTTCCAGGCCCAGCGGGA
CCAAAGGGCGAGAGGGGCAGCAAAGGAGACCCTGGGATGACAGGACCAACGGGAGCAGCT
GGGCTTCCTGGTTTACATGGACCACCCGGGGACAAGGGAAACCGGGGGGAGAGGGGGAAG
AAAGGCTCTAGAGGGCCTAAAGGGGACAAGGGAGACCAAGGAGCGCCTGGATTAGATGCC
CCCTGCCCATTGGGCGAAGATGGCTTACCAGTCCAAGGCTGCTGGAACAAGTGA
Target 14 GenBank Gene ID
Target 14 GeneCard ID COL13A1 Link Image
Target 14 GenAtlas ID COL13A1 Link Image
Target 14 HGNC ID HGNC:2190 Link Image
Target 14 Chromosome Location 10
Target 14 Locus 10q22
Target 14 SNPs SNPJam Report Link Image
Target 14 General References
  1. Pihlajaniemi T, Tamminen M: The alpha 1 chain of type XIII collagen consists of three collagenous and four noncollagenous domains, and its primary transcript undergoes complex alternative splicing. J Biol Chem. 1990 Oct 5;265(28):16922-8. [PubMed Link Image]
  2. Tikka L, Pihlajaniemi T, Henttu P, Prockop DJ, Tryggvason K: Gene structure for the alpha 1 chain of a human short-chain collagen (type XIII) with alternatively spliced transcripts and translation termination codon at the 5' end of the last exon. Proc Natl Acad Sci U S A. 1988 Oct;85(20):7491-5. [PubMed Link Image]
  3. Pihlajaniemi T, Myllyla R, Seyer J, Kurkinen M, Prockop DJ: Partial characterization of a low molecular weight human collagen that undergoes alternative splicing. Proc Natl Acad Sci U S A. 1987 Feb;84(4):940-4. [PubMed Link Image]
Target 14 Drug References
  1. Tian JW, Zhao LY, Wang SW, Zhang HT, Zheng QS, Yang XD, Xu L, Fan YH: [Effects of atorvastatin on the proliferation and collagen synthesis of rat cardiac fibroblasts] Zhonghua Yi Xue Za Zhi. 2003 Jan 25;83(2):118-22. [PubMed Link Image]
  2. McGinn S, Poronnik P, Gallery ED, Pollock CA: The effects of high glucose and atorvastatin on endothelial cell matrix production. Diabet Med. 2004 Oct;21(10):1102-7. [PubMed Link Image]
  3. Martin J, Denver R, Bailey M, Krum H: In vitro inhibitory effects of atorvastatin on cardiac fibroblasts: implications for ventricular remodelling. Clin Exp Pharmacol Physiol. 2005 Sep;32(9):697-701. [PubMed Link Image]
  4. Solem J, Levin M, Karlsson T, Grip L, Albertsson P, Wiklund O: Composition of coronary plaques obtained by directional atherectomy in stable angina: its relation to serum lipids and statin treatment. J Intern Med. 2006 Mar;259(3):267-75. [PubMed Link Image]
  5. Ruiz-Gaspa S, Nogues X, Enjuanes A, Monllau JC, Blanch J, Carreras R, Mellibovsky L, Grinberg D, Balcells S, Diez-Perez A, Pedro-Botet J: Simvastatin and atorvastatin enhance gene expression of collagen type 1 and osteocalcin in primary human osteoblasts and MG-63 cultures. J Cell Biochem. 2007 Aug 15;101(6):1430-8. [PubMed Link Image]
