BRENDA - Enzyme Database
show all sequences of 3.4.22.49

Separases: biochemistry and function

Moschou, P.N.; Bozhkov, P.V.; Physiol. Plant. 145, 67-76 (2012)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
additional information
generation of human cells with one hESP allele-encoding uncleavable protein and another allele harboring a single cleavage site, the cells grow slowly owing to cell cycle delay, in particular during G2/M transition, but not when it was expected, i.e. during anaphase
Homo sapiens
additional information
the loss-of-function of Esp1 activity in yeast cells could be complemented by the tobacco etch virus, TEV, protease, which is also able to cleave Scc1 thus promoting segregation of sister chromatids
Saccharomyces cerevisiae
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
separase is kept inactive in human cells by Cdk(Cdc2)-dependent phosphorylation even when securin is degraded
Homo sapiens
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Arabidopsis thaliana
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Caenorhabditis elegans
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Chlamydomonas reinhardtii
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Cryptosporidium muris
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Drosophila melanogaster
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. Securin is dispensable for the growth of normal human cells, in contrast to cancer cells, where depletion of PTTG1 leads to chromosome instability. The human separase-securin complex shows a whale-type distinct elongated pattern. In this complex, securin is thought to interact with the N-part of separase spanned by the ARM repeats. The N- to C-terminus intramolecular interaction in separase molecules is considered to be necessary for their catalytic activation, and this interaction is abolished by securin binding
Homo sapiens
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Oryza sativa
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Ricinus communis
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. The first 156 amino acids of Esp1 seem imperative for the binding of securin Pds1, it interacts with other parts of Esp1 as well
Saccharomyces cerevisiae
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. Interaction takes place between the N-terminus of separase and the C-terminus of securin
Schizosaccharomyces pombe
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Sorghum bicolor
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Vitis vinifera
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
additional information
human separase is associated with centrosomes but not with spindle before anaphase, featuring predominantly cytoplasmic localization in non-dividing cells
Homo sapiens
-
-
additional information
budding yeast Esp1 is localized to the centrosomes and spindle before anaphase
Saccharomyces cerevisiae
-
-
additional information
in fission yeast Cut1 features similar localization in the beginning of anaphase onset persisting on the spindle until mid-anaphase
Schizosaccharomyces pombe
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
the enzyme contains a Ca2+-binding EF-hand motif, which can possibly affect separase interaction with the spindle, similar to the budding yeast Esp1, or alternatively Ca2+ might be a critical component for (auto-)catalysis
Arabidopsis thaliana
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
cohesin + H2O
Drosophila melanogaster
-
?
-
-
?
cohesin + H2O
Chlamydomonas reinhardtii
-
?
-
-
?
cohesin + H2O
Homo sapiens
-
?
-
-
?
cohesin + H2O
Saccharomyces cerevisiae
-
?
-
-
?
cohesin + H2O
Schizosaccharomyces pombe
-
?
-
-
?
cohesin + H2O
Caenorhabditis elegans
-
?
-
-
?
cohesin + H2O
Ricinus communis
-
?
-
-
?
cohesin + H2O
Sorghum bicolor
-
?
-
-
?
cohesin + H2O
Oryza sativa
-
?
-
-
?
cohesin + H2O
Vitis vinifera
-
?
-
-
?
cohesin + H2O
Arabidopsis thaliana
-
?
-
-
?
cohesin + H2O
Cryptosporidium muris
-
?
-
-
?
additional information
Homo sapiens
autocleavage of human separase is to be essential and results in conformational changes
?
-
-
-
Slk19 + H2O
Saccharomyces cerevisiae
a protein implicated in the mitotic exit via its role in the stabilization of spindle in budding yeast
?
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Arabidopsis thaliana
Q5IBC5
ESP; gene AtESP
-
Caenorhabditis elegans
-
gene Sep-1
-
Chlamydomonas reinhardtii
-
gene ESP1
-
Cryptosporidium muris
-
gene Separase
-
Drosophila melanogaster
-
gene Sse/THR, Drosophila separase is encoded by two different genes: (1) Sse-encoding separase-like protein with protease domain and (2) THR (three rows) for the protein interacting with PIM (pimples), a securin homologue of Drosophila
-
Homo sapiens
-
gene hESP
-
Oryza sativa
-
gene Os02g0770700
-
Ricinus communis
-
gene Separase
-
Saccharomyces cerevisiae
-
gene ESP1
-
Schizosaccharomyces pombe
-
gene Cut1
-
Sorghum bicolor
-
gene XM_002454579
-
Vitis vinifera
-
gene LOC100259948
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
additional information
phosphorylation and potential autocleavage sites span the region of the last ARM repeats and the central unstructured region. Human separase has an N-terminal region spanned by 26 ARM repeats and separated from the two caspase-like domains, one of which is active, by the unstructured region
Homo sapiens
phosphoprotein
phosphorylation sites span the region of the last ARM repeats and the central unstructured region
Homo sapiens
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Arabidopsis thaliana
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Caenorhabditis elegans
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Chlamydomonas reinhardtii
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Cryptosporidium muris
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Drosophila melanogaster
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition. Autocleavage of human separase is to be essential and results in conformational changes. The C-terminal fragment of human separase, which results from autocleavage, is more unstable than the N-terminal one. The C-terminal fragment, which possesses the catalytic domain of separase, is subjected to the N-end rule pathway of protein degradation. Consequently, catalytic activity of separase can persist only for a short period of time facilitating switch off of its proteolytic function upon entering anaphase
Homo sapiens
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Oryza sativa
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Ricinus communis
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Saccharomyces cerevisiae
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Schizosaccharomyces pombe
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Sorghum bicolor
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Vitis vinifera
Source Tissue
Source Tissue
Commentary
Organism
Textmining
additional information
human separase is present in cells as a part of very large protein complex, which in addition to securin contains also Cdk and cyclin B1, both able to inhibit separase
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
cohesin + H2O
-
718194
Drosophila melanogaster
?
