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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2008-08-26 13:56:40
Primary Accession Number DB02854
Secondary Accession Number
  • EXPT00443
Name Aetiocholanolone
Drug Type
  • Experimental
  • Small Molecule
Description The 5-beta-reduced isomer of androsterone. Etiocholanolone is a major metabolite of testosterone and androstenedione in many mammalian species including humans. It is excreted in the urine. [PubChem]
Synonyms Not Available
Brand Names Not Available
Brand Mixtures Not Available
Chemical IUPAC Name (3R,5R,8R,9S,10S,13S,14S)-3-hydroxy-10,13-dimethyl-1,2,3,4,5,6,7,8,9,11,12,14,15,16-tetradecahydrocyclopenta[a]phenanthren-17-one
Chemical Formula C19H30O2
Chemical Structure Structure
CAS Registry Number 53-42-9
InChI Identifier InChI=1/C19H30O2/c1-18-9-7-13(20)11-12(18)3-4-14-15-5-6-17(21)19(15,2)10-8-16(14)18/h12-16,20H,3-11H2,1-2H3
InChI Key QGXBDMJGAMFCBF-UHFFFAOYAM
KEGG Drug Not Available
KEGG Compound C04373 Link Image
PubChem Compound 5880 Link Image
PubChem Substance 102477 Link Image
ChEBI ID 28195 Link Image
PharmGKB ID Not Available
HET ID AE2 Link Image
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link Not Available
PDRhealth Link Not Available
Wikipedia Link Not Available
FDA Label Not Available
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 290.4403
Monoisotopic Molecular Weight 290.2246
State Solid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 6.37e-03 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP 3.71 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -4.66 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 1NFQ Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES C[C@]12CC[C@H](O)C[C@@H]1CC[C@@H]1[C@@H]2CC[C@@]2(C)[C@H]1CCC2=O
Canonical SMILES CC12CCC(O)CC1CCC1C2CCC2(C)C1CCC2=O
Drug Category Not Available
ATC Codes Not Available
AHFS Codes Not Available
Indication Not Available
Pharmacology Not Available
Mechanism of Action Not Available
Absorption Not Available
Toxicity Not Available
Protein Binding Not Available
Biotransformation Not Available
Half Life Not Available
Dosage Forms Not Available
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References Not Available
Organisms Affected Not Available
Targets
  1. Bile salt sulfotransferase
  2. 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase
  3. Retinol dehydratase
  4. Dehydrogenase/reductase SDR family member 8
Drug Target 1 [top]
Target 1 ID 1050
Target 1 Name Bile salt sulfotransferase
Target 1 Synonyms
  1. DHEA-ST
  2. Dehydroepiandrosterone sulfotransferase
  3. EC 2.8.2.14
  4. HST
  5. Hydroxysteroid Sulfotransferase
  6. ST2
  7. ST2A3
Target 1 Gene Name SULT2A1
Target 1 Protein Sequence >Bile salt sulfotransferase 
MSDDFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYPKSGTNWLAEILCLMHSK
GDAKWIQSVPIWERSPWVESEIGYTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLM
RNPRDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSWFDHIHGWMPMREEKNFL
LLSYEELKQDTGRTIEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVV
DKAQLLRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRELFPWE
Target 1 Number of Residues 289
Target 1 Molecular Weight 33780
Target 1 Theoretical pI 5.76
Target 1 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring sulfur-containing groups
sulfotransferase activity
Process
Not Available
Component
Not Available
Target 1 General Function Involved in sulfotransferase activity
Target 1 Specific Function Catalyzes the sulfation of steroids and bile acids in the liver and adrenal glands
Target 1 Pathways Not Available
Target 1 Reactions
  • (1) 3'-phosphoadenylyl sulfate + glycolithocholate = adenosine 3',5'-bisphosphate + glycolithocholate 3-sulfate
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 306702 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q06520 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name ST2A1_HUMAN Link Image
Target 1 PDB ID 1OV4 Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Cytoplasm
Target 1 Gene Sequence >858 bp 
ATGTCGGACGATTTCTTATGGTTTGAAGGCATAGCTTTCCCTACTATGGGTTTCAGATCC
GAAACCTTAAGAAAAGTACGTGATGAGTTCGTGATAAGGGATGAAGATGTAATAATATTG
ACTTACCCCAAATCAGGAACAAACTGGTTGGCTGAGATTCTCTGCCTGATGCACTCCAAG
GGGGATGCCAAGTGGATCCAATCTGTGCCCATCTGGGAGCGATCACCCTGGGTAGAGAGT
GAGATTGGGTATACAGCACTCAGTGAAAGCGAGAGTCCACGTTTATTCTCCTCCCACCTC
CCCATCCAGTTATTCCCCAAGTCTTTCTTCAGTTCCAAGGCCAAGGTGATTTATCTCATG
AGAAATCCCAGAGATGTTTTGGTGTCTGGTTATTTTTTCTGGAAAAACATGAAGTTTATT
AAGAAACCAAAGTCATGGGAAGAATATTTTGAATGGTTTTGTCAAGGAACTGTGCTATAT
GGGTCATGGTTTGACCACATTCATGGCTGGATGCCCATGAGAGAGGAGAAAAACTTCCTG
TTACTGAGTTATGAGGAGCTGAAACAGGACACAGGAAGAACCATAGAGAAGATCTGTCAA
TTCCTGGGAAAGACGTTAGAACCCGAAGAACTGAACTTAATTCTCAAGAACAGCTCCTTT
CAGAGCATGAAAGAAAACAAGATGTCCAATTATTCCCTCCTGAGTGTTGATTATGTAGTG
GACAAAGCACAACTTCTGAGAAAAGGTGTATCTGGGGACTGGAAAAATCACTTCACAGTG
GCCCAAGCTGAAGACTTTGATAAATTGTTCCAAGAGAAGATGGCAGATCTTCCTCGAGAG
CTGTTCCCATGGGAATAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID SULT2A1 Link Image
Target 1 GenAtlas ID SULT2A1 Link Image
Target 1 HGNC ID HGNC:11458 Link Image
Target 1 Chromosome Location 19
Target 1 Locus 19q13.3
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Kong AN, Yang L, Ma M, Tao D, Bjornsson TD: Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of sulfotransferase from human liver. Biochem Biophys Res Commun. 1992 Aug 31;187(1):448-54. [PubMed Link Image]
  2. Otterness DM, Wieben ED, Wood TC, Watson WG, Madden BJ, McCormick DJ, Weinshilboum RM: Human liver dehydroepiandrosterone sulfotransferase: molecular cloning and expression of cDNA. Mol Pharmacol. 1992 May;41(5):865-72. [PubMed Link Image]
  3. Forbes KJ, Hagen M, Glatt H, Hume R, Coughtrie MW: Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable expression in V79 cells and functional characterisation of the expressed enzyme. Mol Cell Endocrinol. 1995 Jul;112(1):53-60. [PubMed Link Image]
