western blotting, immunoprecipitation, immunifluorescence
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Description
p97 is a highly abundant and conserved member of the AAA family of ATPase. It has been termed an ubiquitin selective chaperone as it functions within the ubiquitin and/or proteasome pathway. p97 does not interact with ubiquitinated substrates on its own, but requires specific adapters that interact with ubiquitinated substrates and p97 and recruits p97 to substrates. One family of adapters contains a UBX domain, which has been shown with certain adapters to function as a p97-binding module. UBXD1 is a UBX domain containing protein and p97 adapter. This adapter is unique in that it does not harbor an ubiquitin association domain and binds p97 via its PUG domain (another p97 binding motif). Two isoforms of UBXD1 are produced in cells, a full-length form of approximately 54 kDa, and an alternatively spliced variant that lacks the amino-terminal translational start site, and encodes a 47 kDa protein that is derived from an internal translational initiation site. UBXD1 expression at the RNA level has been shown to trend lower in poor prognostic cancers, including those of the breast and prostate.