A synthesized peptide derived from human TRIP13, corresponding to a region within C-terminal amino acids.
Activating signal co-integrator-1 (ASC-1), originally identified as TRIP4, is a transcriptional co-activator of nuclear receptors that associates with specific components of the RNA polymerase II complex and binds the basal transcription factors TBP and TFIIA. ASC-1 functions with the transcription integrators SRC-1 and CBP/p300 through its zinc finger motif and is dependent on their ligand-dependent transactivation domain, AF2. Endogenous ASC-1 in HeLa cells is predominantly a nuclear protein. Under conditions of serum starvation, ASC-1 localizes to the cytoplasm.
This gene is a member of the zyxin family and encodes a protein with three LIM zinc-binding domains. This protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner and it regulates LPA-induced cell migration. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.
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