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Showing drug card for Etretinate (DB00926)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2008-08-26 14:09:55
Primary Accession Number DB00926
Secondary Accession Number
  • APRD00966
Name Etretinate
Drug Type
  • Small Molecule
  • Withdrawn
Description Etretinate is a medication used to treat severe psoriasis. It is a synthetic aromatic retinoid. The mechanism of action of etretinate is still incompletely understood although, like retinoic acid, it is thought to interfere with the terminal differentiation of keratinocytes. It is thought to bind to the retinoic acid receptors. Etretinate is also believed to enhance the binding of cAMP to the regulatory RI subunit of cAMP dependent protein kinases. It was removed from the United States market in 1998 and the Canadian market in 1996 as a psoriasis medication, due to the high risk of birth defects. Etretinate is now used to treat T-cell lymphomas. It also appears to inhibit NADH oxidase activity.
Synonyms Not Available
Brand Names
  1. Tegison
  2. Tigason
Brand Mixtures Not Available
Chemical IUPAC Name ethyl 9-(4-methoxy-2,3,6-trimethylphenyl)-3,7-dimethylnona-2,4,6,8-tetraenoate
Chemical Formula C23H30O3
Chemical Structure Structure
CAS Registry Number 54350-48-0
InChI Identifier InChI=1/C23H30O3/c1-8-26-23(24)14-17(3)11-9-10-16(2)12-13-21-18(4)15-22(25-7)20(6)19(21)5/h9-15H,8H2,1-7H3
InChI Key HQMNCQVAMBCHCO-UHFFFAOYAW
KEGG Drug D00316 Link Image
KEGG Compound Not Available
PubChem Compound 3312 Link Image
PubChem Substance 7847382 Link Image
ChEBI ID Not Available
PharmGKB ID PA449554 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link Not Available
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Etretinate Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 354.4825
Monoisotopic Molecular Weight 354.2195
State Solid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 4.05e-04 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 6.5 Source: PhysProp
Predicted LogP 6.32 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -5.94 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 CCOC(=O)\C=C(C)\C=C\C=C(C)\C=C\C1=C(C)C(C)=C(OC)C=C1C
Canonical SMILES CCOC(=O)C=C(C)C=CC=C(C)C=CC1=C(C)C(C)=C(OC)C=C1C
Drug Category
  • Keratolytic Agents
ATC Codes
AHFS Codes Not Available
Indication For the treatment of severe psoriasis in adults.
Pharmacology The active metabolite responsible for etretinate's effects, acitretin, is a retinoid. Retinoids have a structure similar to vitamin A and are involved in the normal growth of skin cells. Acitretin works by inhibiting the excessive cell growth and keratinisation (process by which skin cells become thickened due to the deposition of a protein within them) seen in psoriasis. It therefore reduces the thickening of the skin, plaque formation and scaling.
Mechanism of Action The mechanism of action of the active metabolite, acitretin, is unknown, however it is believed to work by targeting specific receptors (retinoid receptors) in the skin which help normalize the growth cycle of skin cells.
Absorption Absorbed in the small intestine. Studies in normal volunteers indicate that the absorption of etretinate is greater in patients consuming whole milk or a high-fat diet than in patients in a fasting state.
Toxicity Symptoms of overdose include headache and vertigo.
Protein Binding More than 99% bound to plasma proteins, predominantly lipoproteins, whereas its active metabolite, acetretin (etretin), is predominantly bound to albumin.
Biotransformation Extensively metabolized, with significant first-pass metabolism to the pharmacologically active acid form. Subsequent metabolism results in the inactive 13-cis acid form, chain-shortened breakdown products, and conjugates that are ultimately excreted.
Half Life In one study, the apparent terminal half-life of etretinate after 6 months of therapy was approximately 120 days. In another study of 47 patients who had undergone chronic therapy with etretinate, 5 patients had detectable serum drug concentrations (0.5 to 12 ng/mL) 2.1 to 2.9 years after therapy was completed.
Dosage Forms
Form Route
Tablet Oral
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions
Drug Interaction
Acenocoumarol Retinoids decreases the anticoagulant effect
Anisindione Retinoids decreases the anticoagulant effect
Demeclocycline Increased risk of intracranial hypertension
Dicumarol Retinoids decreases the anticoagulant effect
Doxycycline Increased risk of intracranial hypertension
Methacycline Increased risk of intracranial hypertension
Methotrexate Acitretin/etretinate increases the effect and toxicity of methotrexate
Minocycline Increased risk of intracranial hypertension
Oxytetracycline Increased risk of intracranial hypertension
Rolitetracycline Increased risk of intracranial hypertension
Tetracycline Increased risk of intracranial hypertension
Warfarin Retinoids decreases the anticoagulant effect
Food Interactions
  • Avoid alcohol completely up to 2 months after discontinuation.
  • Increases absorption, take with food.
Pathways Not Available
General References
  1. Wikipedia Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Retinoic acid receptor RXR-beta
  2. Retinoic acid receptor gamma-1
  3. Retinoic acid receptor beta
  4. Retinoic acid receptor gamma-2
  5. Retinoic acid receptor RXR-alpha
  6. Cellular retinoic acid-binding protein 1