-
-
-
?
cohesin + H2O
-
718194
Chlamydomonas reinhardtii
?
-
-
-
?
cohesin + H2O
-
718194
Homo sapiens
?
-
-
-
?
cohesin + H2O
-
718194
Saccharomyces cerevisiae
?
-
-
-
?
cohesin + H2O
-
718194
Schizosaccharomyces pombe
?
-
-
-
?
cohesin + H2O
-
718194
Caenorhabditis elegans
?
-
-
-
?
cohesin + H2O
-
718194
Ricinus communis
?
-
-
-
?
cohesin + H2O
-
718194
Sorghum bicolor
?
-
-
-
?
cohesin + H2O
-
718194
Oryza sativa
?
-
-
-
?
cohesin + H2O
-
718194
Vitis vinifera
?
-
-
-
?
cohesin + H2O
-
718194
Arabidopsis thaliana
?
-
-
-
?
cohesin + H2O
-
718194
Cryptosporidium muris
?
-
-
-
?
additional information
autocleavage of human separase is to be essential and results in conformational changes
718194
Homo sapiens
?
-
-
-
-
Slk19 + H2O
a protein implicated in the mitotic exit via its role in the stabilization of spindle in budding yeast
718194
Saccharomyces cerevisiae
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
the human separase is composed of three domains: the tail, the trunk, and the head, structure modeling. The first two domains are spanned by Armadillo, ARM, repeats, which are composed of multiple 42 amino acid repeats and are present in the proteomes of all eukaryotic organisms. The ARM repeat domain is highly conserved right-handed super helix of ?-helices, which serves as molecular scaffold for protein-protein interactions. Phosphorylation and potential autocleavage sites span the region of the last ARM repeats and the central unstructured region. Human separase has an N-terminal region spanned by 26 ARM repeats and separated from the
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
generation of human cells with one hESP allele-encoding uncleavable protein and another allele harboring a single cleavage site, the cells grow slowly owing to cell cycle delay, in particular during G2/M transition, but not when it was expected, i.e. during anaphase
Homo sapiens
additional information
the loss-of-function of Esp1 activity in yeast cells could be complemented by the tobacco etch virus, TEV, protease, which is also able to cleave Scc1 thus promoting segregation of sister chromatids
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
separase is kept inactive in human cells by Cdk(Cdc2)-dependent phosphorylation even when securin is degraded
Homo sapiens
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Arabidopsis thaliana
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Caenorhabditis elegans
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Chlamydomonas reinhardtii
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Cryptosporidium muris
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Drosophila melanogaster
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. Securin is dispensable for the growth of normal human cells, in contrast to cancer cells, where depletion of PTTG1 leads to chromosome instability. The human separase-securin complex shows a whale-type distinct elongated pattern. In this complex, securin is thought to interact with the N-part of separase spanned by the ARM repeats. The N- to C-terminus intramolecular interaction in separase molecules is considered to be necessary for their catalytic activation, and this interaction is abolished by securin binding
Homo sapiens
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Oryza sativa
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Ricinus communis
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. The first 156 amino acids of Esp1 seem imperative for the binding of securin Pds1, it interacts with other parts of Esp1 as well
Saccharomyces cerevisiae
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. Interaction takes place between the N-terminus of separase and the C-terminus of securin
Schizosaccharomyces pombe
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Sorghum bicolor
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Vitis vinifera
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
additional information
human separase is associated with centrosomes but not with spindle before anaphase, featuring predominantly cytoplasmic localization in non-dividing cells
Homo sapiens
-
-
additional information
budding yeast Esp1 is localized to the centrosomes and spindle before anaphase
Saccharomyces cerevisiae
-
-
additional information
in fission yeast Cut1 features similar localization in the beginning of anaphase onset persisting on the spindle until mid-anaphase
Schizosaccharomyces pombe
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
the enzyme contains a Ca2+-binding EF-hand motif, which can possibly affect separase interaction with the spindle, similar to the budding yeast Esp1, or alternatively Ca2+ might be a critical component for (auto-)catalysis
Arabidopsis thaliana
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
cohesin + H2O
Drosophila melanogaster
-
?