  4. Luu-The V, Dufort I, Paquet N, Reimnitz G, Labrie F: Structural characterization and expression of the human dehydroepiandrosterone sulfotransferase gene. DNA Cell Biol. 1995 Jun;14(6):511-8. [PubMed Link Image]
  5. Comer KA, Falany JL, Falany CN: Cloning and expression of human liver dehydroepiandrosterone sulphotransferase. Biochem J. 1993 Jan 1;289 ( Pt 1):233-40. [PubMed Link Image]
  6. Otterness DM, Her C, Aksoy S, Kimura S, Wieben ED, Weinshilboum RM: Human dehydroepiandrosterone sulfotransferase gene: molecular cloning and structural characterization. DNA Cell Biol. 1995 Apr;14(4):331-41. [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 3059
Target 2 Name 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase
Target 2 Synonyms
  1. EC 1.1.1.53
Target 2 Gene Name fabG3
Target 2 Protein Sequence >3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase 
MSGRLIGKVALVSGGARGMGASHVRAMVAEGAKVVFGDILDEEGKAVAAELADAARYVHL
DVTQPAQWTAAVDTAVTAFGGLHVLVNNAGILNIGTIEDYALTEWQRILDVNLTGVFLGI
RAVVKPMKEAGRGSIINISSIEGLAGTVACHGYTATKFAVRGLTKSTALELGPSGIRVNS
IHPGLVKTPMTDWVPEDIFQTALGRAAEPVEVSNLVVYLASDESSYSTGAEFVVDGGTVA
GLAHNDFGAVEVSSQPEWVT
Target 2 Number of Residues 264
Target 2 Molecular Weight 27030
Target 2 Theoretical pI 4.79
Target 2 GO Classification
Function
catalytic activity
oxidoreductase activity
Process
physiological process
metabolism
Component
Not Available
Target 2 General Function Lipid transport and metabolism
Target 2 Specific Function Androstan-3-alpha,17-beta-diol + NAD(+) = 17- beta-hydroxyandrostan-3-one + NADH
Target 2 Pathways
Name SMPDB Link KEGG Link
Bile acid biosynthesis SMP00035 Link Image map00120 Link Image
Target 2 Reactions
  • androstan-3alpha,17beta-diol + NAD+ = 17beta-hydroxyandrostan-3-one + NADH + H+
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Essential
Target 2 GenBank ID Protein 3261591 Link Image
Target 2 UniProtKB/Swiss-Prot ID P69167 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name HSD_MYCTU Link Image
Target 2 PDB ID 1NFQ Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location Not Available
Target 2 Gene Sequence >783 bp 
ATGTCTGGACGGTTGATAGGAAAGGTCGCACTTGTCAGCGGCGGGGCGCGCGGTATGGGT
GCATCCCATGTGCGGGCGATGGTGGCCGAAGGCGCAAAGGTTGTGTTCGGCGACATCCTC
GACGAGGAGGGCAAGGCGGTGGCCGCCGAACTGGCCGATGCGGCCCGCTACGTCCATCTC
GACGTTACCCAACCCGCGCAATGGACGGCTGCGGTGGACACCGCGGTCACCGCATTCGGT
GGCCTGCACGTGCTGGTCAACAACGCCGGCATTCTCAACATCGGGACGATCGAGGACTAC
GCCCTCACCGAATGGCAGCGCATCCTCGATGTCAACCTGACCGGAGTCTTCCTGGGCATC
CGCGCTGTCGTCAAGCCAATGAAAGAGGCTGGTCGCGGCTCCATCATCAACATTTCGTCG
ATCGAGGGGCTGGCCGGCACGGTTGCTTGTCATGGCTATACCGCCACCAAGTTCGCCGTG
CGGGGGCTGACCAAGTCCACCGCTCTCGAGTTGGGGCCCAGCGGAATTCGAGTCAACTCG
ATTCACCCTGGGTTGGTCAAGACGCCGATGACTGACTGGGTCCCCGAAGACATCTTCCAG
ACCGCGCTGGGCCGCGCGGCCGAACCCGTGGAAGTGTCCAACCTCGTCGTCTACCTGGCC