  7. Retinoic acid receptor alpha
  8. Retinoic acid receptor RXR-gamma
Drug Target 1 [top]
Target 1 ID 88
Target 1 Name Retinoic acid receptor RXR-beta
Target 1 Synonyms
  1. Retinoid X receptor beta
Target 1 Gene Name RXRB
Target 1 Protein Sequence >Retinoic acid receptor RXR-beta 
MSWAARPPFLPQRHAAGQCGPVGVRKEMHCGVASRWRRRRPWLDPAAAAAAAVAGGEQQT
PEPEPGEAGRDGMGDSGRDSRSPDSSSPNPLPQGVPPPSPPGPPLPPSTAPSLGGSGAPP
PPPMPPPPLGSPFPVISSSMGSPGLPPPAPPGFSGPVSSPQINSTVSLPGGGSGPPEDVK
PPVLGVRGLHCPPPPGGPGAGKRLCAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLTYS
CRDNKDCTVDKRQRNRCQYCRYQKCLATGMKREAVQEERQRGKDKDGDGEGAGGAPEEMP
VDRILEAELAVEQKSDQGVEGPGGTGGSGSSPNDPVTNICQAADKQLFTLVEWAKRIPHF
SSLPLDDQVILLRAGWNELLIASFSHRSIDVRDGILLATGLHVHRNSAHSAGVGAIFDRV
LTELVSKMRDMRMDKTELGCLRAIILFNPDAKGLSNPSEVEVLREKVYASLETYCKQKYP
EQQGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQLA
Target 1 Number of Residues 541
Target 1 Molecular Weight 56922
Target 1 Theoretical pI 8.24
Target 1 GO Classification
Function
steroid binding
signal transducer activity
receptor activity
ligand-dependent nuclear receptor activity
steroid hormone receptor activity
binding
nucleic acid binding
DNA binding
transcription factor activity
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 Cell cycle control, cell division, chromosome partitioning
Target 1 Specific Function Nuclear hormone receptor. Involved in the retinoic acid response pathway. Binds 9-cis retinoic acid (9C-RA)
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 30448 Link Image
Target 1 UniProtKB/Swiss-Prot ID P28702 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name RXRB_HUMAN Link Image
Target 1 PDB ID 1UHL Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Nucleus
Target 1 Gene Sequence >1602 bp 
ATGTCTTGGGCCGCTCGCCCGCCCTTCCTCCCTCAGCGGCATGCCGCAGGGCAGTGTGGG
CCGGTGGGGGTGCGAAAAGAAATGCATTGTGGGGTCGCGTCCCGGTGGCGGCGGCGACGG
CCCTGGCTGGATCCCGCAGCGGCGGCGGCGGCGGCGGTGGCAGGCGGAGAACAACAAACC
CCGGAGCCGGAGCCAGGGGAGGCTGGACGGGACGGGATGGGCGACAGCGGGCGGGACTCC
CGAAGCCCAGACAGCTCCTCCCCAAATCCCCTTCCCCAGGGAGTCCCTCCCCCTTCTCCT
CCTGGGCCACCCCTACCCCCTTCAACAGCTCCATCCCTTGGAGGCTCTGGGGCCCCACCC
CCACCCCCGATGCCACCACCCCCACTGGGCTCTCCCTTTCCAGTCATCAGTTCTTCCATG
GGGTCCCCTGGTCTGCCCCCTCCAGCTCCCCCAGGATTCTCCGGGCCTGTCAGCAGCCCC
CAGATTAACTCAACAGTGTCACTCCCTGGGGGTGGGTCTGGCCCCCCTGAAGATGTGAAG
CCACCAGTCTTAGGGGTCCGGGGCCTGCACTGTCCACCCCCTCCAGGTGGCCCTGGGGCT
GGCAAACGGCTATGTGCAATCTGCGGGGACAGAAGCTCAGGCAAACACTACGGGGTTTAC
AGCTGTGAGGGTTGCAAGGGCTTCTTCAAACGCACCATCCGCAAAGACCTTACATACTCT
TGCCGGGACAACAAAGACTGCACAGTGGACAAGCGCCAGCGGAACCGCTGTCAGTACTGC
CGCTATCAGAAGTGCCTGGCCACTGGCATGAAGAGGGAGGCGGTACAGGAGGAGCGTCAG
CGGGGAAAGGACAAGGATGGGGATGGGGAGGGGGCTGGGGGAGCCCCCGAGGAGATGCCT
GTGGACAGGATCCTGGAGGCAGAGCTTGCTGTGGAACAGAAGAGTGACCAGGGCGTTGAG
GGTCCTGGGGGAACCGGGGGTAGCGGCAGCAGCCCAAATGACCCTGTGACTAACATCTGT
CAGGCAGCTGACAAACAGCTATTCACGCTTGTTGAGTGGGCGAAGAGGATCCCACACTTT
TCCTCCTTGCCTCTGGATGATCAGGTCATATTGCTGCGGGCAGGCTGGAATGAACTCCTC
ATTGCCTCCTTTTCACACCGATCCATTGATGTTCGAGATGGCATCCTCCTTGCCACAGGT
CTTCACGTGCACCGCAACTCAGCCCATTCAGCAGGAGTAGGAGCCATCTTTGATCGGGTG
CTGACAGAGCTAGTGTCCAAAATGCGTGACATGAGGATGGACAAGACAGAGCTTGGCTGC
CTGAGGGCAATCATTCTGTTTAATCCAGATGCCAAGGGCCTCTCCAACCCTAGTGAGGTG
GAGGTCCTGCGGGAGAAAGTGTATGCATCACTGGAGACCTACTGCAAACAGAAGTACCCT
GAGCAGCAGGGACGGTTTGCCAAGCTGCTGCTACGTCTTCCTGCCCTCCGGTCCATTGGC
CTTAAGTGTCTAGAGCATCTGTTTTTCTTCAAGCTCATTGGTGACACCCCCATCGACACC
TTCCTCATGGAGATGCTTGAGGCTCCCCATCAACTGGCCTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID RXRB Link Image
Target 1 GenAtlas ID RXRB Link Image
Target 1 HGNC ID HGNC:10478 Link Image
Target 1 Chromosome Location 6
Target 1 Locus 6p21.3
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Leid M, Kastner P, Lyons R, Nakshatri H, Saunders M, Zacharewski T, Chen JY, Staub A, Garnier JM, Mader S, et al.: Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently. Cell. 1992 Jan 24;68(2):377-95. [PubMed Link Image]
  2. Fleischhauer K, Park JH, DiSanto JP, Marks M, Ozato K, Yang SY: Isolation of a full-length cDNA clone encoding a N-terminally variant form of the human retinoid X receptor beta. Nucleic Acids Res. 1992 Apr 11;20(7):1801. [PubMed Link Image]
  3. Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently. Cell. 1992 Nov 27;71(5):887. [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]
Target 1 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 162
Target 2 Name Retinoic acid receptor gamma-1
Target 2 Synonyms
  1. RAR-gamma-1
Target 2 Gene Name RARG
Target 2 Protein Sequence >Retinoic acid receptor gamma-1 
MATNKERLFAAGALGPGSGYPGAGFPFAFPGALRGSPPFEMLSPSFRGLGQPDLPKEMAS
LSVETQSTSSEEMVPSSPSPPPPPRVYKPCFVCNDKSSGYHYGVSSCEGCKGFFRRSIQK
NMVYTCHRDKNCIINKVTRNRCQYCRLQKCFEVGMSKEAVRNDRNKKKKEVKEEGSPDSY
ELSPQLEELITKVSKAHQETFPSLCQLGKYTTNSSADHRVQLDLGLWDKFSELATKCIIK
IVEFAKRLPGFTGLSIADQITLLKAACLDILMLRICTRYTPEQDTMTFSDGLTLNRTQMH
NAGFGPLTDLVFAFAGQLLPLEMDDTETGLLSAICLICGDRMDLEEPEKVDKLQEPLLEA
LRLYARRRRPSQPYMFPRMLMKITDLRGISTKGAERAITLKMEIPGPMPPLIREMLENPE
MFEDDSSQPGPHPNASSEDEVPGGQGKGGLKSPA
Target 2 Number of Residues 461
Target 2 Molecular Weight 50342
Target 2 Theoretical pI 7.52
Target 2 GO Classification
Function
retinoic acid receptor activity
signal transducer activity
receptor activity
ligand-dependent nuclear receptor activity
steroid hormone receptor activity
binding
nucleic acid binding
DNA binding
transcription factor activity
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 2 General Function Involved in transcription factor activity
