3.4.22.49: separase
This is an abbreviated version!
For detailed information about separase, go to the full flat file.
Word Map on EC 3.4.22.49
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3.4.22.49
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chromatid
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sister
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anaphase
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cohesin
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mitosis
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securin
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spindle
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metaphase
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meiotic
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checkpoint
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centromeres
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kinetochore
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anaphase-promoting
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scc1
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prophase
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aneuploidy
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rec8
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cdc14
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rad21
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metaphase-to-anaphase
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centrosome
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shugoshins
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centriole
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sister-chromatid
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metaphase-anaphase
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disjunction
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medicaid
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disengagement
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prometaphase
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missegregation
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polo-like
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biorientation
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cyclosome
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kleisin
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meiosis-specific
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chiasmata
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pds1
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condensins
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medicine
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diagnostics
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nondisjunction
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molecular biology
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cdk1-dependent
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pp2acdc55
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kinetochore-microtubule
- 3.4.22.49
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chromatid
-
sister
-
anaphase
- cohesin
-
mitosis
- securin
- spindle
-
metaphase
-
meiotic
-
checkpoint
-
centromeres
-
kinetochore
-
anaphase-promoting
- scc1
-
prophase
-
aneuploidy
- rec8
- cdc14
- rad21
-
metaphase-to-anaphase
- centrosome
- shugoshins
- centriole
-
sister-chromatid
-
metaphase-anaphase
-
disjunction
-
medicaid
-
disengagement
-
prometaphase
-
missegregation
-
polo-like
-
biorientation
-
cyclosome
-
kleisin
-
meiosis-specific
-
chiasmata
- pds1
-
condensins
- medicine
- diagnostics
-
nondisjunction
- molecular biology
-
cdk1-dependent
-
pp2acdc55
-
kinetochore-microtubule
Reaction
all bonds known to be hydrolysed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by an hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage =
Synonyms
AESP, AtESP, Cut1, Cut1/separase, ESP, Esp1, ESPL1, sep-1, separase, separin, SSE, TbSep
ECTree
3.4.22.49 separaseAdvanced search results
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Reaction on EC 3.4.22.49 - separase
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
all bonds known to be hydrolysed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by an hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage
all bonds known to be hydrolysed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by an hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage
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all bonds known to be hydrolysed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by an hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage
cohesin cleavage by human separase requires DNA in a sequence-nonspecific manner (in vitro). Autocleavage of separase is not stimulated by DNA. Cleavage of the chromosome-associated cohesins is sensitive to nuclease treatment.
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all bonds known to be hydrolysed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by an hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage
unphosphorylatable form of cohesin subunit Rad21 is less efficiently cleaved by Separase
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