Primary structure of BMK1: a new mammalian map kinase

Biochem Biophys Res Commun. 1995 Aug 15;213(2):715-24. doi: 10.1006/bbrc.1995.2189.


Mitogen-activated protein (MAP) kinases comprise a family of conserved, eukaryotic enzymes that mediate responses to a wide variety of extracellular stimuli. We have identified a new human MAP kinase gene here termed BMK1. BMK1 encodes a protein of 816 amino acid residues and has at least three different forms of mRNA. BMK1 messages are abundant in heart, placenta and kidney but not detectable in liver. Although BMK1 has the dual phosphorylation site of MAP kinases characterized by the TEY sequence found in ERK1 and ERK2, it has a distinct C-terminal and loop-12 structure when compared to other mammalian MAP kinases. This suggests BMK1 may regulate signaling events distinct from those controlled by the ERK group of enzymes.

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
  • Base Sequence
  • Binding Sites
  • Blotting, Northern
  • Calcium-Calmodulin-Dependent Protein Kinases / chemistry*
  • Calcium-Calmodulin-Dependent Protein Kinases / genetics
  • DNA Primers
  • Humans
  • Kidney / enzymology
  • Mitogen-Activated Protein Kinase 7
  • Mitogen-Activated Protein Kinases*
  • Molecular Sequence Data
  • Myocardium / enzymology
  • Phosphorylation
  • Placenta / enzymology
  • Polymerase Chain Reaction
  • RNA, Messenger / analysis
  • RNA, Messenger / chemistry
  • Sequence Homology


  • DNA Primers
  • RNA, Messenger
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Mitogen-Activated Protein Kinase 7
  • Mitogen-Activated Protein Kinases

Associated data

  • GENBANK/U29725
  • GENBANK/U29726
  • GENBANK/U29727