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transglutaminase-2 (tissue transglutaminase, tranglutaminase-C, TGM2)
Function:
- catalyzes the cross-linking of proteins & the conjugation of polyamines to proteins
- gliadin is a preferred substrate
protein glutamine + alkylamine
protein N(5)-alkylglutamine + NH3
Cofactor: binds 1 Ca+2 per subunit (putative)
Structure:
- monomer
- belongs to the transglutaminase superfamily transglutaminase family
Alternative splicing: named isoforms=3
Expression:
- ubiquitous
- induced by retinoic acid
Pathology:
- defects in TGM2 are involved in early-onset diabetes type 2
- autoantigen of celiac disease [2]
Related
anti-tissue transglutaminase IgA autoantibody
celiac sprue (gluten-sensitive enteropathy)
General
phosphoprotein
transglutaminase (protein-glutamine:amine gamma-glutamyltransferase)
Properties
SIZE: entity length = 687 aa
MW = 77 kD
MOTIF: cysteine residue {C277}
histidine residue {H335}
aspartate residue {D358}
Tyr phosphorylation site {Y369}
Ca+2-binding site
SITE: 398-398
Ca+2-binding site
SITE: 400-400
Ser phosphorylation site {S427}
Ca+2-binding site
SITE: 447-447
Ca+2-binding site
SITE: 452-452
STATE: Inactive
Database Correlations
OMIM 190196
UniProt P21980
PFAM correlations
Entrez Gene 7052
Kegg hsa:7052
ENZYME 2.3.2.13
References
- Kim et al J Biol Chem 266:536 1991
- Dieterich W, Ehnis T, Bauer M, Donner P, Volta U, Riecken EO,
Schuppan D.
Identification of tissue transglutaminase as the autoantigen
of celiac disease.
Nat Med. 1997 Jul;3(7):797-801.
PMID: 9212111
- Wikipedia; Note: Tissue transglutaminase entry
http://en.wikipedia.org/wiki/Tissue_transglutaminase
- UniProt :accession P21980