Synthesized peptide derived from human Hic-5 (Phospho-Tyr60)

This antibody detects endogenous levels of Hic-5 (Phospho-Tyr60) at Human, Mouse,Rat.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):HLyST

TGFB1I1 ARA55

Hic-5 (Phospho-Tyr60)

Transforming growth factor beta-1-induced transcript 1 protein ;
Androgen receptor coactivator 55 kDa protein ;
Androgen receptor-associated protein of 55 kDa ;
Hydrogen peroxide-inducible clone 5 protein ;
Hic-5 ;

transforming growth factor beta 1 induced transcript 1(TGFB1I1) Homo sapiens This gene encodes a coactivator of the androgen receptor, a transcription factor which is activated by androgen and has a key role in male sexual differentiation. The encoded protein is thought to regulate androgen receptor activity and may have a role to play in the treatment of prostate cancer. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2009],

Domain:The LD (leucine and aspartate-rich) motif 3 mediates interaction with GIT1 and functions as a nuclear export signal.,Domain:The LIM zinc-binding domains mediate glucocorticoid receptor coactivation and interaction with AR, CRIP2, ILK, LIMS1, NR3C1, PPARG, TCF3, TCF7L2, SLC6A3 and SMAD3. The LIM zinc-binding 2 and LIM zinc-binding 3 domains mediate targeting to focal adhesions and actin stress fibers. The LIM zinc-binding 3 and LIM zinc-binding 4 domains mediate interaction with TRAF4 and MAPK15. The LIM zinc-binding 4 domain mediates interaction with HSPB1, homooligomerization and targeting to the nuclear matrix. The LIM zinc-binding 3 domain mediates interaction with PTPN12.,Function: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.,induction:Up-regulated by TNF-alpha and hydrogen peroxide.,PTM:Phosphorylated by gonadotropin-releasing hormone-activated SRC.,similarity:Belongs to the paxillin family.,similarity:Contains 4 LIM zinc-binding domains.,subcellular location:Associated with the actin cytoskeleton; colocalizes with stress fibers.,subunit:Homooligomer. Interacts with CRIP2, HSPB1, ILK, LIMS1, LIMS2, NCK2, NUDT16L1, PAK, PPARG, PTPN12, TCF3, TCF7L2 and VCL. Forms a complex with GIT1 and ARHGEF7 (By similarity). Interacts with AR/androgen receptor in a ligand-dependent manner. Interacts with CSK, LYN, MAPK15, NR3C1, PPARG, PTK2, PTK2B, SLC6A3, SLC6A4, SMAD3, SRC and talin.,tissue specificity:Expressed in platelets, smooth muscle and prostate stromal cells (at protein level).,

Cell junction, focal adhesion. Nucleus matrix. Cytoplasm, cytoskeleton. Associated with the actin cytoskeleton; colocalizes with stress fibers.