The Class IIB HDACs include HDAC6 and HDAC10. These two HDACs are most closely related to each other in overall sequence. However, HDAC6's catalytic domain is most similar to HDAC9. A unique feature of HDAC6 is that it contains two catalytic domains in tandem of one another. Another unique feature of HDAC6 is the HDAC6-, SP3, and Brap2-related zinc finger motif (HUB) domain in the C-terminus which shows some functions related to ubiquitination, meaning this HDAC is prone to degradation. HDAC10 has two catalytic domains as well. One active domain is located in the N-terminus and a putative catalytic domain is located in the C-terminus  along with an NES domain. Two putative Rb-binding domains have also been found on HDAC10 which shows it may have roles in the regulation of the cell cycle. Two variants of HDAC10 have been found, both having slight differences in length. HDAC6 is the only HDAC to be shown to act on tubulin, acting as a tubulin deacetylase which helps in the regulation of microtubule-dependent cell motility. It is mostly found in the cytoplasm but has been known to be found in the nucleus, complexed together with HDAC11. HDAC10 has been seen to act on HDACs 1, 2, 3 (or SMRT), 4, 5 and 7. Some evidence has been shown that it may have small interactions with HDAC6 as well. This leads researchers to believe that HDAC10 may function more as a recruiter rather than a factor for deacetylation. However, experiments conducted with HDAC10 did indeed show deacetylation activity.