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evolution
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in humans, the SENP/ULP protease family is comprised of seven members, six are SUMO-specific proteases, SENP1, SENP2, SENP3, SENP5, SENP6, and SENP7, whereas one is specific for another ubiquitin-like protein, Nedd8, or SENP8, also named DEN1 or NEDP1. SENP6 and SENP7 are the most divergent members in their conserved catalytic domain
evolution
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Plasmodium falciparum has only two predicted SENP proteases whereas human hosts have six SENPs
evolution
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SENP1 is a member of SENP family
malfunction
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cells lacking SENP6 show defects in spindle assembly and metaphase chromosome congression. A subset of proteins become undetectable on inner kinetochores after SENP6 depletion, particularly the CENP-H/I/K complex, whereas other changes in kinetochore composition mimick defects previously reported to result from CENP-H/I/K depletion, SENP6 depletion results in loss of the CENP-H/I/K complex from kinetochores, detailed overview
malfunction
growth defects caused by loss of ESD4 function are not due to increased synthesis of the stress signal salicylic acid, enzyme depletion causes delay in flowering
malfunction
growth defects caused by loss of ESD4 function are not due to increased synthesis of the stress signal salicylic acid. ELS1 depletion causes no measurable alterations in flowering and leaf development
malfunction
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slencing of SENP1 inhibits growth and colony formation of DLD-1 cells, results in G1-phase arrest, and upregulates the expression of some CDK inhibitors, overview
malfunction
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targeted disruption of SENP2 impairs the G-S transition required for mitotic and endoreupliation cell cycles during expansion of trophoblast stem cells and their differentiation into polyploidy cells, respectively. The disruption disturbs the subcellular distribution and SUMO modification of Mdm2, leading to interference with p53 degradation. SUMO conjugated Mdm2 is elevated in the SENP2-null cells
malfunction
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an ulp1 temperature-sensitive strain ulp1-333SGG with inactivated enzyme Ulp1 at restrictive temperature accumulates unprocessed SUMO protein
malfunction
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an ulp1 temperature-sensitive strain ulp1-333SGG with inactivated enzyme Ulp1 at restrictive temperature accumulates unprocessed SUMO protein
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physiological function
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nucleolar SUMO-specific protease, SMT3IP1/SENP3, controls the p53Mdm2 pathway. SMT3IP1 interacts with p53 and Mdm2, and desumoylates both proteins. SMT3IP1 bound to the acidic domain of Mdm2, which also mediates the p53 interaction, and competes with p53 for binding. Increasing expression of SMT3IP1 suppresses Mdm2-mediated p53 ubiquitination and subsequent proteasomal degradation. Desumoylation activity of SMT3IP1 is not necessary for p53 stabilization
physiological function
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SENP1 is essential for cell growth in the colon cancer cell line. SENP1 might play a role in cell cycle regulation of colon cancer cells
physiological function
SUMO protease ESD4 and ESD4-like SUMO protease 1, i.e. ELS1 or AtULP1a, show close sequence similarity, but different properties and are functionally distinct, overview
physiological function
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SUMO proteases can regulate the amounts of SUMO-conjugated proteins in the cell by cleaving off the isopeptidic bond between SUMO and the target protein
physiological function
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the key genetic pathway SENP2-Mdm2-p53 is essential for trophoblast development, mechanism underlying the isoform-specific SENP2 mediated regulation of Mdm2 critical for genome integrity in p53-induced cellular stress, overview. SENP2 catalyzes the desumoylation process of Mdm2. Dynamic SUMO modification is involved in a variety of cellular processes, including protein trafficking, transcriptional regulation, cell survival and death, and protein stability. High levels of SENP2, but not the other two forms, SENP2-M and SENP2-S, drastically diminished the cellular levels of p53. SENP2-mediated downregulation of p53 and p21, but not SENP2-mediated desumoylation of Mdm2, is sensitive to the Nutlin-3 treatment
physiological function
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the SUMO protease SENP6 is essential for inner kinetochore assembly. SENP6 stabilizes CENP-I by antagonizing RNF4, RNF4, a ubiquitin ligase which targets polysumoylated proteins for proteasomal degradation. CENP-I is degraded through the action of RNF4
physiological function
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Ulp1 facilitates sumoylation by processing precursor SUMO into its conjugation competent form. Conversely, Ulp1 also facilitates desumoylation by removing SUMO from nuclear and cytosolic proteins after conjugation. The essential small ubiquitin-like modifier, SUMO, protease Ulp1 is responsible for both removing SUMO/Smt3 from specific target proteins and for processing precursor SUMO into its conjugation-competent form
physiological function
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the enzyme Ulp1 does not appear to play a major role in the inactivation of the SUMO stress response consisting of consist of a simple SUMO conjugation-deconjugation cycle, overview. Isozyme Ulp1 is required for activation of the SUMO pro-protein, but SUMO stress response does not require proteasome-mediated degradation or Ulp1 activity
physiological function
in fission yeast lacking nucleoporin Nup132 (Sc/HuNUP133), Ulp1 is delocalized and can no longer antagonize sumoylation of the PIAS family SUMO E3 ligase, Pli1. Consequently, SUMO chain-modified Pli1 is targeted for proteasomal degradation by the concerted action of a SUMO-targeted ubiquitin ligase (STUbL) and Cdc48-Ufd1-Npl4
physiological function
in fission yeast lacking nucleoporin Nup132, Ulp1 is delocalized and can no longer antagonize sumoylation of the PIAS family SUMO E3 ligase, Pli1. Pli1 is targeted for proteasomal degradation by the concerted action of a SUMO-targeted ubiquitin ligase (STUbL) and Cdc48-Ufd1-Npl4
physiological function
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the catalytic UD domains of both Saccharomyces cerevisiae ScUlp1 and Kluyveromyces marxianus KmUlp1 show a high degree of sequence conservation, complement a Ulp1 deletion mutant in vivo, and process a SUMO precursor in vitro. Catalytically inactive recombinant fragments of the UD domains are able to efficiently bind a variety of purified SUMO isoforms and bind immobilized SUMO1 with nanomolar affinity
physiological function
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the catalytic UD domains of both Saccharomyces cerevisiae ScUlp1 and Kluyveromyces marxianus KmUlp1 show a high degree of sequence conservation, complement a Ulp1 deletion mutant in vivo, and process a SUMO precursor in vitro. Catalytically inactive recombinant fragments of the UD domains are able to efficiently bind a variety of purified SUMO isoforms and bind immobilized SUMO1 with nanomolar affinity
physiological function
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the catalytic UD domains of both Saccharomyces cerevisiae ScUlp1 and Kluyveromyces marxianus KmUlp1 show a high degree of sequence conservation, complement a Ulp1 deletion mutant in vivo, and process a SUMO precursor in vitro. Catalytically inactive recombinant fragments of the UD domains are able to efficiently bind a variety of purified SUMO isoforms and bind immobilized SUMO1 with nanomolar affinity
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physiological function
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the enzyme Ulp1 does not appear to play a major role in the inactivation of the SUMO stress response consisting of consist of a simple SUMO conjugation-deconjugation cycle, overview. Isozyme Ulp1 is required for activation of the SUMO pro-protein, but SUMO stress response does not require proteasome-mediated degradation or Ulp1 activity
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additional information
active site residue is Cys461
additional information
active site residue is Cys461
additional information
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active site residue is Cys461
additional information
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SUMO conjugation of Mdm2 induces its co-localization and association with SENP2 at the PML bodies