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Showing drug card for Vorinostat (DB02546)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:07:06
Primary Accession Number DB02546
Secondary Accession Number
  • EXPT02902
Name Vorinostat
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description Vorinostat (rINN) or suberoylanilide hydroxamic acid (SAHA), is a drug currently under investigation for the treatment of cutaneous T cell lymphoma (CTCL), a type of skin cancer, to be used when the disease persists, gets worse, or comes back during or after treatment with other medicines. It is the first in a new class of agents known as histone deacetylase inhibitors. A recent study suggested that vorinostat also possesses some activity against recurrent glioblastoma multiforme, resulting in a median overall survival of 5.7 months (compared to 4 - 4.4 months in earlier studies). Further brain tumor trials are planned in which vorinostat will be combined with other drugs. [Wikipedia]
Synonyms
  1. MK0683
  2. N-hydroxy-n'-phenyloctanediamide
  3. N-hyrdroxy-n'-phenyloctanediamide
  4. SAHA
  5. SHH
  6. Suberanilohydroxamic acid
  7. suberoylanilide hydroxamic acid
  8. vorinostat
Brand Names
  1. SAHA
  2. Zolinza
Brand Mixtures Not Available
Chemical IUPAC Name N'-hydroxy-N-phenyloctanediamide
Chemical Formula C14H20N2O3
Chemical Structure Structure
CAS Registry Number 149647-78-9
InChI Identifier InChI=1/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18)/f/h15-16H
InChI Key WAEXFXRVDQXREF-LUXCBXFACF
KEGG Drug Not Available
KEGG Compound Not Available
PubChem Compound 5311 Link Image
PubChem Substance 12015019 Link Image
ChEBI ID Not Available
PharmGKB ID Not Available
HET ID SHH Link Image
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link http://www.rxlist.com/cgi/generic/zolinza.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Vorinostat Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 264.3202
Monoisotopic Molecular Weight 264.1474
State Solid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 7.16e-02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP 1.88 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.57 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 9.2
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 1T69 Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES ONC(=O)CCCCCCC(=O)NC1=CC=CC=C1
Canonical SMILES ONC(=O)CCCCCCC(=O)NC1=CC=CC=C1
Drug Category
  • Anti-Inflammatory Agents, Non-Steroidal
  • Anticarcinogenic Agents
  • Antineoplastic Agents
  • Enzyme Inhibitors
ATC Codes Not Available
AHFS Codes Not Available
Indication For the treatment of cutaneous manifestations in patients with cutaneous T-cell lymphoma who have progressive, persistent or recurrent disease on or following two systemic therapies.
Pharmacology Not Available
Mechanism of Action Vorinostat inhibits the enzymatic activity of histone deacetylases HDAC1, HDAC2 and HDAC3 (Class I) and HDAC6 (Class II) at nanomolar concentrations (IC50< 86 nM). These enzymes catalyze the removal of acetyl groups from the lysine residues of proteins, including histones and transcription factors. In some cancer cells, there is an overexpression of HDACs, or an aberrant recruitment of HDACs to oncogenic transcription factors causing hypoacetylation of core nucleosomal histones. Hypoacetylation of histones is associated with a condensed chromatin structure and repression of gene transcription. Inhibition of HDAC activity allows for the accumulation of acetyl groups on the histone lysine residues resulting in an open chromatin structure and transcriptional activation. In vitro, vorinostat causes the accumulation of acetylated histones and induces cell cycle arrest and/or apoptosis of some transformed cells. The mechanism of the antineoplastic effect of vorinostat has not been fully characterized.
Absorption Not Available
Toxicity Not Available
Protein Binding 71%
Biotransformation The major pathways of vorinostat metabolism involve glucuronidation and hydrolysis followed by β-oxidation. Human serum levels of two metabolites, O-glucuronide of vorinostat and 4-anilino-4-oxobutanoic acid were measured. Both metabolites are pharmacologically inactive. Compared to vorinostat, the mean steady state serum exposures in humans of the O-glucuronide of vorinostat and 4-anilino-4-oxobutanoic acid were 4-fold and 13-fold higher, respectively. In vitro studies using human liver microsomes indicate negligible biotransformation by cytochromes P450 (CYP).
Half Life 2 hours
Dosage Forms
Form Route
Capsule Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
Food Interactions
  • Oral administration with a high-fat meal resulted in an increase (33%) in the extent of absorption and a modest decrease in the rate of absorption (Tmax delayed 2.5 hours) compared to the fasted state.
