| http://purl.uniprot.org/citations/2846539 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2846539 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2846539 | http://www.w3.org/2000/01/rdf-schema#comment | "A single polypeptide acts as the beta subunit of prolyl 4-hydroxylase and the enzyme protein disulfide isomerase and may also function as a cellular thyroid hormone binding protein. We report here that the human gene for this polypeptide is about 18 kilobase pairs and consists of 11 exons. The two thioredoxin-like regions are coded by exons 1-2 and 8-9, respectively. The codons for the two presumed active sites of protein disulfide isomerase, each a Cys-Gly-His-Cys sequence, are located 12 base pairs from the beginning of exons 2 and 9. The last 3 amino acids coded by exons 1 and 8 and the first 9 amino acids coded by exons 2 and 9, including a broken codon for Tyr, are identical in the respective exon-intron junctions. These regions are also highly homologous to the active sites of bacterial thioredoxins. The data suggest that evolution of this gene has involved exon shuffling and duplication of a two-exon unit, in which the internal exon-intron junctions have been entirely conserved. The region between exons 1-2 and 8-9 appears to contain other duplications. The 5' flanking sequences contain a TATA box, six CCAAT boxes, and other elements which may be involved in regulation of the cellular amounts of this polypeptide."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)37581-1"xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)37581-1"xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/author | "Chow L.T."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/author | "Chow L.T."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/author | "Kivirikko K.I."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/author | "Kivirikko K.I."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/author | "Pihlajaniemi T."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/author | "Pihlajaniemi T."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/author | "Tasanen K."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/author | "Tasanen K."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/author | "Parkkonen T."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/author | "Parkkonen T."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/date | "1988"xsd:gYear |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/date | "1988"xsd:gYear |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/pages | "16218-16224"xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/pages | "16218-16224"xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/title | "Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/title | "Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase."xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/volume | "263"xsd:string |
| http://purl.uniprot.org/citations/2846539 | http://purl.uniprot.org/core/volume | "263"xsd:string |