SH3BGRL2 Human

SH3 Domain Binding Glutamic Acid-Rich Protein Like 2 (SH3BGRL2) is a protein encoded by the SH3BGRL2 gene in humans. This protein is part of a family of proteins known for their SH3 domain-binding capabilities and glutamic acid-rich sequences. These proteins play significant roles in various cellular processes, including signal transduction and cytoskeletal organization.

The SH3BGRL2 gene is located on human chromosome 1. The protein encoded by this gene has a thioredoxin-like fold, which is a common structural motif involved in redox reactions. However, unlike typical thioredoxin proteins, SH3BGRL2 lacks the cysteines necessary for catalytic activity . This suggests that while it shares structural similarities with thioredoxins, its function may differ significantly.

SH3BGRL2 is characterized by the presence of a C-terminal proline-rich sequence with SH3 domain- and HOMER EVH1 domain-binding motifs . These motifs are crucial for protein-protein interactions, indicating that SH3BGRL2 may play a role in assembling protein complexes and facilitating intracellular signaling pathways.

Although the precise biological functions of SH3BGRL2 are still under investigation, it is believed to be involved in regulating redox activity within cells. This regulatory role is essential for maintaining cellular homeostasis and protecting cells from oxidative stress. Additionally, proteins with similar structures, such as glutaredoxins and thioredoxins, are known to be upregulated in various cancers, suggesting a potential link between SH3BGRL2 and cancer biology .

Research into SH3BGRL2 is ongoing, with studies focusing on its role in cancer and other diseases. Understanding the function and regulation of this protein could provide insights into new therapeutic targets for treating conditions associated with oxidative stress and abnormal cell signaling.