This entry includes Hub1 from yeasts and Ubl5 from animals. Hub1 is an ubiquitin-like protein that lacks the C-terminal Gly, which is essential for covalent attachment to target protein(s) of ubiquitin and other ubiquitin-like (UBL) modifiers []. Hub1 binds non-covalently to a conserved element termed HIND, which is present in the spliceosomal protein Snu66 in yeast and mammals, and Prp38 in plants [, ]. Hub1 does not affect general splicing, instead, it acts as a modulator of spliceosome performance and facilitator of alternative splicing []. It has been shown to bind to the DEAD-box helicase Prp5 and mediates enhanced, but error-prone splicing [].
