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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:06:20
Primary Accession Number DB00459
Secondary Accession Number
  • APRD00778
Name Acitretin
Drug Type
  • Approved
  • Small Molecule
Description An oral retinoid effective in the treatment of psoriasis. It is the major metabolite of etretinate with the advantage of a much shorter half-life when compared with etretinate. [PubChem]
Synonyms Not Available
Brand Names
  1. Acetretin
  2. Soriatane
Brand Mixtures Not Available
Chemical IUPAC Name (2Z,4E,6E,8E)-9-(4-methoxy-2,3,6-trimethylphenyl)-3,7-dimethylnona-2,4,6,8-tetraenoic acid
Chemical Formula C21H26O3
Chemical Structure Structure
CAS Registry Number 55079-83-9
InChI Identifier InChI=1/C21H26O3/c1-14(8-7-9-15(2)12-21(22)23)10-11-19-16(3)13-20(24-6)18(5)17(19)4/h7-13H,1-6H3,(H,22,23)/b9-7+,11-10+,14-8+,15-12-/f/h22H
InChI Key IHUNBGSDBOWDMA-UZLJJVSQDX
KEGG Drug Not Available
KEGG Compound Not Available
PubChem Compound 6437841 Link Image
PubChem Substance 691722 Link Image
ChEBI ID Not Available
PharmGKB ID Not Available
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02070847 Link Image
RxList Link http://www.rxlist.com/cgi/generic3/acitretin.htm Link Image
PDRhealth Link http://www.pdrhealth.com/drug_info/rxdrugprofiles/drugs/sor1698.shtml Link Image
Wikipedia Link http://en.wikipedia.org/wiki/Acitretin Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 326.4293
Monoisotopic Molecular Weight 326.1882
State Solid
Melting Point 228-230 oC
Experimental Water Solubility 0.0729 mg/L Source: PhysProp
Predicted Water Solubility 4.78e-04 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 5.7 Source: PhysProp
Predicted LogP 5.20 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -5.83 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 COC1=C(C)C(C)=C(\C=C\C(C)=C\C=C\C(C)=C/C(O)=O)C(C)=C1
Canonical SMILES COC1=C(C)C(C)=C(C=CC(C)=CC=CC(C)=CC(O)=O)C(C)=C1
Drug Category
  • Keratolytic Agents
ATC Codes
AHFS Codes
  • 84:92.00
Indication For the treatment of severe psoriasis in adults.
Pharmacology 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 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 Oral absorption of acitretin is optimal when given with food, and is linear and proportional with increasing doses from 25 to 100 mg. Approximately 72% (range 47% to 109%) of the administered dose was absorbed after a single 50 mg dose of acitretin was given to 12 healthy subjects.
Toxicity Oral, rat: LD50 = >4000 mg/kg. Symptoms of overdose include headache and vertigo.
Protein Binding Over 99.9% bound to plasma proteins, primarily albumin.
Biotransformation Following oral absorption, acitretin undergoes extensive metabolism and interconversion by simple isomerization to its 13-cis form (cis-acitretin). Both parent compound and isomer are further metabolized into chain-shortened breakdown products and conjugates, which are excreted.