Drug Target 15 [top]
Target 15 ID 2170
Target 15 Name Transforming protein RhoA
Target 15 Synonyms
  1. H12
  2. Transforming protein RhoA precursor
Target 15 Gene Name RHOA
Target 15 Protein Sequence >Transforming protein RhoA precursor
MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDT
AGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKD
LRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQ
ARRGKKKSGCLVL
Target 15 Number of Residues 196
Target 15 Molecular Weight 21768
Target 15 Theoretical pI 5.89
Target 15 GO Classification
Function
binding
nucleotide binding
purine nucleotide binding
guanyl nucleotide binding
GTP binding
Process
cellular process
cell communication
signal transduction
intracellular signaling cascade
small GTPase mediated signal transduction
Component
Not Available
Target 15 General Function Involved in GTP binding
Target 15 Specific Function Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. May be an activator of PLCE1
Target 15 Pathways Not Available
Target 15 Reactions Not Available
Target 15 Pfam Domain Function
Target 15 Signals
  • None
Target 15 Transmembrane Regions
  • None
Target 15 Essentiality Non-Essential
Target 15 GenBank ID Protein 36030 Link Image
Target 15 UniProtKB/Swiss-Prot ID P61586 Link Image
Target 15 UniProtKB/Swiss-Prot Entry Name RHOA_HUMAN Link Image
Target 15 PDB ID 1X86 Link Image
Target 15 PDB File Show
Target 15 3D Structure
Target 15 Cellular Location
  • Membrane
  • lipid-anchor
Target 15 Gene Sequence >582 bp
ATGGCTGCCATCCGGAAGAAACTGGTGATTGTTGGTGATGGAGCCTGTGGAAAGACATGC
TTGCTCATAGTCTTCAGCAAGGACCAGTTCCCAGAGGTGTATGTGCCCACAGTGTTTGAG
AACTATGTGGCAGATATCGAGGTGGATGGAAAGCAGGTAGAGTTGGCTTTGTGGGACACA
GCTGGGCAGGAAGATTATGATCGCCTGAGGCCCCTCTCCTACCCAGATACCGATGTTATA
CTGATGTGTTTTTCCATCGACAGCCCTGATAGTTTAGAAAACATCCCAGAAAAGTGGACC
CCAGAAGTCAAGCATTTCTGTCCCAACGTGCCCATCATCCTGGTTGGGAATAAGAAGGAT
CTTCGGAATGATGAGCACACAAGGCGGGAGCTAGCCAAGATGAAGCAGGAGCCGGTGAAA
CCTGAAGAAGGCAGAGATATGGCAAACAGGATTGGCGCTTTTGGGTACATGGAGTGTTCA
GCAAAGACCAAAGATGGAGTGAGAGAGGTTTTTGAAATGGCTACGAGAGCTGCTCTGCAA
GCTAGACGTGGGAAGAAAAAATCTGGTTGCCTTGTCTTGTGA
Target 15 GenBank Gene ID
Target 15 GeneCard ID RHOA Link Image
Target 15 GenAtlas ID RHOA Link Image
Target 15 HGNC ID HGNC:667 Link Image
Target 15 Chromosome Location 3
Target 15 Locus 3p21.3
Target 15 SNPs SNPJam Report Link Image
Target 15 General References
