p107

Synthetic peptide corresponding to C-terminus of human p107 protein

NIH3T3 SK-BR-3 MCF-7 cells

Nuclear

10mM Phosphate-buffered saline containing 0. 2% BSA and 0. 1% sodium azide

Nuclear The pocket protein family consists of three structurally and functionally related proteins Rb (retinoblastoma) p107 and p130. This family of tumor suppressors function to regulate important cellular transcription factors such as the E2F family. The E2F proteins regulate the expression of genes whose products are important for cell cycle progression. The inactivation Rb is catalyzed by CDK phosphorylation thereby releasing E2F during the G1-S phase cellular progression. Unchecked inactivation of Rb in G1 phase has been indicated as a universal mechanism underlying cellular transformation . While Rb has been the most studied among the pocket proteins p107 and p130 have also been shown to be key regulators of E2F. Several studies have also provided evidence that p107/p130 provide different functions in E2F regulation than does Rb. Rb p107 and p130 each contain a conserved \' A/B pocket\' which is the target of several viral oncoproteins namely SV40 large T-antigen and adenovirus E1A.

Interacts with SUV420H1 and SUV420H2 (By similarity). Component of the DREAM complex (also named LINC complex) at least composed of E2F4 E2F5 LIN9 LIN37 LIN52 LIN54 MYBL1 MYBL2 RBL1 RBL2 RBBP4 TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9 LIN37 LIN52 and LIN54 form a subcomplex that binds to MYBL2. Interacts with AATF. Interacts with JARID1A.

Exists in both phosphorylated and unphosphorylated forms and T but not E1A binds only to the unphosphorylated form. Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332 Ser-640 Ser-964 and Ser-975 by CDK4.