Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB06905"
Predicate | Value (sorted: default) |
---|---|
rdfs:label |
"(2S,3S,4E,6E,8S,9S)-3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldeca-4,6-dienoic acid"
|
rdf:type | |
drugbank:description |
"
experimental
This compound belongs to the beta amino acids and derivatives. These are amino acids having a (-NH2) group attached to the beta carbon atom.
Beta Amino Acids and Derivatives
Organic Compounds
Organic Acids and Derivatives
Carboxylic Acids and Derivatives
Amino Acids, Peptides, and Analogues
Carbocyclic Fatty Acids
Amino Fatty Acids
Branched Fatty Acids
Benzene and Substituted Derivatives
Unsaturated Fatty Acids
Carboxylic Acids
Enolates
Ethers
Polyamines
Monoalkylamines
Alcohols and Polyols
benzene
enolate
ether
polyamine
carboxylic acid
primary amine
amine
primary aliphatic amine
alcohol
organonitrogen compound
logP
0.71
ALOGPS
logS
-4.6
ALOGPS
Water Solubility
8.13e-03 g/l
ALOGPS
logP
1.41
ChemAxon
IUPAC Name
(2S,3S,4E,6E,8S,9S)-3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldeca-4,6-dienoic acid
ChemAxon
Traditional IUPAC Name
(2S,3S,4E,6E,8S,9S)-3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldeca-4,6-dienoic acid
ChemAxon
Molecular Weight
331.4492
ChemAxon
Monoisotopic Weight
331.214743799
ChemAxon
SMILES
[H][C@](C)(\C=C(/C)\C=C\[C@]([H])(N)[C@]([H])(C)C(O)=O)[C@]([H])(CC1=CC=CC=C1)OC
ChemAxon
Molecular Formula
C20H29NO3
ChemAxon
InChI
InChI=1S/C20H29NO3/c1-14(10-11-18(21)16(3)20(22)23)12-15(2)19(24-4)13-17-8-6-5-7-9-17/h5-12,15-16,18-19H,13,21H2,1-4H3,(H,22,23)/b11-10+,14-12+/t15-,16-,18-,19-/m0/s1
ChemAxon
InChIKey
InChIKey=HJVCHYDYCYBBQX-HLTLHRPFSA-N
ChemAxon
Polar Surface Area (PSA)
72.55
ChemAxon
Refractivity
99.17
ChemAxon
Polarizability
38.17
ChemAxon
Rotatable Bond Count
9
ChemAxon
H Bond Acceptor Count
4
ChemAxon
H Bond Donor Count
2
ChemAxon
pKa (strongest acidic)
4.01
ChemAxon
pKa (strongest basic)
10.01
ChemAxon
Physiological Charge
0
ChemAxon
Number of Rings
1
ChemAxon
Bioavailability
1
ChemAxon
Rule of Five
true
ChemAxon
Ghose Filter
true
ChemAxon
PubChem Compound
14205264
PubChem Substance
99443376
ChemSpider
20137047
PDB
1ZN
BE0003749
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
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
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
Involved in protein binding
The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment
PPP2R5C
14q32.31
Nucleus
None
6.87
61060.2
Human
HUGO Gene Nomenclature Committee (HGNC)
GNC:9311
GeneCards
PPP2R5C
GenBank Gene Database
U37352
GenBank Protein Database
1203812
UniProtKB
Q13362
UniProt Accession
2A5G_HUMAN
PP2A, B subunit, B' gamma isoform
PP2A, B subunit, B56 gamma isoform
PP2A, B subunit, PR61 gamma isoform
PP2A, B subunit, R5 gamma isoform
Renal carcinoma antigen NY-REN-29
>Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
MLTCNKAGSRMVVDAANSNGPFQPVVLLHIRDVPPADQEKLFIQKLRQCCVLFDFVSDPL
SDLKWKEVKRAALSEMVEYITHNRNVITEPIYPEVVHMFAVNMFRTLPPSSNPTGAEFDP
EEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKKYIDQKFVLQLLELFDSEDPRERD
FLKTTLHRIYGKFLGLRAYIRKQINNIFYRFIYETEHHNGIAELLEILGSIINGFALPLK
EEHKIFLLKVLLPLHKVKSLSVYHPQLAYCVVQFLEKDSTLTEPVVMALLKYWPKTHSPK
EVMFLNELEEILDVIEPSEFVKIMEPLFRQLAKCVSSPHFQVAERALYYWNNEYIMSLIS
DNAAKILPIMFPSLYRNSKTHWNKTIHGLIYNALKLFMEMNQKLFDDCTQQFKAEKLKEK
LKMKEREEAWVKIENLAKANPQYTVYSQASTMSIPVAMETDGPLFEDVQMLRKTVKDEAH
QAQKDPKKDRPLARRKSELPQDPHTKKALEAHCRADELASQDGR
>1545 bp
ATGGTGGTGGATGCGGCCAACTCCAATGGGCCTTTCCAGCCCGTGGTCCTTCTCCATATT
CGAGATGTTCCTCCTGCTGATCAAGAGAAGCTTTTTATCCAGAAGTTACGTCAGTGTTGC
GTCCTCTTTGACTTTGTTTCTGATCCACTAAGTGACCTAAAGTGGAAGGAAGTAAAACGA
GCTGCTTTAAGTGAAATGGTAGAATATATCACCCATAATCGGAATGTGATCACAGAGCCT
ATTTACCCAGAAGTAGTCCATATGTTTGCAGTTAACATGTTTCGAACATTACCACCTTCC
TCCAATCCTACGGGAGCGGAATTTGACCCGGAGGAAGATGAACCAACGTTAGAAGCAGCC
TGGCCTCATCTACAGCTTGTTTATGAATTTTTCTTAAGATTTTTAGAGTCTCCAGATTTC
CAACCTAATATAGCGAAGAAATATATTGATCAGAAGTTTGTATTGCAGCTTTTAGAGCTC
TTTGACAGTGAAGATCCTCGGGAGAGAGATTTTCTTAAAACCACCCTTCACAGAATCTAT
GGGAAATTCCTAGGCTTGAGAGCTTACATCAGAAAACAGATAAATAATATATTTTATAGG
TTTATTTATGAAACAGAGCATCATAATGGCATAGCAGAGTTACTGGAAATATTGGGAAGT
ATAATTAATGGATTTGCCTTACCACTAAAAGAAGAGCACAAGATTTTCTTATTGAAGGTG
TTACTACCTTTGCACAAAGTGAAATCTCTGAGTGTCTACCATCCCCAGCTGGCATACTGT
GTAGTGCAGTTTTTAGAAAAGGACAGCACCCTCACGGAACCAGTGGTGATGGCACTTCTC
AAATACTGGCCAAAGACTCACAGTCCAAAAGAAGTAATGTTCTTAAACGAATTAGAAGAG
ATTTTAGATGTCATTGAACCATCAGAATTTGTGAAGATCATGGAACCCCTCTTCCGGCAG
TTGGCCAAATGTGTCTCCAGCCCACACTTCCAGGTGGCAGAGCGAGCTCTCTATTACTGG
AATAATGAATACATCATGAGTTTAATCAGTGACAACGCAGCGAAGATTCTGCCCATCATG
TTTCCTTCCTTGTACCGCAACTCAAAGACCCATTGGAACAAGACAATACATGGCTTGATA
TACAACGCCCTGAAGCTCTTCATGGAGATGAACCAAAAGCTATTTGATGACTGTACACAA
CAGTTCAAAGCAGAGAAACTAAAAGAGAAGCTAAAAATGAAAGAACGGGAAGAAGCATGG
GTTAAAATAGAAAATCTAGCCAAAGCCAATCCCCAGTACACAGTGTATAGTCAAGCCAGC
ACCATGAGCATTCCGGTTGCAATGGAGACAGATGGGCCTTTATTTGAAGATGTGCAGATG
CTGAGAAAGACAGTGAAGGACGAGGCTCATCAGGCACAGAAAGATCCGAAGAAGGACCGT
CCTCTTGCACTCCGCAAGTCCGAGCTGCCTCAGGACCCCCACACCAAGAAAGCCTTGGAA
GCTCACTGCAGGGCCGATGAGCTGGCCTCCCAGGACGGCCGCTAG
PF01603
B56
component
protein serine/threonine phosphatase complex
component
protein phosphatase type 2A complex
component
protein complex
component
unlocalized protein complex
function
protein phosphatase regulator activity
function
protein phosphatase type 2A regulator activity
function
enzyme regulator activity
function
phosphatase regulator activity
process
cellular process
process
cell communication
process
signal transduction
BE0002326
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
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
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
Signal transduction mechanisms
PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Can dephosphorylate SV40 large T antigen and p53. Dephosphorylates SV40 large T antigen, preferentially on serine residues 120, 123, 677, and perhaps 679. The C subunit was most active, followed by the AC form, which was more active than the ABC form, and activity of all three forms was strongly stimulated by manganese, and to a lesser extent by magnesium. Dephosphorylation by the AC form, but not C or ABC form is inhibited by small T antigen