  1. Reynaud C, Fabre S, Jalinot P: The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element. J Biol Chem. 2000 Oct 27;275(43):33962-8. [PubMed Link Image]
  2. 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]
  3. Shao F, Merritt PM, Bao Z, Innes RW, Dixon JE: A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis. Cell. 2002 May 31;109(5):575-88. [PubMed Link Image]
  4. Shao F, Vacratsis PO, Bao Z, Bowers KE, Fierke CA, Dixon JE: Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases. Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):904-9. Epub 2003 Jan 21. [PubMed Link Image]
  5. Moscow JA, Morrow CS, He R, Mullenbach GT, Cowan KH: Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1). J Biol Chem. 1992 Mar 25;267(9):5949-58. [PubMed Link Image]
  6. Yeramian P, Chardin P, Madaule P, Tavitian A: Nucleotide sequence of human rho cDNA clone 12. Nucleic Acids Res. 1987 Feb 25;15(4):1869. [PubMed Link Image]
  7. Moscow JA, He R, Gudas JM, Cowan KH: Utilization of multiple polyadenylation signals in the human RHOA protooncogene. Gene. 1994 Jul 8;144(2):229-36. [PubMed Link Image]
  8. Ishizaki T, Maekawa M, Fujisawa K, Okawa K, Iwamatsu A, Fujita A, Watanabe N, Saito Y, Kakizuka A, Morii N, Narumiya S: The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase. EMBO J. 1996 Apr 15;15(8):1885-93. [PubMed Link Image]
  9. Matsui T, Amano M, Yamamoto T, Chihara K, Nakafuku M, Ito M, Nakano T, Okawa K, Iwamatsu A, Kaibuchi K: Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho. EMBO J. 1996 May 1;15(9):2208-16. [PubMed Link Image]
  10. Wei Y, Zhang Y, Derewenda U, Liu X, Minor W, Nakamoto RK, Somlyo AV, Somlyo AP, Derewenda ZS: Crystal structure of RhoA-GDP and its functional implications. Nat Struct Biol. 1997 Sep;4(9):699-703. [PubMed Link Image]
  11. 9545299 Ihara K, Muraguchi S, Kato M, Shimizu T, Shirakawa M, Kuroda S, Kaibuchi K, Hakoshima T: Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue. J Biol Chem. 1998 Apr 17;273(16):9656-66.
Target 15 Drug References
  1. Ohkawara H, Ishibashi T, Sakamoto T, Sugimoto K, Nagata K, Yokoyama K, Sakamoto N, Kamioka M, Matsuoka I, Fukuhara S, Sugimoto N, Takuwa Y, Maruyama Y: Thrombin-induced rapid geranylgeranylation of RhoA as an essential process for RhoA activation in endothelial cells. J Biol Chem. 2005 Mar 18;280(11):10182-8. Epub 2005 Jan 7. [PubMed Link Image]
