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Description
The p53 tumor suppressor protein plays a major role in cellular response to DNA damage and other genomic aberrations. Activation of p53 can lead to either cell cycle arrest and DNA repair or apoptosis . p53 is phosphorylated at multiple sites in vivo and by several different protein kinases in vitro . DNA damage induces phosphorylation of p53 at Ser15 and Ser20 and leads to a reduced interaction between p53 and its negative regulator, the oncoprotein MDM2 . MDM2 inhibits p53 accumulation by targeting it for ubiquitination and proteasomal degradation . p53 can be phosphorylated by ATM, ATR, and DNA-PK at Ser15 and Ser37. Phosphorylation impairs the ability of MDM2 to bind p53, promoting both the accumulation and activation of p53 in response to DNA damage . Chk2 and Chk1 can phosphorylate p53 at Ser20, enhancing its tetramerization, stability, and activity . p53 is phosphorylated at Ser392 in vivo and by CAK in vitro . Phosphorylation of p53 at Ser392 is increased in human tumors and has been reported to influence the growth suppressor function, DNA binding, and transcriptional activation of p53 . p53 is phosphorylated at Ser6 and Ser9 by CK1delta and CK1epsilon both in vitro and in vivo . Phosphorylation of p53 at Ser46 regulates the ability of p53 to induce apoptosis . Acetylation of p53 is mediated by p300 and CBP acetyltransferases. Inhibition of deacetylation suppressing MDM2 from recruiting HDAC1 complex by p19 (ARF) stabilizes p53. Acetylation appears to play a positive role in the accumulation of p53 protein in stress response . Following DNA damage, human p53 becomes acetylated at Lys382 (Lys379 in mouse) in vivo to enhance p53-DNA binding . Deacetylation of p53 occurs through interaction with the SIRT1 protein, a deacetylase that may be involved in cellular aging and the DNA damage response . Synonyms: TP53, P53, LFS1, TRP53, FLJ92943,
Immunogen
A phospho specific peptide corresponding to residues surrounding pSer15 of human p53