STABP rabbit pAb

catalytic activity:Ubiquitin C-terminal thioester + H(2)O = ubiquitin + a thiol.,cofactor:Binds 2 zinc ion per subunit.,domain:The JAMM motif is essential for the protease activity.,enzyme regulation:Inhibited by N-ethylmaleimide.,function:Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). Functions at the endosome and is able to oppose the ubiquitin-dependent sorting of receptors to lysosomes. Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7.,miscellaneous:X-ray crystallography studies of STAMBPL1, another member of the peptidase M67C family, has shown that Glu-280 binds zinc indirectly via a water molecule. Nevertheless, this residue is essential for catalytic activity.,PTM:Phosphorylated after BMP type I receptor activation.,similarity:Belongs to the peptidase M67C family.,similarity:Contains 1 MPN (JAB/Mov34) domain.,subunit:Interacts with STAM1. Interacts with SMAD6 and SMAD7. Interacts with CHMP3; the interaction appears to relieve the autoinhibition of CHMP3.,tissue specificity:Ubiquitously expressed.,