As part of the ribosome quality control complex (RQC), a ribosome-associated complex, mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes as well as their ubiquitin-mediated proteasomal degradation. Thereby, frees ribosomes from the stalled translation complex and prevents the accumulation of nascent polypeptide chains that are potentially toxic for the cell (PubMed:23178123). RQC2 is responsible for selective recognition of stalled 60S subunits by recognizing an exposed, nascent chain-conjugated tRNA moiety (PubMed:25349383). RQC2 is important for the stable association of the E3 ubiquitin-protein ligase RKR1/LTN1 to the complex (PubMed:23479637). RQC2 is also able to recruit alanine- and threonine-charged tRNA to the A site and directs the elongation of stalled nascent chains independently of mRNA or 40S subunits, leading to non-templated C-terminal Ala and Thr extensions (CAT tails) (PubMed:25554787, PubMed:32934225). CAT tails induce a HSF1-dependent heat shock response (PubMed:25554787). CAT tails also promote the RKR1/LTN1-mediated ubiquitination of incompletely synthesized nascent polypeptides and their subsequent proteasomal degradation (PubMed:32934225). Component of the ribosome quality control complex (RQC), composed of the E3 ubiquitin ligase RKR1/LTN1, RQC1 and RQC2, as well as CDC48 and its ubiquitin-binding cofactors associated with the 60S ribosomal subunit (PubMed:23178123, PubMed:23479637, PubMed:25349383). RQC2 binds to the 40S-binding surface of tRNAs (PubMed:25554787). Present with 7700 molecules/cell in log phase SD medium. Belongs to the NEMF family.