Resource 7-[4-(Dimethylamino)Phenyl]-N-Hydroxy-4,6-Dimethyl-7-Oxo-2,4-Heptadienamide

Predicate	Value (sorted: default)
rdfs:label	"7-[4-(Dimethylamino)Phenyl]-N-Hydroxy-4,6-Dimethyl-7-Oxo-2,4-Heptadienamide"
rdf:type	drugbank:drugs
drugbank:description	" experimental This compound belongs to the acetophenones. These are organic compounds containing the acetophenone structure. Acetophenones Organic Compounds Benzenoids Benzene and Substituted Derivatives Acetophenones Benzoyl Derivatives Enones Hydroxamic Acids Tertiary Amines Enolates Polyamines benzoyl enone tertiary amine hydroxamic acid carboxamide group ketone polyamine carboxylic acid derivative enolate amine carbonyl group organonitrogen compound Antifungal Agents logP 2.36 ALOGPS logS -3.9 ALOGPS Water Solubility 4.25e-02 g/l ALOGPS logP 2.41 ChemAxon IUPAC Name (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide ChemAxon Traditional IUPAC Name trichostatin ChemAxon Molecular Weight 302.3682 ChemAxon Monoisotopic Weight 302.16304258 ChemAxon SMILES ONC(=O)\C=C\C(\C)=C\[C@](C)([H])C(=O)C1=CC=C(N(C)C)C=C1 ChemAxon Molecular Formula C17H22N2O3 ChemAxon InChI InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 ChemAxon InChIKey InChIKey=RTKIYFITIVXBLE-QEQCGCAPSA-N ChemAxon Polar Surface Area (PSA) 69.64 ChemAxon Refractivity 90.24 ChemAxon Polarizability 33.37 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 9.57 ChemAxon pKa (strongest basic) 3.36 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 444732 PubChem Substance 46506659 ChemSpider 392575 BindingDB 19130 PDB TSN BE0001608 Histone deacetylase 8 Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # 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":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Histone deacetylase 8 Chromatin structure and dynamics 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 HDAC8 Xq13 Nucleus. Note=Excluded from the nucleoli None 5.37 41758.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:13315 GenAtlas HDAC8 GeneCards HDAC8 GenBank Gene Database AF230097 GenBank Protein Database 8118721 UniProtKB Q9BY41 UniProt Accession HDAC8_HUMAN HD8 >Histone deacetylase 8 MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPK VASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATI TAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLH HGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKY YQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLI LGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPH RIQQILNYIKGNLKHVV >1134 bp ATGGAGGAGCCGGAGGAACCGGCGGACAGTGGGCAGTCGCTGGTCCCGGTTTATATCTAT AGTCCCGAGTATGTCAGTATGTGTGACTCCCTGGCCAAGATCCCCAAACGGGCCAGTATG GTGCATTCTTTGATTGAAGCATATGCACTGCATAAGCAAATGAGGATAGTTAAGCCTAAA GTGGCCTCCATGGAGGAGATGGCCACCTTCCACACTGATGCTTATCTGCAGCATCTCCAG AAGGTCAGCCAAGAGGGCGATGATGATCATCCGGACTCCATAGAATATGGGCTAGGTTAT GACTGCCCAGCCACTGAAGGGATATTTGACTATGCAGCAGCTATAGGAGGGGCTACGATC ACAGCTGCCCAATGCCTGATTGACGGAATGTGCAAAGTAGCAATTAACTGGTCTGGAGGG TGGCATCATGCAAAGAAAGATGAAGCATCTGGTTTTTGTTATCTCAATGATGCTGTCCTG GGAATATTACGATTGCGACGGAAATTTGAGCGTATTCTCTACGTGGATTTGGATCTGCAC CATGGAGATGGTGTAGAAGACGCATTCAGTTTCACCTCCAAAGTCATGACCGTGTCCCTG CACAAATTCTCCCCAGGATTTTTCCCAGGAACAGGTGACGTGTCTGATGTTGGCCTAGGG AAGGGACGGTACTACAGTGTAAATGTGCCCATTCAGGATGGCATACAAGATGAAAAATAT TACCAGATCTGTGAAAGTGTACTAAAGGAAGTATACCAAGCCTTTAATCCCAAAGCAGTG