AGCGATGAGTCGAGCTATTCCACCGGCGCGGAATTTGTGGTCGACGGCGGGACCGTAGCT
GGCCTGGCACACAACGACTTCGGTGCCGTCGAGGTGTCCTCGCAGCCGGAATGGGTGACG
TAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID Not Available
Target 2 GenAtlas ID Not Available
Target 2 HGNC ID Not Available
Target 2 Chromosome Location Not Available
Target 2 Locus Not Available
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Fleischmann RD, Alland D, Eisen JA, Carpenter L, White O, Peterson J, DeBoy R, Dodson R, Gwinn M, Haft D, Hickey E, Kolonay JF, Nelson WC, Umayam LA, Ermolaeva M, Salzberg SL, Delcher A, Utterback T, Weidman J, Khouri H, Gill J, Mikula A, Bishai W, Jacobs Jr WR Jr, Venter JC, Fraser CM: Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains. J Bacteriol. 2002 Oct;184(19):5479-90. [PubMed Link Image]
  2. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [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 4379
Target 3 Name Retinol dehydratase
Target 3 Synonyms Not Available
Target 3 Gene Name Not Available
Target 3 Protein Sequence >Retinol dehydratase 
MEKQQDLPFPYEFRELNPEEDKLVKANLGAFPTTYVKLGPKGYMVYRPYLKDAANIYNMP
LRPTDVFVASYQRSGTTMTQELVWLIENDLNFEAAKTYMSLRYIYLDGFMIYDPEKQEEY
NDILPNPENLDMERYLGLLEYFSRPGSSLLAAVPPTEKRFVKTHLPLSLMPPNMLDTVKM
VYLARDPRDVAVSSFHHARLLYLLNKQSNFKDFWEMFHRGLYTLTPYFEHVKEAWAKRHD
PNMLFLFYEDYLKDLPGCIARIADFLGKKLSEEQIQRLCEHLNFEKFKNNGAVNMEDYRE
IGILADGEHFIRKGKAGCWRDYFDEEMTKQAEKWIKDNLKDTDLRYPNMEL
Target 3 Number of Residues 356
Target 3 Molecular Weight 41563
Target 3 Theoretical pI 5.50
Target 3 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring sulfur-containing groups
sulfotransferase activity
Process
Not Available
Component
Not Available
Target 3 General Function Involved in sulfotransferase activity
Target 3 Specific Function Not Available
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 Essential
Target 3 GenBank ID Protein Not Available
Target 3 UniProtKB/Swiss-Prot ID Q26490 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name Q26490_SPOFR Link Image
Target 3 PDB ID 1FML Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location Not Available
Target 3 Gene Sequence >1056 bp 
ATGGAGAAACAACAGGATTTGCCATTCCCTTACGAGTTTAGGGAGCTTAACCCCGAAGAA
GATAAATTGGTTAAAGCCAATTTAGGCGCGTTCCCCACAACCTACGTGAAACTGGGGCCT
AAAGGCTACATGGTGTACAGACCCTACTTGAAAGATGCGGCGAATATCTACAACATGCCT
CTAAGACCTACAGACGTGTTCGTTGCCAGTTATCAACGATCAGGAACGACAATGACTCAA
GAACTAGTTTGGCTAATTGAAAACGACTTGAATTTCGAAGCTGCAAAAACATACATGTCC
CTCCGCTACATTTATCTTGACGGCTTCATGATCTACGACCCGGAGAAGCAAGAAGAATAT
AACGACATATTACCAAATCCAGAAAACCTTGATATGGAAAGGTATTTAGGATTGCTAGAA
TACTTTAGTCGTCCAGGGAGCTCATTGCTCGCTGCAGTGCCACCGACAGAGAAAAGATTT
GTGAAGACCCACTTGCCTTTGTCCTTGATGCCTCCCAATATGTTGGATACTGTGAAGATG
GTGTACCTGGCTCGAGACCCTAGAGACGTGGCGGTGTCCAGCTTCCACCACGCCCGGTTA
TTGTATTTGCTGAATAAGCAGAGCAACTTCAAAGATTTCTGGGAAATGTTTCACCGTGGC
CTATATACGCTGACACCATATTTCGAGCACGTCAAGGAAGCTTGGGCAAAGAGACATGAT
