LRSAM1 Polyclonal Antibody, RBITC Conjugated

LRSAM1 is an E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivation of the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos. It selectively regulates cell adhesion molecules and plays a role in receptor endocytosis and viral budding. LRSAM1 contains a RING-type zinc finger, 5 leucine-rich repeats and 1 SAM (sterile alpha motif) domain. The coiled coil domains interact with the SB domain of TSG101. The PTAP motifs mediate the binding to UEV domains. There are 3 isoforms produced by alternative splicing.

E3 ubiquitin protein ligase LRSAM1; hTAL; Leucine rich repeat and sterile alpha mot containing protein 1; RLE; TAL; Tsg101 associated ligase; LRSM1_HUMAN.