GTCTTACAGCTGGGAGCTGACACAATAGCTGGGGATCCCATGTGCTCCTTTAACATGACT CCAGTGGGAATTGGCAAGTGTCTTAAGTACATCCTTCAATGGCAGTTGGCAACACTCATT TTGGGAGGAGGAGGCTATAACCTTGCCAACACGGCTCGATGCTGGACATACTTGACCGGG GTCATCCTAGGGAAAACACTATCCTCTGAGATCCCAGATCATGAGTTTTTCACAGCATAT GGTCCTGATTATGTGCTGGAAATCACGCCAAGCTGCCGGCCAGACCGCAATGAGCCCCAC CGAATCCAACAAATCCTCAACTACATCAAAGGGAATCTGAAGCATGTGGTCTAG PF00850 Hist_deacetyl component organelle component membrane-bound organelle component intracellular membrane-bound organelle component nucleus function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides function catalytic activity function hydrolase activity function histone deacetylase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds process histone deacetylation process macromolecule metabolism process biopolymer metabolism process biopolymer modification process protein modification process physiological process process metabolism process protein amino acid deacetylation BE0002796 Acetoin utilization protein Aquifex aeolicus (strain VF5) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Acetoin utilization protein Involved in histone deacetylase activity acuC1 Cytoplasmic None 5.53 42663.0 Aquifex aeolicus (strain VF5) GenBank Gene Database AE000657 UniProtKB O67135 UniProt Accession O67135_AQUAE >Acetoin utilization protein MKKVKLIGTLDYGKYRYPKNHPLKIPRVSLLLRFLDAMNLIDEKELIKSRPATKEELLLF HTEDYINTLMEAERCQCVPKGAREKYNIGGYENPVSYAMFTGSSLATGSTVQAIEEFLKG NVAFNPAGGMHHAFKSRANGFCYINDPAVGIEYLRKKGFKRILYIDLDAHHCDGVQEAFY DTDQVFVLSLHQSPEYAFPFEKGFLEEIGEGKGKGYNLNIPLPKGLNDNEFLFALEKSLE IVKEVFEPEVYLLQLGTDPLLEDYLSKFNLSNVAFLKAFNIVREVFGEGVYLGGGGYHPY ALARAWTLIWCELSGREVPEKLNNKAKELLKSIDFEEFDDEVDRSYMLETLKDPWRGGEV RKEVKDTLEKAKASS >1128 bp TTAAGATGAGGCTTTCGCCTTTTCAAGCGTATCCTTTACTTCTTTCCTTACCTCTCCTCC TCTCCAGGGGTCCTTTAGGGTTTCGAGCATGTACGAGCGGTCCACCTCGTCGTCAAACTC TTCAAAGTCTATACTCTTTAAAAGCTCTTTTGCTTTATTGTTTAGCTTTTCCGGCACTTC CCTTCCCGAAAGCTCGCACCAGATTAGGGTCCATGCCCTTGCGAGGGCGTAAGGATGGTA TCCGCCTCCTCCGAGGTATACTCCCTCCCCGAAAACCTCACGAACGATGTTGAAAGCTTT TAAAAAGGCAACGTTTGAGAGGTTGAACTTGGAAAGGTAATCTTCAAGGAGTGGGTCAGT TCCGAGTTGAAGAAGGTAAACCTCGGGCTCAAATACTTCTTTGACTATTTCCAGAGATTT TTCTAGGGCAAAGAGGAACTCGTTGTCGTTCAAGCCCTTTGGCAGGGGAATGTTCAGGTT GTAGCCCTTTCCTTTTCCTTCTCCTATCTCCTCCAGGAAGCCCTTCTCAAAGGGAAAGGC GTACTCGGGCGACTGGTGAAGGGACAGGACGAACACCTGGTCTGTATCGTAAAAGGCTTC CTGAACACCGTCGCAGTGGTGGGCATCAAGGTCTATGTAGAGTATTCTCTTAAAGCCTTT TTTTCTCAAGTACTCAATTCCCACAGCGGGGTCGTTTATGTAGCAAAAGCCGTTTGCCCT GCTTTTAAAAGCGTGGTGCATACCTCCCGCGGGATTGAAAGCTACATTTCCCTTTAAAAA TTCCTCTATCGCCTGCACTGTTGAACCCGTTGCGAGAGAAGAGCCTGTAAACATCGCGTA AGATACGGGGTTTTCGTATCCGCCTATGTTGTACTTTTCCCTAGCTCCCTTCGGAACGCA CTGACACCTTTCCGCTTCCATTAAAGTGTTTATGTAGTCTTCCGTGTGGAATAAAAGGAG TTCTTCTTTAGTTGCGGGTCTGCTCTTGATTAATTCCTTCTCATCTATAAGGTTCATGGC ATCTAAAAACCTAAGGAGTAGGGAAACTCTTGGTATTTTAAGAGGATGGTTTTTGGGATA TCTGTACTTTCCGTAGTCTAAAGTTCCGATAAGTTTAACCTTCTTCAT PF00850 Hist_deacetyl component nucleus component organelle component membrane-bound organelle component intracellular membrane-bound organelle function hydrolase activity function histone deacetylase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides function catalytic activity process metabolism process protein amino acid deacetylation process histone deacetylation process macromolecule metabolism process biopolymer metabolism process biopolymer modification process protein modification process physiological process BE0003525 Histone deacetylase 7 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Histone deacetylase 7 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. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity). May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene HDAC7 Nucleus. Cytoplasm None 7.6 102928.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:14067 GenAtlas HDAC7 GenBank Gene Database BC020505 UniProtKB Q8WUI4 UniProt Accession HDAC7_HUMAN HD7a >Histone deacetylase 7a MDLRVGQRPPVEPPPEPTLLALQRPQRLHHHLFLAGLQQQRSVEPMRLSMDTPMPELQVG PQEQELRQLLHKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPNSPGIPYRTLEPL ETEGATRSMLSSFLPPVPSLPSDPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKE SAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPILGSEALLGQRLRLQETSV APFALPTVSLLPAITLGLPAPARADSDRRTHPTLGPRGPILGSPHTPLFLPHGLEPEAGG TLPSRLQPILLLDPSGSHAPLLTVPGLGPLPFHFAQSLMTTERLSGSGLHWPLSRTRSEP LPPSATAPPPPGPMQPRLEQLKTHVQVIKRSAKPSEKPRLRQIPSAEDLETDGGGPGQVV DDGLEHRELGHGQPEARGPAPLQQHPQVLLWEQQRLAGRLPRGSTGDTVLLPLAQGGHRP LSRAQSSPAAPASLSAPEPASQARVLSSSETPARTLPFTTGLIYDSVMLKHQCSCGDNSR HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLD NGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNG FAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQQSKASKILIVDWDVHHGNGTQQTFYQ DPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRI VVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALE GGHDLTAICDASEACVAALLGNRVDPLSEEGWKQKPNLNAIRSLEAVIRVHSKYWGCMQR LASCPDSWVPRVPGADKEEVEAVTALASLSVGILAEDRPSEQLVEEEEPMNL PF00850 Hist_deacetyl "
drugbank:drugCategory	drugcategory:Antifungal Agents
owl:sameAs	drug:EXPT03123

"7-[4-(Dimethylamino)Phenyl]-N-Hydroxy-4,6-Dimethyl-7-Oxo-2,4-Heptadienamide"

" experimental This compound belongs to the acetophenones. These are organic compounds containing the acetophenone structure. Acetophenones Organic Compounds Benzenoids Benzene and Substituted Derivatives Acetophenones Benzoyl Derivatives Enones Hydroxamic Acids Tertiary Amines Enolates Polyamines benzoyl enone tertiary amine hydroxamic acid carboxamide group ketone polyamine carboxylic acid derivative enolate amine carbonyl group organonitrogen compound Antifungal Agents logP 2.36 ALOGPS logS -3.9 ALOGPS Water Solubility 4.25e-02 g/l ALOGPS logP 2.41 ChemAxon IUPAC Name (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide ChemAxon Traditional IUPAC Name trichostatin ChemAxon Molecular Weight 302.3682 ChemAxon Monoisotopic Weight 302.16304258 ChemAxon SMILES ONC(=O)\C=C\C(\C)=C\[C@](C)([H])C(=O)C1=CC=C(N(C)C)C=C1 ChemAxon Molecular Formula C17H22N2O3 ChemAxon InChI InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 ChemAxon InChIKey InChIKey=RTKIYFITIVXBLE-QEQCGCAPSA-N ChemAxon Polar Surface Area (PSA) 69.64 ChemAxon Refractivity 90.24 ChemAxon Polarizability 33.37 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 9.57 ChemAxon pKa (strongest basic) 3.36 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 444732 PubChem Substance 46506659 ChemSpider 392575 BindingDB 19130 PDB TSN BE0001608 Histone deacetylase 8 Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # 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":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Histone deacetylase 8 Chromatin structure and dynamics 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 HDAC8 Xq13 Nucleus. Note=Excluded from the nucleoli None 5.37 41758.