-
-
?
cohesin + H2O
Chlamydomonas reinhardtii
-
?
-
-
?
cohesin + H2O
Homo sapiens
-
?
-
-
?
cohesin + H2O
Saccharomyces cerevisiae
-
?
-
-
?
cohesin + H2O
Schizosaccharomyces pombe
-
?
-
-
?
cohesin + H2O
Caenorhabditis elegans
-
?
-
-
?
cohesin + H2O
Ricinus communis
-
?
-
-
?
cohesin + H2O
Sorghum bicolor
-
?
-
-
?
cohesin + H2O
Oryza sativa
-
?
-
-
?
cohesin + H2O
Vitis vinifera
-
?
-
-
?
cohesin + H2O
Arabidopsis thaliana
-
?
-
-
?
cohesin + H2O
Cryptosporidium muris
-
?
-
-
?
additional information
Homo sapiens
autocleavage of human separase is to be essential and results in conformational changes
?
-
-
-
Slk19 + H2O
Saccharomyces cerevisiae
a protein implicated in the mitotic exit via its role in the stabilization of spindle in budding yeast
?
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
additional information
phosphorylation and potential autocleavage sites span the region of the last ARM repeats and the central unstructured region. Human separase has an N-terminal region spanned by 26 ARM repeats and separated from the two caspase-like domains, one of which is active, by the unstructured region
Homo sapiens
phosphoprotein
phosphorylation sites span the region of the last ARM repeats and the central unstructured region
Homo sapiens
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Arabidopsis thaliana
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Caenorhabditis elegans
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Chlamydomonas reinhardtii
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Cryptosporidium muris
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Drosophila melanogaster
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition. Autocleavage of human separase is to be essential and results in conformational changes. The C-terminal fragment of human separase, which results from autocleavage, is more unstable than the N-terminal one. The C-terminal fragment, which possesses the catalytic domain of separase, is subjected to the N-end rule pathway of protein degradation. Consequently, catalytic activity of separase can persist only for a short period of time facilitating switch off of its proteolytic function upon entering anaphase
Homo sapiens
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Oryza sativa
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Ricinus communis
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Saccharomyces cerevisiae
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Schizosaccharomyces pombe
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Sorghum bicolor
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
Vitis vinifera
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
additional information
human separase is present in cells as a part of very large protein complex, which in addition to securin contains also Cdk and cyclin B1, both able to inhibit separase
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
cohesin + H2O
-
718194
Drosophila melanogaster
?
-
-
-
?
cohesin + H2O
-
718194
Chlamydomonas reinhardtii
?
-
-
-
?
cohesin + H2O
-
718194
Homo sapiens
?
-
-
-
?
cohesin + H2O
-
718194
Saccharomyces cerevisiae
?
-
-
-
?
cohesin + H2O
-
718194
Schizosaccharomyces pombe
?
-
-
-
?
cohesin + H2O
-
718194
Caenorhabditis elegans
?
-
-
-
?
cohesin + H2O
-
718194
Ricinus communis
?
-
-
-
?
cohesin + H2O
-
718194
Sorghum bicolor
?
-
-
-
?
cohesin + H2O
-
718194
Oryza sativa
?
-
-
-
?
cohesin + H2O
-
718194
Vitis vinifera
?
-
-
-
?
cohesin + H2O
-
718194
Arabidopsis thaliana
?
-
-
-
?
cohesin + H2O
-
718194
Cryptosporidium muris
?
-
-
-
?
additional information
autocleavage of human separase is to be essential and results in conformational changes
718194
Homo sapiens
?