Target 2 Specific Function This is a receptor for retinoic acid. This metabolite has profound effects on vertebrate development. Retinoic acid is a morphogen and is a powerful teratogen. This receptor controls cell function by directly regulating gene expression
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 306887 Link Image
Target 2 UniProtKB/Swiss-Prot ID P13631 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name RARG1_HUMAN Link Image
Target 2 PDB ID 1EXX Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Nucleus
Target 2 Gene Sequence >1365 bp 
ATGGCCACCAATAAGGAGCGACTCTTTGCGGCTGGTGCCCTGGGGCCTGGATCTGGCTAC
CCAGGGGCAGGTTTCCCCTTCGCCTTCCCAGGGGCACTCAGGGGGTCTCCGCCTTTCGAG
ATGCTGAGCCCTAGCTTCCGGGGCCTGGGCCAGCCTGACCTCCCCAAGGAGATGGCCTCT
CTGTCGGTGGAGACACAGAGCACCAGCTCAGAGGAGATGGTGCCAAGCTCGCCCTCGCCC
CCTCCGCCTCCTCGGGTCTACAAGCCATGCTTCGTGTGCAATGACAAGTCCTCTGGCTAC
CACTATGGGGTCAGCTCTTGTGAAGGCTGCAAGGGCTTCTTTCGCCGAAGCATCCAGAAG
AACATGGTGTACACGTGTCACCGCGACAAAAACTGTATCATCAACAAGGTGACCAGGAAT
CGCTGCCAGTACTGCCGGCTACAGAAGTGCTTCGAAGTGGGCATGTCCAAGGAAGCTGTG
CGAAATGACCGGAACAAGAAGAAGAAAGAGGTGAAGGAAGAAGGGTCACCTGACAGCTAT
GAGCTGAGCCCTCAGTTAGAAGAGCTCATCACCAAGGTCAGCAAAGCCCATCAGGAGACT
TTCCCCTCGCTCTGCCAGCTGGGCAAGTATACCACGAACTCCAGTGCAGACCACCGCGTG
CAGCTGGATCTGGGGCTGTGGGACAAGTTCAGTGAGCTGGCTACCAAGTGCATCATCAAG
ATCGTGGAGTTTGCCAAGCGGTTGCCTGGCTTTACAGGGCTCAGCATTGCTGACCAGATC
ACTCTGCTCAAAGCTGCCTGCCTAGATATCCTGATGCTGCGTATCTGCACAAGGTACACC
CCAGAGCAGGACACCATGACCTTCTCCGACGGGCTGACCCTGAACCGGACCCAGATGCAC
AATGCCGGCTTCGGGCCCCTCACAGACCTTGTCTTTGCCTTTGCTGGGCAGCTCCTGCCC
CTGGAGATGGATGACACCGAGACAGGGCTGCTCAGCGCCATCTGCCTCATCTGCGGAGAC
CGCATGGACCTGGAGGAGCCCGAAAAAGTGGACAAGCTGCAGGAGCCACTGCTGGAAGCC
CTGAGGCTGTACGCCCGGCGCCGGCGGCCCAGCCAGCCCTACATGTTCCCAAGGATGCTA
ATGAAAATCACCGACCTCCGGGGCATCAGCACTAAGGGAGCTGAAAGGGCCATTACTCTG
AAGATGGAGATTCCAGGCCCGATGCCTCCCTTAATCCGAGAGATGCTGGAGAACCCTGAA
ATGTTTGAGGATGACTCCTCGCAGCCTGGTCCCCACCCCAATGCCTCTAGCGAGGATGAG
GTTCCTGGGGGCCAGGGCAAAGGGGGCCTGAAGTCCCCAGCCTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID RARG Link Image
Target 2 GenAtlas ID RARG Link Image
Target 2 HGNC ID HGNC:9866 Link Image
Target 2 Chromosome Location 12
Target 2 Locus 12q13
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Lehmann JM, Hoffmann B, Pfahl M: Genomic organization of the retinoic acid receptor gamma gene. Nucleic Acids Res. 1991 Feb 11;19(3):573-8. [PubMed Link Image]
  2. Ishikawa T, Umesono K, Mangelsdorf DJ, Aburatani H, Stanger BZ, Shibasaki Y, Imawari M, Evans RM, Takaku F: A functional retinoic acid receptor encoded by the gene on human chromosome 12. Mol Endocrinol. 1990 Jun;4(6):837-44. [PubMed Link Image]
  3. Krust A, Kastner P, Petkovich M, Zelent A, Chambon P: A third human retinoic acid receptor, hRAR-gamma. Proc Natl Acad Sci U S A. 1989 Jul;86(14):5310-4. [PubMed Link Image]
  4. Renaud JP, Rochel N, Ruff M, Vivat V, Chambon P, Gronemeyer H, Moras D: Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid. Nature. 1995 Dec 14;378(6558):681-9. [PubMed Link Image]
  5. Klaholz BP, Renaud JP, Mitschler A, Zusi C, Chambon P, Gronemeyer H, Moras D: Conformational adaptation of agonists to the human nuclear receptor RAR gamma. Nat Struct Biol. 1998 Mar;5(3):199-202. [PubMed Link Image]
Target 2 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 229
Target 3 Name Retinoic acid receptor beta
Target 3 Synonyms
  1. HBV-activated protein
  2. RAR-beta
  3. RAR-epsilon
Target 3 Gene Name RARB
Target 3 Protein Sequence >Retinoic acid receptor beta 
MTTSGHACPVPAVNGHMTHYPATPYPLLFPPVIGGLSLPPLHGLHGHPPPSGCSTPSPAT
IETQSTSSEELVPSPPSPLPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNM
IYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKETSKQECTESYEM
TAELDDLTEKIRKAHQETFPSLCQLGKYTTNSSADHRVRLDLGLWDKFSELATKCIIKIV
EFAKRLPGFTGLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNA
GFGPLTDLVFTFANQLLPLEMDDTETGLLSAICLICGDRQDLEEPTKVDKLQEPLLEALK
IYIRKRRPSKPHMFPKILMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGH
EPLTPSSSGNTAEHSPSISPSSVENSGVSQSPLVQ
Target 3 Number of Residues 462
Target 3 Molecular Weight 50490
Target 3 Theoretical pI 7.86
Target 3 GO Classification
Function
retinoic acid receptor activity
signal transducer activity
receptor activity
ligand-dependent nuclear receptor activity
steroid hormone receptor activity
binding
nucleic acid binding
DNA binding
transcription factor activity
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 transcription factor activity
Target 3 Specific Function This is a receptor for retinoic acid. This metabolite has profound effects on vertebrate development. Retinoic acid is a morphogen and is a powerful teratogen. This receptor controls cell function by directly regulating gene expression
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 35883 Link Image
Target 3 UniProtKB/Swiss-Prot ID P10826 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name RARB_HUMAN Link Image
Target 3 PDB ID 1XDK Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location
  • Isoform beta-1, isoform beta-2:Nucleus. Isoform beta-4:Cytoplasm
Target 3 Gene Sequence >1347 bp 
ATGTTTGACTGTATGGATGTTCTGTCAGTGAGTCCTGGGCAAATCCTGGATTTCTACACT
GCGAGTCCGTCTTCCTGCATGCTCCAGGAGAAAGCTCTCAAAGCATGCTTCAGTGGATTG
ACCCAAACCGAATGGCAGCATCGGCACACTGCTCAATCAATTGAAACACAGAGCACCAGC
TCTGAGGAACTCGTCCCAAGCCCCCCATCTCCACTTCCTCCCCCTCGAGTGTACAAACCC
TGCTTCGTCTGCCAGGACAAATCATCAGGGTACCACTATGGGGTCAGCGCCTGTGAGGGA
TGTAAGGGCTTTTTCCGCAGAAGTATTCAGAAGAATATGATTTACACTTGTCACCGAGAT