Half Life 49 hours (range 33 to 96 hours)
Dosage Forms
Form Route
Capsule Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Demeclocycline Increased risk of intracranial hypertension
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
Norethindrone Acitretine may cause a loss of contraceptive effect
Oxytetracycline Increased risk of intracranial hypertension
Rolitetracycline Increased risk of intracranial hypertension
Tetracycline Increased risk of intracranial hypertension
Food Interactions Not Available
Pathways Not Available
General References
  1. Wikipedia Link Image
  2. RxList Link Image
  3. PDRhealth 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. Serum albumin
  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. Zouboulis CC: Retinoids--which dermatological indications will benefit in the near future? Skin Pharmacol Appl Skin Physiol. 2001 Sep-Oct;14(5):303-15. [PubMed Link Image]
  2. Berggren Soderlund M, Johannesson G, Fex G: Expression of human all-trans-retinoic acid receptor beta and its ligand-binding domain in Escherichia coli. Biochem J. 1995 May 15;308 ( Pt 1):353-9. [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. 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]
  2. Tian K, Norris AW, Lin CL, Li E: The isolation and characterization of purified heterocomplexes of recombinant retinoic acid receptor and retinoid X receptor ligand binding domains. Biochemistry. 1997 May 13;36(19):5669-76. [PubMed Link Image]
Drug Target 6 [top]
Target 6 ID 587
Target 6 Name Serum albumin
Target 6 Synonyms
  1. Serum albumin precursor
Target 6 Gene Name ALB
Target 6 Protein Sequence >Serum albumin precursor 
MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPF
EDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEP
ERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLF
FAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAV
ARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLK
ECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYAR
RHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFE
QLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVV
LNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTL
SEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLV
AASQAALGL
Target 6 Number of Residues 619
Target 6 Molecular Weight 69367
Target 6 Theoretical pI 6.21
Target 6 GO Classification
Function
transporter activity
carrier activity
Process
physiological process
cellular physiological process
transport
Component
extracellular region
extracellular space
Target 6 General Function Involved in antioxidant activity
Target 6 Specific Function Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood
Target 6 Pathways Not Available
Target 6 Reactions Not Available
Target 6 Pfam Domain Function
Target 6 Signals
  • 1-18
Target 6 Transmembrane Regions
  • None
Target 6 Essentiality Non-Essential
Target 6 GenBank ID Protein 28590 Link Image
Target 6 UniProtKB/Swiss-Prot ID P02768 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name ALBU_HUMAN Link Image
Target 6 PDB ID 1HA2 Link Image
Target 6 PDB File Show
Target 6 3D Structure
Target 6 Cellular Location
  • Secreted protein
Target 6 Gene Sequence >1830 bp 
ATGAAGTGGGTAACCTTTATTTCCCTTCTTTTTCTCTTTAGCTCGGCTTATTCCAGGGGT
GTGTTTCGTCGAGATGCACACAAGAGTGAGGTTGCTCATCGGTTTAAAGATTTGGGAGAA
GAAAATTTCAAAGCCTTGGTGTTGATTGCCTTTGCTCAGTATCTTCAGCAGTGTCCATTT
GAAGATCATGTAAAATTAGTGAATGAAGTAACTGAATTTGCAAAAACATGTGTTGCTGAT
GAGTCAGCTGAAAATTGTGACAAATCACTTCATACCCTTTTTGGAGACAAATTATGCACA
GTTGCAACTCTTCGTGAAACCTATGGTGAAATGGCTGACTGCTGTGCAAAACAAGAACCT
GGGAGAAATGAATGCTTCTTGCAACACAAAGATGACAACCCAAACCTCCCCCGATTGGTG
AGACCAGAGGTTGATGTGATGTGCACTGCTTTTCATGACAATGAAGAGACATTTTTGAAA
AAATACTTATATGAAATTGCCAGAAGACATCCTTACTTTTATGCCCCGGAACTCCTTTTC
TTTGCTAAAAGGTATAAAGCTGCTTTTACAGAATGTTGCCAAGCTGCTGATAAAGCTGCC
TGCCTGTTGCCAAAGCTCGATGAACTTCGGGATGAAGGGAAGGCTTCGTCTGCCAAACAG
AGACTCAAGTGTGCCAGTCTCCAAAAATTTGGAGAAAGAGCTTTCAAAGCATGGGCAGTA