-
-
-
-
Slk19 + H2O
a protein implicated in the mitotic exit via its role in the stabilization of spindle in budding yeast
718194
Saccharomyces cerevisiae
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
the human separase is composed of three domains: the tail, the trunk, and the head, structure modeling. The first two domains are spanned by Armadillo, ARM, repeats, which are composed of multiple 42 amino acid repeats and are present in the proteomes of all eukaryotic organisms. The ARM repeat domain is highly conserved right-handed super helix of ?-helices, which serves as molecular scaffold for protein-protein interactions. Phosphorylation and potential autocleavage sites span the region of the last ARM repeats and the central unstructured region. Human separase has an N-terminal region spanned by 26 ARM repeats and separated from the
Homo sapiens
General Information
General Information
Commentary
Organism
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The catalytic domain of Arabidopsis separase exhibits 31 and 32% identity to the corresponding domains of human and budding yeast homologues, respectively, while the identity exceeds 50% within plant kingdom showing that the proteolytic domain of separases is the most conserved one. The sequence identity drops dramatically for the N-termini of separases. For example, the identity of the first 600 amino acid residues between Arabidopsis and Vitis vinifera separases does not exceed 39%, and it is only 30% between Arabidopsis and rice. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Arabidopsis thaliana
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Caenorhabditis elegans
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Chlamydomonas reinhardtii
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Cryptosporidium muris
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Drosophila melanogaster
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The catalytic domain of Arabidopsis thaliana separase exhibits 31 and 32% identity to the corresponding domains of human and budding yeast homologues, respectively. The sequence identity drops dramatically for the N-termini of separases. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Homo sapiens
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The sequence identity exceeds 50% within plant kingdom showing that the proteolytic domain of separases is the most conserved one. The sequence identity drops dramatically for the N-termini of separases. For example, the identity of the first 600 amino acid residues between Arabidopsis thaliana and Oryza sativa is only 30%. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Oryza sativa
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Ricinus communis
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The catalytic domain of Arabidopsis thaliana separase exhibits 31 and 32% identity to the corresponding domains of human and budding yeast homologues, respectively. The sequence identity drops dramatically for the N-termini of separases. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Saccharomyces cerevisiae
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Schizosaccharomyces pombe
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Sorghum bicolor
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The sequence identity exceeds 50% within plant kingdom showing that the proteolytic domain of separases is the most conserved one. The sequence identity drops dramatically for the N-termini of separases. For example, the identity of the first 600 amino acid residues between Arabidopsis thaliana and Vitis vinifera separases does not exceed 39%. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Vitis vinifera
malfunction
knocking down AtESP in meiocytes using RNAi unexpectedly converts the symmetric radial microtubule systems that form after telophase II into asymmetric structures partially resembling phragmoplasts
Arabidopsis thaliana
malfunction
loss of either APC or separase results in a failure of the transduction of the presumed polarity signal from the centrosome cortex
Drosophila melanogaster
malfunction
human cells with one hESP allele-encoding uncleavable protein and another allele harboring a single cleavage site grow slowly owing to cell cycle delay, in particular during G2/M transition, but not when it was expected, i.e. during anaphase
Homo sapiens
malfunction
in the cells lacking securin Pds1, Esp1 distribution is largely restricted to the cytoplasm
Saccharomyces cerevisiae
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Arabidopsis thaliana
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Caenorhabditis elegans
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Chlamydomonas reinhardtii
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Cryptosporidium muris
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Drosophila melanogaster
additional information
human separase is present in cells as a part of very large protein complex, which in addition to securin contains also Cdk and cyclin B1, both able to inhibit separase. Securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. The human separase-securin complex shows a whale-type distinct elongated pattern. In this complex, securin is thought to interact with the N-part of separase spanned by the ARM repeats. The N- to C-terminus intramolecular interaction in separase molecules is considered to be necessary for their catalytic activation, and this interaction is abolished by securin binding
Homo sapiens
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Oryza sativa
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Ricinus communis
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. Securin is dispensable for the growth of normal human cells. The first 156 amino acids of Esp1 seem imperative for the binding of securin Pds1, it interacts with other parts of Esp1 as well. Securin is not only a guardian of separase, but is also responsible for its translocation to the nucleus in the budding yeast
Saccharomyces cerevisiae
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. Interaction takes place between the N-terminus of separase and the C-terminus of securin
Schizosaccharomyces pombe
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Sorghum bicolor
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Vitis vinifera
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive. AtESP plays a role in microtubule organization or cell polarity, and an additional role for AtESP beyond cohesin cleavage
Arabidopsis thaliana
physiological function
function of separases in metaphase to anaphase transition, overview
Caenorhabditis elegans
physiological function
function of separases in metaphase to anaphase transition, overview
Chlamydomonas reinhardtii
physiological function
function of separases in metaphase to anaphase transition, overview
Cryptosporidium muris
physiological function
function of separases in metaphase to anaphase transition, overview. The activated APCCdc20/separase pathway plays a fundamental role in the establishment of the anterior-posterior axis
Drosophila melanogaster
physiological function
function of separases in metaphase to anaphase transition, overview. Human separase is a potential oncogene and hESP transcripts are accumulated in a large number of tumors
Homo sapiens
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive
Oryza sativa
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive
Ricinus communis
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In yeasts, separase is responsible for the removal of both arm and centromeric cohesin after its phosphorylation by Cdc5 or other Plks. Esp1 action is not limited to this stage. When securin is depleted in yeast cells, the proteolytic activity of Esp1 is no longer cell cycle regulated, while Scc1 is cleaved on schedule suggesting the existence of additional regulatory elements
Saccharomyces cerevisiae
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In yeasts, separase is responsible for the removal of both arm and centromeric cohesin after its phosphorylation by Cdc5 or other Plks. Separase can target both centromeric cohesin and cohesin of chromosomal arms. Cohesin is implicated in transcriptional regulation in Schizosaccharomyces pombe. When securin is depleted in yeast cells, the proteolytic activity of Esp1 is no longer cell cycle regulated, while Scc1 is cleaved on schedule suggesting the existence of additional regulatory elements
