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PredicateValue (sorted: default)
rdfs:label
"2,6,8-Trimethyl-3-Amino-9-Benzyl-9-Methoxynonanoic Acid"
rdf:type
ns1:drugs
ns1: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 Branched Fatty Acids Amino Fatty Acids Benzene and Substituted Derivatives Enolates Ethers Polyamines Carboxylic Acids Monoalkylamines Alcohols and Polyols benzene enolate ether polyamine carboxylic acid primary amine amine primary aliphatic amine alcohol organonitrogen compound logP 1.32 ALOGPS logS -4.9 ALOGPS Water Solubility 4.20e-03 g/l ALOGPS logP 2.02 ChemAxon IUPAC Name (2S,3S,6R,8S,9S)-3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldecanoic acid ChemAxon Traditional IUPAC Name (2S,3S,6R,8S,9S)-3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldecanoic acid ChemAxon Molecular Weight 335.4809 ChemAxon Monoisotopic Weight 335.246043927 ChemAxon SMILES [H][C@@](C)(CC[C@]([H])(N)[C@]([H])(C)C(O)=O)C[C@]([H])(C)[C@]([H])(CC1=CC=CC=C1)OC ChemAxon Molecular Formula C20H33NO3 ChemAxon InChI InChI=1S/C20H33NO3/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/h5-9,14-16,18-19H,10-13,21H2,1-4H3,(H,22,23)/t14-,15+,16+,18+,19+/m1/s1 ChemAxon InChIKey InChIKey=SWTFXINHZPXNOX-DZBHQSCQSA-N ChemAxon Polar Surface Area (PSA) 72.55 ChemAxon Refractivity 97.36 ChemAxon Polarizability 39.68 ChemAxon Rotatable Bond Count 11 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 4.1 ChemAxon pKa (strongest basic) 10.59 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 17753820 PubChem Substance 46508526 ChemSpider 16743816 PDB ADD BE0003810 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit 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 PP1-alpha catalytic subunit Signal transduction mechanisms Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II PPP1CA 11q13 Cytoplasm (By similarity) None 6.25 37511.7 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9281 GeneCards PPP1CA GenBank Gene Database X70848 GenBank Protein Database 35451 UniProtKB P62136 UniProt Accession PP1A_HUMAN PP-1A >Serine/threonine-protein phosphatase PP1-alpha catalytic subunit MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLK ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHD LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD KNKGKYGQFSGLNPGGRPITPPRNSAKAKK >993 bp ATGTCCGACAGCGAGAAGCTCAACCTGGACTCGATCATCGGGCGCCTGCTGGAAGTGCAG GGCTCGCGGCCTGGCAAGAATGTACAGCTGACAGAGAACGAGATCCGCGGTCTGTGCCTG AAATCCCGGGAGATTTTTCTGAGCCAGCCCATTCTTCTGGAGCTGGAGGCACCCCTCAAG ATCTGCGGTGACATACACGGCCAGTACTACGACCTTCTGCGACTATTTGAGTATGGCGGT TTCCCTCCCGAGAGCAACTACCTCTTTCTGGGGGACTATGTGGACAGGGGCAAGCAGTCC TTGGAGACCATCTGCCTGCTGCTGGCCTATAAGATCAAGTACCCCGAGAACTTCTTCCTG CTCCGTGGGAACCACGAGTGTGCCAGCATCAACCGCATCTATGGTTTCTACGATGAGTGC AAGAGACGCTACAACATCAAACTGTGGAAAACCTTCACTGACTGCTTCAACTGCCTGCCC ATCGCGGCCATAGTGGACGAAAAGATCTTCTGCTGCCACGGAGGCCTGTCCCCGGACCTG CAGTCTATGGAGCAGATTCGGCGGATCATGCGGCCCACAGATGTGCCTGACCAGGGCCTG CTGTGTGACCTGCTGTGGTCTGACCCTGACAAGGACGTGCAGGGCTGGGGCGAGAACGAC CGTGGCGTCTCTTTTACCTTTGGAGCCGAGGTGGTGGCCAAGTTCCTCCACAAGCACGAC TTGGACCTCATCTGCCGAGCACACCAGGTGGTAGAAGACGGCTACGAGTTCTTTGCCAAG CGGCAGCTGGTGACACTTTTCTCAGCTCCCAACTACTGTGGCGAGTTTGACAATGCTGGC GCCATGATGAGTGTGGACGAGACCCTCATGTGCTCTTTCCAGATCCTCAAGCCCGCCGAC AAGAACAAGGGGAAGTACGGGCAGTTCAGTGGCCTGAACCCTGGAGGCCGACCCATCACC CCACCCCGCAATTCCGCCAAAGCCAAGAAATAG 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 