Literature summary for 3.4.22.B72 extracted from

Yan, S.; Sun, X.; Xiang, B.; Cang, H.; Kang, X.; Chen, Y.; Li, H.; Shi, G.; Yeh, E.T.; Wang, B.; Wang, X.; Yi, J.
Redox regulation of the stability of the SUMO protease SENP3 via interactions with CHIP and Hsp90 (2010), EMBO J., 29, 3773-3786.

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General Stability

General Stability	Organism
SENP3 is maintained at a low basal level under non-stress condition due to heat shock protein 90 (Hsp90)-independent Hsc70-interacting protein (CHIP)-mediated ubiquitination. Upon mild oxidative stress, SENP3 undergoes thiol modification, which recruits Hsp90. Hsp90/SENP3 association protects SENP3 from CHIP-mediated ubiquitination and subsequent degradation. This effect of Hsp90 requires the presence of CHIP	Homo sapiens

Organism

SENP3 is maintained at a low basal level under non-stress condition due to heat shock protein 90 (Hsp90)-independent Hsc70-interacting protein (CHIP)-mediated ubiquitination. Upon mild oxidative stress, SENP3 undergoes thiol modification, which recruits Hsp90. Hsp90/SENP3 association protects SENP3 from CHIP-mediated ubiquitination and subsequent degradation. This effect of Hsp90 requires the presence of CHIP

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9H4L4	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
polyubiquitination	SUMO2/3 protease SENP3 is regulated by Hsc70-interacting protein (CHIP) and heat shock protein 90 (Hsp90)	Homo sapiens

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Release 2023.1 (January 2023)