Schizosaccharomyces pombe
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive
Sorghum bicolor
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive
Vitis vinifera
General Information (protein specific)
General Information
Commentary
Organism
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The catalytic domain of Arabidopsis separase exhibits 31 and 32% identity to the corresponding domains of human and budding yeast homologues, respectively, while the identity exceeds 50% within plant kingdom showing that the proteolytic domain of separases is the most conserved one. The sequence identity drops dramatically for the N-termini of separases. For example, the identity of the first 600 amino acid residues between Arabidopsis and Vitis vinifera separases does not exceed 39%, and it is only 30% between Arabidopsis and rice. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Arabidopsis thaliana
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Caenorhabditis elegans
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Chlamydomonas reinhardtii
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Cryptosporidium muris
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Drosophila melanogaster
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The catalytic domain of Arabidopsis thaliana separase exhibits 31 and 32% identity to the corresponding domains of human and budding yeast homologues, respectively. The sequence identity drops dramatically for the N-termini of separases. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Homo sapiens
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The sequence identity exceeds 50% within plant kingdom showing that the proteolytic domain of separases is the most conserved one. The sequence identity drops dramatically for the N-termini of separases. For example, the identity of the first 600 amino acid residues between Arabidopsis thaliana and Oryza sativa is only 30%. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Oryza sativa
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Ricinus communis
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The catalytic domain of Arabidopsis thaliana separase exhibits 31 and 32% identity to the corresponding domains of human and budding yeast homologues, respectively. The sequence identity drops dramatically for the N-termini of separases. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Saccharomyces cerevisiae
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Schizosaccharomyces pombe
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Sorghum bicolor
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The sequence identity exceeds 50% within plant kingdom showing that the proteolytic domain of separases is the most conserved one. The sequence identity drops dramatically for the N-termini of separases. For example, the identity of the first 600 amino acid residues between Arabidopsis thaliana and Vitis vinifera separases does not exceed 39%. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
Vitis vinifera
malfunction
knocking down AtESP in meiocytes using RNAi unexpectedly converts the symmetric radial microtubule systems that form after telophase II into asymmetric structures partially resembling phragmoplasts
Arabidopsis thaliana
malfunction
loss of either APC or separase results in a failure of the transduction of the presumed polarity signal from the centrosome cortex
Drosophila melanogaster
malfunction
human cells with one hESP allele-encoding uncleavable protein and another allele harboring a single cleavage site grow slowly owing to cell cycle delay, in particular during G2/M transition, but not when it was expected, i.e. during anaphase
Homo sapiens
malfunction
in the cells lacking securin Pds1, Esp1 distribution is largely restricted to the cytoplasm
Saccharomyces cerevisiae
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Arabidopsis thaliana
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Caenorhabditis elegans
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Chlamydomonas reinhardtii
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Cryptosporidium muris
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Drosophila melanogaster
additional information
human separase is present in cells as a part of very large protein complex, which in addition to securin contains also Cdk and cyclin B1, both able to inhibit separase. Securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. The human separase-securin complex shows a whale-type distinct elongated pattern. In this complex, securin is thought to interact with the N-part of separase spanned by the ARM repeats. The N- to C-terminus intramolecular interaction in separase molecules is considered to be necessary for their catalytic activation, and this interaction is abolished by securin binding
Homo sapiens
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Oryza sativa
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Ricinus communis
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. Securin is dispensable for the growth of normal human cells. The first 156 amino acids of Esp1 seem imperative for the binding of securin Pds1, it interacts with other parts of Esp1 as well. Securin is not only a guardian of separase, but is also responsible for its translocation to the nucleus in the budding yeast
Saccharomyces cerevisiae
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. Interaction takes place between the N-terminus of separase and the C-terminus of securin
Schizosaccharomyces pombe
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Sorghum bicolor
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
Vitis vinifera
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive. AtESP plays a role in microtubule organization or cell polarity, and an additional role for AtESP beyond cohesin cleavage
Arabidopsis thaliana
physiological function
function of separases in metaphase to anaphase transition, overview
Caenorhabditis elegans
physiological function
function of separases in metaphase to anaphase transition, overview
Chlamydomonas reinhardtii
physiological function
function of separases in metaphase to anaphase transition, overview
Cryptosporidium muris
physiological function
function of separases in metaphase to anaphase transition, overview. The activated APCCdc20/separase pathway plays a fundamental role in the establishment of the anterior-posterior axis
Drosophila melanogaster
physiological function
function of separases in metaphase to anaphase transition, overview. Human separase is a potential oncogene and hESP transcripts are accumulated in a large number of tumors
Homo sapiens
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive
Oryza sativa
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive
Ricinus communis
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In yeasts, separase is responsible for the removal of both arm and centromeric cohesin after its phosphorylation by Cdc5 or other Plks. Esp1 action is not limited to this stage. When securin is depleted in yeast cells, the proteolytic activity of Esp1 is no longer cell cycle regulated, while Scc1 is cleaved on schedule suggesting the existence of additional regulatory elements
Saccharomyces cerevisiae
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In yeasts, separase is responsible for the removal of both arm and centromeric cohesin after its phosphorylation by Cdc5 or other Plks. Separase can target both centromeric cohesin and cohesin of chromosomal arms. Cohesin is implicated in transcriptional regulation in Schizosaccharomyces pombe. When securin is depleted in yeast cells, the proteolytic activity of Esp1 is no longer cell cycle regulated, while Scc1 is cleaved on schedule suggesting the existence of additional regulatory elements
Schizosaccharomyces pombe
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive
Sorghum bicolor
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive
Vitis vinifera
Other publictions for EC 3.4.22.49
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
732187
Hellmuth
Positive and negative regulati ...