  2. Argmann CA, Edwards JY, Sawyez CG, O'Neil CH, Hegele RA, Pickering JG, Huff MW: Regulation of macrophage cholesterol efflux through hydroxymethylglutaryl-CoA reductase inhibition: a role for RhoA in ABCA1-mediated cholesterol efflux. J Biol Chem. 2005 Jun 10;280(23):22212-21. Epub 2005 Apr 6. [PubMed Link Image]
  3. Li M, Liu Y, Dutt P, Fanburg BL, Toksoz D: Inhibition of serotonin-induced mitogenesis, migration, and ERK MAPK nuclear translocation in vascular smooth muscle cells by atorvastatin. Am J Physiol Lung Cell Mol Physiol. 2007 Aug;293(2):L463-71. Epub 2007 Jun 1. [PubMed Link Image]
  4. Trebicka J, Hennenberg M, Laleman W, Shelest N, Biecker E, Schepke M, Nevens F, Sauerbruch T, Heller J: Atorvastatin lowers portal pressure in cirrhotic rats by inhibition of RhoA/Rho-kinase and activation of endothelial nitric oxide synthase. Hepatology. 2007 Jul;46(1):242-53. [PubMed Link Image]
Drug Target 16 [top]
Target 16 ID 3930
Target 16 Name DNA replication licensing factor MCM7
Target 16 Synonyms
  1. CDC47 homolog
  2. P1.1-MCM3
Target 16 Gene Name MCM7
Target 16 Protein Sequence >DNA replication licensing factor MCM7
MALKDYALEKEKVKKFLQEFYQDDELGKKQFKYGNQLVRLAHREQVALYVDLDDVAEDDP
ELVDSICENARRYAKLFADAVQELLPQYKEREVVNKDVLDVYIEHRLMMEQRSRDPGMVR
SPQNQYPAELMRRFELYFQGPSSNKPRVIREVRADSVGKLVTVRGIVTRVSEVKPKMVVA
TYTCDQCGAETYQPIQSPTFMPLIMCPSQECQTNRSGGRLYLQTRGSRFIKFQEMKMQEH
SDQVPVGNIPRSITVLVEGENTRIAQPGDHVSVTGIFLPILRTGFRQVVQGLLSETYLEA
HRIVKMNKSEDDESGAGELTREELRQIAEEDFYEKLAASIAPEIYGHEDVKKALLLLLVG
GVDQSPRGMKIRGNINICLMGDPGVAKSQLLSYIDRLAPRSQYTTGRGSSGVGLTAAVLR
DSVSGELTLEGGALVLADQGVCCIDEFDKMAEADRTAIHEVMEQQTISIAKAGILTTLNA
RCSILAAANPAYGRYNPRRSLEQNIQLPAALLSRFDLLWLIQDRPDRDNDLRLAQHITYV
HQHSRQPPSQFEPLDMKLMRRYIAMCREKQPMVPESLADYITAAYVEMRREAWASKDATY
TSARTLLAILRLSTALARLRMVDVVEKEDVNEAIRLMEMSKDSLLGDKGQTARTQRPADV
IFATVRELVSGGRSVRFSEAEQRCVSRGFTPAQFQAALDEYEELNVWQVNASRTRITFV
Target 16 Number of Residues 730
Target 16 Molecular Weight 81309
Target 16 Theoretical pI 6.38
Target 16 GO Classification
Function
ATPase activity
ATPase activity, coupled
DNA-dependent ATPase activity
purine nucleotide binding
adenyl nucleotide binding
ATP binding
nucleic acid binding
DNA binding
catalytic activity
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
pyrophosphatase activity
nucleoside-triphosphatase activity
binding
nucleotide binding
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
DNA replication
DNA-dependent DNA replication
DNA replication initiation
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
Target 16 General Function Replication, recombination and repair
