an enzyme of the transglutaminase family that catalyzes the crosslinking of proteins and the conjugation of polyamines to proteins. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. . Is the autoantigen in coeliac disease and plays a role in apoptosis, cellular differentiation and matrix stabilisation. Three alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Molecular Function: protein domain specific binding; protein binding; GTP binding; protein-glutamine gamma-glutamyltransferase activity; metal ion binding
Biological Process: elevation of cytosolic calcium ion concentration during G-protein signaling, coupled to IP3 second messenger (phospholipase C activating); positive regulation of cell adhesion; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of apoptosis; isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine; reduction of endoplasmic reticulum calcium ion concentration; positive regulation of smooth muscle cell proliferation; blood vessel remodeling; apoptotic cell clearance; protein homooligomerization; positive regulation of inflammatory response; elevation of mitochondrial calcium ion concentration
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.