Anti-UBR7 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

UBR7 also known as E3 ubiquitin-protein ligase UBR7 is a protein encoded by the UBR7 gene. The molecular mass of UBR7 is approximately 82 kDa. This protein is expressed in various human tissues with notable higher levels in the liver kidney and heart. Mechanically UBR7 functions as an E3 ubiquitin ligase which means it plays a role in attaching ubiquitin molecules to specific substrates marking them for degradation by the proteasome.

Biological function summary

UBR7 acts within cellular protein quality control by ensuring misfolded or damaged proteins are ubiquitinated for degradation. It is part of a larger ubiquitin-proteasome system which tightly controls protein turnover and homeostasis within the cell. This system helps maintain cell functions by regulating the abundance of key proteins involved in various cellular processes such as signal transduction and cell cycle control.

Pathways

The ubiquitin-proteasome system where UBR7 plays a significant role intersects with the cell cycle regulation and DNA damage response pathways. UBR7 interacts with proteins like p53 a well-known tumor suppressor playing a regulatory role in its stability and activity. Additionally it is involved in pathways concerning apoptosis contributing to programmed cell death when abnormal cells are detected.

Associated diseases and disorders

Aberrations in UBR7 activity have been linked to cancer particularly related to disruptions in the regulation of p53. The dysregulation can lead to uncontrolled cell growth and tumor development. UBR7 also associates with neurodegenerative disorders where the accumulation of misfolded proteins due to impaired ubiquitination contributes to neuronal damage. Here its connection with proteins such as Tau is significant as abnormal ubiquitination patterns have been observed in cases of Alzheimer's disease.