AAGAACTGTGTTATTAATAAAGTCACCAGGAATCGATGCCAATACTGTCGACTCCAGAAG
TGCTTTGAAGTGGGAATGTCCAAAGAATCTGTCAGGAATGACAGGAACAAGAAAAAAAAG
GAGACTTCGAAGCAAGAATGCACAGAGAGCTATGAAATGACAGCTGAGTTGGACGATCTC
ACAGAGAAGATCCGAAAAGCTCACCAGGAAACTTTCCCTTCACTCTGCCAGCTGGGTAAA
TACACCACGAATTCCAGTGCTGACCATCGAGTCCGACTGGACCTGGGCCTCTGGGACAAA
TTCAGTGAACTGGCCACCAAGTGCATTATTAAGATCGTGGAGTTTGCTAAACGTCTGCCT
GGTTTCACTGGCTTGACCATCGCAGACCAAATTACCCTGCTGAAGGCCGCCTGCCTGGAC
ATCCTGATTCTTAGAATTTGCACCAGGTATACCCCAGAACAAGACACCATGACTTTCTCA
GACGGCCTTACCCTAAATCGAACTCAGATGCACAATGCTGGATTTGGTCCTCTGACTGAC
CTTGTGTTCACCTTTGCCAACCAGCTCCAGCCTTTGGAAATGGATGACACAGAAACAGGC
CTTCTCAGTGCCATCTGCTTAATCTGTGGAGACCGCCAGGACCTTGAGGAACCGACAAAA
GTAGATAAGCTACAAGAACCATTGCTGGAAGCACTAAAAATTTATATCAGAAAAAGACGA
CCCAGCAAGCCTCACATGTTTCCAAAGATCTTAATGAAAATCACAGATCTCCGTAGCATC
AGTGCTAAAGGTGCAGAGCGTGTAATTACCTTGAAAATGGAAATTCCTGGATCAATGCCA
CCTCTCATTCAAGAAATGCTGGAGAATTCTGAAGGACATGAACCCTTGACCCCAAGTTCA
AGTGGGAACACAGCAGAGCACAGTCCTAGCATCTCACCCAGCTCAGTGGAAAACAGTGGG
GTCAGTCAGTCACCACTCCTGCAATAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID RARB Link Image
Target 3 GenAtlas ID RARB Link Image
Target 3 HGNC ID HGNC:9865 Link Image
Target 3 Chromosome Location 3
Target 3 Locus 3p24
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Sommer KM, Chen LI, Treuting PM, Smith LT, Swisshelm K: Elevated retinoic acid receptor beta(4) protein in human breast tumor cells with nuclear and cytoplasmic localization. Proc Natl Acad Sci U S A. 1999 Jul 20;96(15):8651-6. [PubMed Link Image]
  2. Katahira M, Knegtel RM, Boelens R, Eib D, Schilthuis JG, van der Saag PT, Kaptein R: Homo- and heteronuclear NMR studies of the human retinoic acid receptor beta DNA-binding domain: sequential assignments and identification of secondary structure elements. Biochemistry. 1992 Jul 21;31(28):6474-80. [PubMed Link Image]
  3. Shen S, Kruyt FA, den Hertog J, van der Saag PT, Kruijer W: Mouse and human retinoic acid receptor beta 2 promoters: sequence comparison and localization of retinoic acid responsiveness. DNA Seq. 1991;2(2):111-9. [PubMed Link Image]
  4. Dejean A, de The H: Hepatitis B virus as an insertional mutagene in a human hepatocellular carcinoma. Mol Biol Med. 1990 Jun;7(3):213-22. [PubMed Link Image]
  5. de The H, Marchio A, Tiollais P, Dejean A: A novel steroid thyroid hormone receptor-related gene inappropriately expressed in human hepatocellular carcinoma. Nature. 1987 Dec 17-23;330(6149):667-70. [PubMed Link Image]
  6. Brand N, Petkovich M, Krust A, Chambon P, de The H, Marchio A, Tiollais P, Dejean A: Identification of a second human retinoic acid receptor. Nature. 1988 Apr 28;332(6167):850-3. [PubMed Link Image]
  7. Benbrook D, Lernhardt E, Pfahl M: A new retinoic acid receptor identified from a hepatocellular carcinoma. Nature. 1988 Jun 16;333(6174):669-72. [PubMed Link Image]
  8. Dejean A, Bougueleret L, Grzeschik KH, Tiollais P: Hepatitis B virus DNA integration in a sequence homologous to v-erb-A and steroid receptor genes in a hepatocellular carcinoma. Nature. 1986 Jul 3-9;322(6074):70-2. [PubMed Link Image]
  9. Houle B, Pelletier M, Wu J, Goodyer C, Bradley WE: Fetal isoform of human retinoic acid receptor beta expressed in small cell lung cancer lines. Cancer Res. 1994 Jan 15;54(2):365-9. [PubMed Link Image]
  10. Knegtel RM, Katahira M, Schilthuis JG, Bonvin AM, Boelens R, Eib D, van der Saag PT, Kaptein R: The solution structure of the human retinoic acid receptor-beta DNA-binding domain. J Biomol NMR. 1993 Jan;3(1):1-17. [PubMed Link Image]
Target 3 Drug References
  1. Zitnik RJ, Kotloff RM, Latifpour J, Zheng T, Whiting NL, Schwalb J, Elias JA: Retinoic acid inhibition of IL-1-induced IL-6 production by human lung fibroblasts. J Immunol. 1994 Feb 1;152(3):1419-27. [PubMed Link Image]
  2. Billoni N, Gautier B, Mahe YF, Bernard BA: Expression of retinoid nuclear receptor superfamily members in human hair follicles and its implication in hair growth. Acta Derm Venereol. 1997 Sep;77(5):350-5. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 409
Target 4 Name Retinoic acid receptor gamma-2
Target 4 Synonyms
  1. RAR-gamma-2
Target 4 Gene Name RARG
Target 4 Protein Sequence >Retinoic acid receptor gamma-2 
MYDCMETFAPGPRRLYGAAGPGAGLLRRATGGSCFAGLESFAWPQPASLQSVETQSTSSE
EMVPSSPSPPPPPRVYKPCFVCNDKSSGYHYGVSSCEGCKGFFRRSIQKNMVYTCHRDKN
CIINKVTRNRCQYCRLQKCFEVGMSKEAVRNDRNKKKKEVKEEGSPDSYELSPQLEELIT
KVSKAHQETFPSLCQLGKYTTNSSADHRVQLDLGLWDKFSELATKCIIKIVEFAKRLPGF
TGLSIADQITLLKAACLDILMLRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLV
FAFAGQLLPLEMDDTETGLLSAICLICGDRMDLEEPEKVDKLQEPLLEALRLYARRRRPS
QPYMFPRMLMKITDLRGISTKGAERAITLKMEIPGPMPPLIREMLENPEMFEDDSSQPGP
HPNASSEDEVPGGQGKGGLKSPA
Target 4 Number of Residues 450
Target 4 Molecular Weight 49308
Target 4 Theoretical pI 7.48
Target 4 GO Classification
Function
retinoic acid receptor activity
signal transducer activity
receptor activity
ligand-dependent nuclear receptor activity
steroid hormone receptor activity
binding
nucleic acid binding
DNA binding
transcription factor activity
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 4 General Function Involved in transcription factor activity
Target 4 Specific Function This is a receptor for retinoic acid. This metabolite has profound effects on vertebrate development. Retinoic acid is a morphogen and is a powerful teratogen. This receptor controls cell function by directly regulating gene expression
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein Not Available
