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FLASH GENE
Symbol WBP11 contributors: mct/npt - updated : 08-07-2010
HGNC name WW domain binding protein 11
HGNC id 16461
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • nuclear localization signal in the N-terminus ,
  • two distinct PP1-binding domains involving a RVXF (Arg-Val-Xaa-Phe) motif
  • proline-rich C-terminal domain required for its subnuclear targeting to the speckles and binding PQBP1
  • mono polymer heteromer , dimer
    HOMOLOGY
    interspecies ortholog to murine Wbp11
    Homologene
    FAMILY
    CATEGORY DNA associated
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm
    intracellular,nucleus,nucleoplasm,nuclear bodies,nuclear speckles
    text
  • largely nuclear, but it accumulated in the cytoplasm following UV- or X-radiation
  • colocalized with mRNA splicing factors and intermediate filament containing perinuclear networks
  • basic FUNCTION
  • functioning as an mRNA factory in the nucleus
  • may function as a component of an mRNA factory in the nucleus
  • nucleocytoplasmic shuttling protein, implicated in pre-mRNA splicing, by nucleocytoplasmic shuttling
  • pre-mRNA splicing factor WBP11, is a protein ligand of PQBP1 (Nicolaescu 2008)
  • essential roles for PQBP1 and a binding partner, WBP11, in early development
  • CELLULAR PROCESS nucleotide, RNA splicing
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
  • PQBP1, WBP11 complex
  • component of the spliceosomes
  • WBP11-PQBP1-induced nuclear inclusions are distinct from the protein aggregates that are associated with polyglutamine diseases and represent dynamic nucleoplasmic heteropolymers of WBP11 and PQBP1 (Nicolaescu 2008)
  • one of the functional partners of PQBP1 from a potentially large repertoire of other signaling ligands
  • INTERACTION
    DNA binding to poly (rG) and G-rich single strand
    RNA
    small molecule
    protein
  • interacts with protein Ser/Thr phosphatase-1 (PP1) and with the polyglutamine-tract-binding protein 1 (PQBP1)
  • interacting with WBP4 (significantly, tandem WW domains of WBP4 are connected by a highly flexible region, enabling their simultaneous interaction with two proline-rich motifs of WBP11) (Huang 2009)
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    ANIMAL & CELL MODELS