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Literature summary for 3.4.22.56 extracted from

  • Luo, M.; Lu, Z.; Sun, H.; Yuan, K.; Zhang, Q.; Meng, S.; Wang, F.; Guo, H.; Ju, X.; Liu, Y.; Ye, T.; Lu, Z.; Zhai, Z.
    Nuclear entry of active caspase-3 is facilitated by its p3-recognition-based specific cleavage activity (2010), Cell Res., 20, 211-222.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
GFP-tagged subunit and enzyme expression, the small subunit as well as the full-length caspase-3 display evident cytoplasm localization, while the large subunit and its truncated forms are distributed throughout the whole cell Homo sapiens

Protein Variants

Protein Variants Comment Organism
R207E/C163S site-directed mutagenesis, the mutant resides in the cytoplasm Homo sapiens
R64E site-directed mutagenesis, the mutant existed in the nuclear fraction, the subcellular localization signal in the rev-caspase-3 is not disrupted by the R64E mutation Homo sapiens
R64E/C163S site-directed mutagenesis, the mutant resides in the cytoplasm Homo sapiens
R64E/R207E site-directed mutagenesis, the mutant resides in the cytoplasm Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm pro-enzyme Homo sapiens 5737
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additional information p3-mediated cleavage activity abrogates the functions of other crm-1-dependent nuclear export signals with low nuclear export signal activity Homo sapiens
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nucleus activated enzyme, the enzyme harbors one crm-1-independent nuclear export signal but no nuclear localization signal residing at the small subunit of caspase-3. The nuclear entry of active caspase-3 is not mediated by passive diffusion, but by its p3-recognition-based specific cleavage activity. The p3-mediated cleavage activity abrogates the function of the nuclear localization signal in caspase-3, which is essential for the active caspase-3 to enter into the nucleus Homo sapiens 5634
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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General Information

General Information Comment Organism
malfunction mutations disrupting the cleavage activity or the p3 recognition site cause a defect in the nuclear entry of active caspase-3 Homo sapiens
physiological function caspase-3 exists in the form of pro-enzyme, and is located predominantly in the cytoplasm of cells. During apoptosis, caspase-3 is cleaved and activated by upstream caspases, and is translocated into the nucleus to cleave its nuclear substrates, resulting in characteristic apoptotic nuclear changes such as DNA fragmentation, chromatin condensation and nuclear disruption Homo sapiens