p(HGNC:MAPT, pmod(Ph, Ser, 202)) positiveCorrelation a(CHEBI:"okadaic acid")

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PubMed:16464864

Both brain proteins were preferentially modified by SUMO1, as compared with SUMO2 or SUMO3. Tau contains two SUMO consensus sequences with Lys(340) as the major sumoylation site. Although both tau and alpha-synuclein are targets for proteasomal degradation, only tau sumoylation was affected by inhibitors of the proteasome pathway. Treatment with the phosphatase inhibitor, okadaic acid, or the microtubule depolymerizing drug, colchicine, up-regulated tau sumoylation.

Related Edges 7

• a(CHEBI:"okadaic acid") increases p(HGNC:MAPT, pmod(Sumo, Lys, 340))
• a(CHEBI:"okadaic acid") positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 202))
• a(CHEBI:colchicine) increases p(HGNC:MAPT, pmod(Sumo, Lys, 340))
• p(HGNC:SUMO1) increases p(HGNC:MAPT, pmod(Sumo, Lys, 340))
• p(HGNC:SUMO1) increases p(HGNC:SNCA, pmod(Sumo))
• p(HGNC:MAPT, pmod(Ph, Ser, 202)) positiveCorrelation p(HGNC:MAPT, pmod(Sumo, Lys, 340))
• p(HGNC:MAPT, pmod(Sumo, Lys, 340)) positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 202))

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