Pathways Not Available
General References
  1. Munshi A, Tanaka T, Hobbs ML, Tucker SL, Richon VM, Meyn RE: Vorinostat, a histone deacetylase inhibitor, enhances the response of human tumor cells to ionizing radiation through prolongation of gamma-H2AX foci. Mol Cancer Ther. 2006 Aug;5(8):1967-74. [PubMed Link Image]
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Histone deacetylase 8
  2. Histone deacetylase 1
  3. Histone deacetylase 2
  4. Histone deacetylase 3
  5. Histone deacetylase 6
  6. Acetoin utilization protein
Drug Target 1 [top]
Target 1 ID 2921
Target 1 Name Histone deacetylase 8
Target 1 Synonyms
  1. HD8
Target 1 Gene Name HDAC8
Target 1 Protein Sequence >Histone deacetylase 8 
MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPK
VASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATI
TAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLH
HGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKY
YQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLI
LGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPH
RIQQILNYIKGNLKHVV
Target 1 Number of Residues 383
Target 1 Molecular Weight 41758
Target 1 Theoretical pI 5.37
Target 1 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
histone deacetylase activity
Process
physiological process
metabolism
macromolecule metabolism
biopolymer metabolism
biopolymer modification
protein modification
protein amino acid deacetylation
histone deacetylation
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
Target 1 General Function Chromatin structure and dynamics
Target 1 Specific Function Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes
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 8118721 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q9BY41 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name HDAC8_HUMAN Link Image
Target 1 PDB ID 1VKG Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Nucleus. Note=Excluded from the nucleoli
Target 1 Gene Sequence >1134 bp 
ATGGAGGAGCCGGAGGAACCGGCGGACAGTGGGCAGTCGCTGGTCCCGGTTTATATCTAT
AGTCCCGAGTATGTCAGTATGTGTGACTCCCTGGCCAAGATCCCCAAACGGGCCAGTATG
GTGCATTCTTTGATTGAAGCATATGCACTGCATAAGCAAATGAGGATAGTTAAGCCTAAA
GTGGCCTCCATGGAGGAGATGGCCACCTTCCACACTGATGCTTATCTGCAGCATCTCCAG
AAGGTCAGCCAAGAGGGCGATGATGATCATCCGGACTCCATAGAATATGGGCTAGGTTAT
GACTGCCCAGCCACTGAAGGGATATTTGACTATGCAGCAGCTATAGGAGGGGCTACGATC
ACAGCTGCCCAATGCCTGATTGACGGAATGTGCAAAGTAGCAATTAACTGGTCTGGAGGG
TGGCATCATGCAAAGAAAGATGAAGCATCTGGTTTTTGTTATCTCAATGATGCTGTCCTG
GGAATATTACGATTGCGACGGAAATTTGAGCGTATTCTCTACGTGGATTTGGATCTGCAC
CATGGAGATGGTGTAGAAGACGCATTCAGTTTCACCTCCAAAGTCATGACCGTGTCCCTG
CACAAATTCTCCCCAGGATTTTTCCCAGGAACAGGTGACGTGTCTGATGTTGGCCTAGGG
AAGGGACGGTACTACAGTGTAAATGTGCCCATTCAGGATGGCATACAAGATGAAAAATAT
TACCAGATCTGTGAAAGTGTACTAAAGGAAGTATACCAAGCCTTTAATCCCAAAGCAGTG
GTCTTACAGCTGGGAGCTGACACAATAGCTGGGGATCCCATGTGCTCCTTTAACATGACT
CCAGTGGGAATTGGCAAGTGTCTTAAGTACATCCTTCAATGGCAGTTGGCAACACTCATT
TTGGGAGGAGGAGGCTATAACCTTGCCAACACGGCTCGATGCTGGACATACTTGACCGGG
GTCATCCTAGGGAAAACACTATCCTCTGAGATCCCAGATCATGAGTTTTTCACAGCATAT
GGTCCTGATTATGTGCTGGAAATCACGCCAAGCTGCCGGCCAGACCGCAATGAGCCCCAC
CGAATCCAACAAATCCTCAACTACATCAAAGGGAATCTGAAGCATGTGGTCTAG
Target 1 GenBank Gene ID
Target 1 GeneCard ID HDAC8 Link Image
Target 1 GenAtlas ID HDAC8 Link Image
Target 1 HGNC ID HGNC:13315 Link Image
Target 1 Chromosome Location X
Target 1 Locus Xq13
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Hu E, Chen Z, Fredrickson T, Zhu Y, Kirkpatrick R, Zhang GF, Johanson K, Sung CM, Liu R, Winkler J: Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor. J Biol Chem. 2000 May 19;275(20):15254-64. [PubMed Link Image]
  2. McDonell N, Ramser J, Francis F, Vinet MC, Rider S, Sudbrak R, Riesselman L, Yaspo ML, Reinhardt R, Monaco AP, Ross F, Kahn A, Kearney L, Buckle V, Chelly J: Characterization of a highly complex region in Xq13 and mapping of three isodicentric breakpoints associated with preleukemia. Genomics. 2000 Mar 15;64(3):221-9. [PubMed Link Image]
  3. Van den Wyngaert I, de Vries W, Kremer A, Neefs J, Verhasselt P, Luyten WH, Kass SU: Cloning and characterization of human histone deacetylase 8. FEBS Lett. 2000 Jul 28;478(1-2):77-83. [PubMed Link Image]