PPP2CA
5q31.1
Cytoplasm
None
5.22
35595.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:9299
GenAtlas
PPP2CA
GeneCards
PPP2CA
GenBank Gene Database
X12646
GenBank Protein Database
36120
UniProtKB
P67775
UniProt Accession
PP2AA_HUMAN
EC 3.1.3.16
PP2A-alpha
Replication protein C
RP-C
>Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHG
QFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHES
RQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHI
RALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRA
HQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHV
TRRTPDYFL
>930 bp
ATGGACGAGAAGGTGTTCACCAAGGAGCTGGACCAGTGGATCGAGCAGCTGAACGAGTGC
AAGCAGCTGTCCGAGTCCCAGGTCAAGAGCCTCTGCGAGAAGGCTAAAGAAATCCTGACA
AAAGAATCCAACGTGCAAGAGGTTCGATGTCCAGTTACTGTCTGTGGAGATGTGCATGGG
CAATTTCATGATCTCATGGAACTGTTTAGAATTGGTGGCAAATCACCAGATACAAATTAC
TTGTTTATGGGAGATTATGTTGACAGAGGATATTATTCAGTTGAAACAGTTACACTGCTT
GTAGCTCTTAAGGTTCGTTACCGTGAACGCATCACCATTCTTCGAGGGAATCATGAGAGC
AGACAGATCACACAAGTTTATGGTTTCTATGATGAATGTTTAAGAAAATATGGAAATGCA
AATGTTTGGAAATATTTTACAGATCTTTTTGACTATCTTCCTCTCACTGCCTTGGTGGAT
GGGCAGATCTTCTGTCTACATGGTGGTCTCTCGCCATCTATAGATACACTGGATCATATC
AGAGCACTTGATCGCCTACAAGAAGTTCCCCATGAGGGTCCAATGTGTGACTTGCTGTGG
TCAGATCCAGATGACCGTGGTGGTTGGGGTATATCTCCTCGAGGAGCTGGTTACACCTTT
GGGCAAGATATTTCTGAGACATTTAATCATGCCAATGGCCTCACGTTGGTGTCTAGAGCT
CACCAGCTAGTGATGGAGGGATATAACTGGTGCCATGACCGGAATGTAGTAACGATTTTC
AGTGCTCCAAACTATTGTTATCGTTGTGGTAACCAAGCTGCAATCATGGAACTTGACGAT
ACTCTAAAATACTCTTTCTTGCAGTTTGACCCAGCACCTCGTAGAGGCGAGCCACATGTT
ACTCGTCGTACCCCAGACTACTTCCTGTAA
PF00149
Metallophos
function
catalytic activity
function
hydrolase activity
BE0003750
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
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
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Involved in antigen binding
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit
PPP2R1A
19q13.41
None
4.75
65307.8
Human
HUGO Gene Nomenclature Committee (HGNC)
GNC:9302
GeneCards
PPP2R1A
GenBank Gene Database
M31786
GenBank Protein Database
178663
UniProtKB
P30153
UniProt Accession
2AAA_HUMAN
Medium tumor antigen-associated 61 kDa protein
PP2A, subunit A, PR65-alpha isoform
PP2A, subunit A, R1-alpha isoform
>Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIY
DEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHS
PSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPM
VRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDL
EALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRA
AASHKVKEFCENLSADCRENVIMSQILPCIKELVSDANQHVKSALASVIMGLSPILGKDN
TIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVR
LAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHA
TIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNV
AKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA
PF02985
HEAT
function
binding
"
|
All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines3/drugbank_small.nt
The resource does not appear as an object