Table 2.
Anatomy and functions of PBF
| Domaina | Disordered or ordered structureb | Probable phosphorylation sitesc | Probable binding sites to cellular factorsd | Function |
|---|---|---|---|---|
| I (1–125) | Disordered region (1–72) Ordered region (86–128) | 7 sites | 1 site (1–22) | Unknown |
| II (126–215) | Disordered region (131–216) | 8 sites | 2 sites (166–182; 193–206) | Unknown |
| III (216–301) | Ordered region (279–302) | 11 sites | 1 site (277–304) | -Monopartite NLS (PAPRKRKNSVK, 267–277)e |
| -Zinc finger domain (279–302) | ||||
| -Rich G-C DNA binding site of HPV type 8 [1] | ||||
| IV (302–483) | Disordered region (304–513) | 18 sites | 3 sites (320–341; 359–372; 393–416) | -Binding to 14-3-3β (393–398; 444–453). PBF must be phosphorylated at Ser 447, 449 and 451 [5]. |
| -Sequence recognized by cytotoxic T cells in the context HLA-A24 [2]. |
Parentheses indicate the amino acid residues position. Bold residues indicate the high affinity site. Identified in this paper using: aMammoth analysis; bIntfold, disEMBL and Metadisorder analyses; cNetPhos 2.0; dANCHOR; ecNLS Mapper, NucPred, and PSORT II analyses.