Recombinant human SAE1 + UBA2 protein (Active)

Supplementary info

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

Activity summary

SAE1 also known as SUMO-activating enzyme subunit 1 and UBA2 known as SUMO-activating enzyme subunit 2 work together as a heterodimer to activate small ubiquitin-related modifier (SUMO) proteins. SAE1 has a molecular weight of about 40 kDa. These proteins operate mainly in the nucleus where they facilitate the conjugation of SUMO to target proteins. SAE1 and UBA2 initiate the SUMOylation process by forming a thioester bond between the SUMO molecule and a catalytic cysteine residue on UBA2 through ATP hydrolysis.

Biological function summary

SAE1 and UBA2 play important roles in cellular processes like DNA repair transcriptional regulation and chromosome segregation. This heterodimer forms the initial step in the SUMOylation cascade which is important for modulating protein interactions locations and stability. These processes regulate gene expression and maintain genomic integrity. By modifying several key proteins SAE1 and UBA2 affect cellular responses to stress and DNA damage.

Pathways

Many cellular mechanisms rely on the SUMOylation pathway that SAE1 and UBA2 facilitate. The SUMOylation pathway interacts closely with the ubiquitin-proteasome system as both systems regulate protein homeostasis. Key proteins such as PIAS and SENP families are also involved in the SUMO pathway either as ligases or proteases and they modulate the effects initiated by SAE1 and UBA2. Additionally the pathway influences the response to cellular stress by modulating transcription factors and DNA repair enzymes.

Associated diseases and disorders

The function of SAE1 and UBA2 holds significance in cancer development and neurodegenerative diseases. In various cancer types alterations in SUMOylation controlled by SAE1 and UBA2 can lead to unchecked cellular proliferation and survival. UBA2 in particular often becomes a focus in cancer biology for its role in cellular stress pathways. In neurodegenerative diseases these proteins influence the aggregation and degradation of proteins such as tau and alpha-synuclein linking SUMOylation deficits to disease progression.