  4. Buggy JJ, Sideris ML, Mak P, Lorimer DD, McIntosh B, Clark JM: Cloning and characterization of a novel human histone deacetylase, HDAC8. Biochem J. 2000 Aug 15;350 Pt 1:199-205. [PubMed Link Image]
  5. Durst KL, Lutterbach B, Kummalue T, Friedman AD, Hiebert SW: The inv(16) fusion protein associates with corepressors via a smooth muscle myosin heavy-chain domain. Mol Cell Biol. 2003 Jan;23(2):607-19. [PubMed Link Image]
Target 1 Drug References Not Available
Drug Target 2 [top]
Target 2 ID 4121
Target 2 Name Histone deacetylase 1
Target 2 Synonyms
  1. HD1
Target 2 Gene Name HDAC1
Target 2 Protein Sequence >Histone deacetylase 1 
MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKAN
AEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAS
AVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHG
DGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAI
FKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGG
GGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLE
KIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEF
SDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVK
LA
Target 2 Number of Residues 490
Target 2 Molecular Weight 55104
Target 2 Theoretical pI 5.16
Target 2 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
histone deacetylase activity
Process
physiological process
metabolism
macromolecule metabolism
biopolymer metabolism
biopolymer modification
protein modification
protein amino acid deacetylation
histone deacetylation
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
Target 2 General Function Chromatin structure and dynamics
Target 2 Specific Function Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes
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 1277084 Link Image
Target 2 UniProtKB/Swiss-Prot ID Q13547 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name HDAC1_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Nucleus
Target 2 Gene Sequence >1449 bp 
ATGGCGCAGACGCAGGGCACCCGGAGGAAAGTCTGTTACTACTACGACGGGGATGTTGGA
AATTACTATTATGGACAAGGCCACCCAATGAAGCCTCACCGAATCCGCATGACTCATAAT
TTGCTGCTCAACTATGGTCTCTACCGAAAAATGGAAATCTATCGCCCTCACAAAGCCAAT
GCTGAGGAGATGACCAAGTACCACAGCGATGACTACATTAAATTCTTGCGCTCCATCCGT
CCAGATAACATGTCGGAGTACAGCAAGCAGATGCAGAGATTCAACGTTGGTGAGGACTGT
CCAGTATTCGATGGCCTGTTTGAGTTCTGTCAGTTGTCTACTGGTGGTTCTGTGGCAAGT
GCTGTGAAACTTAATAAGCAGCAGACGGACATCGCTGTGAATTGGGCTGGGGGCCTGCAC
CATGCAAAGAAGTCCGAGGCATCTGGCTTCTGTTACGTCAATGATATCGTCTTGGCCATC
CTGGAACTGCTAAAGTATCACCAGAGGGTGCTGTACATTGACATTGATATTCACCATGGT
GACGGCGTGGAAGAGGCCTTCTACACCACGGACCGGGTCATGACTGTGTCCTTTCATAAG
TATGGAGAGTACTTCCCAGGAACTGGGGACCTACGGGATATCGGGGCTGGCAAAGGCAAG
TATTATGCTGTTAACTACCCGCTCCGAGACGGGATTGATGACGAGTCCTATGAGGCCATT
TTCAAGCCGGTCATGTCCAAAGTAATGGAGATGTTCCAGCCTAGTGCGGTGGTCTTACAG
TGTGGCTCAGACTCCCTATCTGGGGATCGGTTAGGTTGCTTCAATCTAACTATCAAAGGA
CACGCCAAGTGTGTGGAATTTGTCAAGAGCTTTAACCTGCCTATGCTGATGCTGGGAGGC
GGTGGTTACACCATTCGTAACGTTGCCCGGTGCTGGACATATGAGACAGCTGTGGCCCTG
GATACGGAGATCCCTAATGAGCTTCCATACAATGACTACTTTGAATACTTTGGACCAGAT
TTCAAGCTCCACATCAGTCCTTCCAATATGACTAACCAGAACACGAATGAGTACCTGGAG
AAGATCAAACAGCGACTGTTTGAGAACCTTAGAATGCTGCCGCACGCACCTGGGGTCCAA
ATGCAGGCGATTCCTGAGGACGCCATCCCTGAGGAGAGTGGCGATGAGGACGAAGACGAC
CCTGACAAGCGCATCTCGATCTGCTCCTCTGACAAACGAATTGCCTGTGAGGAAGAGTTC
TCCGATTCTGAAGAGGAGGGAGAGGGGGGCCGCAAGAACTCTTCCAACTTCAAAAAAGCC
AAGAGAGTCAAAACAGAGGATGAAAAAGAGAAAGACCCAGAGGAGAAGAAAGAAGTCACC
GAAGAGGAGAAAACCAAGGAGGAGAAGCCAGAAGCCAAAGGGGTCAAGGAGGAGGTCAAG
TTGGCCTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID HDAC1 Link Image
Target 2 GenAtlas ID HDAC1 Link Image
Target 2 HGNC ID HGNC:4852 Link Image
Target 2 Chromosome Location 1
Target 2 Locus 1p34
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Sparrow DB, Miska EA, Langley E, Reynaud-Deonauth S, Kotecha S, Towers N, Spohr G, Kouzarides T, Mohun TJ: MEF-2 function is modified by a novel co-repressor, MITR. EMBO J. 1999 Sep 15;18(18):5085-98. [PubMed Link Image]
  2. Li H, Leo C, Zhu J, Wu X, O'Neil J, Park EJ, Chen JD: Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol Cell Biol. 2000 Mar;20(5):1784-96. [PubMed Link Image]