GCTCGCCTGAGCCAGAGATTTCCCAAAGCTGAGTTTGCAGAAGTTTCCAAGTTAGTGACA
GATCTTACCAAAGTCCACACGGAATGCTGCCATGGAGATCTGCTTGAATGTGCTGATGAC
AGGGCGGACCTTGCCAAGTATATCTGTGAAAATCAAGATTCGATCTCCAGTAAACTGAAG
GAATGCTGTGAAAAACCTCTGTTGGAAAAATCCCACTGCATTGCCGAAGTGGAAAATGAT
GAGATGCCTGCTGACTTGCCTTCATTAGCTGCTGATTTTGTTGAAAGTAAGGATGTTTGC
AAAAACTATGCTGAGGCAAAGGATGTCTTCTTGGGCATGTTTTTGTATGAATATGCAAGA
AGGCATCCTGATTACTCTGTCGTGCTGCTGCTGAGACTTGCCAAGACATATGAAACCACT
CTAGAGAAGTGCTGTGCCGCTGCAGATCCTCATGAATGCTATGCCAAAGTGTTCGATGAA
TTTAAACCTCTTGTGGAAGAGCCTCAGAATTTAATCAAACAAAATTGTGAGCTTTTTGAG
CAGCTTGGAGAGTACAAATTCCAGAATGCGCTGTTAGTTCGTTACACCAAGAAAGTACCC
GAAGTGTCAACTCCAACTCTTGTAGAGGTCTCAAGAAACCTAGGAAAAGTGGGCAGCAAA
TGTTGTAAACATCCTGAAGCAAAAAGAATGCCCTGTGCAGAAGACTATCTATCCGTGGTC
CTGAACCAGTTATGTGTGTTGCATGAGAAAACGCCAGTAAGTGACAGAGTCACCAAATGC
TGCACAGAATCCTTGGTGAACAGGCGACCATGCTTTTCAGCTCTGGAAGTCGATGAAACA
TACGTTCCCAAAGAGTTTAATGCTGAAACATTCACCTTCCATGCAGATATATGCACACTT
TCTGAGAAGGAGAGACAAATCAAGAAACAAACTGCACTTGTTGAGCTCGTGAAACACAAG
CCCAAGGCAACAAAAGAGCAACTGAAAGCTGTTATGGATGATTTCGCTGCTTTTGTAGAG
AAGTGCTGCAAGGCTGACGATAAGGAGACCTGCTTTGCCGAGGAGGGTAAAAAACTTGTT
GCTGCAAGTCAAGCTGCCTTAGGCTTATAA
Target 6 GenBank Gene ID
Target 6 GeneCard ID ALB Link Image
Target 6 GenAtlas ID ALB Link Image
Target 6 HGNC ID HGNC:399 Link Image
Target 6 Chromosome Location 4
Target 6 Locus 4q11-q13
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K: Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng. 1999 Jun;12(6):439-46. [PubMed Link Image]
  2. Bhattacharya AA, Curry S, Franks NP: Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures. J Biol Chem. 2000 Dec 8;275(49):38731-8. [PubMed Link Image]
  3. Minchiotti L, Campagnoli M, Rossi A, Cosulich ME, Monti M, Pucci P, Kragh-Hansen U, Granel B, Disdier P, Weiller PJ, Galliano M: A nucleotide insertion and frameshift cause albumin Kenitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges. Eur J Biochem. 2001 Jan;268(2):344-52. [PubMed Link Image]
  4. Yu Y, Zhang C, Zhou G, Wu S, Qu X, Wei H, Xing G, Dong C, Zhai Y, Wan J, Ouyang S, Li L, Zhang S, Zhou K, Zhang Y, Wu C, He F: Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs. Genome Res. 2001 Aug;11(8):1392-403. [PubMed Link Image]
  5. Spahr CS, Davis MT, McGinley MD, Robinson JH, Bures EJ, Beierle J, Mort J, Courchesne PL, Chen K, Wahl RC, Yu W, Luethy R, Patterson SD: Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. I. Profiling an unfractionated tryptic digest. Proteomics. 2001 Jan;1(1):93-107. [PubMed Link Image]
  6. Petitpas I, Grune T, Bhattacharya AA, Curry S: Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids. J Mol Biol. 2001 Dec 14;314(5):955-60. [PubMed Link Image]
  7. Meloun B, Moravek L, Kostka V: Complete amino acid sequence of human serum albumin. FEBS Lett. 1975 Oct 15;58(1):134-7. [PubMed Link Image]
  8. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  9. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  10. Minchiotti L, Galliano M, Stoppini M, Ferri G, Crespeau H, Rochu D, Porta F: Two alloalbumins with identical electrophoretic mobility are produced by differently charged amino acid substitutions. Biochim Biophys Acta. 1992 Mar 12;1119(3):232-8. [PubMed Link Image]
  11. 1518850 Carlson J, Sakamoto Y, Laurell CB, Madison J, Watkins S, Putnam FW: Alloalbuminemia in Sweden: structural study and phenotypic distribution of nine albumin variants. Proc Natl Acad Sci U S A. 1992 Sep 1;89(17):8225-9.
  12. 1630489 He XM, Carter DC: Atomic structure and chemistry of human serum albumin. Nature. 1992 Jul 16;358(6383):209-15.
  13. 1859851 Peach RJ, Brennan SO: Structural characterization of a glycoprotein variant of human serum albumin: albumin Casebrook (494 Asp----Asn). Biochim Biophys Acta. 1991 Jul 26;1097(1):49-54.
  14. 1946412 Madison J, Arai K, Sakamoto Y, Feld RD, Kyle RA, Watkins S, Davis E, Matsuda Y, Amaki I, Putnam FW: Genetic variants of serum albumin in Americans and Japanese. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9853-7.
