ID O08579; PN Emerin; GN Emd; OS 10090; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0179; SL Nucleus Position: SL-0182; SL Nucleus Position: SL-0183; SL Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:P50402}; Single-pass membrane protein; Nucleoplasmic side {ECO:0000250|UniProtKB:P50402}. Nucleus outer membrane. Note=Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus (By similarity). {ECO:0000250}. DR UNIPROT: O08579; DR UNIPROT: Q3TIH6; DR UNIPROT: Q3UJP3; DR Pfam: PF03020; DR PROSITE: PS50954; DE Function: 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 a CRM1- dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non- farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells. {ECO:0000250|UniProtKB:P50402}. DE Reference Proteome: Yes; DE Interaction: P20263; IntAct: EBI-3043810; Score: 0.35 DE Interaction: P52927; IntAct: EBI-9986179; Score: 0.35 DE Interaction: Q8NF91; IntAct: EBI-10760599; Score: 0.27 DE Interaction: Q8WXH0; IntAct: EBI-10760623; Score: 0.27 DE Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35 GO GO:0032541; GO GO:0005737; GO GO:0005783; GO GO:0016021; GO GO:0005874; GO GO:0005635; GO GO:0005637; GO GO:0005652; GO GO:0031965; GO GO:0005640; GO GO:0005654; GO GO:0005634; GO GO:0005819; GO GO:0031616; GO GO:0003779; GO GO:0048487; GO GO:0071363; GO GO:0090090; GO GO:0048147; GO GO:0071763; GO GO:0046827; GO GO:0060828; GO GO:0035914; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MDDYAVLSDTELAAVLRQYNIPHGPIVGSTRKLYEKKIFEYETQRRRLLPPNSSSSSFSYQFSDLDSAAVDSDMYDLPKK SQ EDALLYQSKDYNDDYYEESYLTTKTYGEPESVGMSKSFRQPGTSLVDADTFHHQVRDDIFSSLEEEGKDRERLIYGQDSA SQ YQSIAHYRPISNVSRSSLGLSYYPTSSTSSVSSSSSSPSSWLTRRAIRPEKQAPAAALGQDRQVPLWGQLLLFLVFAAFL SQ LFVYYSIQAEEGNPFWMDP //