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Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone.

Actin-binding protein. Plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. Modulates the cell surface expression of IL2RA/CD25 and CD69.$nTissue specificity;Detected in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia, in spleen and other lymph node-containing organs. Expressed in peripheral blood T lymphocytes, neutrophils, monocytes, B lymphocytes, and myeloid cells.

Sam 68 is a protein that is phosphorylated on tyrosine and functions as a substrate for Src family tyrosine kinases during mitosis. Sam 68 also associates with several SH2 and SH3 domain-containing signaling proteins, such as GRB2 and PLC ?. Originally cloned as Ras GAP-associated p62, further investigations have shown that Sam 68 and Ras GAP-associated p62 are not antigenically related, nor are they encoded by the same gene. Like Sam 68, the Sam 68-like mammalian proteins, SLM-1 and SLM-

This gene encodes a protein involved in endoplasmic reticulum (ER)-associated degradation. The encoded protein removes unfolded proteins, accumulated during ER stress, by retrograde transport to the cytosol from the ER. This protein also uses the ubiquitin-proteasome system for additional degradation of unfolded proteins. Sequence analysis identified two transcript variants that encode different isoforms. [provided by RefSeq, May 2011]

Sam 68 is a protein that is phosphorylated on tyrosine and functions as a substrate for Src family tyrosine kinases during mitosis. Sam 68 also associates with several SH2 and SH3 domain-containing signaling proteins, such as GRB2 and PLC ?. Originally cloned as Ras GAP-associated p62, further investigations have shown that Sam 68 and Ras GAP-associated p62 are not antigenically related, nor are they encoded by the same gene. Like Sam 68, the Sam 68-like mammalian proteins, SLM-1 and SLM-

GLUT4 is the facilitated glucose transporter expressed exclusively in adipocytes and muscle cells, and is also known as the “insulin-responsive“ glucose transporter. GLUT4 translocates from an ill-defined intracellular compartment to the plasma membrane in response to insulin. The total cellular content of GLUT4 is significantly decreased in adipose cells from many patients with Type II diabetes mellitus, and animals with some types of experimental diabetes.