Molecular characterization of AKAP149, a novel A kinase anchor protein with a KH domain

Biochem Biophys Res Commun. 1996 Aug 5;225(1):313-9. doi: 10.1006/bbrc.1996.1172.


The cytosolic cAMP activates in eukaryotic cells several isoforms of cAMP-dependent protein kinase (PKAs) involved in signal transduction. The effects of individual PKA isoforms are determined by their cellular localisation, specified through binding to distinct A Kinase Anchor Proteins (AKAPs). A new member of the AKAP family, a membrane-anchored 903 amino acid long protein, designated AKAP149, is characterized in the present work. It is a putative splicing variant of S-AKAP84 with the important new feature of a RNA-binding motif (KH domain). This domain together with the known characteristics of AKAPs suggests the involvement of AKAP149 in the phosphorylation-dependent regulation of RNA-processing.

Publication types

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

MeSH terms

  • A Kinase Anchor Proteins
  • Adaptor Proteins, Signal Transducing*
  • Alternative Splicing
  • Amino Acid Sequence
  • Antibodies
  • Binding Sites
  • Blotting, Southern
  • Blotting, Western
  • Carrier Proteins*
  • Colon
  • Consensus Sequence
  • Cyclic AMP-Dependent Protein Kinases / metabolism*
  • DNA Probes
  • Gene Library
  • Humans
  • Membrane Proteins*
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / immunology
  • RNA-Binding Proteins / biosynthesis*
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / metabolism
  • Sequence Homology, Amino Acid


  • A Kinase Anchor Proteins
  • AKAP1 protein, human
  • Adaptor Proteins, Signal Transducing
  • Antibodies
  • Carrier Proteins
  • DNA Probes
  • Membrane Proteins
  • Peptide Fragments
  • RNA-Binding Proteins
  • Cyclic AMP-Dependent Protein Kinases

Associated data

  • GENBANK/X97335