Target 16 Specific Function Acts as a factor that allows the DNA to undergo a single round of replication per cell cycle. Required for DNA replication and cell proliferation. Required for S-phase checkpoint activation upon UV-induced damage
Target 16 Pathways Not Available
Target 16 Reactions Not Available
Target 16 Pfam Domain Function
Target 16 Signals
  • None
Target 16 Transmembrane Regions
  • None
Target 16 Essentiality Non-Essential
Target 16 GenBank ID Protein 1255617 Link Image
Target 16 UniProtKB/Swiss-Prot ID P33993 Link Image
Target 16 UniProtKB/Swiss-Prot Entry Name MCM7_HUMAN Link Image
Target 16 PDB ID Not Available
Target 16 Cellular Location
  • Nucleus
Target 16 Gene Sequence >2160 bp
ATGGCACTGAAGGACTACGCGCTAGAGAAGGAAAAGGTTAAGAAGTTCTTACAAGAGTTC
TACCAGGATGATGAACTCGGGAAGAAGCAGTTCAAGTATGGGAACCAGTTGGTTCGGCTG
GCTCATCGGGAACAGGTGGCTCTGTATGTGGACCTGGACGACGTAGCCGAGGATGACCCC
GAGTTGGTGGACTCAATTTGTGAGAATGCCAGGCGCTACGCGAAGCTCTTTGCTGATGCC
GTACAAGAGCTGCTGCCTCAGTACAAGGAGAGGGAAGTGGTAAATAAAGATGTCCTGGAC
GTTTACATTGAGCATCGGCTAATGATGGAGCAGCGGAGTCGGGACCCTGGGATGGTCCGA
AGCCCCCAGAACCAGTACCCTGCTGAACTCATGCGCAGATTTGAGCTGTATTTTCAAGGC
CCTAGCAGCAGCAAGCCTCGTGTGATCCGGGAAGTGCGGGCTGACTCTGTGGGGAAGTTG
GTAACTGTGCGTGGAATCGTCACTCGTGTCTCTGAAGTCAAACCCAAGATGGTGGTGGCC
ACTTACACTTGTGACCAGTGTGGGGCAGAGACCTACCAGCCGATCCAGTCTCCCACTTTC
ATGCCTCTGATCATGTGCCCAAGCCAGGAGTGCCAAACCAACCGCTCAGGAGGGCGGCTG
TATCTGCAGACACGGGGCTCCAGATTCATCAAATTCCAGGAGATGAAGATGCAAGAACAT
AGTGATCAGGTGCCTGTGGGAAATATCCCTCGTAGTATCACGGTGCTGGTAGAAGGAGAG
AACACAAGGATTGCCCAGCCTGGAGACCACGTCAGCGTCACTGGTATTTTCTTGCCAATC
CTGCGCACTGGGTTCCGACAGGTGGTACAGGGTTTACTCTCAGAAACCTACCTGGAAGCC
CATCGGATTGTGAAGATGAACAAGAGTGAGGATGATGAGTCTGGGGCTGGAGAGCTCACC
AGGGAGGAGCTGAGGCAAATTGCAGAGGAGGATTTCTACGAAAAGCTGGCAGCTTCAATC
GCCCCAGAAATATACGGGCATGAAGATGTGAAGAAGGCACTGCTGCTCCTGCTAGTCGGG
GGTGTGGACCAGTCTCCTCGAGGCATGAAAATCCGGGGCAACATCAACATCTGTCTGATG
GGGGATCCTGGTGTGGCCAAGTCTCAGCTCCTGTCATACATTGATCGACTGGCGCCTCGC
AGCCAGTACACAACAGGCCGGGGCTCCTCAGGAGTGGGGCTTACGGCAGCTGTGCTGAGA
GACTCCGTGAGTGGAGAACTGACCTTAGAGGGTGGGGCCCTGGTGCTGGCTGACCAGGGT
GTGTGCTGCATTGATGAGTTCGACAAGATGGCTGAGGCCGACCGCACAGCCATCCACGAG
GTCATGGAGCAGCAGACCATCTCCATTGCCAAGGCCGGCATTCTCACCACACTCAATGCC
CGCTGCTCCATCCTGGCTGCCGCCAACCCTGCCTACGGGCGCTACAACCCTCGCCGCAGC
CTGGAGCAGAACATACAGCTACCTGCTGCACTGCTCTCCCGGTTTGACCTCCTCTGGCTG
ATTCAGGACCGGCCCGACCGAGACAATGACCTACGGTTGGCCCAGCACATCACCTATGTG
CACCAGCACAGCCGGCAGCCCCCCTCCCAGTTTGAACCTCTGGACATGAAGCTCATGAGG
CGTTACATAGCCATGTGCCGCGAGAAGCAGCCCATGGTGCCAGAGTCTCTGGCTGACTAC
ATCACAGCAGCATACGTGGAGATGAGGCGAGAGGCTTGGGCTAGTAAGGATGCCACCTAT
ACTTCTGCCCGGACCCTGCTGGCTATCCTGCGCCTTTCCACTGCTCTGGCACGTCTGAGA