  3. Huynh KD, Fischle W, Verdin E, Bardwell VJ: BCoR, a novel corepressor involved in BCL-6 repression. Genes Dev. 2000 Jul 15;14(14):1810-23. [PubMed Link Image]
  4. Pflum MK, Tong JK, Lane WS, Schreiber SL: Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation. J Biol Chem. 2001 Dec 14;276(50):47733-41. Epub 2001 Oct 15. [PubMed Link Image]
  5. Taunton J, Hassig CA, Schreiber SL: A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science. 1996 Apr 19;272(5260):408-11. [PubMed Link Image]
  6. Furukawa Y, Kawakami T, Sudo K, Inazawa J, Matsumine A, Akiyama T, Nakamura Y: Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae. Cytogenet Cell Genet. 1996;73(1-2):130-3. [PubMed Link Image]
Target 2 Drug References
  1. Xu WS, Parmigiani RB, Marks PA: Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene. 2007 Aug 13;26(37):5541-52. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 4122
Target 3 Name Histone deacetylase 2
Target 3 Synonyms
  1. HD2
Target 3 Gene Name HDAC2
Target 3 Protein Sequence >Histone deacetylase 2 
MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKA
TAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVA
GAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHH
GDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQ
IFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLG
GGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYM
EKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEE
FSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGT
KSEQLSNP
Target 3 Number of Residues 496
Target 3 Molecular Weight 55365
Target 3 Theoretical pI 5.75
Target 3 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
histone deacetylase activity
Process
physiological process
metabolism
macromolecule metabolism
biopolymer metabolism
biopolymer modification
protein modification
protein amino acid deacetylation
histone deacetylation
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
Target 3 General Function Chromatin structure and dynamics
Target 3 Specific Function Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1
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 1667394 Link Image
Target 3 UniProtKB/Swiss-Prot ID Q92769 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name HDAC2_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Nucleus
Target 3 Gene Sequence >1467 bp 
ATGGCGTACAGTCAAGGAGGCGGCAAAAAAAAAGTCTGCTACTACTACGACGGTGATATT
GGAAATTATTATTATGGACAGGGTCATCCCATGAAGCCTCATAGAATCCGCATGACCCAT
AACTTGCTGTTAAATTATGGCTTATACAGAAAAATGGAAATATATAGGCCCCATAAAGCC
ACTGCCGAAGAAATGACAAAATATCACAGTGATGAGTATATCAAATTTCTACGGTCAATA
AGACCAGATAACATGTCTGAGTATAGTAAGCAGATGCATATATTTAATGTTGGAGAAGAT
TGTCCAGCGTTTGATGGACTCTTTGAGTTTTGTCAGCTCTCAACTGGCGGTTCAGTTGCT
GGAGCTGTGAAGTTAAACCGACAACAGACTGATATGGCTGTTAATTGGGCTGGAGGATTA
CATCATGCTAAGAAATACGAAGCATCAGGATTCTGTTACGTTAATGATATTGTGCTTGCC
ATCCTTGAATTACTAAAGTATCATCAGAGAGTCTTATATATTGATATAGATATTCATCAT
GGTGATGGTGTTGAAGAAGCTTTTTATACAACAGATCGTGTAATGACGGTATCATTCCAT
AAATATGGGGAATACTTTCCTGGCACAGGAGACTTGAGGGATATTGGTGCTGGAAAAGGC
AAATACTATGCTGTCAATTTTCCAATGTGTGATGGTATAGATGATGAGTCATATGGGCAG
ATATTTAAGCCTATTATCTCAAAGGTGATGGAGATGTATCAACCTAGTGCTGTGGTATTA
CAGTGTGGTGCAGACTCATTATCTGGTGATAGACTGGGTTGTTTCAATCTAACAGTCAAA
GGTCATGCTAAATGTGTAGAAGTTGTAAAAACTTTTAACTTACCATTACTGATGCTTGGA
GGAGGTGGCTACACAATCCGTAATGTTGCTCGATGTTGGACATATGAGACTGCAGTTGCC
CTTGATTGTGAGATTCCCAATGAGTTGCCATATAATGATTACTTTGAGTATTTTGGACCA
GACTTCAAACTGCATATTAGTCCTTCAAACATGACAAACCAGAACACTCCAGAATATATG
GAAAAGATAAAACAGCGTTTGTTTGAAAATTTGCGCATGTTACCTCATGCACCTGGTGTC
CAGATGCAAGCTATTCCAGAAGATGCTGTTCATGAAGACAGTGGAGATGAAGATGGAGAA
GATCCAGACAAGAGAATTTCTATTCGAGCATCAGACAAGCGGATAGCTTGTGATGAAGAA
TTCTCAGATTCTGAGGATGAAGGAGAAGGAGGTCGAAGAAATGTGGCTGATCATAAGAAA
GGAGCAAAGAAAGCTAGAATTGAAGAAGATAAGAAAGAAACAGAGGACAAAAAAACAGAC
GTTAAGGAAGAAGATAAATCCAAGGACAACAGTGGTGAAAAAACAGATACCAAAGGAACC
AAATCAGAACAGCTCAGCAACCCCTGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID HDAC2 Link Image
Target 3 GenAtlas ID HDAC2 Link Image
Target 3 HGNC ID HGNC:4853 Link Image
Target 3 Chromosome Location 6
Target 3 Locus 6q21
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Rountree MR, Bachman KE, Baylin SB: DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci. Nat Genet. 2000 Jul;25(3):269-77. [PubMed Link Image]
