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CREM is a a bZIP transcription factor that binds to the cAMP responsive element found in many viral and cellular promoters. It is derived from a multiexonic gene that encodes both activators and antagonists of cAMP-inducible transcription by differential splicing. Splice variants with antagonistic function lack 2 glutamine-rich domains and block cAMP-induced transcription, whereas an isoform that includes these glutamine-rich domains is a transcriptional activator.

CREM is a a bZIP transcription factor that binds to the cAMP responsive element found in many viral and cellular promoters. It is derived from a multiexonic gene that encodes both activators and antagonists of cAMP-inducible transcription by differential splicing. Splice variants with antagonistic function lack 2 glutamine-rich domains and block cAMP-induced transcription, whereas an isoform that includes these glutamine-rich domains is a transcriptional activator.

The protein encoded by this gene is a glycoprotein, belonging to the pentraxin family of proteins, which has a characteristic pentameric organization. These family members have considerable sequence homology which is thought to be the result of gene duplication. The binding of the encoded protein to proteins in the pathological amyloid cross-beta fold suggests its possible role as a chaperone. This protein is also thought to control the degradation of chromatin. It has been demonstrated that th

Cytokeratin 20 is a type I keratin which is primarily expressed in gastric and intestinal epithelium, urothelium, and Merkel-cells. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. Their genes are clustered in a region of chromosome 17q12-q21. Cytokeratin 20 is a major

This gene encodes the coagulation factor XIII A subunit. Coagulation factor XIII is the last zymogen to become activated in the blood coagulation cascade. Plasma factor XIII is a heterotetramer composed of 2 A subunits and 2 B subunits. The A subunits have catalytic function, and the B subunits do not have enzymatic activity and may serve as plasma carrier molecules. Platelet factor XIII is comprised only of 2 A subunits, which are identical to those of plasma origin. Upon cleavage of the ac

This gene encodes the coagulation factor XIII A subunit. Coagulation factor XIII is the last zymogen to become activated in the blood coagulation cascade. Plasma factor XIII is a heterotetramer composed of 2 A subunits and 2 B subunits. The A subunits have catalytic function, and the B subunits do not have enzymatic activity and may serve as plasma carrier molecules. Platelet factor XIII is comprised only of 2 A subunits, which are identical to those of plasma origin. Upon cleavage of the ac