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PTK2B — TGFB1I1

Pathways - manually collected, often from reviews:

• NCI Pathway Database Coregulation of Androgen receptor activity: ARA55 (TGFB1I1) → PYK2 (PTK2B) (transcription, activates) Wang et al., J Biol Chem 2002*
  Evidence: mutant phenotype, reporter gene

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: TGFB1I1 — PTK2B (direct interaction, two hybrid) Matsuya et al., J Biol Chem 1998*
• IRef Biogrid Interaction: TGFB1I1 — PTK2B (direct interaction, two hybrid) Wang et al., J Biol Chem 2002*
• IRef Biogrid Interaction: TGFB1I1 — PTK2B (direct interaction, pull down) Wang et al., J Biol Chem 2002*
• IRef Biogrid Interaction: TGFB1I1 — PTK2B (physical association, affinity chromatography technology) Wang et al., J Biol Chem 2002*
• IRef Biogrid Interaction: TGFB1I1 — PTK2B (direct interaction, pull down) Matsuya et al., J Biol Chem 1998*
• IRef Biogrid Interaction: TGFB1I1 — PTK2B (physical association, affinity chromatography technology) Matsuya et al., J Biol Chem 1998*
• IRef Biogrid Interaction: TGFB1I1 — PTK2B (direct interaction, pull down) Thomas et al., J Cell Sci 1999*
• IRef Hprd Interaction: TGFB1I1 — PTK2B (in vivo) Wang et al., J Biol Chem 2002*, Aoto et al., Cell Struct Funct 2002*, Matsuya et al., J Biol Chem 1998*
• IRef Hprd Interaction: TGFB1I1 — PTK2B (in vitro) Wang et al., J Biol Chem 2002*, Aoto et al., Cell Struct Funct 2002*, Matsuya et al., J Biol Chem 1998*
• IRef Mppi Interaction: TGFB1I1 — PTK2B (coimmunoprecipitation) Matsuya et al., J Biol Chem 1998*
• IRef Ophid Interaction: TGFB1I1 — PTK2B (aggregation, interologs mapping) Brown et al., Bioinformatics 2005
• STRING interaction: PTK2B — TGFB1I1 (interaction, mapped from grid kegg_pathways intact)
• STRING interaction: TGFB1I1 — PTK2B (interaction, mapped from grid kegg_pathways mint intact)

Text-mined interactions from Literome

Ishino et al., FEBS Lett 2000 : Here we show that overexpression of CAKbeta or Fyn, but not FAK, enhanced the tyrosine phosphorylation of coexpressed Hic-5 in COS-7 cells ... Coexpression experiments revealed that the phosphorylation of Hic-5 by CAKbeta required the kinase activation of CAKbeta and binding of Hic-5 by CAKbeta
Aoto et al., Cell Struct Funct 2002 : These findings on nuclear translocation of CAK beta imply that CAKbeta may regulate nuclear processes such as transcription, particularly because Hic-5 was recently shown to be a coactivator of nuclear receptors