CCGAACATGCTGTTTTTGTTTTACGAAGACTACTTAAAGGACTTACCAGGCTGCATTGCA
CGTATCGCTGACTTCTTGGGCAAGAAGTTGAGTGAGGAACAAATTCAGCGCCTCTGCGAA
CACCTGAATTTCGAAAAGTTCAAAAACAATGGCGCTGTCAATATGGAGGACTACAGGGAA
ATTGGAATACTCGCTGACGGGGAGCATTTCATTAGAAAAGGTAAAGCAGGATGCTGGCGC
GACTACTTCGACGAGGAGATGACGAAACAAGCTGAGAAATGGATCAAGGACAACCTGAAG
GATACTGATCTGCGCTACCCAAATATGGAATTATAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID Not Available
Target 3 GenAtlas ID Not Available
Target 3 HGNC ID Not Available
Target 3 Chromosome Location Not Available
Target 3 Locus Not Available
Target 3 SNPs Not Available
Target 3 General References
  1. Pakhomova S, Kobayashi M, Buck J, Newcomer ME: A helical lid converts a sulfotransferase to a dehydratase. Nat Struct Biol. 2001 May;8(5):447-51. [PubMed Link Image]
  2. Komatsu K, Driscoll WJ, Koh YC, Strott CA: A P-loop related motif (GxxGxxK) highly conserved in sulfotransferases is required for binding the activated sulfate donor. Biochem Biophys Res Commun. 1994 Nov 15;204(3):1178-85. [PubMed Link Image]
  3. Zheng Y, Bergold A, Duffel MW: Affinity labeling of aryl sulfotransferase IV. Identification of a peptide sequence at the binding site for 3'-phosphoadenosine-5'-phosphosulfate. J Biol Chem. 1994 Dec 2;269(48):30313-9. [PubMed Link Image]
  4. Grun F, Noy N, Hammerling U, Buck J: Purification, cloning, and bacterial expression of retinol dehydratase from Spodoptera frugiperda. J Biol Chem. 1996 Jul 5;271(27):16135-8. [PubMed Link Image]
Target 3 Drug References Not Available
Drug Target 4 [top]
Target 4 ID 4824
Target 4 Name Dehydrogenase/reductase SDR family member 8
Target 4 Synonyms
  1. 17-beta- HSD XI
  2. 17-beta-HSD 11
  3. 17-beta-hydroxysteroid dehydrogenase 11
  4. 17bHSD11
  5. 17betaHSD11
  6. 17betaHSDXI
  7. CTCL tumor antigen HD-CL-03
  8. Cutaneous T-cell lymphoma- associated antigen HD-CL-03
  9. Dehydrogenase/reductase SDR family member 8 precursor
  10. EC 1.1.1.-
  11. Retinal short-chain dehydrogenase/reductase 2
  12. retSDR2
Target 4 Gene Name DHRS8
Target 4 Protein Sequence >Dehydrogenase/reductase SDR family member 8 
MKFLLDILLLLPLLIVCSLESFVKLFIPKRRKSVTGEIVLITGAGHGIGRLTAYEFAKLK
SKLVLWDINKHGLEETAAKCKGLGAKVHTFVVDCSNREDIYSSAKKVKAEIGDVSILVNN
AGVVYTSDLFATQDPQIEKTFEVNVLAHFWTTKAFLPAMTKNNHGHIVTVASAAGHVSVP
FLLAYCSSKFAAVGFHKTLTDELAALQITGVKTTCLCPNFVNTGFIKNPSTSLGPTLEPE
EVVNRLMHGILTEQKMIFIPSSIAFLTTLERILPERFLAVLKRKISVKFDAVIGYKMKAQ
Target 4 Number of Residues 305
Target 4 Molecular Weight 32964
Target 4 Theoretical pI 9.70
Target 4 GO Classification
Function
catalytic activity
oxidoreductase activity
Process
physiological process
metabolism
Component
Not Available
Target 4 General Function Involved in oxidoreductase activity
