Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB07771"

Predicate	Value (sorted: none)
drugbank:description	" experimental This compound belongs to the sesquiterpenes. These are terpenes with three consecutive isoprene units. Sesquiterpenes Organic Compounds Lipids Prenol Lipids Sesquiterpenes Organic Phosphonic Acids Polyamines Enolates Carboxylic Acid Amides phosphonic acid derivative phosphonic acid carboxamide group carboxylic acid derivative polyamine enolate amine organonitrogen compound logP 2.79 ALOGPS logS -4.9 ALOGPS Water Solubility 4.40e-03 g/l ALOGPS logP 2.61 ChemAxon IUPAC Name [({[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy}carbamoyl)methyl]phosphonic acid ChemAxon Traditional IUPAC Name ({[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy}carbamoyl)methylphosphonic acid ChemAxon Molecular Weight 359.3976 ChemAxon Monoisotopic Weight 359.186159587 ChemAxon SMILES CC(C)=CCC\C(C)=C\CC\C(C)=C\CONC(=O)CP(O)(O)=O ChemAxon Molecular Formula C17H30NO5P ChemAxon InChI InChI=1S/C17H30NO5P/c1-14(2)7-5-8-15(3)9-6-10-16(4)11-12-23-18-17(19)13-24(20,21)22/h7,9,11H,5-6,8,10,12-13H2,1-4H3,(H,18,19)(H2,20,21,22)/b15-9+,16-11+ ChemAxon InChIKey InChIKey=JAOBYUCYSAOLHS-XGGJEREUSA-N ChemAxon Polar Surface Area (PSA) 95.86 ChemAxon Refractivity 98.43 ChemAxon Polarizability 39.39 ChemAxon Rotatable Bond Count 11 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 1.66 ChemAxon pKa (strongest basic) -4.6 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 445015 PubChem Substance 99444242 ChemSpider 392777 PDB FII BE0004071 GTPase KRas 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 GTPase KRas Involved in GTP binding Ras proteins bind GDP/GTP and possess intrinsic GTPase activity KRAS 12p12.1 Cell membrane None 6.76 21655.7 Human HUGO Gene Nomenclature Committee (HGNC) GNC:6407 GeneCards KRAS GenBank Gene Database M54968 GenBank Protein Database 186764 UniProtKB P01116 UniProt Accession RASK_HUMAN c-K-ras c-Ki-ras GTPase KRas, N-terminally processed K-Ras 2 Ki-Ras >GTPase KRas MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG QEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDL PSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGC VKIKKCIIM >567 bp ATGACTGAATATAAACTTGTGGTAGTTGGAGCTTGTGGCGTAGGCAAGAGTGCCTTGACG ATACAGCTAATTCAGAATCATTTTGTGGACGAATATGATCCAACAATAGAGGATTCCTAC AGGAAGCAAGTAGTAATTGATGGAGAAACCTGTCTCTTGGATATTCTCGACACAGCAGGT CAAGAGGAGTACAGTGCAATGAGGGACCAGTACATGAGGACTGGGGAGGGCTTTCTTTGT GTATTTGCCATAAATAATACTAAATCATTTGAAGATATTCACCATTATAGAGAACAAATT AAAAGAGTTAAGGACTCTGAAGATGTACCTATGGTCCTAGTAGGAAATAAATGTGATTTG CCTTCTAGAACAGTAGACACAAAACAGGCTCAGGACTTAGCAAGAAGTTATGGAATTCCT TTTATTGAAACATCAGCAAAGACAAGACAGGGTGTTGATGATGCCTTCTATACATTAGTT CGAGAAATTCGAAAACATAAAGAAAAGATGAGCAAAGATGGTAAAAAGAAGAAAAAGAAG TCAAAGACAAAGTGTGTAATTATGTAA PF00071 Ras function nucleotide binding function purine nucleotide binding function guanyl nucleotide binding function GTP binding function binding process cellular process process cell communication process signal transduction process intracellular signaling cascade process small GTPase mediated signal transduction BE0002373 Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha 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 Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Involved in protein prenyltransferase activity Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate FNTA 8p11 None 4.72 44409.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3782 GenAtlas FNTA GeneCards FNTA GenBank Gene Database L10413 UniProtKB P49354 UniProt Accession FNTA_HUMAN CAAX farnesyltransferase alpha subunit EC 2.5.1.58 EC 2.5.1.59 FTase-alpha GGTase-I-alpha Ras proteins prenyltransferase alpha Type I protein geranyl-geranyltransferase alpha subunit >Protein farnesyltransferase/geranylgeranyltransferase type I alpha subunit MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDS PSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLT RDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLR DPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQR YFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLL DLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIG RSLQSKHSTENDSPTNVQQ >1140 bp ATGGCGGCCACCGAGGGGGTCGGGGAGGCTGCGCAAGGGGGCGAGCCCGGGCAGCCGGCG