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The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Additionally we are shipping UBE3B Antibodies (14) and UBE3B Proteins (3) and many more products for this protein.
UBE3B encodes a widely expressed protein ubiquitin ligase E3B, which, when mutated in both alleles, causes Kaufman oculocerebrofacial syndrome.
UBE3B mutations cause a clinically recognizable and possibly underdiagnosed syndrome named the Kaufman oculocerebrofacial syndrome
data provide evidence that Kaufman oculocerebrofacial syndrome is caused by UBE3B loss of function, and further demonstrate the impact of misregulation of protein ubiquitination on development and growth.
Our data reveal the pleiotropic effects of UBE3B deficiency and reinforce the physiological importance of ubiquitination in neuronal development and function in mammals.
UBE3B is a novel E3 ligase, with a HECT-domain which constitutes the active site for ubiquitin transfer
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: E1 ubiquitin-activating enzymes, E2 ubiquitin-conjugating enzymes, and E3 ubiquitin-protein ligases. This gene encodes a member of the E3 ubiquitin-conjugating enzyme family which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme and transfers the ubiquitin to the targeted substrates. A HECT (homology to E6-AP C-terminus) domain in the C-terminus of the longer isoform of this protein is the catalytic site of ubiquitin transfer and forms a complex with E2 conjugases. Shorter isoforms of this protein which lack the C-terminal HECT domain are therefore unlikely to bind E2 enzymes. Alternatively spliced transcript variants encoding distinct isoforms have been identified for this gene.
ubiquitin-protein ligase E3B
, ubiquitin protein ligase E3B
, ubiquitin-protein ligase E3B-like
, ubiquitin protein ligase E3