  2. Ahringer J: NuRD and SIN3 histone deacetylase complexes in development. Trends Genet. 2000 Aug;16(8):351-6. [PubMed Link Image]
  3. Shi Y, Downes M, Xie W, Kao HY, Ordentlich P, Tsai CC, Hon M, Evans RM: Sharp, an inducible cofactor that integrates nuclear receptor repression and activation. Genes Dev. 2001 May 1;15(9):1140-51. [PubMed Link Image]
  4. Fischer DD, Cai R, Bhatia U, Asselbergs FA, Song C, Terry R, Trogani N, Widmer R, Atadja P, Cohen D: Isolation and characterization of a novel class II histone deacetylase, HDAC10. J Biol Chem. 2002 Feb 22;277(8):6656-66. Epub 2001 Dec 5. [PubMed Link Image]
  5. Hollenbach AD, McPherson CJ, Mientjes EJ, Iyengar R, Grosveld G: Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek. J Cell Sci. 2002 Aug 15;115(Pt 16):3319-30. [PubMed Link Image]
  6. 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]
  7. Yang WM, Inouye C, Zeng Y, Bearss D, Seto E: Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3. Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12845-50. [PubMed Link Image]
Target 3 Drug References
  1. Xu WS, Parmigiani RB, Marks PA: Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene. 2007 Aug 13;26(37):5541-52. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 4123
Target 4 Name Histone deacetylase 3
Target 4 Synonyms
  1. HD3
  2. RPD3-2
  3. SMAP45
Target 4 Gene Name HDAC3
Target 4 Protein Sequence >Histone deacetylase 3 
MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCR
FHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNN
KICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEA
FYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVI
NQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTV
RNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQ
TIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDN
DKESDVEI
Target 4 Number of Residues 435
Target 4 Molecular Weight 48848
Target 4 Theoretical pI 4.79
Target 4 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
histone deacetylase activity
Process
physiological process
metabolism
macromolecule metabolism
biopolymer metabolism
biopolymer modification
protein modification
protein amino acid deacetylation
histone deacetylation
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
Target 4 General Function Chromatin structure and dynamics
Target 4 Specific Function Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Probably participates in the regulation of transcription through its binding to the zinc-finger transcription factor YY1; increases YY1 repression activity. Required to repress transcription of the POU1F1 transcription factor
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 2326173 Link Image
Target 4 UniProtKB/Swiss-Prot ID O15379 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name HDAC3_HUMAN Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location
  • Nucleus
Target 4 Gene Sequence >1287 bp 
ATGGCCAAGACCGTGGCCTATTTCTACGACCCCGACGTGGGCAACTTCCACTACGGAGCT
GGACACCCTATGAAGCCCCATCGCCTGGCATTGACCCATAGCCTGGTCCTGCATTACGGT
CTCTATAAGAAGATGATCGTCTTCAAGCCATACCAGGCCTCCCAACATGACATGTGCCGC
TTCCACTCCGAGGACTACATTGACTTCCTGCAGAGAGTCAGCCCCACCAATATGCAAGGC
TTCACCAAGAGTCTTAATGCCTTCAACGTAGGCGATGACTGCCCAGTGTTTCCCGGGCTC
TTTGAGTTCTGCTCGCGTTACACAGGCGCATCTCTGCAAGGAGCAACCCAGCTGAACAAC
AAGATCTGTGATATTGCCATTAACTGGGCTGGTGGTCTGCACCATGCCAAGAAGTTTGAG
GCCTCTGGCTTCTGCTATGTCAACGACATTGTGATTGGCATCCTGGAGCTGCTCAAGTAC
CACCCTCGGGTGCTCTACATTGACATTGACATCCACCATGGTGACGGGGTTCAAGAAGCT
TTCTACCTCACTGACCGGGTCATGACGGTGTCCTTCCACAAATACGGAAATTACTTCTTC
CCTGGCACAGGTGACATGTATGAAGTCGGGGCAGAGAGTGGCCGCTACTACTGTCTGAAC
GTGCCCCTGCGGGATGGCATTGATGACCAGAGTTACAAGCACCTTTTCCAGCCGGTTATC
AACCAGGTAGTGGACTTCTACCAACCCACGTGCATTGTGCTCCAGTGTGGAGCTGACTCT
CTGGGCTGTGATCGATTGGGCTGCTTTAACCTCAGCATCCGAGGGCATGGGGAATGCGTT
GAATATGTCAAGAGCTTCAATATCCCTCTACTCGTGCTGGGTGGTGGTGGTTATACTGTC
CGAAATGTTGCCCGCTGCTGGACATATGAGACATCGCTGCTGGTAGAAGAGGCCATTAGT
GAGGAGCTTCCCTATAGTGAATACTTCGAGTACTTTGCCCCAGACTTCACACTTCATCCA
GATGTCAGCACCCGCATCGAGAATCAGAACTCACGCCAGTATCTGGACCAGATCCTCCAG
ACAATCTTTGAAAACCTGAAGATGCTGAACCATGCACCTAGTGTCCAGATTCATGACGTG
