SUMO3
SUMO3 (Small Ubiquitin-like Modifier 3) is a protein that in humans is encoded by the SUMO3 gene. SUMO3 is a member of the SUMO (Small Ubiquitin-like Modifier) protein family, which plays a crucial role in post-translational modification of proteins. SUMOylation, the process of adding SUMO proteins to target proteins, is involved in various cellular processes including nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and cell cycle progression.
Function[edit | edit source]
SUMO3, like other SUMO proteins, is involved in modifying other proteins by covalently attaching to them in a process known as SUMOylation. This modification can alter the activity of the target protein, its interaction with other proteins, its location within the cell, and its stability. SUMO3 is highly similar to SUMO2 and shares about 50% similarity with SUMO1, another member of the SUMO family. However, SUMO2 and SUMO3 are nearly identical, differing in only a few amino acids. This close similarity suggests that SUMO2 and SUMO3 may have redundant or overlapping functions in cells.
SUMOylation by SUMO3 has been implicated in a variety of cellular processes. For example, it plays a role in the regulation of transcription factors, thereby influencing gene expression. It is also involved in the maintenance of genome stability, the regulation of the cell cycle, and the response to stress. SUMO3 modification of proteins is reversible, and specific enzymes known as SENPs (Sentrin/SUMO-specific proteases) can remove SUMO3, thus allowing dynamic regulation of SUMOylation in response to cellular signals.
Gene[edit | edit source]
The SUMO3 gene is located on chromosome 21 in humans. It encodes the SUMO3 protein, which is expressed in various tissues throughout the body. The gene undergoes transcription and translation to produce the SUMO3 protein, which is then processed to expose a C-terminal diglycine motif necessary for its conjugation to target proteins.
Clinical Significance[edit | edit source]
Alterations in SUMOylation patterns, including those mediated by SUMO3, have been associated with various diseases, including cancer, neurodegenerative diseases, and heart disease. Abnormal SUMOylation can affect the stability, localization, and function of proteins involved in critical cellular pathways, leading to disease. Research into SUMO3 and its role in SUMOylation may provide insights into the mechanisms of these diseases and potential therapeutic targets.
See Also[edit | edit source]
References[edit | edit source]
This article is a molecular biology stub. You can help WikiMD by expanding it!
Search WikiMD
Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD
WikiMD's Wellness Encyclopedia |
Let Food Be Thy Medicine Medicine Thy Food - Hippocrates |
Translate this page: - East Asian
中文,
日本,
한국어,
South Asian
हिन्दी,
தமிழ்,
తెలుగు,
Urdu,
ಕನ್ನಡ,
Southeast Asian
Indonesian,
Vietnamese,
Thai,
မြန်မာဘာသာ,
বাংলা
European
español,
Deutsch,
français,
Greek,
português do Brasil,
polski,
română,
русский,
Nederlands,
norsk,
svenska,
suomi,
Italian
Middle Eastern & African
عربى,
Turkish,
Persian,
Hebrew,
Afrikaans,
isiZulu,
Kiswahili,
Other
Bulgarian,
Hungarian,
Czech,
Swedish,
മലയാളം,
मराठी,
ਪੰਜਾਬੀ,
ગુજરાતી,
Portuguese,
Ukrainian
Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.
Contributors: Prab R. Tumpati, MD