cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein

Biochem Biophys Res Commun. 1992 Apr 30;184(2):733-8. doi: 10.1016/0006-291x(92)90651-z.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Carrier Proteins / genetics*
  • Carrier Proteins / metabolism
  • Cattle
  • Cloning, Molecular
  • Gene Library
  • Humans
  • Immunosuppressive Agents / metabolism
  • Molecular Sequence Data
  • Molecular Weight
  • Oligodeoxyribonucleotides
  • Oligonucleotide Probes
  • Open Reading Frames
  • Polyenes / metabolism*
  • Sequence Homology, Nucleic Acid
  • Sirolimus
  • Tacrolimus / metabolism*
  • Tacrolimus Binding Proteins

Substances

  • Carrier Proteins
  • Immunosuppressive Agents
  • Oligodeoxyribonucleotides
  • Oligonucleotide Probes
  • Polyenes
  • Tacrolimus Binding Proteins
  • Sirolimus
  • Tacrolimus

Associated data

  • GENBANK/D10556
  • GENBANK/M90309
  • GENBANK/M97582
  • GENBANK/M97583
  • GENBANK/M97584
  • GENBANK/M97585
  • GENBANK/M97586
  • GENBANK/M97587
  • GENBANK/M97588
  • GENBANK/M97589