G6B is a 241aa novel regulatory nuclear chloride ion channel protein belonging to the immunoglobulin (Ig) super family. It is a glycosylated receptor, present both as soluble and transmembrane isoforms where the soluble proteins show expression in endoplasmic reticulum and Golgi before being secreted. It contains a leader sequence and an extracellular Ig domain which binds to heparin and helps to modulate the interaction of G6B with an unknown protein ligand. It also has an intracellular, proline-rich potential SH3-binding domain, and two putative phosphorylated tyrosine motifs with an SH2-binding domain that is recruited to the receptor and dephosphorylates membrane-bound phosphoproteins and thus modulates the signaling cascade. It is commonly expressed in certain hematopoietic cell lines including K562, Molt4, and Jurkat.