Target 4 UniProtKB/Swiss-Prot ID P22932 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name RARG2_HUMAN Link Image
Target 4 PDB ID 1EXX Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location
  • Nucleus
Target 4 Gene Sequence >1365 bp 
ATGGCCACCAATAAGGAGCGACTCTTTGCGGCTGGTGCCCTGGGGCCTGGATCTGGCTAC
CCAGGGGCAGGTTTCCCCTTCGCCTTCCCAGGGGCACTCAGGGGGTCTCCGCCTTTCGAG
ATGCTGAGCCCTAGCTTCCGGGGCCTGGGCCAGCCTGACCTCCCCAAGGAGATGGCCTCT
CTGTCGGTGGAGACACAGAGCACCAGCTCAGAGGAGATGGTGCCAAGCTCGCCCTCGCCC
CCTCCGCCTCCTCGGGTCTACAAGCCATGCTTCGTGTGCAATGACAAGTCCTCTGGCTAC
CACTATGGGGTCAGCTCTTGTGAAGGCTGCAAGGGCTTCTTTCGCCGAAGCATCCAGAAG
AACATGGTGTACACGTGTCACCGCGACAAAAACTGTATCATCAACAAGGTGACCAGGAAT
CGCTGCCAGTACTGCCGGCTACAGAAGTGCTTCGAAGTGGGCATGTCCAAGGAAGCTGTG
CGAAATGACCGGAACAAGAAGAAGAAAGAGGTGAAGGAAGAAGGGTCACCTGACAGCTAT
GAGCTGAGCCCTCAGTTAGAAGAGCTCATCACCAAGGTCAGCAAAGCCCATCAGGAGACT
TTCCCCTCGCTCTGCCAGCTGGGCAAGTATACCACGAACTCCAGTGCAGACCACCGCGTG
CAGCTGGATCTGGGGCTGTGGGACAAGTTCAGTGAGCTGGCTACCAAGTGCATCATCAAG
ATCGTGGAGTTTGCCAAGCGGTTGCCTGGCTTTACAGGGCTCAGCATTGCTGACCAGATC
ACTCTGCTCAAAGCTGCCTGCCTAGATATCCTGATGCTGCGTATCTGCACAAGGTACACC
CCAGAGCAGGACACCATGACCTTCTCCGACGGGCTGACCCTGAACCGGACCCAGATGCAC
AATGCCGGCTTCGGGCCCCTCACAGACCTTGTCTTTGCCTTTGCTGGGCAGCTCCTGCCC
CTGGAGATGGATGACACCGAGACAGGGCTGCTCAGCGCCATCTGCCTCATCTGCGGAGAC
CGCATGGACCTGGAGGAGCCCGAAAAAGTGGACAAGCTGCAGGAGCCACTGCTGGAAGCC
CTGAGGCTGTACGCCCGGCGCCGGCGGCCCAGCCAGCCCTACATGTTCCCAAGGATGCTA
ATGAAAATCACCGACCTCCGGGGCATCAGCACTAAGGGAGCTGAAAGGGCCATTACTCTG
AAGATGGAGATTCCAGGCCCGATGCCTCCCTTAATCCGAGAGATGCTGGAGAACCCTGAA
ATGTTTGAGGATGACTCCTCGCAGCCTGGTCCCCACCCCAATGCCTCTAGCGAGGATGAG
GTTCCTGGGGGCCAGGGCAAAGGGGGCCTGAAGTCCCCAGCCTGA
Target 4 GenBank Gene ID
Target 4 GeneCard ID RARG Link Image
Target 4 GenAtlas ID RARG Link Image
Target 4 HGNC ID HGNC:9866 Link Image
Target 4 Chromosome Location 12
Target 4 Locus 12q13
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Lehmann JM, Zhang XK, Pfahl M: RAR gamma 2 expression is regulated through a retinoic acid response element embedded in Sp1 sites. Mol Cell Biol. 1992 Jul;12(7):2976-85. [PubMed Link Image]
  2. Kastner P, Krust A, Mendelsohn C, Garnier JM, Zelent A, Leroy P, Staub A, Chambon P: Murine isoforms of retinoic acid receptor gamma with specific patterns of expression. Proc Natl Acad Sci U S A. 1990 Apr;87(7):2700-4. [PubMed Link Image]
  3. Krust A, Kastner P, Petkovich M, Zelent A, Chambon P: A third human retinoic acid receptor, hRAR-gamma. Proc Natl Acad Sci U S A. 1989 Jul;86(14):5310-4. [PubMed Link Image]
  4. Renaud JP, Rochel N, Ruff M, Vivat V, Chambon P, Gronemeyer H, Moras D: Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid. Nature. 1995 Dec 14;378(6558):681-9. [PubMed Link Image]
  5. Klaholz BP, Renaud JP, Mitschler A, Zusi C, Chambon P, Gronemeyer H, Moras D: Conformational adaptation of agonists to the human nuclear receptor RAR gamma. Nat Struct Biol. 1998 Mar;5(3):199-202. [PubMed Link Image]
Target 4 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 459
Target 5 Name Retinoic acid receptor RXR-alpha
Target 5 Synonyms
  1. Retinoid X receptor alpha
Target 5 Gene Name RXRA
Target 5 Protein Sequence >Retinoic acid receptor RXR-alpha 
MDTKHFLPLDFSTQVNSSLTSPTGRGSMAAPSLHPSLGPGIGSPGQLHSPISTLSSPING
MGPPFSVISSPMGPHSMSVPTTPTLGFSTGSPQLSSPMNPVSSSEDIKPPLGLNGVLKVP
AHPSGNMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLID
KRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKDRNENEVESTSSANEDMPVERILEAEL
AVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVIL
LRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDM
QMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLL
RLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT
Target 5 Number of Residues 469
Target 5 Molecular Weight 50812
Target 5 Theoretical pI 7.86
Target 5 GO Classification
Function
steroid binding
signal transducer activity
receptor activity
ligand-dependent nuclear receptor activity
steroid hormone receptor activity
binding
nucleic acid binding
DNA binding
transcription factor activity
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 5 General Function Involved in transcription factor activity
Target 5 Specific Function Nuclear hormone receptor. Involved in the retinoic acid response pathway. Binds 9-cis retinoic acid (9C-RA). ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer
Target 5 Pathways Not Available
Target 5 Reactions Not Available
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 35885 Link Image
Target 5 UniProtKB/Swiss-Prot ID P19793 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name RXRA_HUMAN Link Image
Target 5 PDB ID 1LBD Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location
  • Nucleus
Target 5 Gene Sequence >1389 bp 
ATGGACACCAAACATTTCCTGCCGCTCGATTTCTCCACCCAGGTGAACTCCTCCCTCACC
TCCCCGACGGGGCGAGGCTCCATGGCTGCCCCCTCGCTGCACCCGTCCCTGGGGCCTGGC
ATCGGCTCCCCGGGACAGCTGCATTCTCCCATCAGCACCCTGAGCTCCCCCATCAACGGC
ATGGGCCCGCCTTTCTCGGTCATCAGCTCCCCCATGGGCCCCCACTCCATGTCGGTGCCC
ACCACACCCACCCTGGGCTTCAGCACTGGCAGCCCCCAGCTCAGCTCACCTATGAACCCC
GTCAGCAGCAGCGAGGACATCAAGCCCCCCCTGGGCCTCAATGGCGTCCTCAAGGTCCCC
GCCCACCCCTCAGGAAACATGGCTTCCTTCACCAAGCACATCTGCGCCATCTGCGGGGAC
CGCTCCTCAGGCAAGCACTATGGAGTGTACAGCTGCGAGGGGTGCAAGGGCTTCTTCAAG
CGGACGGTGCGCAAGGACCTGACCTACACCTGCCGCGACAACAAGGACTGCCTGATTGAC
AAGCGGCAGCGGAACCGGTGCCAGTACTGCCGCTACCAGAAGTGCCTGGCCATGGGCATG
AAGCGGGAAGCCGTGCAGGAGGAGCGGCAGCGTGGCAAGGACCGGAACGAGAATGAGGTG
GAGTCGACCAGCAGCGCCAACGAGGACATGCCGGTGGAGAGGATCCTGGAGGCTGAGCTG
