wbp 1

WW Domain-Binding Protein 1 (WBP1) is widely expressed in many tissues, but it is lowly expressed in the lung, placenta, kidney, and liver. WBP1 contains two WW-binding motifs: WW-binding 1 and WW-binding 2 that are involved in mediating protein-protein interactions through the binding of polyproline ligands. The WW-binding domain is composed of 38 to 40 semi-conserved amino acids shared by proteins with diverse functions including structural, regulatory, and signaling proteins. In addition, WBP1 also encodes a ligand of the WW domain of the Yes kinase-associated protein. This function has not been determined.

The enzyme oligosaccharyltransferase (dolichyl-diphosphooligosaccharide-protein glycosyltransferase) (DDOST), or 48-kDa subunit (OST48) is one of the catalytic subunits in this complex, exerts a typical type I membrane topology, containing a large luminal domain, a hydrophobic transmembrane domain and a short cytosolic peptide tail. DDOST/OST48 catalyzes the transfer of a high-mannose oligosaccharide (GlcNac2Man9Glc3) from a dolichol-linked oligosaccharide donor (dolichol-P-GlcNac2Man9Glc3) onto the asparagine acceptor site within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains across the membrane of the endoplasmic reticulum. The mammalian oligosaccharyltransferase (OST) is an oligomeric complex composed of three type I transmembrane proteins of the endoplasmic reticulum: ribophorin I (RI), ribophorin II (RII), and OST48. OST48 is not a glycoprotein and is not recognized by antibodies to either ribophorin. Like ribophorins I and II, OST48 was found to be an integral membrane protein, with the majority of the polypeptide located within the lumen of the endoplasmic reticulum (ER). OST48 does not show significant amino acid sequence homology to either ribophorin I or II. It had been found that only the luminal domain of RI contains ER retention information. The dilysine motif in OST48 functions as an ER localization motif because OST48 in which the two lysine residues are replaced by serine (OST48ss) is no longer retained in the ER and is found instead also at the plasma membrane.

WW Domain-Binding Protein 2 (WBP2) is a ubiquitous protein that contains one GRAM domain. The WW domain is composed of 38 to 40 semi-conserved AA shared by proteins of diverse functions including structural, regulatory, and signaling proteins. The domain is participated in mediating protein-protein interactions. WBP2 binds to the WW domain of YAP1, WWP1 and WWP2. The WW-binding 1 motif of WBP2 mediates interaction with NEDD4. The function of this protein WBP2 has not been determined. Some researches demonstrate that WBP-2 also interacts with the thyroid-specific transcription factor Pax8.