Target 4 Specific Function Can convert androstan-3-alpha,17-beta-diol (3alpha-diol) to androsterone in vitro, suggesting that it may participate in androgen metabolism during steroidogenesis. May act by metabolizing compounds that stimulate steroid synthesis and/or by generating metabolites that inhibit it. Has no activity toward DHEA (dehydroepiandrosterone), or A-dione (4-androste-3,17-dione), and only a slight activity toward testosterone to A-dione. Tumor- associated antigen in cutaneous T-cell lymphoma
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • 1-19
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non Essential
Target 4 GenBank ID Protein Not Available
Target 4 UniProtKB/Swiss-Prot ID Q8NBQ5 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name DHRS8_HUMAN Link Image
Target 4 PDB ID 1YB1 Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location
  • Secreted protein (Potential)
Target 4 Gene Sequence >903 bp 
ATGAAATTTCTTCTGGACATCCTCCTGCTTCTCCCGTTACTGATCGTCTGCTCCCTAGAG
TCCTTCGTGAAGCTTTTTATTCCTAAGAGGAGAAAATCAGTCACCGGCGAAATCGTGCTG
ATTACAGGAGCTGGGCATGGAATTGGGAGACTGACTGCCTATGAATTTGCTAAACTTAAA
AGCAAGCTGGTTCTCTGGGATATAAATAAGCATGGACTGGAGGAAACAGCTGCCAAATGC
AAGGGACTGGGTGCCAAGGTTCATACCTTTGTGGTAGACTGCAGCAACCGAGAAGATATT
TACAGCTCTGCAAAGAAGGTGAAGGCAGAAATTGGAGATGTTAGTATTTTAGTAAATAAT
GCTGGTGTAGTCTATACATCAGATTTGTTTGCTACACAAGATCCTCAGATTGAAAAGACT
TTTGAAGTTAATGTACTTGCACATTTCTGGACTACAAAGGCATTTCTTCCTGCAATGACG
AAGAATAACCATGGCCATATTGTCACTGTGGCTTCGGCAGCTGGACATGTCTCGGTCCCC
TTCTTACTGGCTTACTGTTCAAGCAAGTTTGCTGCTGTTGGATTTCATAAAACTTTGACA
GATGAACTGGCTGCCTTACAAATAACTGGAGTCAAAACAACATGTCTGTGTCCTAATTTC
GTAAACACTGGCTTCATCAAAAATCCAAGTACAAGTTTGGGACCCACTCTGGAACCCGAG
GAAGTGGTAAACAGGCTGATGCATGGGATTCTGACTGAGCAGAAGATGATTTTTATTCCA
TCTTCTATAGCTTTTTTAACAACATTGGAAAGGATCCTTCCTGAGCGTTTCCTGGCAGTT
TTAAAACGAAAAATCAGTGTTAAGTTTGATGCAGTTATTGGATATAAAATGAAAGCGCAA
TAA
Target 4 GenBank Gene ID
Target 4 GeneCard ID Not Available
Target 4 GenAtlas ID HSD17B11 Link Image
Target 4 HGNC ID HGNC:22960 Link Image
Target 4 Chromosome Location 4
Target 4 Locus 4q22.1
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Haeseleer F, Palczewski K: Short-chain dehydrogenases/reductases in retina. Methods Enzymol. 2000;316:372-83. [PubMed Link Image]
  2. Brereton P, Suzuki T, Sasano H, Li K, Duarte C, Obeyesekere V, Haeseleer F, Palczewski K, Smith I, Komesaroff P, Krozowski Z: Pan1b (17betaHSD11)-enzymatic activity and distribution in the lung. Mol Cell Endocrinol. 2001 Jan 22;171(1-2):111-7. [PubMed Link Image]
  3. Chai Z, Brereton P, Suzuki T, Sasano H, Obeyesekere V, Escher G, Saffery R, Fuller P, Enriquez C, Krozowski Z: 17 beta-hydroxysteroid dehydrogenase type XI localizes to human steroidogenic cells. Endocrinology. 2003 May;144(5):2084-91. [PubMed Link Image]
  4. 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]
  5. Li KX, Smith RE, Krozowski ZS: Cloning and expression of a novel tissue specific 17beta-hydroxysteroid dehydrogenase. Endocr Res. 1998 Aug-Nov;24(3-4):663-7. [PubMed Link Image]
Target 4 Drug References Not Available

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.