GCCGTGGAGCCCAAGACCGAGACCTACGTGGAGGCAAACATGGGGCTGAACCCCAGCTCG
CCGAACGACCCTGTCACCAACATTTGCCAAGCAGCCGACAAACAGCTTTTCACCCTGGTG
GAGTGGGCCAAGCGGATCCCACACTTCTCAGAGCTGCCCCTGGACGACCAGGTCATCCTG
CTGCGGGCAGGCTGGAATGAGCTGCTCATCGCCTCCTTCTCCCACCGCTCCATCGCCGTG
AAGGACGGGATCCTCCTGGCCACCGGGCTGCACGTCCACCGGAACAGCGCCCACAGCGCA
GGGGTGGGCGCCATCTTTGACAGGGTGCTGACGGAGCTTGTGTCCAAGATGCGGGACATG
CAGATGGACAAGACGGAGCTGGGCTGCCTGCGCGCCATCGTCCTCTTTAACCCTGACTCC
AAGGGGCTCTCGAACCCGGCCGAGGTGGAGGCGCTGAGGGAGAAGGTCTATGCGTCCTTG
GAGGCCTACTGCAAGCACAAGTACCCAGAGCAGCCGGGAAGGTTCGCTAAGCTCTTGCTC
CGCCTGCCGGCTCTGCGCTCCATCGGGCTCAAATGCCTGGAACATCTCTTCTTCTTCAAG
CTCATCGGGGACACACCCATTGACACCTTCCTTATGGAGATGCTGGAGGCGCCGCACCAA
ATGACTTAG
Target 5 GenBank Gene ID
Target 5 GeneCard ID RXRA Link Image
Target 5 GenAtlas ID RXRA Link Image
Target 5 HGNC ID HGNC:10477 Link Image
Target 5 Chromosome Location 9
Target 5 Locus 9q34.3
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Lee SK, Anzick SL, Choi JE, Bubendorf L, Guan XY, Jung YK, Kallioniemi OP, Kononen J, Trent JM, Azorsa D, Jhun BH, Cheong JH, Lee YC, Meltzer PS, Lee JW: A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo. J Biol Chem. 1999 Nov 26;274(48):34283-93. [PubMed Link Image]
  2. Mathur M, Tucker PW, Samuels HH: PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors. Mol Cell Biol. 2001 Apr;21(7):2298-311. [PubMed Link Image]
  3. Heyman RA, Mangelsdorf DJ, Dyck JA, Stein RB, Eichele G, Evans RM, Thaller C: 9-cis retinoic acid is a high affinity ligand for the retinoid X receptor. Cell. 1992 Jan 24;68(2):397-406. [PubMed Link Image]
  4. Mangelsdorf DJ, Ong ES, Dyck JA, Evans RM: Nuclear receptor that identifies a novel retinoic acid response pathway. Nature. 1990 May 17;345(6272):224-9. [PubMed Link Image]
  5. Rastinejad F, Perlmann T, Evans RM, Sigler PB: Structural determinants of nuclear receptor assembly on DNA direct repeats. Nature. 1995 May 18;375(6528):203-11. [PubMed Link Image]
  6. Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D: Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature. 1995 Jun 1;375(6530):377-82. [PubMed Link Image]
  7. Lee MS, Sem DS, Kliewer SA, Provencal J, Evans RM, Wright PE: NMR assignments and secondary structure of the retinoid X receptor alpha DNA-binding domain. Evidence for the novel C-terminal helix. Eur J Biochem. 1994 Sep 1;224(2):639-50. [PubMed Link Image]
  8. Chen H, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM: Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell. 1997 Aug 8;90(3):569-80. [PubMed Link Image]
  9. Holmbeck SM, Foster MP, Casimiro DR, Sem DS, Dyson HJ, Wright PE: High-resolution solution structure of the retinoid X receptor DNA-binding domain. J Mol Biol. 1998 Aug 14;281(2):271-84. [PubMed Link Image]
Target 5 Drug References
  1. Zitnik RJ, Kotloff RM, Latifpour J, Zheng T, Whiting NL, Schwalb J, Elias JA: Retinoic acid inhibition of IL-1-induced IL-6 production by human lung fibroblasts. J Immunol. 1994 Feb 1;152(3):1419-27. [PubMed Link Image]
  2. Orfanos CE, Zouboulis CC, Almond-Roesler B, Geilen CC: Current use and future potential role of retinoids in dermatology. Drugs. 1997 Mar;53(3):358-88. [PubMed Link Image]
  3. Billoni N, Gautier B, Mahe YF, Bernard BA: Expression of retinoid nuclear receptor superfamily members in human hair follicles and its implication in hair growth. Acta Derm Venereol. 1997 Sep;77(5):350-5. [PubMed Link Image]
Drug Target 6 [top]
Target 6 ID 564
Target 6 Name Cellular retinoic acid-binding protein 1
Target 6 Synonyms
  1. CRABP-I
  2. Cellular retinoic acid- binding protein I
  3. Retinoic acid-binding protein I, cellular
Target 6 Gene Name CRABP1
Target 6 Protein Sequence >Cellular retinoic acid-binding protein 1 
PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRT
TEINFKVGEGFEEETVDGRKCRSLATWENENKIHCTQTLLEGDGPKTYWTRELANDELIL
TFGADDVVCTRIYVRE
Target 6 Number of Residues 138
Target 6 Molecular Weight 15434
Target 6 Theoretical pI 5.03
Target 6 GO Classification
Function
lipid binding
binding
Process
physiological process
cellular physiological process
transport
Component
Not Available
Target 6 General Function Involved in retinoid binding
Target 6 Specific Function Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors
Target 6 Pathways Not Available
Target 6 Reactions Not Available
Target 6 Pfam Domain Function
Target 6 Signals
  • None
Target 6 Transmembrane Regions
  • None
Target 6 Essentiality Non-Essential
Target 6 GenBank ID Protein 241542 Link Image
Target 6 UniProtKB/Swiss-Prot ID P29762 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name RABP1_HUMAN Link Image
Target 6 PDB ID 2CBR Link Image
Target 6 PDB File Show
Target 6 3D Structure
Target 6 Cellular Location
  • Cytoplasm
Target 6 Gene Sequence >414 bp 
ATGCCCAACTTCGCCGGCACCTGGAAGATGCGCAGCAGCGAGAATTTCGACGAGCTGCTG
AAGGCACTGGGTGTGAACGCCATGCTGAGGAAAGTGGCCGTAGCGGCTGCGTCCAAGCCG
CACGTGGAGATCCGCCAGGACGGGGATCAGTTCTACATCAAGACATCCACCACCGTGCGC
ACCACTGAGATCAACTTCAAGGTCGGAGAAGGCTTTGAGGAGGAGACCGTGGACGGACGC
AAGTGCAGGAGTTTAGCCACTTGGGAGAATGAGAACAAGATCCACTGCACCCAAACTCTT
CTTGAAGGGGACGGCCCCAAAACCTACTGGACCCGTGAGCTGGCCAACGATGAACTTATC
CTGACGTTTGGCGCCGATGACGTGGTCTGCACCAGAATTTATGTCCGGGAATGA
Target 6 GenBank Gene ID
Target 6 GeneCard ID CRABP1 Link Image
Target 6 GenAtlas ID CRABP1 Link Image
Target 6 HGNC ID HGNC:2338 Link Image
Target 6 Chromosome Location 15
Target 6 Locus 15q24
