Rulten, SL, Kinloch, RA, Tateossian, H, Robinson, C, Gettins, L and Kay, JE (2006) The human FK506-binding proteins: characterization of human FKBP19. Mammalian Genome, 17 (4). pp. 322-331. ISSN 0938-8990
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Analysis of the human repertoire of the FK506-binding protein (FKBP) family of peptidyl-prolyl cis/trans isomerases has identified an expansion of genes that code for human FKBPs in the secretory pathway. There are distinct differences in tissue distribution and expression levels of each variant. In this article we describe the characterization of human FKBP19 (Entrez Gene ID: FKBP11), an FK506-binding protein predominantly expressed in vertebrate secretory tissues. The FKBP19 sequence comprises a cleavable N-terminal signal sequence followed by a putative peptidyl-prolyl cis/trans isomerase domain with homology to FKBP12. This domain binds FK506 weakly in vitro. FKBP19 mRNA is abundant in human pancreas and other secretory tissues and high levels of FKBP19 protein are detected in the acinar cells of mouse pancreas.
|Schools and Departments:||Brighton and Sussex Medical School > Brighton and Sussex Medical School
School of Life Sciences
|Subjects:||Q Science > QP Physiology|
|Depositing User:||Stuart Rulten|
|Date Deposited:||12 Dec 2006|
|Last Modified:||09 Mar 2017 06:27|
|Google Scholar:||20 Citations|
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The human FK506-binding proteins: characterization of human FKBP19. (deposited 12 Dec 2006)
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