Members of the junctional adhesion molecule (JAM) family are type I transmembrane glycoproteins of the immunoglobulin (Ig) superfamily that are localized in the tight junctions between endothelial or epithelial cells and appear to be involved in leukocyte transmigration. JAM-A, also known as platelet adhesion molecule 1 (PAM-1) and platelet F11 receptor, contains two V-type Ig-like domains, forms homodimers, and interacts with LFA-1. JAM-B (vasculoendothelial or VE-JAM) and JAM-C each contain two Ig domains (one V-type and one C2-type), a cytoplasmic PDZ-binding motif and a PKC phosphorylation site. JAM-C interacts with MAC-1 and facilitates JAM-B interaction with integrin alpha 4 beta 1. Junctional adhesion molecule 2 (JAM2), also know as JAMB, is a member of the newly reported glycoprotein family of adhesion molecules found at intercellular junctions of endothelial cells and lymphocytes (human). In adult murine tissue JAM2 expression is restricted to high endothelial venules of lymphoid organs, lymphoendothelial cells and endothelial cells in kidney.Synonyms: C21orf43, JAM-B, Junctional adhesion molecule 2, Junctional adhesion molecule B, VEJAM, Vascular endothelial junction-associated molecule