This pleckstrin homology (PH)-like domain can be found at the N terminus of some ubiquitin carboxyl-terminal hydrolases, including USP26, USP29 and USP37. USP37 antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), resulting in promoting S phase entry []. USP26 is a regulator of androgen receptor (AR) signaling []. Both USP26 and USP37 are critical for double-strand breaks repair by homologous recombination []. USP29 plays a role in apoptosis and oxidative stress [].PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner []. They share little sequence conservation, but all have a common fold, which is electrostatically polarized.
This entry represents a pleckstrin homology (PH)-like domain found at the N terminus of some ubiquitin carboxyl-terminal hydrolases, including USP26, USP29 and USP37. USP37 antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), resulting in promoting S phase entry []. USP26 is a regulator of androgen receptor (AR) signaling []. Both USP26 and USP37 are critical for double-strand breaks repair by homologous recombination []. USP29 plays a role in apoptosis and oxidative stress [].PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner []. They share little sequence conservation, but all have a common fold, which is electrostatically polarized.