ATGGTGGATGTGGTGGAGAAAGAAGATGTGAATGAAGCCATCAGGCTAATGGAGATGTCA
AAGGACTCTCTTCTAGGAGACAAGGGGCAGACAGCTAGGACTCAGAGACCAGCAGATGTG
ATATTTGCCACCGTCCGTGAACTGGTCTCAGGGGGCCGAAGTGTCCGGTTCTCTGAGGCA
GAGCAGCGCTGTGTATCTCGTGGCTTCACACCCGCCCAGTTCCAGGCGGCTCTGGATGAA
TATGAGGAGCTCAATGTCTGGCAGGTCAATGCTTCCCGGACACGGATCACTTTTGTCTGA
Target 16 GenBank Gene ID
Target 16 GeneCard ID MCM7 Link Image
Target 16 GenAtlas ID MCM7 Link Image
Target 16 HGNC ID HGNC:6950 Link Image
Target 16 Chromosome Location 7
Target 16 Locus 7q21.3-q22.1
Target 16 SNPs SNPJam Report Link Image
Target 16 General References
  1. Nakatsuru S, Sudo K, Nakamura Y: Isolation and mapping of a human gene (MCM2) encoding a product homologous to yeast proteins involved in DNA replication. Cytogenet Cell Genet. 1995;68(3-4):226-30. [PubMed Link Image]
  2. Hu B, Burkhart R, Schulte D, Musahl C, Knippers R: The P1 family: a new class of nuclear mammalian proteins related to the yeast Mcm replication proteins. Nucleic Acids Res. 1993 Nov 25;21(23):5289-93. [PubMed Link Image]
  3. Fujita M, Kiyono T, Hayashi Y, Ishibashi M: hCDC47, a human member of the MCM family. Dissociation of the nucleus-bound form during S phase. J Biol Chem. 1996 Feb 23;271(8):4349-54. [PubMed Link Image]
Target 16 Drug References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed Link Image]
Drug Target 17 [top]
Target 17 ID 3963
Target 17 Name DNA replication licensing factor MCM6
Target 17 Synonyms
  1. p105MCM
Target 17 Gene Name MCM6
Target 17 Protein Sequence >DNA replication licensing factor MCM6
MDLAAAAEPGAGSQHLEVRDEVAEKCQKLFLDFLEEFQSSDGEIKYLQLAEELIRPERNT
LVVSFVDLEQFNQQLSTTIQEEFYRVYPYLCRALKTFVKDRKEIPLAKDFYVAFQDLPTR
HKIRELTSSRIGLLTRISGQVVRTHPVHPELVSGTFLCLDCQTVIRDVEQQFKYTQPNIC
RNPVCANRRRFLLDTNKSRFVDFQKVRIQETQAELPRGSIPRSLEVILRAEAVESAQAGD
KCDFTGTLIVVPDVSKLSTPGARAETNSRVSGVDGYETEGIRGLRALGVRDLSYRLVFLA
CCVAPTNPRFGGKELRDEEQTAESIKNQMTVKEWEKVFEMSQDKNLYHNLCTSLFPTIHG
NDEVKRGVLLMLFGGVPKTTGEGTSLRGDINVCIVGDPSTAKSQFLKHVEEFSPRAVYTS
GKASSAAGLTAAVVRDEESHEFVIEAGALMLADNGVCCIDEFDKMDVRDQVAIHEAMEQQ
TISITKAGVKATLNARTSILAAANPISGHYDRSKSLKQNINLSAPIMSRFDLFFILVDEC
NEVTDYAIARRIVDLHSRIEESIDRVYSLDDIRRYLLFARQFKPKISKESEDFIVEQYKH
LRQRDGSGVTKSSWRITVRQLESMIRLSEAMARMHCCDEVQPKHVKEAFRLLNKSIIRVE
TPDVNLDQEEEIQMEVDEGAGGINGHADSPAPVNGINGYNEDINQESAPKASLRLGFSEY
CRISNLIVLHLRKVEEEEDESALKRSELVNWYLKEIESEIDSEEELINKKRIIEKVIHRL
THYDHVLIELTQAGLKGSTEGSESYEEDPYLVVNPNYLLED
Target 17 Number of Residues 834
Target 17 Molecular Weight 92890
Target 17 Theoretical pI 5.09
Target 17 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
