UBAP2L

UBAP2L is a human gene that encodes for a protein called Ubiquitin Associated Protein 2 Like. This protein is thought to be involved in various cellular processes, including protein trafficking, endocytosis, and DNA damage response.

Gene Information:

The UBAP2L gene is located on chromosome 17q21.31 in humans. It is approximately 160 kb in length and contains multiple exons. Alternative splicing of the UBAP2L gene results in several transcript variants encoding different isoforms of the UBAP2L protein.

Protein Information:

The UBAP2L protein is a modular protein containing several functional domains. These domains include:

• Ubiquitin Associated (UBA) domain: This domain mediates interaction with ubiquitin, a small regulatory protein involved in tagging proteins for degradation or altering their function.
• Coiled-coil domains: These domains mediate protein-protein interactions and are important for the assembly of multiprotein complexes.
• Other domains: The protein also contains other domains of unknown function.

Function:

While the precise function of UBAP2L is not fully understood, it is believed to play a role in the following cellular processes:

• Protein trafficking: UBAP2L may be involved in the transport of proteins within the cell.
• Endocytosis: UBAP2L may participate in the internalization of molecules from the cell surface.
• DNA damage response: UBAP2L has been implicated in the cellular response to DNA damage.
• Cellular Homeostasis: Emerging research suggests a role in maintaining the stability and proper functioning of cellular components.

Clinical Significance:

Research suggests a potential association between variations in the UBAP2L gene and certain diseases, including some types of cancer and neurological disorders. However, further research is needed to fully elucidate the clinical significance of UBAP2L. Understanding the role of UBAP2L in these pathways may provide insights into the development of novel therapeutic strategies.

Interactions:

The UBAP2L protein is known to interact with several other proteins, suggesting that it functions as part of a larger protein complex. Further research is ongoing to identify and characterize these interacting proteins.