Function
Atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues. Shows esterification activity towards both threonine and serine, with a preference for threonine, and acts via two essential catalytic cysteine residues that relay ubiquitin to its substrate via thioester intermediates. Interacts with the E2 enzymes UBE2D1, UBE2D3, UBE2E1 and UBE2L3.
Biological Context
Subcellular Location: Nucleus; Cell projection, axon; Cytoplasm, cytoskeleton
Tissue Specificity: Expressed in all tissues examined, expression is exceptionally abundant in brain and thymus. Colocalizes with TSC1 and TSC2 along the neurites and in the growth cones. Highly expressed in peripheral and central neurons. Colocalized with TSC1 in one of the filopodial extensions at the tip of a growth cone
Pathway: Protein modification; protein ubiquitination
Product Specifications
Recombinant Human E3 ubiquitin-protein ligase MYCBP2 (MYCBP2), partial is a recombinant protein from Homo sapiens (Human), expressed in E.coli, covering amino acids 4417-4676aa, with C-terminal 6xHis-tagged tag, molecular weight 36.3kDa, purity Greater than 90% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications. Explore more Enzyme proteins →