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Eller MS, Oleksiak MF, McQuaid TJ, McAfee SG, Gilchrest BA: The molecular cloning and expression of two CRABP cDNAs from human skin. Exp Cell Res. 1992 Feb;198(2):328-36. [PubMed Link Image]
  2. Astrom A, Tavakkol A, Pettersson U, Cromie M, Elder JT, Voorhees JJ: Molecular cloning of two human cellular retinoic acid-binding proteins (CRABP). Retinoic acid-induced expression of CRABP-II but not CRABP-I in adult human skin in vivo and in skin fibroblasts in vitro. J Biol Chem. 1991 Sep 15;266(26):17662-6. [PubMed Link Image]
Target 6 Drug References
  1. Madani K, Bazzano G, Chou A: Evaluation of retinoids as inhibitors of [3H] all-trans retinoic acid binding to cellular retinoic acid-binding protein in rat skin and testes. Arch Dermatol Res. 1986;278(4):302-6. [PubMed Link Image]
Drug Target 7 [top]
Target 7 ID 730
Target 7 Name Retinoic acid receptor alpha
Target 7 Synonyms
  1. RAR-alpha
Target 7 Gene Name RARA
Target 7 Protein Sequence >Retinoic acid receptor alpha 
MASNSSSCPTPGGGHLNGYPVPPYAFFFPPMLGGLSPPGALTTLQHQLPVSGYSTPSPAT
IETQSSSSEEIVPSPPSPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNM
VYTCHRDKNCIINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKEVPKPECSESYTL
TPEVGELIEKVRKAHQETFPALCQLGKYTTNNSSEQRVSLDIDLWDKFSELSTKCIIKTV
EFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNA
GFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLICGDRQDLEQPDRVDMLQEPLLEALK
VYVRKRRPSRPHMFPKMLMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGL
DTLSGQPGGGGRDGGGLAPPPGSCSPSLSPSSNRSSPATHSP
Target 7 Number of Residues 469
Target 7 Molecular Weight 50772
Target 7 Theoretical pI 7.95
Target 7 GO Classification
Function
retinoic acid receptor activity
signal transducer activity
receptor activity
ligand-dependent nuclear receptor activity
steroid hormone receptor activity
binding
nucleic acid binding
DNA binding
transcription factor activity
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 7 General Function Involved in transcription factor activity
Target 7 Specific Function This is a receptor for retinoic acid. This metabolite has profound effects on vertebrate development. Retinoic acid is a morphogen and is a powerful teratogen. This receptor controls cell function by directly regulating gene expression
Target 7 Pathways Not Available
Target 7 Reactions Not Available
Target 7 Pfam Domain Function
Target 7 Signals
  • None
Target 7 Transmembrane Regions
  • None
Target 7 Essentiality Non-Essential
Target 7 GenBank ID Protein 36157 Link Image
Target 7 UniProtKB/Swiss-Prot ID P10276 Link Image
Target 7 UniProtKB/Swiss-Prot Entry Name RARA_HUMAN Link Image
Target 7 PDB ID Not Available
Target 7 Cellular Location
  • Nucleus
Target 7 Gene Sequence >1389 bp 
ATGGCCAGCAACAGCAGCTCCTGCCCGACACCTGGGGGCGGGCACCTCAATGGGTACCCG
GTGCCTCCCTACGCCTTCTTCTTCCCCCCTATGCTGGGTGGACTCTCCCCGCCAGGCGCT
CTGACCACTCTCCAGCACCAGCTTCCAGTTAGTGGATATAGCACACCATCCCCAGCCACC
ATTGAGACCCAGAGCAGCAGTTCTGAAGAGATAGTGCCCAGCCCTCCCTCGCCACCCCCT
CTACCCCGCATCTACAAGCCTTGCTTTGTCTGTCAGGACAAGTCCTCAGGCTACCACTAT
GGGGTCAGCGCCTGTGAGGGCTGCAAGGGCTTCTTCCGCCGCAGCATCCAGAAGAACATG
GTGTACACGTGTCACCGGGACAAGAACTGCATCATCAACAAGGTGACCCGGAACCGCTGC
CAGTACTGCCGACTGCAGAAGTGCTTTGAAGTGGGCATGTCCAAGGAGTCTGTGAGAAAC
GACCGAAACAAGAAGAAGAAGGAGGTGCCCAAGCCCGAGTGCTCTGAGAGCTACACGCTG
ACGCCGGAGGTGGGGGAGCTCATTGAGAAGGTGCGCAAAGCGCACCAGGAAACCTTCCCT
GCCCTCTGCCAGCTGGGCAAATACACTACGAACAACAGCTCAGAACAACGTGTCTCTCTG
GACATTGACCTCTGGGACAAGTTCAGTGAACTCTCCACCAAGTGCATCATTAAGACTGTG
GAGTTCGCCAAGCAGCTGCCCGGCTTCACCACCCTCACCATCGCCGACCAGATCACCCTC
CTCAAGGCTGCCTGCCTGGACATCCTGATCCTGCGGATCTGCACGCGGTACACGCCCGAG
CAGGACACCATGACCTTCTCGGACGGGCTGACCCTGAACCGGACCCAGATGCACAACGCT
GGCTTCGGCCCCCTCACCGACCTGGTCTTTGCCTTCGCCAACCAGCTGCTGCCCCTGGAG
ATGGATGATGCGGAGACGGGGCTGCTCAGCGCCATCTGCCTCATCTGCGGAGACCGCCAG
GACCTGGAGCAGCCGGACCGGGTGGACATGCTGCAGGAGCCGCTGCTGGAGGCGCTAAAG
GTCTACGTGCGGAAGCGGAGGCCCAGCCGCCCCCACATGTTCCCCAAGATGCTAATGAAG
ATTACTGACCTGCGAAGCATCAGCGCCAAGGGGGCTGAGCGGGTGATCACGCTGAAGATG
GAGATCCCGGGCTCCATGCCGCCTCTCATCCAGGAAATGTTGGAGAACTCAGAGGGCCTG
GACACTCTGAGCGGACAGCCGGGGGGTGGGGGGCGGGACGGGGGTGGCCTGGCCCCCCCG
CCAGGCAGCTGTAGCCCCAGCCTCAGCCCCAGCTCCAACAGAAGCAGCCCGGCCACCCAC
TCCCCGTGA
Target 7 GenBank Gene ID
Target 7 GeneCard ID RARA Link Image
Target 7 GenAtlas ID RARA Link Image
Target 7 HGNC ID HGNC:9864 Link Image
Target 7 Chromosome Location 17
Target 7 Locus 17q21
Target 7 SNPs SNPJam Report Link Image
Target 7 General References
  1. Hjalt TA, Murray JC: Genomic structure of the human retinoic acid receptor-alpha1 gene. Mamm Genome. 1999 May;10(5):528-9. [PubMed Link Image]
  2. Lee SK, Anzick SL, Choi JE, Bubendorf L, Guan XY, Jung YK, Kallioniemi OP, Kononen J, Trent JM, Azorsa D, Jhun BH, Cheong JH, Lee YC, Meltzer PS, Lee JW: A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo. J Biol Chem. 1999 Nov 26;274(48):34283-93. [PubMed Link Image]
  3. 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]
  4. Brand NJ, Petkovich M, Chambon P: Characterization of a functional promoter for the human retinoic acid receptor-alpha (hRAR-alpha). Nucleic Acids Res. 1990 Dec 11;18(23):6799-806. [PubMed Link Image]
  5. Petkovich M, Brand NJ, Krust A, Chambon P: A human retinoic acid receptor which belongs to the family of nuclear receptors. Nature. 1987 Dec 3-9;330(6147):444-50. [PubMed Link Image]
  6. Giguere V, Ong ES, Segui P, Evans RM: Identification of a receptor for the morphogen retinoic acid. Nature. 1987 Dec 17-23;330(6149):624-9. [PubMed Link Image]
