EC Number   |
General Information |
Reference |
|---|
   3.4.22.B70 | evolution |
C13orf22l is a member of the C19 cysteine protease USP family, two families of SUMO isopeptidases are known, and C13orf22l represents a third type of SUMO protease. Zebrafish C13orf22l is a functional homologue of human USPL1 |
731714 |
| 3.4.22.B70 | evolution |
the enzyme belongs to the superfamily of Ubl-specific proteases being Cys proteases. In all SENPs, an aromatic side chain, such as that of Trp or Phe, forms the channel lid. The catalytic Cys residues are located within the closed catalytic channels for binding the C-termini of ubiquitin-likes, and the catalytic residues undergo conformational changes when these proteases form complexes with their substrates. SENP1 is a model system for the Ubl-specific proteases in the Cys protease superfamily because it shares the same biochemical mechanism and its catalytic Cys is similarly buried as those of other Ubl-specific proteases. The mode of substrate recognition and binding of SENP1 may be shared by other de-Ubl enzymes |
732570 |
| 3.4.22.B70 | evolution |
USPL1 is a member of the C19 cysteine protease USP family, two families of SUMO isopeptidases are known, and USPL1 represents a third type of SUMO protease. W229, W237, Q405 and H421 are strictly conserved in USPL1 proteins, but different from residues in all other USPs |
731714 |
| 3.4.22.B70 | malfunction |
creation of SENP1 knockout mice based on a Cre-loxP system. Global deletion of SENP1 causes anemia and embryonic lethality between embryonic day 13.5 and postnatal day 1, correlating with erythropoiesis defects in the fetal liver |
715772 |
| 3.4.22.B70 | malfunction |
defects in adipocyte differentiation as well as PPARgamma expression in Senp1-/- mouse embryonic fibroblast cells induced by adipogenic stimuli. Deficiency in SUMOylation reduces Sharp-1 suppression of adipogenesis |
732144 |
| 3.4.22.B70 | malfunction |
differential localization of nucleoporins upon codepletion of SENP1 and SENP2 in HeLa cells, immunohistochemic analysis, overview |
732483 |
| 3.4.22.B70 | malfunction |
embryos homozygous for this mutant allele, Senp1M1Mku show phenotypic abnormalities beginning at embryonic day (E) 11.5 with the majority dying between E12.5 and E14.5. Enzyme defects lead to accumulation of Sumo1-modified proteins in homozygous embryos, a lethal process, phenotypes, overview. Senp1Gt mutants express a truncated Senp1 affecting Sumo2/3 levels |
731615 |
| 3.4.22.B70 | malfunction |
enzyme USPL1 depletion does not affect global sumoylation, but causes striking coilin mislocalization and impairs cell proliferation, functions that are not dependent on USPL1 catalytic activity |
731714 |
| 3.4.22.B70 | malfunction |
inhibition of endogenous enzyme SENP1 via the SENP1 dominant-negative mutant or shRNA-induced Pin1 SUMOylation in vivo. Knockdown of endogenous enzyme SENP1 expression also reduces Pin1-mediated cyclin D1 activation and again the enhanced ability of Pin1K6/63R to activate the cyclin D1 promoter is not reduced by enzyme SENP1 |
731577 |
| 3.4.22.B70 | malfunction |
knockdown of SENP1 by SENP1-siRNA inhibits pancreatic cancer cell proliferation, migration, and invasion. Silencing of SENP1 results in downregulation of MMP-9, which is pivotal for PDAC cell growth and migration |
732963 |