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:13315 GenAtlas HDAC8 GeneCards HDAC8 GenBank Gene Database AF230097 GenBank Protein Database 8118721 UniProtKB Q9BY41 UniProt Accession HDAC8_HUMAN HD8 >Histone deacetylase 8 MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPK VASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATI TAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLH HGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKY YQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLI LGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPH RIQQILNYIKGNLKHVV >1134 bp ATGGAGGAGCCGGAGGAACCGGCGGACAGTGGGCAGTCGCTGGTCCCGGTTTATATCTAT AGTCCCGAGTATGTCAGTATGTGTGACTCCCTGGCCAAGATCCCCAAACGGGCCAGTATG GTGCATTCTTTGATTGAAGCATATGCACTGCATAAGCAAATGAGGATAGTTAAGCCTAAA GTGGCCTCCATGGAGGAGATGGCCACCTTCCACACTGATGCTTATCTGCAGCATCTCCAG AAGGTCAGCCAAGAGGGCGATGATGATCATCCGGACTCCATAGAATATGGGCTAGGTTAT GACTGCCCAGCCACTGAAGGGATATTTGACTATGCAGCAGCTATAGGAGGGGCTACGATC ACAGCTGCCCAATGCCTGATTGACGGAATGTGCAAAGTAGCAATTAACTGGTCTGGAGGG TGGCATCATGCAAAGAAAGATGAAGCATCTGGTTTTTGTTATCTCAATGATGCTGTCCTG GGAATATTACGATTGCGACGGAAATTTGAGCGTATTCTCTACGTGGATTTGGATCTGCAC CATGGAGATGGTGTAGAAGACGCATTCAGTTTCACCTCCAAAGTCATGACCGTGTCCCTG CACAAATTCTCCCCAGGATTTTTCCCAGGAACAGGTGACGTGTCTGATGTTGGCCTAGGG AAGGGACGGTACTACAGTGTAAATGTGCCCATTCAGGATGGCATACAAGATGAAAAATAT TACCAGATCTGTGAAAGTGTACTAAAGGAAGTATACCAAGCCTTTAATCCCAAAGCAGTG GTCTTACAGCTGGGAGCTGACACAATAGCTGGGGATCCCATGTGCTCCTTTAACATGACT CCAGTGGGAATTGGCAAGTGTCTTAAGTACATCCTTCAATGGCAGTTGGCAACACTCATT TTGGGAGGAGGAGGCTATAACCTTGCCAACACGGCTCGATGCTGGACATACTTGACCGGG GTCATCCTAGGGAAAACACTATCCTCTGAGATCCCAGATCATGAGTTTTTCACAGCATAT GGTCCTGATTATGTGCTGGAAATCACGCCAAGCTGCCGGCCAGACCGCAATGAGCCCCAC CGAATCCAACAAATCCTCAACTACATCAAAGGGAATCTGAAGCATGTGGTCTAG PF00850 Hist_deacetyl component organelle component membrane-bound organelle component intracellular membrane-bound organelle component nucleus function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides function catalytic activity function hydrolase activity function histone deacetylase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds process histone deacetylation process macromolecule metabolism process biopolymer metabolism process biopolymer modification process protein modification process physiological process process metabolism process protein amino acid deacetylation BE0002796 Acetoin utilization protein Aquifex aeolicus (strain VF5) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Acetoin utilization protein Involved in histone deacetylase activity acuC1 Cytoplasmic None 5.53 42663.0 Aquifex aeolicus (strain VF5) GenBank Gene Database AE000657 UniProtKB O67135 UniProt Accession O67135_AQUAE >Acetoin utilization protein MKKVKLIGTLDYGKYRYPKNHPLKIPRVSLLLRFLDAMNLIDEKELIKSRPATKEELLLF HTEDYINTLMEAERCQCVPKGAREKYNIGGYENPVSYAMFTGSSLATGSTVQAIEEFLKG NVAFNPAGGMHHAFKSRANGFCYINDPAVGIEYLRKKGFKRILYIDLDAHHCDGVQEAFY DTDQVFVLSLHQSPEYAFPFEKGFLEEIGEGKGKGYNLNIPLPKGLNDNEFLFALEKSLE IVKEVFEPEVYLLQLGTDPLLEDYLSKFNLSNVAFLKAFNIVREVFGEGVYLGGGGYHPY ALARAWTLIWCELSGREVPEKLNNKAKELLKSIDFEEFDDEVDRSYMLETLKDPWRGGEV RKEVKDTLEKAKASS >1128 bp