Homo sapiens
J. Biol. Chem.
290
8002-8010
2015
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732670
Ho
A role for the budding yeast s ...
Saccharomyces cerevisiae
PLoS Genet.
11
e1005109
2015
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732669
Agircan
Sensors at centrosomes reveal ...
Homo sapiens
PLoS Genet.
10
e1004672
2014
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3
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732505
Han
Critical differences between i ...
Saccharomyces cerevisiae
Mol. Cell. Biol.
33
3400-3415
2013
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718194
Moschou
Separases: biochemistry and fu ...
Arabidopsis thaliana, Caenorhabditis elegans, Chlamydomonas reinhardtii, Cryptosporidium muris, Drosophila melanogaster, Homo sapiens, Oryza sativa, Ricinus communis, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Sorghum bicolor, Vitis vinifera
Physiol. Plant.
145
67-76
2012
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731689
Matsuo
Kendrin is a novel substrate f ...
Homo sapiens
Curr. Biol.
22
915-921
2012
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731697
Shindo
Separase sensor reveals dual r ...
Mus musculus
Dev. Cell
23
112-123
2012
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731698
Yaakov
Separase biosensor reveals tha ...
Saccharomyces cerevisiae
Dev. Cell
23
124-136
2012
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732703
Haass
The proteolytic activity of se ...
Homo sapiens
PLoS ONE
7
e42863
2012
4
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718037
Vinod
Computational modelling of mit ...
Saccharomyces cerevisiae
J. R. Soc. Interface
8
1128-1141
2011
1
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2
2
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718177
Kucej
DNA-dependent cohesin cleavage ...
Homo sapiens, Mus musculus, Saccharomyces cerevisiae
Nucleus
1
4-7
2011
4
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6
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6
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6
6
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718433
Bacac
Securin and separase modulate ...
Homo sapiens
Traffic
12
615-626
2011
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2
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4
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2
2
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-
708239
Bembenek
A role for separase in the reg ...
Caenorhabditis elegans
Curr. Biol.
20
259-264
2010
-
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2
2
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708282
Katis
Rec8 phosphorylation by casein ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae SK1
Dev. Cell
18
397-409
2010
-
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4
-
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4
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708285
Wu
A conditional mutation in Arab ...
Arabidopsis thaliana
Development
137
953-961
2010
-
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1
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4
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1
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2
2
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710036
Ishiguro
Shugoshin-PP2A counteracts cas ...
Homo sapiens
Nat. Cell Biol.
12
500-506
2010
-
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1
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2
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1
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718320
Yim
Cell division cycle 6, a mitot ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
107
19742-19747
2010
1
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2
-
1
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1
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3
3
-
-
-
697240
Sun
Separase is recruited to mitot ...
Homo sapiens
Cell
137
123-132
2009
-
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-
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-
-
1
-
-
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-
2
-
-
-
1
-
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1
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-
-
-
-
-
-
-
-
-
-
-
697382
Meyer
Overexpression and mislocaliza ...
Homo sapiens
Clin. Cancer Res.
15
2703-2710
2009
-
-
1
-
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-
3
-
-
-
-
3
-
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4
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-
-
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-
-
-
-
698110
Clift
Shugoshin prevents cohesin cle ...
Anaplasma marginale
Genes Dev.
23
766-780
2009
-
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-
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-
3
-
-
-
-
-
-
2
-
-
-
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-
-
-
-
-
-
-
-
-
-
700098
Lu
Mitotic exit in the absence of ...
Saccharomyces cerevisiae
Mol. Biol. Cell
20
1576-1591
2009
-
-
-
-
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1
-
1
-
-
-
-
3
-
-
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-
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1
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1
1
-
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-
-
-
-
-
-
-
-
-
-
-
-
700165
Huang
Preimplantation mouse embryos ...
Mus musculus
Mol. Cell. Biol.
29
1498-1505
2009
-
-
-
-
1
-
1
-
1
-
-
-
-
5
-
1
-
-
-
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-
-
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-
-
-
-
-
-
-
700280
Bessat
Functional characterization of ...
Trypanosoma brucei
Mol. Microbiol.
71
1371-1385
2009
-
-
1
-
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-
-
-
2
-
1
1
-
3
-
-
-
-
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-
1
-
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-
-
-
-
-
-
-
-
-
-
-
-
707105
Basu
Development and validation of ...
