| ID | Sequence | Length | GC content |
|---|---|---|---|
| ACAGUGGAUCCGGAAGCACAGGAGACCAAGAGACCAGAGAUACCAGGAU… | 5042 nt | 0.5470 | |
| AGUGCCAGCCGCCAGUGGUCGCACUUGGAGGGUCUCGCCGCCAGUGGAA… | 4727 nt | 0.5420 | |
| AGUGCCAGCCGCCAGUGGUCGCACUUGGAGGGUCUCGCCGCCAGUGGAA… | 4790 nt | 0.5441 | |
| AGUGCCAGCCGCCAGUGGUCGCACUUGGAGGGUCUCGCCGCCAGUGGAA… | 4970 nt | 0.5469 | |
| AGUGCCAGCCGCCAGUGGUCGCACUUGGAGGGUCUCGCCGCCAGUGGAA… | 1857 nt | 0.5994 |
Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. 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. Finally, the encoded protein is the autoantigen implicated in celiac disease. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
A study in mice and humans identified the TGM2 as a novel disease gene for sepsis-induced myocardial dysfunction, showing it was up-regulated in LPS-treated mouse models and validated by qRT-PCR and external datasets [Yao et al. DOI:10.1016/j.ygeno.2024.110911]. In a separate study, the TGM2 was found to be up-regulated in human and rat skin following UVB-induced inflammation, with a fold change of 12.5 in human skin and 4.4 in rat skin, indicating its role in inflammatory hyperalgesia [Dawes et al. DOI:10.1371/journal.pone.0093338].