|
Signal transducer and activator of transcription 5A is a protein that in humans is encoded by the ''STAT5A'' gene. ''STAT5A'' orthologs have been identified in several placentals for which complete genome data are available. == Structure == STAT5a shares the same six functional domains as the other members of the STAT family. It contains 20 amino acids unique to its C-terminal domain and is 96% similar to its homolog, STAT5b. The six functional domains and their corresponding amino acid positions are as follows: * N-Terminal domain (aa1-144): stabilized interactions to form tetramers * Coiled-coil domain (aa145-330): interacts with chaperones and facilitates protein-protein interactions for transcriptional regulation * DNA binding domain (aa331-496): permits binding to consensus gamma-interferon activation sequence (GAS) * Linker domain (aa497-592): stabilizes DNA binding * Src Homology 2 domain (aa593-685): mediates receptor-specific recruitment and STAT dimerization via phosphorylated tyrosine residue * Transcriptional activation domain (aa702-794): interacts with critical co-activators In addition to the six functional domains, specific amino acids have been identified as key mediators of STAT5a function. Phosphorylation of tyrosine 694 and glycosylation of threonine 92 are important for STAT5a activity. Mutation of serine 710 to phenylalanine results in constitutive activation. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「STAT5A」の詳細全文を読む スポンサード リンク
|