CCTGCAGACCTCCTGACCTATGACAGGACTGATGAGGCTGATGCAGAGGAGAGGGGTCCT
GAGGAGAACTATAGCAGGCCAGAGGCACCCAATGAGTTCTATGATGGAGACCATGACAAT
GACAAGGAAAGCGATGTGGAGATTTAA
Target 4 GenBank Gene ID
Target 4 GeneCard ID HDAC3 Link Image
Target 4 GenAtlas ID HDAC3 Link Image
Target 4 HGNC ID HGNC:4854 Link Image
Target 4 Chromosome Location 5
Target 4 Locus 5q31
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Mahlknecht U, Emiliani S, Najfeld V, Young S, Verdin E: Genomic organization and chromosomal localization of the human histone deacetylase 3 gene. Genomics. 1999 Mar 1;56(2):197-202. [PubMed Link Image]
  2. Li H, Leo C, Zhu J, Wu X, O'Neil J, Park EJ, Chen JD: Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol Cell Biol. 2000 Mar;20(5):1784-96. [PubMed Link Image]
  3. Wen YD, Perissi V, Staszewski LM, Yang WM, Krones A, Glass CK, Rosenfeld MG, Seto E: The histone deacetylase-3 complex contains nuclear receptor corepressors. Proc Natl Acad Sci U S A. 2000 Jun 20;97(13):7202-7. [PubMed Link Image]
  4. Yang WM, Yao YL, Sun JM, Davie JR, Seto E: Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family. J Biol Chem. 1997 Oct 31;272(44):28001-7. [PubMed Link Image]
  5. Dangond F, Hafler DA, Tong JK, Randall J, Kojima R, Utku N, Gullans SR: Differential display cloning of a novel human histone deacetylase (HDAC3) cDNA from PHA-activated immune cells. Biochem Biophys Res Commun. 1998 Jan 26;242(3):648-52. [PubMed Link Image]
  6. Emiliani S, Fischle W, Van Lint C, Al-Abed Y, Verdin E: Characterization of a human RPD3 ortholog, HDAC3. Proc Natl Acad Sci U S A. 1998 Mar 17;95(6):2795-800. [PubMed Link Image]
Target 4 Drug References
  1. Xu WS, Parmigiani RB, Marks PA: Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene. 2007 Aug 13;26(37):5541-52. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 4124
Target 5 Name Histone deacetylase 6
Target 5 Synonyms
  1. HD6
Target 5 Gene Name HDAC6
Target 5 Protein Sequence >Histone deacetylase 6 
MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLG
QAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLI
QEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNS
YSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQ
KHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQG
QGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATP
AGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSA
QASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSR
TGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCH
SAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLN
GAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMF
EDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWH
RLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEG
GYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVE
DREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSET
AVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGA
ILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTISEAAMEGATLDQTTSEEAPGGTELIQ
TPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEA
AGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQ
ENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKN
IAHQNKFGEDMPHPH
Target 5 Number of Residues 1235
Target 5 Molecular Weight 131433
Target 5 Theoretical pI 4.98
Target 5 GO Classification Not Available
Target 5 General Function Not Available
Target 5 Specific Function Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin
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 4754911 Link Image
Target 5 UniProtKB/Swiss-Prot ID Q9UBN7 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name HDAC6_HUMAN Link Image
Target 5 PDB ID Not Available
Target 5 Cellular Location
  • Nucleus. Cytoplasm
Target 5 Gene Sequence >3648 bp 
ATGACCTCAACCGGCCAGGATTCCACCACAACCAGGCAGCGAAGAAGTAGGCAGAACCCC
CAGTCGCCCCCTCAGGACTCCAGTGTCACTTCGAAGCGAAATATTAAAAAGGGAGCCGTT
CCCCGCTCTATCCCCAATCTAGCGGAGGTAAAGAAGAAAGGCAAAATGAAGAAGCTCGGC
CAAGCAATGGAAGAAGACCTAATCGTGGGACTGCAAGGGATGGATCTGAACCTTGAGGCT
GAAGCACTGGCTGGCACTGGCTTGGTGTTGGATGAGCAGTTAAATGAATTCCATTGCCTC
TGGGATGACAGCTTCCCGGAAGGCCCTGAGCGGCTCCATGCCATCAAGGAGCAACTGATC
CAGGAGGGCCTCCTAGATCGCTGCGTGTCCTTTCAGGCCCGGTTTGCTGAAAAGGAAGAG
