cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein.
The abilities of FK506 and rapamycin to block distinct signal transduction pathways are mediated by soluble binding proteins. Previously, a family of these receptors has been recognized that includes a 25 kDa protein, FKBP25. We now report the isolation of a cDNA for FKBP25 from a human hippocampal cDNA library by oligonucleotide screening. The nucleotide sequence reveals an open reading frame that encodes a 224 amino acid polypeptide. Human FKBP25 shows 97% amino acid identity with bovine FKBP25 and 62% homology with human FKBP12.
Hung
D T
DT
Department of Chemistry, Harvard University, Cambridge, Massachusetts 02138.
Schreiber
S L
SL
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics* / Q000378:metabolism; D002417:Cattle; D003001:Cloning, Molecular; D015723:Gene Library; D006801:Humans; D007166:Immunosuppressive Agents / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009838:Oligodeoxyribonucleotides; D015345:Oligonucleotide Probes; D016366:Open Reading Frames; D011090:Polyenes / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D020123:Sirolimus; D016559:Tacrolimus / Q000378:metabolism*; D022021:Tacrolimus Binding Proteins
D002352:Carrier Proteins; D007166:Immunosuppressive Agents; D009838:Oligodeoxyribonucleotides; D015345:Oligonucleotide Probes; D011090:Polyenes; D022021:Tacrolimus Binding Proteins; D020123:Sirolimus; D016559:Tacrolimus