3.4.22.B71: SENP2 peptidase

This is an abbreviated version!
For detailed information about SENP2 peptidase, go to the full flat file.

Word Map on EC 3.4.22.B71

3.4.22.B71

sumoylation

medicine

atherosclerosis

aorta

d-flow

d-flow-induced

erk5

de-sumoylation

p90rsk

senps

epilepsy

Reaction

Synonyms

(SUMO-1)-specific protease 2, SENP2, sentrin/SUMO-specific protease 2, small ubiquitin-like modifier-specific protease, small ubiquitin-like modifier-specific protease 2, small ubiquitin-related modifier-specific isopeptidase, SUMO-specific isopeptidase, SUMO-specific protease, SUMO-specific protease 2

ECTree

3 Hydrolases

3.4 Acting on peptide bonds (peptidases)

3.4.22 Cysteine endopeptidases

3.4.22.B71 SENP2 peptidase

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Results	in table
1	Activating Compound
2	AA Sequence
4	Application
6	Cloned(Commentary)
3	Crystallization (Commentary)
5	Disease/ Diagnostics
4	Expression
37	General Information
5	kcat/KM [mM/s]
5	KM Value [mM]
9	Localization
9	Natural Substrates/ Products (Substrates)
167	Organism
4	pH Optimum
1	Posttranslational Modification
16	Protein Variants
4	Purification (Commentary)
1	Reaction
28	Reference
37	Source Tissue
37	Substrates and Products (Substrate)
26	Synonyms
4	Temperature Optimum [°C]
5	Turnover Number [1/s]

Natural Substrates Products

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Natural Substrates Products on EC 3.4.22.B71 - SENP2 peptidase

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(SUMO-1)-Mdm2 conjugate + H2O

SUMO + Mdm2

Mus musculus

SUMO conjugation of Mdm2 induces its co-localization and association with SENP2 at the PML bodies. SENP2 catalyzes the desumoylation process of Mdm2. SENP2 mediated regulation of Mdm2 critical for genome integrity in p53-dependent stress responses

714673

poly-SUMO-2/3-Aurora-B conjugate + H2O

Homo sapiens

specifically deconjugates SUMO from mitotic kinase Aurora-B. Lys202 on human Aurora-B is preferentially modified by SUMO, and enhancement of SUMOylation in cells facilitates Aurora-B autophosphorylation, which is essential for its activation. Conversely, SENP2-mediated deSUMOylation of Aurora-B down-regulates its autophosphorylation in cells and also impairs its re-activation in Aurora inhibitor VX-680-treated mitotic cells. Poly-SUMO-2 conjugation of Aurora-B occurs during the M phase ofthe cell cycle, and both SUMO-2 and PIAS3 are localized adjacent to Aurora-B in the kinetochores in early mitosis. Aurora-B is a mitotic SUMO substrate and its kinase activity is fine-tuned by the SUMO system

715109

SUMO-C/EBPbeta + H2O

SUMO + C/EBPbeta

Mus musculus

Q91ZX6

sumoylation causes destabilization of the C/EBPbeta protein and that this process can be reversed by SENP2

716210

SUMO-Mdm2 conjugate + H2O

SUMO + Mdm2

Mus musculus

Mdm2 is an important negative regulator of the p53 tumor suppressor. The SENP2 mediated SUMO modification of Mdm2 appears to be crucial for its subcellular trafficking

716658

SUMO-Pc2/CBX4 conjugate + H2O

SUMO + Pc2/CBX4

Mus musculus

Q91ZX6

Pc2/CBX4 is a polycomb repressive complex 1 (PRC1) subunit. SENP2 specifically controls Pc2/CBX4 contained PRC1 activity through regulation of the SUMOylation status of Pc2/CBX4, which facilitates its binding to H3K27me3 in mammalian cells to mediate transcriptional repression

716221

SUMOylated myocyte-specific enhancer factor-2A + H2O

deSUMOylated myocyte-specific enhancer factor-2A + SUMO

3 entries

additional information

Homo sapiens

nucleoporin Nup153 binds to SENP2 by interacting with the unique N-terminal domain of Nup153 as well as a specific region within the C-terminal FG-rich region. Nup153 is a substrate for SUMOylation, with this modification kept in check by the SUMO protease

732590