TTAAGATGAGGCTTTCGCCTTTTCAAGCGTATCCTTTACTTCTTTCCTTACCTCTCCTCC TCTCCAGGGGTCCTTTAGGGTTTCGAGCATGTACGAGCGGTCCACCTCGTCGTCAAACTC TTCAAAGTCTATACTCTTTAAAAGCTCTTTTGCTTTATTGTTTAGCTTTTCCGGCACTTC CCTTCCCGAAAGCTCGCACCAGATTAGGGTCCATGCCCTTGCGAGGGCGTAAGGATGGTA TCCGCCTCCTCCGAGGTATACTCCCTCCCCGAAAACCTCACGAACGATGTTGAAAGCTTT TAAAAAGGCAACGTTTGAGAGGTTGAACTTGGAAAGGTAATCTTCAAGGAGTGGGTCAGT TCCGAGTTGAAGAAGGTAAACCTCGGGCTCAAATACTTCTTTGACTATTTCCAGAGATTT TTCTAGGGCAAAGAGGAACTCGTTGTCGTTCAAGCCCTTTGGCAGGGGAATGTTCAGGTT GTAGCCCTTTCCTTTTCCTTCTCCTATCTCCTCCAGGAAGCCCTTCTCAAAGGGAAAGGC GTACTCGGGCGACTGGTGAAGGGACAGGACGAACACCTGGTCTGTATCGTAAAAGGCTTC CTGAACACCGTCGCAGTGGTGGGCATCAAGGTCTATGTAGAGTATTCTCTTAAAGCCTTT TTTTCTCAAGTACTCAATTCCCACAGCGGGGTCGTTTATGTAGCAAAAGCCGTTTGCCCT GCTTTTAAAAGCGTGGTGCATACCTCCCGCGGGATTGAAAGCTACATTTCCCTTTAAAAA TTCCTCTATCGCCTGCACTGTTGAACCCGTTGCGAGAGAAGAGCCTGTAAACATCGCGTA AGATACGGGGTTTTCGTATCCGCCTATGTTGTACTTTTCCCTAGCTCCCTTCGGAACGCA CTGACACCTTTCCGCTTCCATTAAAGTGTTTATGTAGTCTTCCGTGTGGAATAAAAGGAG TTCTTCTTTAGTTGCGGGTCTGCTCTTGATTAATTCCTTCTCATCTATAAGGTTCATGGC ATCTAAAAACCTAAGGAGTAGGGAAACTCTTGGTATTTTAAGAGGATGGTTTTTGGGATA TCTGTACTTTCCGTAGTCTAAAGTTCCGATAAGTTTAACCTTCTTCAT PF00850 Hist_deacetyl component nucleus component organelle component membrane-bound organelle component intracellular membrane-bound organelle function hydrolase activity function histone deacetylase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides function catalytic activity process metabolism process protein amino acid deacetylation process histone deacetylation process macromolecule metabolism process biopolymer metabolism process biopolymer modification process protein modification process physiological process BE0003525 Histone deacetylase 7 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Histone deacetylase 7 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. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity). May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene HDAC7 Nucleus. Cytoplasm None 7.6 102928.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:14067 GenAtlas HDAC7 GenBank Gene Database BC020505 UniProtKB Q8WUI4 UniProt Accession HDAC7_HUMAN HD7a >Histone deacetylase 7a MDLRVGQRPPVEPPPEPTLLALQRPQRLHHHLFLAGLQQQRSVEPMRLSMDTPMPELQVG PQEQELRQLLHKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPNSPGIPYRTLEPL ETEGATRSMLSSFLPPVPSLPSDPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKE SAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPILGSEALLGQRLRLQETSV APFALPTVSLLPAITLGLPAPARADSDRRTHPTLGPRGPILGSPHTPLFLPHGLEPEAGG TLPSRLQPILLLDPSGSHAPLLTVPGLGPLPFHFAQSLMTTERLSGSGLHWPLSRTRSEP LPPSATAPPPPGPMQPRLEQLKTHVQVIKRSAKPSEKPRLRQIPSAEDLETDGGGPGQVV DDGLEHRELGHGQPEARGPAPLQQHPQVLLWEQQRLAGRLPRGSTGDTVLLPLAQGGHRP LSRAQSSPAAPASLSAPEPASQARVLSSSETPARTLPFTTGLIYDSVMLKHQCSCGDNSR HPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLD NGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNG FAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQQSKASKILIVDWDVHHGNGTQQTFYQ DPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRI VVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALE GGHDLTAICDASEACVAALLGNRVDPLSEEGWKQKPNLNAIRSLEAVIRVHSKYWGCMQR LASCPDSWVPRVPGADKEEVEAVTALASLSVGILAEDRPSEQLVEEEEPMNL PF00850 Hist_deacetyl "

owl:sameAs

drug:EXPT03123

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