High impact information on RNF7

• Mutational analysis indicates that CKII phosphorylates threonine at residue 10 within CKBBP1 [1].
• Complementation experiment showed that the lethal phenotype induced by the ySAG deletion is fully rescued by wildtype SAG, but not by several hSAG mutants [2].
• However, the stable expression of Ring-H2 finger-disrupted CKBBP1 in HeLa cells suppresses cell proliferation and causes the accumulation of the G1/G0 peak of the cell cycle [3].
• One SCF component, SAG/ROC2/Rbx2/Hrt2, a RING finger protein, was first identified as a redox-inducible protein, which, when overexpressed, inhibited apoptosis both in vitro and in vivo [4].
• Previously we have shown that CKIIbeta interacts with ribosomal proteins L5 and L41, DNA topoisomerase IIbeta, and SAG/CKBBP1 [5].

Biological context of RNF7

• The results indicated that the region between residues 1 and 167 of CKIIbeta is common binding site for L5, topoisomerase IIbeta, SAG/CKBBP1, and L41 [5].

Anatomical context of RNF7

• In this report, we demonstrate that CKBBP1 is efficiently phosphorylated in vitro by purified CKII in the presence of GTP and by heparin-sensitive protein kinase in HeLa cell extract [1].

Other interactions of RNF7

• We recently reported that the beta subunit of protein kinase CKII (CKIIbeta) associates with CKBBP1 that contains the Ring-H2 finger motif in the yeast two-hybrid system [3].
• In this study, the two-hybrid system was used to define the subregions of CKIIbeta that are involved in the interaction with L5, L41, topoisomerase IIbeta, SAG/CKBBP1, and unknown proteins, CKBBP2 and CKBBP3 [5].

References