CSMD1 🐢

"CSMD1 CUB and Sushi multiple domains 1 is a protein that in humans is encoded by the CSMD1 gene. Structure CSMD1 contains 14 N-terminal CUB domains that are separated from each other by a Sushi domains followed by an additional 15 tandem Sushi domain segment. Function Based on analogy to other proteins that contain Sushi domains, it is believed that the gene product of CSMD1 functions as a Complement control protein. Clinical significance It is a potential tumour suppressor, the deletion of which may result in head and neck carcinomas behaving more aggressively.* CSMD1 protein expression was found to be reduced in patients with invasive breast cancer. Functional studies showed that CSMD1 reduction causes cells to transform to a cancer form by increasing their ability to divide, migrate and invade. In a three dimensional model of breast ducts, reduced CSMD1 expression failed breast duct formation. Certain CSMD1 genetic variants have been found to show an association with risk of developing schizophrenia, consistent with emerging evidence that some forms of schizophrenia may result from dysregulated complement activation in the central nervous system resulting in excessive synaptic pruning. References External links * * Further reading "

CDCP1 🐢

"CUB domain-containing protein 1 (CDCP1) is a protein that in humans is encoded by the CDCP1 gene. CDCP1 has also been designated as CD318 (cluster of differentiation 318) and Trask (Transmembrane and associated with src kinases). Alternatively spliced transcript variants encoding distinct isoforms have been reported. Function CDCP1/Trask is not important for the development of the mouse. Adult mice lacking CDCP1 do not exhibit gross morphologic, reproductive or behavioral abnormalities compared with wild-type mice, and histologic examination of multiple organ systems has shown no significant pathology and no observed histologic differences. CDCP1 is a ligand for CD6, a receptor molecule expressed on certain T-cells and may play a role in their migration and chemotaxis. As such CDCP1 may contribute to autoimmune diseases such as encephalomyelitis, multiple sclerosis and inflammatory arthritis. CDCP1 is a 140 kD transmembrane glycoprotein with a large extracellular domain (ECD) containing two CUB domains, and a smaller intracellular domain (ICD). CDCP1 is cleaved by serine proteases at the extracellular domain next to Arg368 to generate a truncated molecule of 80 kDa size. Different cell lines express different amounts of p140 and p80, depending on the activity of endogenous serine proteases. In vivo, CDCP1 is not cleaved during normal physiological circumstances, but its cleavage can be induced during tumorigenesis or tissue injury. The intracellular domain of CDCP1 contains five tyrosine residues - Y707, Y734, Y743, Y762 and Y806. Phosphorylation of CDCP1 is exclusively mediated by Src kinases and depends on the adherence state of the cells. The tyrosine phosphorylation of CDCP1 in cultured cells occurs when cells are induced to detach by trypsin or EDTA, or seen spontaneously during mitotic detachment. The loss of anchorage or cellular detachment is associated with the phosphorylation of CDCP1 as well as the concomitant dephosphorylation of focal adhesion proteins, consistent with the dismantling of focal adhesions. Contrary, during cellular attachment CDCP1 is dephosphorylated, allowing the phosphorylation of focal adhesion proteins. The anti-adhesion and anti-migratory functions of CDCP1 are mediated through negative regulation on integrin receptors. Clinical significance The phosphorylation of CDCP1 is seen in many cancers, including some pre-invasive cancers as well as in invasive tumors and in tumor metastases. References Further reading External links * * Category:Clusters of differentiation "

UPF3A 🐢

"Regulator of nonsense transcripts 3A is a protein that in humans is encoded by the UPF3A gene. This gene encodes a protein that is part of a post-splicing multiprotein complex involved in both mRNA nuclear export and mRNA surveillance. The encoded protein is one of two functional homologs to yeast Upf3p. mRNA surveillance detects exported mRNAs with truncated open reading frames and initiates nonsense-mediated mRNA decay (NMD). When translation ends upstream from the last exon-exon junction, this triggers NMD to degrade mRNAs containing premature stop codons. This protein binds to the mRNA and remains bound after nuclear export, acting as a nucleocytoplasmic shuttling protein. It forms with Y14 a complex that binds specifically 20 nt upstream of exon- exon junctions. This gene is located on the long arm of chromosome 13. Two splice variants encoding different isoforms have been found for this gene. Interactions UPF3A has been shown to interact with RBM8A, UPF2 and UPF1. References Further reading * "