Homo sapiens
Anal. Biochem.
392
133-138
2009
1
-
1
-
-
-
1
1
-
-
-
1
-
3
-
-
-
-
-
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-
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3
-
1
1
1
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1
1
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1
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1
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1
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1
-
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-
-
-
2
-
4
3
-
1
1
1
-
1
1
-
-
1
1
1
1
-
-
708281
Tsou
Polo kinase and separase regul ...
Homo sapiens
Dev. Cell
17
344-354
2009
-
-
-
-
-
-
1
-
1
-
2
1
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
2
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
709217
Nakamura
Centrosomal Aki1 and cohesin f ...
Homo sapiens
J. Cell Biol.
187
607-614
2009
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
709220
Kudo
Role of cleavage by separase o ...
Homo sapiens
J. Cell Sci.
122
2686-2698
2009
-
-
1
-
2
-
1
-
1
-
-
-
-
4
-
-
1
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
1
-
-
1
-
-
-
-
-
-
1
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
710317
Yang
Arabidopsis separase functions ...
Arabidopsis thaliana
Plant Physiol.
151
323-333
2009
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
680926
Boos
Phosphorylation-dependent bind ...
Homo sapiens
J. Biol. Chem.
283
816-823
2008
-
-
-
-
5
-
2
-
-
-
-
-
-
4
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
2
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
682481
Huang
Inhibitory phosphorylation of ...
Mus musculus
PLoS Biol.
6
e15
2008
-
1
-
-
1
-
1
-
-
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
697171
Adachi
Cut1/separase-dependent roles ...
Schizosaccharomyces pombe
Cell Cycle
7
765-776
2008
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
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-
-
-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
697184
Sak
Effect of separase depletion o ...
Homo sapiens
Cell Prolif.
41
660-670
2008
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
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1
-
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2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
698119
Baskerville
The protease activity of yeast ...
Saccharomyces cerevisiae
Genetics
178
2361-2372
2008
-
-
1
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
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1
-
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-
-
-
-
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1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
699095
Queralt
Separase cooperates with Zds1 ...
Saccharomyces cerevisiae
J. Cell Biol.
182
873-883
2008
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
700096
Fujita
Regulation of the anaphase-pro ...
Mus musculus
Mol. Biol. Cell
19
5446-5455
2008
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
700945
Zhang
Overexpression of Separase ind ...
Homo sapiens, Mus musculus
Proc. Natl. Acad. Sci. USA
105
13033-13038
2008
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
679433
Bembenek
Cortical granule exocytosis in ...
Caenorhabditis elegans
Development
134
3837-3848
2007
-
1
-
-
1
-
-
-
2
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
680013
Shepard
A mutation in separase causes ...
Danio rerio
Genes Dev.
21
55-59
2007
-
1
-
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
681015
Nakajima
The complete removal of cohesi ...
Homo sapiens
J. Cell Sci.
120
4188-4196
2007
-
1
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
681037
Pemberton
Separase, securin and Rad21 in ...
Homo sapiens, Mus musculus
J. Cell. Physiol.
213
45-53
2007
-
2
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
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-
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-
-
-
-
-
-
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-
-
-
664544
Queralt
Downregulation of PP2A(Cdc55) ...
Saccharomyces cerevisiae
Cell
125
719-732
2006
-
-
-
-
-
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-
-
1
-
2
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
664545
Kudo
Resolution of chiasmata in ooc ...
Mus musculus
Cell
126
135-146
2006
-
-
-
-
-
-
-
-
1
-
-
1
-
5
-
-
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-
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2
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-
664552
Kawasaki
Fission yeast MAP kinase is re ...
Schizosaccharomyces pombe
Cell Cycle
5
1831-1839
2006
-
-
-
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1
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1
-
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-
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-
-
-
-
-
-
-
-
-
-
-
664553
Fan
Regulation of Separase in meio ...
Xenopus sp.
Cell Cycle
5
198-204
2006
1
-
1
-
-
-
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1
-
-
1
-
5
-
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-
-
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-
-
-
-
-
665049
Nagao
Securin can have a separase cl ...
Schizosaccharomyces pombe
Genes Cells
11
247-260
2006
1
-
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-
-
-
-
-
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-
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2
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-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
665797
Wirth
Separase: a universal trigger ...
Mus musculus
J. Cell Biol.
172
847-860
2006
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
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1
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-
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-
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
666177
Ikai
Cdc48 is required for the stab ...
Schizosaccharomyces pombe
J. Struct. Biol.
156
50-61
2006
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
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1
-
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1
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-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
666581
Liu
Arabidopsis separase AESP is e ...
Arabidopsis thaliana
Plant Cell
18
1213-1225
2006
-
-
-
-
-
-
-
-
1
-
-
1
-
4
-
-
-
-
-
2
-
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1
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1
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1
-
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-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
682062
Gorr
Essential CDK1-inhibitory role ...
