a single pass membrane protein that spans the inner nuclear membrane. A serine-rich nuclear membrane protein and a member of the nuclear lamina-associated protein family. It interacts with lamins A and C, and mediates membrane anchorage to the cytoskeleton. Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through an exportin 1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Colocalized with BAF at the central region of the assembling nuclear rim, near spindle-attachment sites. Hyper-phosphorylated on tyrosine in cells overexpressing HER2. Directly phosphorylated by Src and Abl. Phosphorylated by Src at Y59, Y74 and Y95. May function as a downstream effector and signal integrator for tyrosine kinase signaling pathways at the nuclear envelope. Dreifuss-Emery muscular dystrophy is an X-linked inherited degenerative myopathy resulting from mutation in the emerin gene. Note: This description may include information from UniProtKB.
Protein type: Cytoskeletal protein; Membrane protein, integral
Cellular Component: nuclear outer membrane; microtubule; nuclear membrane; endoplasmic reticulum; integral to membrane; nuclear inner membrane; nuclear envelope
Molecular Function: protein binding; beta-tubulin binding; actin binding
Biological Process: positive regulation of protein export from nucleus; muscle development; mitotic nuclear envelope reassembly; muscle contraction; negative regulation of fibroblast proliferation; mitotic nuclear envelope disassembly; mitotic cell cycle
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.