Nanopublications

Matches in Nanopublications for { ?s ?p ?o <http://www.tkuhn.ch/bel2nanopub/RA_AsV-UUbw9P833a-cnQsaOHjDOCoCBbZCOGH66NeUJs#provenance>. }

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_4 label "Selventa" provenance.
large_corpus.bel title "BEL Framework Large Corpus Document" provenance.
large_corpus.bel description "Approximately 61,000 statements." provenance.
large_corpus.bel version "1.4" provenance.
large_corpus.bel authoredBy _4 provenance.
assertion wasDerivedFrom large_corpus.bel provenance.
assertion wasDerivedFrom _3 provenance.
assertion hadPrimarySource 16987807 provenance.
_3 wasQuotedFrom 16987807 provenance.
_3 value "This is suggested to be relevant for neuronal differentiation. Finally it should be noted that phosphopeptide mapping has revealed additional phosphorylation sites in MYC (37). These include Ser-71, Ser-82, Ser-162 or -164, Ser-293, and possibly Ser-343/344. With the exception of Ser-162 and Ser-343, all other sites contain a Pro at thekappa1 position and are thus potential substrates for Pro-directed kinases. At present kinases possibly involved in modifying these phosphorylation sites and their functional relevance have not been defined. Phosphorylation of N-terminal Sites Regulates MYC-dependent Gene Transcription Because of the location of the phosphorylation sites at Thr-58 and Ser-62 within the TAD, it was speculated early on that these sites are involved in the regulation of gene transcription. However, these findings have been controversial (2). Although the differences between the published studies could not be clarified, the recent findings connecting these phosphorylation sites to protein turnover indicate that distinct effects might have been mingled, potentially explaining the inconclusive results. More recently this discussion has been revived. It has been suggested that Ser-62 phosphorylation modulates gene expression (26). In response to oxidative stress Ser-62 becomes phosphorylated, which correlates with increased recruitment of MYC to specific promoters but not with stabilization." provenance.