pyrophosphatase activity
nucleoside-triphosphatase activity
ATPase activity
ATPase activity, coupled
DNA-dependent ATPase activity
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
binding
nucleic acid binding
DNA binding
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
DNA replication
DNA-dependent DNA replication
DNA replication initiation
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
Target 17 General Function Replication, recombination and repair
Target 17 Specific Function May be involved in the control of a single round of DNA replication during S phase. Binds to chromatin during G1 and detach from it during S phase as if it licenses the chromatin to replicate
Target 17 Pathways Not Available
Target 17 Reactions Not Available
Target 17 Pfam Domain Function
Target 17 Signals
  • None
Target 17 Transmembrane Regions
  • None
Target 17 Essentiality Non-Essential
Target 17 GenBank ID Protein 1688042 Link Image
Target 17 UniProtKB/Swiss-Prot ID Q14566 Link Image
Target 17 UniProtKB/Swiss-Prot Entry Name MCM6_HUMAN Link Image
Target 17 PDB ID Not Available
Target 17 Cellular Location
  • Nucleus
Target 17 Gene Sequence >2466 bp
ATGGACCTCGCGGCGGCAGCGGAGCCGGGCGCCGGCAGCCAGCACCTGGAGGTCCGCGAC
GAGGTGGCCGAGAAGTGCCAGAAACTGTTCCTGGACTTCTTGGAGGAGTTTCAGAGCAGC
GATGGAGAAATTAAATACTTGCAATTAGCAGAGGAACTGATTCGTCCTGAGAGAAACACA
TTGGTTGTGAGTTTTGTGGACCTGGAACAATTTAACCAGCAACTTTCCACCACCATTCAA
GAGGAGTTCTATAGAGTTTACCCTTACCTGTGTCGGGCCTTGAAAACATTCGTCAAAGAC
CGTAAAGAGATCCCTCTTGCCAAGGATTTTTATGTTGCATTCCAAGACCTGCCTACCAGA
CACAAGATTCGAGAGCTCACCTCATCCAGAATTGGTTTGCTCACTCGCATCAGTGGGCAG
GTGGTGCGGACTCACCCAGTTCACCCAGAGCTTGTGAGCGGAACTTTTCTGTGCTTGGAC
TGTCAGACAGTGATCAGGGATGTAGAACAGCAGTTCAAATACACACAGCCAAACATCTGC
CGAAATCCAGTTTGTGCCAACAGGAGGAGATTCTTACTGGATACAAATAAATCAAGATTT
GTTGATTTTCAAAAGGTTCGTATTCAAGAGACCCAAGCTGAGCTTCCTCGAGGGAGTATC
CCCCGCAGTTTAGAAGTAATTTTAAGGGCTGAAGCTGTGGAATCAGCTCAAGCTGGTGAC
AAGTGTGACTTTACAGGGACACTGATTGTTGTGCCTGACGTCTCCAAGCTTAGCACACCA
GGAGCACGTGCAGAAACTAATTCCCGTGTCAGTGGTGTTGATGGATATGAGACAGAAGGC
ATTCGAGGACTCCGGGCCCTTGGTGTTAGGGACCTTTCTTATAGGCTGGTCTTTCTTGCC
TGCTGTGTTGCGCCAACCAACCCAAGGTTTGGGGGGAAAGAGCTCAGAGATGAGGAACAG
ACAGCTGAGAGCATTAAGAACCAAATGACTGTGAAAGAATGGGAGAAAGTGTTTGAGATG
AGTCAAGATAAAAATCTATACCACAATCTTTGTACCAGCCTGTTCCCTACTATACATGGC
AATGATGAAGTAAAACGGGGTGTCCTGCTGATGCTCTTTGGTGGCGTTCCAAAGACAACA
GGAGAAGGGACCTCTCTTCGAGGGGACATAAATGTTTGCATTGTTGGTGACCCAAGTACA
GCTAAGAGCCAATTTCTCAAGCACGTGGAGGAGTTCAGCCCCAGAGCTGTCTACACCAGT
GGTAAAGCGTCCAGTGCTGCTGGCTTAACAGCAGCTGTTGTGAGAGATGAAGAATCTCAT
