Table 3.

STATs structure

DomainRoleReference
Oligomerization domain Interacts with other proteins and mediates oligomerization of STAT dimers to form tetramers. 40,41  
DNA binding domain Defines the DNA-binding specificity and mediates distinct signals for specific ligands. 42-44  
SH2 domain Mediates specific interactions between STAT-receptor, STAT-JAK, and STAT-STAT. 45-49 
Carboxyl-terminal domain Transcriptional activation domain that is thought to regulate the transcriptional activity of STATs and provide functional specificity. 50-53  
Tyrosine residue Phosphorylation site in the c-terminal domain approximately 700 residues from the N-terminus that regulates the DNA-binding activity of all STATs. On phosphorylation, mediates STAT dimerization by binding to the SH2 domain of the reciprocal STAT molecule. 10,12 
Serine residue3-150 A second phosphorylation site in the c-terminal domain.3-151 54,55 
DomainRoleReference
Oligomerization domain Interacts with other proteins and mediates oligomerization of STAT dimers to form tetramers. 40,41  
DNA binding domain Defines the DNA-binding specificity and mediates distinct signals for specific ligands. 42-44  
SH2 domain Mediates specific interactions between STAT-receptor, STAT-JAK, and STAT-STAT. 45-49 
Carboxyl-terminal domain Transcriptional activation domain that is thought to regulate the transcriptional activity of STATs and provide functional specificity. 50-53  
Tyrosine residue Phosphorylation site in the c-terminal domain approximately 700 residues from the N-terminus that regulates the DNA-binding activity of all STATs. On phosphorylation, mediates STAT dimerization by binding to the SH2 domain of the reciprocal STAT molecule. 10,12 
Serine residue3-150 A second phosphorylation site in the c-terminal domain.3-151 54,55 
F3-150

All except STAT2 and STAT6.

F3-151

In STAT1 and STAT3, the phosphorylation of Ser-727 enhances DNA binding affinity56 and activation of transcription57 and is necessary for optimal biologic activity of STAT3 in cellular transformation induced by Src.58 59 

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