It really depends on your prior experience with the same protein in the same buffer.
In general, you could check for degradation by running a gel and looking out for strange bands that haven't been there before (degradation products). If the degradation is severe, you will either see no bands at all (degradated into very small fragments that elute from the gel) or a smear.
Of course it could be that upon precipitation your protein was denaturated. In that case, it _might_ theoretically re-dissolve (though it might as well not, really depends on your protein) and give you a band of the correct size. But your protein's activity might not be there any more. If you have a readout assay for the activity of your protein, use that to verify sample quality.
If the activity is there and the protein band(s) look normal, everything should be alright.
If you don't have an activity assay or if you are in any doubt, I would rather discard the protein and get a new aliquot rather than second-guessing your downstream applications.