CTGATGTTGGTTCACAGCCTAGAATATATTGATCTGATGGAAACAACCCAGTACATGAAT
GAGGGAGAACTCCGTGTCCTAGCAGACACCTACGACTCAGTTTATCTGCATCCGAACTCA
TACTCCTGTGCCTGCCTGGCCTCAGGCTCTGTCCTCAGGCTGGTGGATGCGGTCCTGGGG
GCTGAGATCCGGAATGGCATGGCCATCATTAGGCCTCCTGGACATCACGCCCAGCACAGT
CTTATGGATGGCTATTGCATGTTCAACCACGTGGCTGTGGCAGCCCGCTATGCTCAACAG
AAACACCGCATCCGGAGGGTCCTTATCGTAGATTGGGATGTGCACCACGGTCAAGGAACA
CAGTTCACCTTCGACCAGGACCCCAGTGTCCTCTATTTCTCCATCCACCGCTACGAGCAG
GGTAGGTTCTGGCCCCACCTGAAGGCCTCTAACTGGTCCACCACAGGTTTCGGCCAAGGC
CAAGGATATACCATCAATGTGCCTTGGAACCAGGTGGGGATGCGGGATGCTGACTACATT
GCTGCTTTCCTGCACGTCCTGCTGCCAGTCGCCCTCGAGTTCCAGCCTCAGCTGGTCCTG
GTGGCTGCTGGATTTGATGCCCTGCAAGGGGACCCCAAGGGTGAGATGGCCGCCACTCCG
GCAGGGTTCGCCCAGCTAACCCACCTGCTCATGGGTCTGGCAGGAGGCAAGCTGATCCTG
TCTCTGGAGGGTGGCTACAACCTCCGCGCCCTGGCTGAAGGCGTCAGTGCTTCGCTCCAC
ACCCTTCTGGGAGACCCTTGCCCCATGCTGGAGTCACCTGGTGCCCCCTGCCGGAGTGCC
CAGGCTTCAGTTTCCTGTGCTCTGGAAGCCCTTGAGCCCTTCTGGGAGGTTCTTGTGAGA
TCAACTGAGACCGTGGAGAGGGACAACATGGAGGAGGACAATGTAGAGGAGAGCGAGGAG
GAAGGACCCTGGGAGCCCCCTGTGCTCCCAATCCTGACATGGCCAGTGCTACAGTCTCGC
ACAGGGCTGGTCTATGACCAAAATATGATGAATCACTGCAACTTGTGGGACAGCCACCAC
CCTGAGGTACCCCAGCGCATCTTGCGGATCATGTGCCGTCTGGAGGAGCTGGGCCTTGCC
GGGCGCTGCCTCACCCTGACACCGCGCCCTGCCACAGAGGCTGAGCTGCTCACCTGTCAC
AGTGCTGAGTACGTGGGTCATCTCCGGGCCACAGAGAAAATGAAAACCCGGGAGCTGCAC
CGTGAGAGTTCCAACTTTGACTCCATCTATATCTGCCCCAGTACCTTCGCCTGTGCACAG
CTTGCCACTGGCGCTGCCTGCCGCCTGGTGGAGGCTGTGCTCTCAGGAGAGGTTCTGAAT
GGTGCTGCTGTGGTGCGTCCCCCAGGACACCACGCAGAGCAGGATGCAGCTTGCGGTTTT
TGCTTTTTCAACTCTGTGGCTGTGGCTGCTCGCCATGCCCAGACTATCAGTGGGCATGCC
CTACGGATCCTGATTGTGGATTGGGATGTCCACCACGGTAATGGAACTCAGCACATGTTT
GAGGATGACCCCAGTGTGCTATATGTGTCCCTGCACCGCTATGATCATGGCACCTTCTTC
CCCATGGGGGATGAGGGTGCCAGCAGCCAGATCGGCCGGGCTGCGGGCACAGGCTTCACC
GTCAACGTGGCATGGAACGGGCCCCGCATGGGTGATGCTGACTACCTAGCTGCCTGGCAT
CGCCTGGTGCTTCCCATTGCCTACGAGTTTAACCCAGAACTGGTGCTGGTCTCAGCTGGC
TTTGATGCTGCACGGGGGGATCCGCTGGGGGGCTGCCAGGTGTCACCTGAGGGTTATGCC
CACCTCACCCACCTGCTGATGGGCCTTGCCAGTGGCCGCATTATCCTTATCCTAGAGGGT
GGCTATAACCTGACATCCATCTCAGAGTCCATGGCTGCCTGCACTCGCTCCCTCCTTGGA
GACCCACCACCCCTGCTGACCCTGCCACGGCCCCCACTATCAGGGGCCCTGGCCTCAATC
ACTGAGACCATCCAAGTCCATCGCAGATACTGGCGCAGCTTACGGGTCATGAAGGTAGAA
GACAGAGAAGGACCCTCCAGTTCTAAGTTGGTCACCAAGAAGGCACCCCAACCAGCCAAA
CCTAGGTTAGCTGAGCGGATGACCACACGAGAAAAGAAGGTTCTGGAAGCAGGCATGGGG
AAAGTCACCTCGGCATCATTTGGGGAAGAGTCCACTCCAGGCCAGACTAACTCAGAGACA
GCTGTGGTGGCCCTCACTCAGGACCAGCCCTCAGAGGCAGCCACAGGGGGAGCCACTCTG
GCCCAGACCATTTCTGAGGCAGCCATTGGGGGAGCCATGCTGGGCCAGACCACCTCAGAG
GAGGCTGTCGGGGGAGCCACTCCGGACCAGACCACCTCAGAGGAGACTGTGGGAGGAGCC
ATTCTGGACCAGACCACCTCAGAGGATGCTGTTGGGGGAGCCACGCTGGGCCAGACTACC
TCAGAGGAGGCTGTAGGAGGAGCTACACTGGCCCAGACCATCTCGGAGGCAGCCATGGAG
GGAGCCACACTGGACCAGACTACGTCAGAGGAGGCTCCAGGGGGCACCGAGCTGATCCAA
ACTCCTCTAGCCTCGAGCACAGACCACCAGACCCCCCCAACCTCACCTGTGCAGGGAACT
ACACCCCAGATATCTCCCAGTACACTGATTGGGAGTCTCAGGACCTTGGAGCTAGGCAGC
GAATCTCAGGGGGCCTCAGAATCTCAGGCCCCAGGAGAGGAGAACCTACTAGGAGAGGCA
GCTGGAGGTCAGGACATGGCTGATTCGATGCTGATGCAGGGATCTAGGGGCCTCACTGAT
CAGGCCATATTTTATGCTGTGACACCACTGCCCTGGTGTCCCCATTTGGTGGCAGTATGC
CCCATACCTGCAGCAGGCCTAGACGTGACCCAACCTTGTGGGGACTGTGGAACAATCCAA
GAGAATTGGGTGTGTCTCTCTTGCTATCAGGTCTACTGTGGTCGTTACATCAATGGCCAC
ATGCTCCAACACCATGGAAATTCTGGACACCCGCTGGTCCTCAGCTACATCGACCTGTCA
GCCTGGTGTTACTACTGTCAGGCCTATGTCCACCACCAGGCTCTCCTAGATGTGAAGAAC
ATCGCCCACCAGAACAAGTTTGGGGAGGATATGCCCCACCCACACTAA
Target 5 GenBank Gene ID
Target 5 GeneCard ID HDAC6 Link Image
Target 5 GenAtlas ID HDAC6 Link Image
Target 5 HGNC ID HGNC:14064 Link Image
Target 5 Chromosome Location X
Target 5 Locus Xp11.23
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Grozinger CM, Hassig CA, Schreiber SL: Three proteins define a class of human histone deacetylases related to yeast Hda1p. Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):4868-73. [PubMed Link Image]
  2. Gao L, Cueto MA, Asselbergs F, Atadja P: Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family. J Biol Chem. 2002 Jul 12;277(28):25748-55. Epub 2002 Apr 10. [PubMed Link Image]
  3. Hubbert C, Guardiola A, Shao R, Kawaguchi Y, Ito A, Nixon A, Yoshida M, Wang XF, Yao TP: HDAC6 is a microtubule-associated deacetylase. Nature. 2002 May 23;417(6887):455-8. [PubMed Link Image]