  15. 2068071 Watkins S, Madison J, Davis E, Sakamoto Y, Galliano M, Minchiotti L, Putnam FW: A donor splice mutation and a single-base deletion produce two carboxyl-terminal variants of human serum albumin. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):5959-63.
  16. 2104980 Brennan SO, Myles T, Peach RJ, Donaldson D, George PM: Albumin Redhill (-1 Arg, 320 Ala----Thr): a glycoprotein variant of human serum albumin whose precursor has an aberrant signal peptidase cleavage site. Proc Natl Acad Sci U S A. 1990 Jan;87(1):26-30.
  17. 2247440 Galliano M, Minchiotti L, Porta F, Rossi A, Ferri G, Madison J, Watkins S, Putnam FW: Mutations in genetic variants of human serum albumin found in Italy. Proc Natl Acad Sci U S A. 1990 Nov;87(22):8721-5.
  18. 2374930 Carter DC, He XM: Structure of human serum albumin. Science. 1990 Jul 20;249(4966):302-3.
  19. 2404284 Arai K, Madison J, Shimizu A, Putnam FW: Point substitutions in albumin genetic variants from Asia. Proc Natl Acad Sci U S A. 1990 Jan;87(1):497-501.
  20. 2419329 Urano Y, Watanabe K, Sakai M, Tamaoki T: The human albumin gene. Characterization of the 5' and 3' flanking regions and the polymorphic gene transcripts. J Biol Chem. 1986 Mar 5;261(7):3244-51.
  21. 2437111 Carraway RE, Mitra SP, Cochrane DE: Structure of a biologically active neurotensin-related peptide obtained from pepsin-treated albumin(s). J Biol Chem. 1987 May 5;262(13):5968-73.
  22. 2727704 Carter DC, He XM, Munson SH, Twigg PD, Gernert KM, Broom MB, Miller TY: Three-dimensional structure of human serum albumin. Science. 1989 Jun 9;244(4909):1195-8.
  23. 2762316 Arai K, Madison J, Huss K, Ishioka N, Satoh C, Fujita M, Neel JV, Sakurabayashi I, Putnam FW: Point substitutions in Japanese alloalbumins. Proc Natl Acad Sci U S A. 1989 Aug;86(16):6092-6.
  24. 2911589 Arai K, Ishioka N, Huss K, Madison J, Putnam FW: Identical structural changes in inherited albumin variants from different populations. Proc Natl Acad Sci U S A. 1989 Jan;86(2):434-8.
  25. 3009475 Minghetti PP, Ruffner DE, Kuang WJ, Dennison OE, Hawkins JW, Beattie WG, Dugaiczyk A: Molecular structure of the human albumin gene is revealed by nucleotide sequence within q11-22 of chromosome 4. J Biol Chem. 1986 May 25;261(15):6747-57.
  26. 3087352 Mogard MH, Kobayashi R, Chen CF, Lee TD, Reeve JR Jr, Shively JE, Walsh JH: The amino acid sequence of kinetensin, a novel peptide isolated from pepsin-treated human plasma: homology with human serum albumin, neurotensin and angiotensin. Biochem Biophys Res Commun. 1986 May 14;136(3):983-8.
  27. 3474609 Takahashi N, Takahashi Y, Blumberg BS, Putnam FW: Amino acid substitutions in genetic variants of human serum albumin and in sequences inferred from molecular cloning. Proc Natl Acad Sci U S A. 1987 Jul;84(13):4413-7.
  28. 3479777 Takahashi N, Takahashi Y, Isobe T, Putnam FW, Fujita M, Satoh C, Neel JV: Amino acid substitutions in inherited albumin variants from Amerindian and Japanese populations. Proc Natl Acad Sci U S A. 1987 Nov;84(22):8001-5.
  29. 3828358 Brennan SO, Herbert P: Albumin Canterbury (313 Lys----Asn). A point mutation in the second domain of serum albumin. Biochim Biophys Acta. 1987 Apr 8;912(2):191-7.
  30. 6171778 Lawn RM, Adelman J, Bock SC, Franke AE, Houck CM, Najarian RC, Seeburg PH, Wion KL: The sequence of human serum albumin cDNA and its expression in E. coli. Nucleic Acids Res. 1981 Nov 25;9(22):6103-114.