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 hydrolase activity function catalytic activity 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 enzyme regulator activity function phosphatase regulator activity function protein phosphatase regulator activity function protein phosphatase type 2A regulator activity process cellular process process cell communication process signal transduction BE0003811 Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B 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 55 kDa regulatory subunit B alpha 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 PPP2R2A 8p21.2 None 6.11 51691.6 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9304 GeneCards PPP2R2A GenBank Gene Database M64929 GenBank Protein Database 190422 UniProtKB P63151 UniProt Accession 2ABA_HUMAN PP2A, subunit B, B-alpha isoform PP2A, subunit B, B55-alpha isoform PP2A, subunit B, PR55-alpha isoform PP2A, subunit B, R2-alpha isoform >Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform MAGAGGGNDIQWCFSQVKGAVDDDVAEADIISTVEFNHSGELLATGDKGGRVVIFQQEQE NKIQSHSRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQKNAAQFLLSTNDKTIK LWKISERDKRPEGYNLKEEDGRYRDPTTVTTLRVPVFRPMDLMVEASPRRIFANAHTYHI NSISINSDYETYLSADDLRINLWHLEITDRSFNIVDIKPANMEELTEVITAAEFHPNSCN TFVYSSSKGTIRLCDMRASALCDRHSKLFEEPEDPSNRSFFSEIISSISDVKFSHSGRYM MTRDYLSVKIWDLNMENRPVETYQVHEYLRSKLCSLYENDCIFDKFECCWNGSDSVVMTG SYNNFFRMFDRNTKRDITLEASRENNKPRTVLKPRKVCASGKRKKDEISVDSLDFNKKIL HTAWHPKENIIAVATTNNLYIFQDKVN >1344 bp ATGGCAGGAGCTGGAGGAGGGAATGATATTCAGTGGTGTTTTTCTCAGGTGAAAGGAGCA GTAGATGATGATGTAGCAGAAGCAGATATAATTTCTACAGTAGAATTTAATCATTCTGGA GAATTACTAGCAACAGGAGATAAAGGTGGTAGAGTTGTCATCTTTCAACAGGAGCAGGAG AACAAAATCCAGTCTCATAGCAGAGGAGAATATAATGTTTACAGCACCTTCCAGAGCCAT GAACCAGAGTTTGACTACTTGAAAAGTTTAGAAATAGAAGAAAAGATCAATAAAATTAGG TGGTTACCCCAGAAAAATGCTGCTCAGTTTTTATTGTCTACCAATGATAAAACAATAAAA TTATGGAAAATCAGTGAAAGGGACAAAAGACCAGAAGGGTATAACTTGAAAGAGGAGGAT GGAAGGTATAGAGATCCTACTACAGTTACTACACTACGAGTGCCAGTCTTTAGGCCTATG GATCTAATGGTTGAGGCCAGTCCACGAAGAATATTTGCCAATGCTCATACATATCACATC AACTCAATTTCTATTAATAGTGATTATGAAACATATTTATCTGCAGATGATTTGCGGATT AATCTTTGGCATCTGGAAATTACAGACAGGAGTTTTAACATTGTGGATATCAAGCCTGCC AATATGGAAGAGCTAACAGAGGTGATTACAGCAGCAGAATTTCATCCAAACAGCTGTAAC ACATTTGTATACAGCAGCAGTAAAGGAACTATTCGGCTATGTGACATGAGGGCATCTGCC CTCTGTGATAGACATTCTAAATTGTTTGAAGAACCTGAAGATCCCAGTAACAGGTCATTT TTTTCCGAAATCATCTCCTCTATTTCGGATGTAAAATTCAGCCATAGTGGTCGATATATG ATGACTAGAGACTATTTGTCAGTCAAAATTTGGGACTTAAATATGGAAAACAGGCCTGTG GAAACATACCAGGTGCATGAATACCTCAGAAGTAAACTCTGTTCACTGTATGAAAATGAC TGCATATTTGACAAATTTGAATGTTGTTGGAATGGATCTGACAGTGTTGTCATGACTGGA TCTTACAATAATTTCTTCAGAATGTTTGACAGAAACACAAAGCGAGACATAACCCTAGAA GCATCGCGGGAAAACAATAAGCCTCGCACAGTTCTGAAGCCTCGCAAAGTCTGTGCAAGT GGCAAGCGAAAGAAAGATGAAATAAGTGTTGACAGCCTAGACTTCAATAAGAAAATCCTT CACACAGCCTGGCACCCCAAGGAAAATATCATTGCCGTAGCTACTACAAACAATCTGTAT ATATTTCAAGACAAAGTGAATTAG PF10586 PP2A_B_N PF10594 PP2A_B_subs_rcg component unlocalized protein complex component protein serine/threonine phosphatase complex component protein phosphatase type 2A complex component protein complex function enzyme regulator activity function phosphatase regulator activity function protein phosphatase regulator activity function protein phosphatase type 2A regulator activity process cell communication process signal transduction process cellular process "
owl:sameAs
?:EXPT00428

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