WWP, a new amino acid motif present in single or multiple copies in various proteins including dystrophin and the SH3-binding Yes-associated protein YAP65

Biochem Biophys Res Commun. 1994 Dec 15;205(2):1201-5. doi: 10.1006/bbrc.1994.2793.

Abstract

A new repeating amino acid motif, which we called WWP, was found in several proteins of yeast, nematod or vertebrate origin. Among these are dystrophin, the product of the Duchenne muscular dystrophy locus, a protein (YAP65) which associates in vitro with the Src homology domain 3 (SH3) of the Yes proto-oncogene product, and a human putative GTPase-activating protein. As is the case for proteins which contain the SH2, SH3 and PH domains, at least some of the WWP-containing proteins appear to be signaling or cytoskeletal proteins, associated with plasma or organellar membranes, and specific protein-protein contacts are likely to be crucial to their function.

Publication types

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

MeSH terms

  • Adaptor Proteins, Signal Transducing*
  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / chemistry*
  • Cell Cycle Proteins
  • Dystrophin / chemistry*
  • Humans
  • Mice
  • Molecular Sequence Data
  • Nematoda
  • Phosphoproteins / chemistry*
  • Saccharomyces cerevisiae
  • Sequence Homology, Amino Acid
  • Transcription Factors

Substances

  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins
  • Cell Cycle Proteins
  • Dystrophin
  • Phosphoproteins
  • Transcription Factors
  • YAP1 protein, human
  • Yap1 protein, mouse

Associated data

  • GENBANK/D10714
  • GENBANK/D29640
  • GENBANK/D34959
  • GENBANK/D35947
  • GENBANK/L11119
  • GENBANK/M60954
  • GENBANK/S53418
  • GENBANK/X80507
  • GENBANK/X80508
  • GENBANK/Z22176