  4. Kirsh O, Seeler JS, Pichler A, Gast A, Muller S, Miska E, Mathieu M, Harel-Bellan A, Kouzarides T, Melchior F, Dejean A: The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase. EMBO J. 2002 Jun 3;21(11):2682-91. [PubMed Link Image]
  5. Hook SS, Orian A, Cowley SM, Eisenman RN: Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13425-30. Epub 2002 Sep 27. [PubMed Link Image]
  6. North BJ, Marshall BL, Borra MT, Denu JM, Verdin E: The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell. 2003 Feb;11(2):437-44. [PubMed Link Image]
Target 5 Drug References
  1. Xu WS, Parmigiani RB, Marks PA: Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene. 2007 Aug 13;26(37):5541-52. [PubMed Link Image]
Drug Target 6 [top]
Target 6 ID 4762
Target 6 Name Acetoin utilization protein
Target 6 Synonyms Not Available
Target 6 Gene Name acuC1
Target 6 Protein Sequence >Acetoin utilization protein 
MKKVKLIGTLDYGKYRYPKNHPLKIPRVSLLLRFLDAMNLIDEKELIKSRPATKEELLLF
HTEDYINTLMEAERCQCVPKGAREKYNIGGYENPVSYAMFTGSSLATGSTVQAIEEFLKG
NVAFNPAGGMHHAFKSRANGFCYINDPAVGIEYLRKKGFKRILYIDLDAHHCDGVQEAFY
DTDQVFVLSLHQSPEYAFPFEKGFLEEIGEGKGKGYNLNIPLPKGLNDNEFLFALEKSLE
IVKEVFEPEVYLLQLGTDPLLEDYLSKFNLSNVAFLKAFNIVREVFGEGVYLGGGGYHPY
ALARAWTLIWCELSGREVPEKLNNKAKELLKSIDFEEFDDEVDRSYMLETLKDPWRGGEV
RKEVKDTLEKAKASS
Target 6 Number of Residues 381
Target 6 Molecular Weight 42663
Target 6 Theoretical pI 5.53
Target 6 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
histone deacetylase activity
Process
physiological process
metabolism
macromolecule metabolism
biopolymer metabolism
biopolymer modification
protein modification
protein amino acid deacetylation
histone deacetylation
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
Target 6 General Function Involved in histone deacetylase activity
Target 6 Specific Function Not Available
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 Essential
Target 6 GenBank ID Protein Not Available
Target 6 UniProtKB/Swiss-Prot ID O67135 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name O67135_AQUAE Link Image
Target 6 PDB ID 1C3P Link Image
Target 6 PDB File Show
Target 6 3D Structure
Target 6 Cellular Location
  • Cytoplasmic
Target 6 Gene Sequence >1128 bp 
TTAAGATGAGGCTTTCGCCTTTTCAAGCGTATCCTTTACTTCTTTCCTTACCTCTCCTCC
TCTCCAGGGGTCCTTTAGGGTTTCGAGCATGTACGAGCGGTCCACCTCGTCGTCAAACTC
TTCAAAGTCTATACTCTTTAAAAGCTCTTTTGCTTTATTGTTTAGCTTTTCCGGCACTTC
CCTTCCCGAAAGCTCGCACCAGATTAGGGTCCATGCCCTTGCGAGGGCGTAAGGATGGTA
TCCGCCTCCTCCGAGGTATACTCCCTCCCCGAAAACCTCACGAACGATGTTGAAAGCTTT
TAAAAAGGCAACGTTTGAGAGGTTGAACTTGGAAAGGTAATCTTCAAGGAGTGGGTCAGT
TCCGAGTTGAAGAAGGTAAACCTCGGGCTCAAATACTTCTTTGACTATTTCCAGAGATTT
TTCTAGGGCAAAGAGGAACTCGTTGTCGTTCAAGCCCTTTGGCAGGGGAATGTTCAGGTT
GTAGCCCTTTCCTTTTCCTTCTCCTATCTCCTCCAGGAAGCCCTTCTCAAAGGGAAAGGC
GTACTCGGGCGACTGGTGAAGGGACAGGACGAACACCTGGTCTGTATCGTAAAAGGCTTC
CTGAACACCGTCGCAGTGGTGGGCATCAAGGTCTATGTAGAGTATTCTCTTAAAGCCTTT
TTTTCTCAAGTACTCAATTCCCACAGCGGGGTCGTTTATGTAGCAAAAGCCGTTTGCCCT
GCTTTTAAAAGCGTGGTGCATACCTCCCGCGGGATTGAAAGCTACATTTCCCTTTAAAAA
TTCCTCTATCGCCTGCACTGTTGAACCCGTTGCGAGAGAAGAGCCTGTAAACATCGCGTA
AGATACGGGGTTTTCGTATCCGCCTATGTTGTACTTTTCCCTAGCTCCCTTCGGAACGCA
CTGACACCTTTCCGCTTCCATTAAAGTGTTTATGTAGTCTTCCGTGTGGAATAAAAGGAG
TTCTTCTTTAGTTGCGGGTCTGCTCTTGATTAATTCCTTCTCATCTATAAGGTTCATGGC
ATCTAAAAACCTAAGGAGTAGGGAAACTCTTGGTATTTTAAGAGGATGGTTTTTGGGATA
TCTGTACTTTCCGTAGTCTAAAGTTCCGATAAGTTTAACCTTCTTCAT
Target 6 GenBank Gene ID
Target 6 GeneCard ID Not Available
Target 6 GenAtlas ID Not Available
Target 6 HGNC ID Not Available
Target 6 Chromosome Location Not Available
Target 6 Locus Not Available
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Finnin MS, Donigian JR, Cohen A, Richon VM, Rifkind RA, Marks PA, Breslow R, Pavletich NP: Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature. 1999 Sep 9;401(6749):188-93. [PubMed Link Image]
  2. Deckert G, Warren PV, Gaasterland T, Young WG, Lenox AL, Graham DE, Overbeek R, Snead MA, Keller M, Aujay M, Huber R, Feldman RA, Short JM, Olsen GJ, Swanson RV: The complete genome of the hyperthermophilic bacterium Aquifex aeolicus. Nature. 1998 Mar 26;392(6674):353-8. [PubMed Link Image]
Target 6 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.