Protein domains, posttranslational modification sites, and proteins that interact with human p53

The 393 amino acid human p53 polypeptide is represented schematically with postulated functional regions and domains indicated. Residues ~1-40 (TAD1) and 41-83 (TAD2) comprise independent tandem transactivation domains; residues ~61-94 represent a proline-rich (PRD), Src homology 3-like (SH3) domain which overlaps a poorly conserved segment (33-80) that lies mostly in TAD2. Residues 100-116 constitute a recently described N-terminal repression domain that is required for repressing basal p53 activity in some cell types. Residues ~102-292 contain the central, sequence-specific, DNA binding core region; residues 305-321 contains the primary bi-partite nuclear localization signal (NLS); residues 324-356 comprise the tetramerization domain (TET) which contains a nuclear export signal within residues 339-350; residues 363-393 (REG) negatively regulate DNA binding by the central core to consensus recognition sites in oligonucleotides and interact in a sequence-independent manner with single- and double-stranded nucleic acids but contribute positively to chromatin binding and transactivation in vivo. Posttranslational modification sites (P, phosphorylation; Ac, acetylation; G, glycosylation; Me, methylation, N8, neddylation; Ub, ubiquination) are indicated together with enzymes that can accomplish the modifications in vitro. The C-terminal six lysines (K370, K372, K373, K381, K382, and K386) can be ubiquinated; K373, K372, and K373 are likely sites of attachment for the ubiquitin-like protein NEDD8; Lys386 may be modified by conjugation with SUMO1, a ubiquitin-like peptide. Interaction regions for selected proteins are indicated below the polypeptide. Updated from Anderson and Appella, in Handbook of Cell Signaling, Academic Press, 2003. This is figure 3 in the webpages of Carl W. Anderson.

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