Put another way, one of the key findings of structural biology is that many protein biological functions are performed by sequence regions without rigid secondary or tertiary structure.

The same applies to any protein/RNA general survey study that attempts to extract a hypothesis from the resulting data. The fact that these studies aren't reproducible simply points to a failure of the ideas behind the experimental design. It was worth exploring, but it doesn't work.

While ANKRD11:p may not be top of the pops in the proteomics world, it does have a broad, significant role as a transcription-associated controller even though it eschews the notions key to "structural biology".
onlinelibrary.wiley.com/doi/10.1111/...

Can anyone from the protein-protein/protein-nucleic-acid binding world identify what those 2 big ankyrin repeat domains are clamping themselves onto?

An ankyrin repeat domain is ideally a 33 residue helix-loop-helix-loop gadget. When these are strung out into extended tandem repeats, they generate a PTM resistant region, which has no internal S/T/Y phosphorylation, R methylation or K acetylation & only very rarely K ubiquitination.

I can't let the use of "proto-oncogene" go by with out, yet again, commenting on what a terrible idea it is to label a protein with this dopey term.