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http://purl.uniprot.org/citations/22160262http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22160262http://www.w3.org/2000/01/rdf-schema#comment"Transglutaminase 2 (TG2) is a multifunctional member of an enzyme family: it modifies glutamine residues by cross-linking proteins and incorporating primary amines into them, has protein disulphide isomerase and protein kinase activities, mediates trans-membrane signal transduction and interactions between cell surface proteins and the extracellular matrix. These unusual multiple roles encoded into one polypeptide chain suggest that genomic variations in the TGM2 gene should be limited. Indeed, the available information in databases shows that unlike in the case of most other transglutaminases there are no common single nucleotide polymorphisms in exons of human TGM2. We collected data on and produced some of the rare genetic variants of TGM2 by site directed mutagenesis and found that some were less stable than the most abundant (wild type) enzyme variant and the majority had deficient transamidating activity. Further studies are required to clarify the pathologic significance of these rare TGM2 alleles in the human population."xsd:string
http://purl.uniprot.org/citations/22160262http://purl.org/dc/terms/identifier"doi:10.1007/s00726-011-1194-6"xsd:string
http://purl.uniprot.org/citations/22160262http://purl.uniprot.org/core/author"Barta E."xsd:string
http://purl.uniprot.org/citations/22160262http://purl.uniprot.org/core/author"Fesus L."xsd:string
http://purl.uniprot.org/citations/22160262http://purl.uniprot.org/core/author"Kiraly R."xsd:string
http://purl.uniprot.org/citations/22160262http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/22160262http://purl.uniprot.org/core/name"Amino Acids"xsd:string
http://purl.uniprot.org/citations/22160262http://purl.uniprot.org/core/pages"215-225"xsd:string
http://purl.uniprot.org/citations/22160262http://purl.uniprot.org/core/title"Polymorphism of transglutaminase 2: unusually low frequency of genomic variants with deficient functions."xsd:string
http://purl.uniprot.org/citations/22160262http://purl.uniprot.org/core/volume"44"xsd:string
http://purl.uniprot.org/citations/22160262http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22160262
http://purl.uniprot.org/citations/22160262http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22160262
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http://purl.uniprot.org/uniprot/#_P21980-mappedCitation-22160262http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22160262
http://purl.uniprot.org/uniprot/#_Q6DKH2-mappedCitation-22160262http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22160262
http://purl.uniprot.org/uniprot/#_Q9BXQ0-mappedCitation-22160262http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22160262
http://purl.uniprot.org/uniprot/#_V9HWG3-mappedCitation-22160262http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22160262
http://purl.uniprot.org/uniprot/B4DTN7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22160262
http://purl.uniprot.org/uniprot/Q9BXQ0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22160262
http://purl.uniprot.org/uniprot/Q6DKH2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22160262
http://purl.uniprot.org/uniprot/B4DIT7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22160262
http://purl.uniprot.org/uniprot/P21980http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22160262
http://purl.uniprot.org/uniprot/V9HWG3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22160262