3.4.22.B70: SENP1 peptidase
This is an abbreviated version!
For detailed information about SENP1 peptidase, go to the full flat file.
Reaction
The enzyme catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO-1, SUMO-2 and SUMO-3 to their mature forms and deconjugation of SUMO-1, SUMO-2 and SUMO-3 from targeted proteins. Deconjugates SUMO-1 from homeodomain-interacting protein kinase 2. Deconjugates SUMO-1 from histone deacetylase 1, which decreases its transcriptional repression activity. Cleavage of Gly97-/-His98 bond in the SUMO-1 precursor with release of the propeptide His-Ser-Thr-Val. Cleavage of Gly93-/-Val94 bond in the SUMO-2 precursor with release of the propeptide Val94-Thyr. Cleavage of the Gly92-/-Val93 in the SUMO-3 precursor with release of the propeptide Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe.
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Synonyms
C13orf22l, SENP, SENP1, sentrin-specific protease 1, sentrin/SUMO-specific protease 1, small ubiquitin-like modifier protein-specific protease 1, small ubiquitin-related modifier-specific isopeptidase, SUMO isopeptidase, SUMO protease, SUMO protein-specific protease 1, SUMO-specific isopeptidase, SUMO-specific protease, SUMO-specific protease 1, ubiquitin-specific protease-like 1, USPL1
ECTree
Localization
Localization on EC 3.4.22.B70 - SENP1 peptidase
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enzyme USPL1 is a low-abundance protein that colocalizes with coilin in cajal bodies. USPL1 is an essential Cajal body component
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C603S is exclusively nuclear in comparison with the wild-type SENP1, which is consistently present in the cytoplasm, albeit at low steady state levels
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SENP1 is localized in the cytoplasm where it is complexed with an antioxidant protein thioredoxin. Tumor necrosis factor (TNF) induces the release of SENP1 from thioredoxin as well as nuclear translocation of SENP1
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SENP1 shuttles between the cytoplasm and the nucleus. SENP1 contains the nuclear export sequence (NES) within the extreme carboxyl-terminal region, and SENP1 is exported to the cytoplasm in a NES-dependent manner
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SENP1 expresses nuclear export sequences that allow these 2 SENPs to shuttle in and out of the nucleus
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C603S is exclusively nuclear in comparison with the wild-type SENP1, which is consistently present in the cytoplasm, albeit at low steady state levels. Presence of a single nonconsensus nuclear localization signal within the N-terminus of the protein. Residues within the predicted NLS1 region around positions 170-180 are critical for the nuclear localization of SENP1. SENP1 localization may be influenced by the expression of proteins that are targets of SUMO-1 modification, such as HDAC4 and PML, which affects the relative levels and localization of SUMO-1 conjugates within the cell
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SENP1 is localized in the cytoplasm where it is complexed with an antioxidant protein thioredoxin. Tumor necrosis factor (TNF) induces the release of SENP1 from thioredoxin as well as nuclear translocation of SENP1
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SENP1 shuttles between the cytoplasm and the nucleus. SENP1 contains the nuclear export sequence (NES) within the extreme carboxyl-terminal region, and SENP1 is exported to the cytoplasm in a NES-dependent manner. As sumoylations are nuclear events and most SUMO-conjugates are located within the nucleus, it appears that SENP1 might find its cellular targets subsequent to its nuclear relocalization
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SENP1 is primarily localized in the nucleus
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the enzyme SENP1 is targeted to kinetochores in mitosis
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