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Epstein Barr virus (EBV) is a member of the herpesvirus family and one of the most common human viruses. Most people become infected with EBV during their lives. Primary infections usually results in infectious mononucleosis (glandular fever) but the virus can also lay dormant in B lymphocytes and when reactivated become associated with more serious disease such as Burkitt's lymphoma, nasopharyngeal carcinoma and Hodgkin's disease. EBV latently infects B lymphocytes. Infected B cells expre

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hema

The BTB (broad-complex, Tramtrack and Bric a brac) domain, also known as the POZ (Poxvirus and zinc finger) domain, is an N-terminal homodimerization domain that contains multiple copies of kelch repeats and/or C2H2-type zinc fingers. Proteins that contain BTB domains are thought to be involved in transcriptional regulation via control of chromatin structure and function. BTBD17 (BTB/POZ domain-containing protein 17), also known as BTBD17A, galectin-3-binding protein-like or LGALS3BPL, is a

GPM6A (Glycoprotein M6A) is a Protein Coding gene. GO annotations related to this gene include calcium channel activity. An important paralog of this gene is GPM6B.

The cadherins represent a family of Ca2+-dependent adhesion molecules that function to mediate cell to cell binding that is critical for the maintenance of structure and morphogenesis. Cadherins each contain a large extracellular domain at the N-terminus, which is characterized by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity. The relatively short C-terminal intracellular domain interacts with a variety of cytoplasmic protein

The protein encoded by this gene is the most abundant protein in mammalian urine under physiological conditions. Its excretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. This protein may act as a constitutive inhibitor of calcium crystallization in renal fluids. Excretion of this protein in urine may provide defense against urinary tract infections caused by