Philosophiae Doctor - PhD (Biochemistry) / Human Retinoblastoma Binding Protein 6 (RBBP6) is a 200 kDa protein that has been
implicated in a number of crucial cellular processes. It forms part of the mRNA 3'-end
processing complex in both humans and yeast, and it contains an RS-like domain and interacts
with core splicing proteins, suggesting multiple roles in mRNA processing. Through its RING
finger domain it has been implicated in catalysing ubiquitination of the tumour suppressor p53,
the oncogene Y-Box Binding Protein 1 (YB-1) and the DNA replication-associated protein
zBTB38. It is one of only a few proteins known to bind to both p53 and pRb. At the N-terminus
of the protein is the DWNN domain, an ubiquitin-like domain which is found only in this protein
family. Four protein isoforms of RBBP6 have been identified in humans, all of which contain the
DWNN domain: isoform 1 contains 1972 residues, isoform 2 contains 1758 residues and
isoform 4 contains 952 residues. Isoform 3, which contains the first 101 residues of the full
length protein (isoform 1), including the DWNN domain, followed by an unique 17-amino acid
tail, is reported to be expressed independently of the other isoforms and to be down-regulated
in a number of cancers.
| Identifer | oai:union.ndltd.org:netd.ac.za/oai:union.ndltd.org:uwc/oai:etd.uwc.ac.za:11394/6436 |
| Date | January 2017 |
| Creators | Szmyd-Potapczuk, Anna Victoria |
| Contributors | Pugh, David JR |
| Publisher | University of the Western Cape |
| Source Sets | South African National ETD Portal |
| Language | English |
| Detected Language | English |
| Rights | University of the Western Cape |
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