CAACCCCCGCCCCAGCCGCACCCACCGCCGCCCCAGCAGCAGCACAAGGAAGAGATGGCG GCCGAGGCTGGGGAAGCCGTGGCGTCCCCCATGGACGACGGGTTTGTGAGCCTGGACTCG CCCTCCTATGTCCTGTACAGGGACAGAGCAGAATGGGCTGATATAGATCCGGTGCCGCAG AATGATGGCCCCAATCCCGTGGTCCAGATCATTTATAGTGACAAATTTAGAGATGTTTAT GATTACTTCCGAGCTGTCCTGCAGCGTGATGAAAGAAGTGAACGAGCTTTTAAGCTAACC CGGGATGCTATTGAGTTAAATGCAGCCAATTATACAGTGTGGCATTTCCGGAGAGTTCTT TTGAAGTCACTTCAGAAGGATCTACATGAGGAAATGAACTACATCACTGCAATAATTGAG GAGCAGCCCAAAAACTATCAAGTTTGGCATCATAGGCGAGTATTAGTGGAATGGCTAAGA GATCCATCTCAGGAGCTTGAATTTATTGCTGATATTCTTAATCAGGATGCAAAGAATTAT CATGCCTGGCAGCATCGACAATGGGTTATTCAGGAATTTAAACTTTGGGATAATGAGCTG CAGTATGTGGACCAACTTCTGAAAGAGGATGTGAGAAATAACTCTGTCTGGAACCAAAGA TACTTCGTTATTTCTAACACCACTGGCTACAATGATCGTGCTGTATTGGAGAGAGAAGTC CAATACACTCTGGAAATGATTAAACTAGTACCACATAATGAAAGTGCATGGAACTATTTG AAAGGGATTTTGCAGGATCGTGGTCTTTCCAAATATCCTAATCTGTTAAATCAATTACTT GATTTACAACCAAGTCATAGTTCCCCCTACCTAATTGCCTTTCTTGTGGATATCTATGAA GACATGCTAGAAAATCAGTGTGACAATAAGGAAGACATTCTTAATAAAGCATTAGAGTTA TGTGAAATCCTAGCTAAAGAAAAGGACACTATAAGAAAGGAATATTGGAGATACATTGGA AGATCCCTTCAAAGCAAACACAGCACAGAAAATGACTCACCAACAAATGTACAGCAATAA PF01239 PPTA function transferase activity function transferase activity, transferring alkyl or aryl (other than methyl) groups function prenyltransferase activity function protein prenyltransferase activity function catalytic activity process biopolymer modification process protein modification process protein amino acid lipidation process physiological process process protein prenylation process metabolism process protein amino acid prenylation process macromolecule metabolism process biopolymer metabolism BE0002372 Protein farnesyltransferase subunit beta 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 Protein farnesyltransferase subunit beta Involved in catalytic activity Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding FNTB 14q23-q24 None 5.67 48774.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3785 GenAtlas FNTB GeneCards FNTB GenBank Gene Database L00635 UniProtKB P49356 UniProt Accession FNTB_HUMAN CAAX farnesyltransferase subunit beta EC 2.5.1.58 FTase-beta RAS proteins prenyltransferase beta >Protein farnesyltransferase subunit beta MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFS SYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQ IVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQY LYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIG GVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCY SFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDF YHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPV PGFEELKDETSAEPATD >1314 bp ATGGCTTCTCCGAGTTCTTTCACCTACTATTGCCCTCCATCTTCCTCCCCCGTCTGGTCA GAGCCGCTGTACAGTCTGAGGCCCGAGCACGCGCGAGAGCGGTTGCAGGACGACTCGGTG GAAACAGTCACGTCCATAGAACAGGCAAAAGTAGAAGAAAAGATCCAAGAGGTCTTCAGT TCTTACAAGTTCAACCACCTTGTACCAAGGCTTGTTTTGCAGAGGGAGAAGCACTTCCAT TATCTGAAAAGAGGCCTTCGACAACTGACAGATGCCTATGAGTGTCTGGATGCCAGCCGC CCATGGCTCTGCTATTGGATCCTGCACAGCTTGGAACTGCTAGATGAACCCATCCCCCAG ATAGTGGCTACAGATGTGTGTCAGTTCCTGGAGCTGTGTCAGAGCCCAGAAGGTGGCTTT GGAGGAGGACCCGGTCAGTATCCACACCTTGCACCCACATATGCAGCAGTCAATGCATTG TGCATCATTGGCACCGAGGAGGCCTATGACATCATTAACAGAGAGAAGCTTCTTCAGTAT TTGTACTCCCTGAAGCAACCTGACGGCTCCTTTCTCATGCATGTCGGAGGTGAGGTGGAT GTGAGAAGCGCATACTGTGCTGCCTCCGTAGCCTCGCTGACCAACATCATCACTCCAGAC CTCTTTGAGGGCACTGCTGAATGGATAGCAAGGTGTCAGAACTGGGAAGGTGGCATTGGC GGGGTACCAGGGATGGAAGCCCATGGTGGCTATACCTTCTGTGGCCTGGCCGCGCTGGTA ATCCTCAAGAGGGAACGTTCCTTGAACTTGAAGAGCTTATTACAATGGGTGACAAGCCGG CAGATGCGATTTGAAGGAGGATTTCAGGGCCGCTGCAACAAGCTGGTGGATGGCTGCTAC TCCTTCTGGCAGGCGGGGCTCCTGCCCCTGCTCCACCGCGCACTGCACGCCCAAGGTGAC CCTGCCCTTAGCATGAGCCACTGGATGTTCCATCAGCAGGCCCTGCAGGAGTACATCCTG ATGTGCTGCCAGTGCCCTGCGGGGGGGCTTCTGGATAAACCTGGCAAGTCGCGTGATTTC TACCACACCTGCTACTGCCTGAGCGGCCTGTCCATAGCCCAGCACTTCGGCAGCGGAGCC ATGTTGCATGATGTGGTCCTGGGTGTGCCCGAAAACGCTCTGCAGCCCACTCACCCAGTG TACAACATTGGACCAGACAAGGTGATCCAGGCCACTACATACTTTCTACAGAAGCCAGTC CCAGGTTTTGAGGAGCTTAAGGATGAGACATCGGCAGAGCCTGCAACCGACTAG PF00432 Prenyltrans function catalytic activity "
rdf:type	drugbank:drugs
rdfs:label	"[(3,7,11-TRIMETHYL-DODECA-2,6,10-TRIENYLOXYCARBAMOYL)-METHYL]-PHOSPHONIC ACID"

All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines3/drugbank_small.nt

The resource does not appear as an object

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