  31. 6275391 Dugaiczyk A, Law SW, Dennison OE: Nucleotide sequence and the encoded amino acids of human serum albumin mRNA. Proc Natl Acad Sci U S A. 1982 Jan;79(1):71-5.
  32. 656055 Jacobsen C: Lysine residue 240 of human serum albumin is involved in high-affinity binding of bilirubin. Biochem J. 1978 May 1;171(2):453-9.
  33. 7852505 Rushbrook JI, Becker E, Schussler GC, Divino CM: Identification of a human serum albumin species associated with familial dysalbuminemic hyperthyroxinemia. J Clin Endocrinol Metab. 1995 Feb;80(2):461-7.
  34. 7895732 Corbett JM, Wheeler CH, Baker CS, Yacoub MH, Dunn MJ: The human myocardial two-dimensional gel protein database: update 1994. Electrophoresis. 1994 Nov;15(11):1459-65.
  35. 7902134 Galliano M, Minchiotti L, Iadarola P, Stoppini M, Giagnoni P, Watkins S, Madison J, Putnam FW: Protein and DNA sequence analysis of a 'private' genetic variant: albumin Ortonovo (Glu-505-->Lys). Biochim Biophys Acta. 1993 Nov 25;1225(1):27-32.
  36. 8022807 Madison J, Galliano M, Watkins S, Minchiotti L, Porta F, Rossi A, Putnam FW: Genetic variants of human serum albumin in Italy: point mutants and a carboxyl-terminal variant. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6476-80.
  37. 8048949 Sunthornthepvarakul T, Angkeow P, Weiss RE, Hayashi Y, Refetoff S: An identical missense mutation in the albumin gene results in familial dysalbuminemic hyperthyroxinemia in 8 unrelated families. Biochem Biophys Res Commun. 1994 Jul 29;202(2):781-7.
  38. 8347685 Brennan SO, Fellowes AP: Albumin Hawkes Bay; a low level variant caused by loss of a sulphydryl group at position 177. Biochim Biophys Acta. 1993 Aug 4;1182(1):46-50.
  39. 8513793 Minchiotti L, Galliano M, Zapponi MC, Tenni R: The structural characterization and bilirubin-binding properties of albumin Herborn, a [Lys240-->Glu] albumin mutant. Eur J Biochem. 1993 Jun 1;214(2):437-44.
  40. 9329347 Wada N, Chiba H, Shimizu C, Kijima H, Kubo M, Koike T: A novel missense mutation in codon 218 of the albumin gene in a distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese kindred. J Clin Endocrinol Metab. 1997 Oct;82(10):3246-50.
  41. 955075 Walker JE: Lysine residue 199 of human serum albumin is modified by acetylsalicyclic acid. FEBS Lett. 1976 Jul 15;66(2):173-5.
  42. 9589637 Sunthornthepvarakul T, Likitmaskul S, Ngowngarmratana S, Angsusingha K, Kitvitayasak S, Scherberg NH, Refetoff S: Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly inherited albumin defect. J Clin Endocrinol Metab. 1998 May;83(5):1448-54.
  43. 9731778 Curry S, Mandelkow H, Brick P, Franks N: Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat Struct Biol. 1998 Sep;5(9):827-35.
Target 6 Drug References
  1. Urien S, Claudepierre P, Meyer J, Brandt R, Tillement JP: Comparative binding of etretinate and acitretin to plasma proteins and erythrocytes. Biochem Pharmacol. 1992 Nov 3;44(9):1891-3. [PubMed Link Image]
  2. Preiss JC, Zouboulis CC, Zeitz M, Duchmann R: [Severe erythrodermic psoriasis in a patient with 22q11 deletion syndrome] Med Klin (Munich). 2005 May 13;100(5):275-8. [PubMed Link Image]
  3. Carillet V, Morliere P, Maziere JC, Huppe G, Santus R, Dubertret L: In vitro interactions of the aromatic retinoids Ro 10-9359 (etretinate) and Ro 10-1670 (acitretin), its main metabolite, with human serum lipoproteins and albumin. Biochim Biophys Acta. 1990 Nov 12;1055(2):98-101. [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. 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. Tian K, Norris AW, Lin CL, Li E: The isolation and characterization of purified heterocomplexes of recombinant retinoic acid receptor and retinoid X receptor ligand binding domains. Biochemistry. 1997 May 13;36(19):5669-76. [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.