Hic-5: Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA- binding activity. Homooligomer. Interacts with CRIP2, HSPB1, ILK, LIMS1, LIMS2, NCK2, NUDT16L1, PAK, PPARG, PTPN12, TCF3, TCF7L2 and VCL. Forms a complex with GIT1 and ARHGEF7. Interacts with AR/androgen receptor in a ligand-dependent manner. Interacts with CSK, LYN, MAPK15, NR3C1, PPARG, PTK2/FAK1, PTK2B/PYK2, SLC6A3, SLC6A4, SMAD3, SRC and talin. Up-regulated by TNF and hydrogen peroxide. Expressed in platelets, smooth muscle and prostate stromal cells. Belongs to the paxillin family. 2 isoforms of the human protein are produced by alternative splicing.
Protein type: Transcription, coactivator/corepressor; Nuclear receptor co-regulator; Motility/polarity/chemotaxis
Cellular Component: extracellular matrix; focal adhesion; cytoskeleton; cytoplasm; intracellular; nucleus; cell junction
Molecular Function: protein binding; Roundabout binding; androgen receptor binding; zinc ion binding; metal ion binding; transcription coactivator activity
Biological Process: morphogenesis of embryonic epithelium; cell fate commitment; Wnt receptor signaling pathway; epithelial cell differentiation; response to heat; positive regulation of transcription, DNA-dependent; positive regulation of transforming growth factor beta receptor signaling pathway; cell differentiation; negative regulation of transforming growth factor beta receptor signaling pathway; ubiquitin-dependent SMAD protein catabolic process; negative regulation of fat cell differentiation
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