Xenopus laevis
Nat. Cell Biol.
8
1035-1037
2006
-
-
-
-
3
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
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3
-
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-
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1
-
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
682065
Terret
Meiosis: separase strikes twic ...
Mus musculus, Saccharomyces cerevisiae
Nat. Cell Biol.
8
910-911
2006
-
2
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
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2
-
-
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1
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-
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
664551
Gimenez-Abian
Separase is required at multip ...
Homo sapiens
Cell Cycle
4
1576-1584
2005
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
665802
Pandey
Epithelial re-organization and ...
Drosophila sp. (in: Insecta)
J. Cell Sci.
118
733-742
2005
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
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1
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1
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-
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-
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1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
666319
Gorr
Mutual inhibition of separase ...
Xenopus sp.
Mol. Cell
19
135-141
2005
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
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1
-
-
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-
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-
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-
-
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-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
666418
Papi
Multiple roles for separase au ...
Homo sapiens
Nat. Cell Biol.
7
1029-1035
2005
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
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-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
665495
Sullivan
Studies on substrate recogniti ...
Saccharomyces cerevisiae
J. Biol. Chem.
279
1191-1196
2004
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
666436
Nagao
Separase-mediated cleavage of ...
Schizosaccharomyces pombe
Nature
430
1044-1048
2004
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
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1
-
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-
-
-
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-
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-
-
-
-
1
-
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-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
638867
Buonomo
Division of the nucleolus and ...
Saccharomyces cerevisiae
Dev. Cell
4
727-739
2003
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
638868
Sullivan
A non-proteolytic function of ...
Saccharomyces cerevisiae
Nat. Cell Biol.
5
249-254
2003
-
-
-
-
-
-
1
-
-
-
-
1
-
2
-
-
-
-
-
-
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1
-
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-
-
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-
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-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
638869
Chestukhin
Processing, localization, and ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
100
4574-4579
2003
-
-
1
-
4
-
-
-
1
-
1
-
-
5
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
4
-
-
-
-
-
1
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
664676
Terret
The meiosis I-to-meiosis II tr ...
Mus musculus
Curr. Biol.
13
1797-1802
2003
-
-
-
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
664744
Kitajima
Rec8 cleavage by separase is r ...
Schizosaccharomyces pombe
EMBO J.
22
5643-5653
2003
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
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-
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-
-
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-
-
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-
-
-
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-
1
-
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-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
666918
Pereira
Separase regulates INCENP-Auro ...
Saccharomyces cerevisiae
Science
302
2120-2124
2003
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
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-
-
-
-
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-
-
-
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-
-
-
1
-
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-
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-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
638862
Ross
Separase: a conserved protease ...
Drosophila melanogaster, Homo sapiens, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Xenopus laevis
Trends Cell Biol.
12
1-3
2002
3
-
-
-
-
-
4
-
-
3
-
4
-
5
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
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-
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-
3
-
4
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-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
638863
Zou
Anaphase specific auto-cleavag ...
Homo sapiens
FEBS Lett.
528
246-250
2002
-
-
1
-
3
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
638864
Hornig
The dual mechanism of separase ...
Saccharomyces cerevisiae
Curr. Biol.
12
973-982
2002
1
-
-
-
1
-
1
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
638865
Waizenegger
Regulation of human separase b ...
Homo sapiens
Curr. Biol.
12
1368-1378
2002
-
-
-
-
2
-
2
-
-
-
-
1
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
2
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
638866
Stegmeier
Separase, polo kinase, the kin ...
Saccharomyces cerevisiae
Cell
108
207-220
2002
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
638857
Sullivan
Orchestrating anaphase and mit ...
Saccharomyces cerevisiae
Nat. Cell Biol.
3
771-777
2001
-
-
-
-
-
-
-
-
2
-
-
3
-
2
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
3
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
638858
Amon
Together until separin do us p ...
Homo sapiens, Saccharomyces cerevisiae, Schizosaccharomyces pombe
Nat. Cell Biol.
3
E12-14
2001
-
-
-
-
-
-
-
-
-
-
-
8
-
5
-
-
-
-
-
-
-
-
14
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
14
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
638859
Siomos
Separase is required for chrom ...
Caenorhabditis elegans, Saccharomyces cerevisiae
Curr. Biol.
11
1825-1835
2001
-
-
-
-
-
-
-
-
1
-
-
2
-
5
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
638860
Jager
Drosophila separase is require ...
Drosophila melanogaster
Genes Dev.
15
2572-2584
2001
-
-
-
-
-
-
1
-
-
-
1
-
-
3
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1
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1
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638861
Hauf
Cohesin cleavage by separase r ...
Homo sapiens
Science
293
1320-1323
2001
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1
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4
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1
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638856
Yanagida
Cell cycle mechanisms of siste ...
Homo sapiens, Saccharomyces cerevisiae, Schizosaccharomyces pombe
Genes Cells
5
1-8
2000
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7
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1
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6
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3
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3
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6
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