| http://purl.uniprot.org/citations/1358880 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1358880 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1358880 | http://www.w3.org/2000/01/rdf-schema#comment | "A 1.9-kilobase (kb) cDNA for a new transglutaminase protein has been cloned and sequenced from retinoic acid-induced human erythroleukemia (HEL) cells. Full-length cDNA analysis reveals an open reading frame coding for a polypeptide of 548 amino acid residues with a molecular weight of 61,740. The deduced amino acid sequence exhibited 98% identity to the human cellular transglutaminase sequence. The cysteine at position 277 in the active site and the putative Ca(2+)-binding pocket at residues 446-453 of cellular transglutaminase are conserved. Such evidence predicts that the encoded protein product is likely to be a transglutaminase homologue (TGase-H). Immunoprecipitation of the in vitro translation products from a synthetic TGase-H mRNA and from total protein of cultured erythroleukemia HEL cells revealed a protein with a molecular weight of 63,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Northern blot analysis of HEL cells and normal human fibroblast cells WI-38 using a cellular TGase probe detected the 1.9- and 4.0-kb RNA species at a relative abundance of 1:3 and 1:7, respectively. The 3'-end of the human cellular transglutaminase mRNA was also cloned and sequenced to allow comparison to the 3'-end of TGase-H reported here. This new piece gives a full length of 4012 nucleotides (4.0 kb) for human cellular transglutaminase. Comparison of the 5'-end (bases 1-1747) of the 1.9- and 4.0-kb cDNA sequences revealed a very high degree of identity. Beginning with base 1748, the sequences diverge showing no homology. The divergence point correlates with known intron-exon consensus boundaries indicative of alternative splicing."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)41717-6"xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)41717-6"xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/author | "Lee K.N."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/author | "Lee K.N."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/author | "Birckbichler P.J."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/author | "Birckbichler P.J."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/author | "Patterson M.K. Jr."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/author | "Patterson M.K. Jr."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/author | "Gonzales R.A."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/author | "Gonzales R.A."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/author | "Fraij B.M."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/author | "Fraij B.M."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/pages | "22616-22623"xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/pages | "22616-22623"xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/title | "A retinoic acid-inducible mRNA from human erythroleukemia cells encodes a novel tissue transglutaminase homologue."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/title | "A retinoic acid-inducible mRNA from human erythroleukemia cells encodes a novel tissue transglutaminase homologue."xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/volume | "267"xsd:string |
| http://purl.uniprot.org/citations/1358880 | http://purl.uniprot.org/core/volume | "267"xsd:string |