  7. Chen Z, Guidez F, Rousselot P, Agadir A, Chen SJ, Wang ZY, Degos L, Zelent A, Waxman S, Chomienne C: PLZF-RAR alpha fusion proteins generated from the variant t(11;17)(q23;q21) translocation in acute promyelocytic leukemia inhibit ligand-dependent transactivation of wild-type retinoic acid receptors. Proc Natl Acad Sci U S A. 1994 Feb 1;91(3):1178-82. [PubMed Link Image]
  8. Redner RL, Rush EA, Faas S, Rudert WA, Corey SJ: The t(5;17) variant of acute promyelocytic leukemia expresses a nucleophosmin-retinoic acid receptor fusion. Blood. 1996 Feb 1;87(3):882-6. [PubMed Link Image]
  9. Chen H, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM: Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell. 1997 Aug 8;90(3):569-80. [PubMed Link Image]
Target 7 Drug References
  1. Saurat JH: Retinoids and psoriasis: novel issues in retinoid pharmacology and implications for psoriasis treatment. J Am Acad Dermatol. 1999 Sep;41(3 Pt 2):S2-6. [PubMed Link Image]
  2. Harnish DC, Barua AB, Soprano KJ, Soprano DR: Induction of beta-retinoic acid receptor mRNA by teratogenic doses of retinoids in murine fetuses. Differentiation. 1990 Nov;45(2):103-8. [PubMed Link Image]
  3. Zitnik RJ, Kotloff RM, Latifpour J, Zheng T, Whiting NL, Schwalb J, Elias JA: Retinoic acid inhibition of IL-1-induced IL-6 production by human lung fibroblasts. J Immunol. 1994 Feb 1;152(3):1419-27. [PubMed Link Image]
  4. Orfanos CE, Zouboulis CC, Almond-Roesler B, Geilen CC: Current use and future potential role of retinoids in dermatology. Drugs. 1997 Mar;53(3):358-88. [PubMed Link Image]
  5. Billoni N, Gautier B, Mahe YF, Bernard BA: Expression of retinoid nuclear receptor superfamily members in human hair follicles and its implication in hair growth. Acta Derm Venereol. 1997 Sep;77(5):350-5. [PubMed Link Image]
Drug Target 8 [top]
Target 8 ID 780
Target 8 Name Retinoic acid receptor RXR-gamma
Target 8 Synonyms
  1. Retinoid X receptor gamma
Target 8 Gene Name RXRG
Target 8 Protein Sequence >Retinoic acid receptor RXR-gamma 
MYGNYSHFMKFPAGYGGSPGHTGSTSMSPSAALSTGKPMDSHPSYTDTPVSAPRTLSAVG
TPLNALGSPYRVITSAMGPPSGALAAPPGINLVAPPSSQLNVVNSVSSSEDIKPLPGLPG
IGNMNYPSTSPGSLVKHICAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLIYTCRDNKD
CLIDKRQRNRCQYCRYQKCLVMGMKREAVQEERQRSRERAESEAECATSGHEDMPVERIL
EAELAVEPKTESYGDMNMENSTNDPVTNICHAADKQLFTLVEWAKRIPHFSDLTLEDQVI
LLRAGWNELLIASFSHRSVSVQDGILLATGLHVHRSSAHSAGVGSIFDRVLTELVSKMKD
MQMDKSELGCLRAIVLFNPDAKGLSNPSEVETLREKVYATLEAYTKQKYPEQPGRFAKLL
LRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLETPLQIT
Target 8 Number of Residues 470
Target 8 Molecular Weight 50872
Target 8 Theoretical pI 7.67
Target 8 GO Classification
Function
steroid binding
signal transducer activity
receptor activity
ligand-dependent nuclear receptor activity
steroid hormone receptor activity
binding
nucleic acid binding
DNA binding
transcription factor activity
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 8 General Function Involved in transcription factor activity
Target 8 Specific Function Nuclear hormone receptor. Involved in the retinoic acid response pathway. Binds 9-cis retinoic acid (9C-RA)
Target 8 Pathways Not Available
Target 8 Reactions Not Available
Target 8 Pfam Domain Function
Target 8 Signals
  • None
Target 8 Transmembrane Regions
  • None
Target 8 Essentiality Non-Essential
Target 8 GenBank ID Protein 1053069 Link Image
Target 8 UniProtKB/Swiss-Prot ID P48443 Link Image
Target 8 UniProtKB/Swiss-Prot Entry Name RXRG_HUMAN Link Image
Target 8 PDB ID Not Available
Target 8 Cellular Location
  • Nucleus
Target 8 Gene Sequence >1392 bp 
ATGTATGGAAATTATTCTCACTTCATGAAGTTTCCCGCAGGCTATGGAGGCTCCCCTGGC
CACACTGGCTCTACATCCATGAGCCCATCAGCAGCCTTGTCCACAGGGAAGCCAATGGAC
AGCCACCCCAGCTACACAGATACCCCAGTGAGTGCCCCACGGACTCTGAGTGCAGTGGGG
ACCCCCCTCAATGCCCTGGGCTCTCCATATCGAGTCATCACCTCTGCCATGGGCCCACCC
TCAGGAGCACTTGCAGCGCCTCCAGGAATCAACTTGGTTGCCCCACCCAGCTCTCAGCTA
AATGTGGTCAACAGTGTCAGCAGTTCAGAGGACATCAAGCCCTTACCAGGGCTTCCCGGG
ATTGGAAACATGAACTACCCATCCACCAGCCCCGGATCTCTGGTTAAACACATCTGTGCT
ATCTGTGGAGACAGATCCTCAGGAAAGCACTACGGGGTATACAGTTGTGAAGGCTGCAAA
GGGTTCTTCAAGAGGACGATAAGGAAGGACCTCATCTACACGTGTCGGGATAATAAAGAC
TGCCTCATTGACAAGCGTCAGCGCAACCGCTGCCAGTACTGTCGCTATCAGAAGTGCCTT
GTCATGGGCATGAAGAGGGAAGCTGTGCAAGAAGAAAGACAGAGGAGCCGAGAGCGAGCT
GAGAGTGAGGCAGAATGTGCTACCAGTGGTCATGAAGACATGCCTGTGGAGAGGATTCTA
GAAGCTGAACTTGCTGTTGAACCAAAGACAGAATCCTATGGTGACATGAATATGGAGAAC
TCGACAAATGACCCTGTTACCAACATATGTCATGCTGCTGACAAGCAGCTTTTCACCCTC
GTTGAATGGGCCAAGCGTATTCCCCACTTCTCTGACCTCACCTTGGAGGACCAGGTCATT
TTGCTTCGGGCAGGGTGGAATGAATTGCTGATTGCCTCTTTCTCCCACCGCTCAGTTTCC
GTGCAGGATGGCATCCTTCTGGCCACGGGTTTACATGTCCACCGGAGCAGTGCCCACAGT
GCTGGGGTCGGCTCCATCTTTGACAGAGTTCTAACTGAGCTGGTTTCCAAAATGAAAGAC
ATGCAGATGGACAAGTCGGAACTGGGATGCCTGCGAGCCATTGTACTCTTTAACCCAGAT
GCCAAGGGCCTGTCCAACCCCTCTGAGGTGGAGACTCTGCGAGAGAAGGTTTATGCCACC
CTTGAGGCCTACACCAAGCAGAAGTATCCGGAACAGCCAGGCAGGTTTGCCAAGCTGCTG
CTGCGCCTCCCAGCTCTGCGTTCCATTGGCTTGAAATGCCTGGAGCACCTCTTCTTCTTC
AAGCTCATCGGGGACACCCCCATTGACACCTTCCTCATGGAGATGTTGGAGACCCCGCTG
CAGATCACCTGA
Target 8 GenBank Gene ID
Target 8 GeneCard ID RXRG Link Image
Target 8 GenAtlas ID RXRG Link Image
Target 8 HGNC ID HGNC:10479 Link Image
Target 8 Chromosome Location 1
Target 8 Locus 1q22-q23
Target 8 SNPs SNPJam Report Link Image
Target 8 General References Not Available
Target 8 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [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.