GAGTTTGTCATTGAGGCTGGAGCTTTGATGTTGGCTGATAATGGTGTGTGTTGTATTGAT
GAATTTGATAAGATGGACGTGCGGGATCAAGTTGCTATTCATGAAGCTATGGAACAGCAG
ACCATATCCATCACTAAAGCAGGAGTGAAGGCTACTCTGAACGCCCGGACGTCCATTTTG
GCAGCAGCAAACCCAATCAGTGGACACTATGACAGATCAAAATCATTGAAACAGAATATA
AATTTGTCAGCTCCCATCATGTCCCGATTCGATCTCTTCTTTATCCTTGTGGATGAATGT
AATGAGGTTACAGATTATGCCATTGCCAGGCGCATAGTAGATTTGCATTCAAGAATTGAG
GAATCAATTGATCGTGTCTATTCCCTCGATGATATCAGAAGATATCTTCTCTTTGCAAGA
CAGTTTAAACCCAAGATTTCCAAAGAGTCAGAGGACTTCATTGTGGAGCAATATAAACAT
CTCCGCCAGAGAGATGGTTCTGGAGTGACCAAGTCTTCATGGAGGATTACAGTGCGACAG
CTTGAGAGCATGATTCGTCTCTCTGAAGCTATGGCTCGGATGCACTGCTGTGATGAGGTC
CAACCTAAACATGTGAAGGAAGCTTTCCGGTTACTGAATAAATCAATCATCCGTGTGGAA
ACACCTGATGTCAATCTAGATCAAGAGGAAGAGATCCAGATGGAGGTAGATGAGGGTGCT
GGTGGCATCAATGGTCATGCTGACAGCCCTGCTCCTGTGAACGGGATCAATGGCTACAAT
GAAGACATAAATCAAGAGTCTGCTCCCAAAGCCTCCTTAAGGCTGGGCTTCTCTGAGTAC
TGCCGAATCTCTAACCTTATTGTGCTTCACCTCAGAAAGGTGGAAGAAGAAGAGGACGAG
TCAGCATTAAAGAGGAGCGAGCTTGTTAACTGGTACTTGAAGGAAATCGAATCAGAGATA
GACTCTGAAGAAGAACTTATAAATAAAAAAAGAATCATAGAGAAAGTTATTCATCGACTC
ACACACTATGATCATGTTCTAATTGAGCTCACCCAGGCTGGATTGAAAGGCTCCACAGAG
GGAAGTGAGAGCTATGAAGAAGATCCCTACTTGGTAGTTAACCCTAACTACTTGCTCGAA
GATTGA
Target 17 GenBank Gene ID
Target 17 GeneCard ID MCM6 Link Image
Target 17 GenAtlas ID MCM6 Link Image
Target 17 HGNC ID HGNC:6949 Link Image
Target 17 Chromosome Location 2
Target 17 Locus 2q21
Target 17 SNPs SNPJam Report Link Image
Target 17 General References
  1. Izumi M, Yanagi K, Mizuno T, Yokoi M, Kawasaki Y, Moon KY, Hurwitz J, Yatagai F, Hanaoka F: The human homolog of Saccharomyces cerevisiae Mcm10 interacts with replication factors and dissociates from nuclease-resistant nuclear structures in G(2) phase. Nucleic Acids Res. 2000 Dec 1;28(23):4769-77. [PubMed Link Image]
  2. Harvey CB, Wang Y, Darmoul D, Phillips A, Mantei N, Swallow DM: Characterisation of a human homologue of a yeast cell division cycle gene, MCM6, located adjacent to the 5' end of the lactase gene on chromosome 2q21. FEBS Lett. 1996 Dec 2;398(2-3):135-40. [PubMed Link Image]
  3. Tsuruga H, Yabuta N, Hosoya S, Tamura K, Endo Y, Nojima H: HsMCM6: a new member of the human MCM/P1 family encodes a protein homologous to fission yeast Mis5. Genes Cells. 1997 Jun;2(6):381-99. [PubMed Link Image]
  4. Holthoff HP, Baack M, Richter A, Ritzi M, Knippers R: Human protein MCM6 on HeLa cell chromatin. J Biol Chem. 1998 Mar 27;273(13):7320-5. [PubMed Link Image]
Target 17 Drug References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.