IndraLab

Statements


SMYD2 methylates TP53 on K370. 24 / 24
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reach
"Smyd2 monomethylates p53 at lysine 370 [XREF_BIBR]."

reach
"KMT3C, a member of the Smyd (SET and MYND domain) subfamily of SET domain containing proteins, mono-methylates p53 at K370."

sparser
"It has been reported that the methyltransferase SMYD2 could methylate p53 at K370 in cancer cells xref ."

reach
"P53 is methylated at K370 by Smyd2, K372 by Set 7/9, and K382 by Set8 (ref."

sparser
"SMYD2 mono-methylates p53 on lysine K370 (p53K370me1), xref , xref while SET7 monomethylates p53 on lysine K372 (p53K372me1) xref in the regulatory domain."

No evidence text available

reach
"SMYD2 monomethylates Lys-370 of p53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53."

sparser
"For instance, methylation of p53 on K370 by SMYD2 [ xref ] or on K382 by SETD8 [ xref ] results in transcriptional repression, whereas methylation at K372 by SET7/9 leads to activation of transcription [ xref ]."

reach
"In this regard, it has been reported that SMYD2 can methylate p53 on Lys 370 and that this methylation leads to repression of its activity."

sparser
"However, the methylation at p53-K372 by KMT5 prevents the methylation at p53-K370 by KMT3C ( xref )."

reach
"It has been reported that the methyltransferase SMYD2 could methylate p53 at K370 in cancer cells ."

reach
"SMYD2 mono-methylates p53 on lysine K370 (p53K370me1), XREF_BIBR, XREF_BIBR while SET7 monomethylates p53 on lysine K372 (p53K372me1) XREF_BIBR in the regulatory domain."

reach
"Here we report that SMYD2 prefers to methylate p53 Lys 370 over histone substrates in vitro."

sparser
"P53 is methylated by SMYD2 on lysine 370 (K370me1/me2); this modification is required for its association with the co-activator p53 Binding Protein 1 (53BP1) [ xref , xref ]."

reach
"It has been reported that SMYD2 monomethylates p53 at Lys370, which led to p53 inactivation by decreasing the binding activity of p53 to its target genes[22]."

sparser
"Conversely, methylation on K370 of human p53 by Smyd2 was shown to inhibit p53 activity ( Huang et al., 2006 )."

reach
"P53 is methylated at K370 by Smyd2 (Set and MYND Domain-2), K372 by Set 7/9 (Su (var) 3-9 and " Enhancer of zeste " protein 7/9), and K382 by Set8 (Su (var) 3-9 and " Enhancer of zeste " protein 8) [XREF_BIBR, XREF_BIBR, XREF_BIBR, XREF_BIBR, XREF_BIBR]."

sparser
"P53 is methylated at K370 by Smyd2, K372 by Set 7/9, and K382 by Set8 (ref. xref – xref )."

sparser
"P53 is methylated at K370 by Smyd2 (Set/MYND Domain-2), K372 by Set 7/9 (Su(var)3-9 and “Enhancer of zeste” protein 7/9), and K382 by Set8 (Su(var)3-9 and “Enhancer of zeste” protein 8) [ xref , xref , xref , xref , xref ]."

sparser
"It is thought that mono-methylation by SMYD2 of lysine Lys 370 on p53 creates a steric blockage that impedes p53 from binding its target gene promoters, and knockdown of SMYD2 prevents DNA damage-induced, p53-dependent apoptosis ( xref )."

reach
"LLY-507 Inhibits SMYD2 mediated Methylation of p53 Lys 370 in Cells."

sparser
"In this regard, it has been reported that SMYD2 can methylate p53 on Lys 370 and that this methylation leads to repression of its activity. xref As p21 is also a key mediator of p53-dependent cell cycle arrest, SMYD2-mediated p53 methylation and inactivation may decrease expression of p21 expression, thereby increasing activation of CDK4 and CDK6 and expression of cyclinD1, promoting cell cycle progression."

No evidence text available

sparser
"Although methylation by Smyd2 at p53 site K370 results in an inhibitory effect of p53 activity, dimethylation at this same site promotes the interaction of 53BP1 binding cofactor resulting in enhanced transcriptional activity and protein expression of puma, MDM2, and p21 upon adriamycin treatment [ xref ]."