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Themis is a 641 amino acid nuclear and cytoplasmic protein that exists as three alternatively spliced isoforms. Themis belongs to the themis family and interacts with PLC γ1, Emt and GRB2. Acting through T-cell antigen receptor (TCR) signaling and through the regulation of calcium influx and phosphorylation of ERK 1, Themis plays a central role in late thymocyte development by controlling both positive and negative T-cell selection. Themis is phosphorylated on Tyr residues quickly after

QKI is a 341 amino acid protein that localizes to both the cytoplasm and the nucleus and contains one KH domain. Expressed in the frontal cortex of the brain, QKI functions as an RNA-binding protein that plays an important role in myelinization and specifically binds to the RNA core sequence 5'-NACUAAY-N(1,20)-UAAY-3'. Additionally, QKI regulates pre-mRNA splicing, and mRNA export and is involved in protecting and promoting the stability of select mRNAs. QKI may be methylated by PRMT1

The protein encoded by this gene is of unknown function. However, it is orthologous to the mouse Trmt2a gene and contains an RNA methyltransferase domain. Expression of this gene varies during the cell cycle, with aberrant expression being a possible biomarker in certain breast cancers. Several transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Apr 2012]

Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD

This gene encodes a large protein that resides in the limiting membrane of endosomes and lysosomes and mediates intracellular cholesterol trafficking via binding of cholesterol to its N-terminal domain. It is predicted to have a cytoplasmic C-terminus, 13 transmembrane domains, and 3 large loops in the lumen of the endosome - the last loop being at the N-terminus. This protein transports low-density lipoproteins to late endosomal/lysosomal compartments where they are hydrolized and released